methods

Abstract

The invention provides advantageous methods for determining the location of the binding site of an RNA binding protein on a RNA nucleic acid.

Description

[0001]METHODS CROSS REFERENCE TO RELATED APPLICATIONS The present application claims priority to U.S. Application No. 63 / 496,906, filed 05 / 08, 2023, the disclosures of which is incorporated herein by reference in its entirety. Background RNA transcripts are bound and regulated by RNA-binding proteins (RBP), which mediate diverse functions including post-transcriptional control of gene expression and splicing regulation. Identifying RBP–RNA interactions is therefore critical in understanding the complex role of these interactions in different cellular processes, including disease- associated molecular processes. There are a number of biochemical assays to screen or map for interactions between RBPs and RNA, including technically challenging in vivo screening methods. Among these methods are TRIBE (targets of RNA-binding proteins identified by editing) and hyperTRIBE. TRIBE is a technique that couples an RBP to the catalytic domain of the Drosophila RNA- modifying enzyme ADAR (ADARcd) and expresses the fusion protein in cultured cells of interest or in vivo, and is described in McMahon et al., 2016, Cell, 165(3):742-753 (hereinincorporated by reference). In hyperTRIBE, the wild-type Drosophila ADAR is replacedwith a Drosophila ADARcd having an E488Q mutation. hyperTRIBE is described in Rahman et al., 2018, Nat. Protoc. 13:1829-1849 (hereby incorporated by reference). ADAR is an RNA adenosine deaminase that catalyses A to I transitions in a semi- indiscriminate manner and is therefore able to deaminate target A residues in most contexts. The principle behind TRIBE and hyperTRIBE is that dADAR or ADARcd respectively is recruited to the binding site of the RBP through the fusion protein and subsequently marks any binding site through catalysing A to I edits, which following RNA- seq is read as G. Thus, through identifying regions of RNA where A to G edits are enriched relative to background it is possible to map the binding sites of the probe RBP on a transcriptome wide level. The TRIBE system is constrained by a low editing efficiency and editing-sequence bias from the ADARcd. As described in Rahman et al., 2018, the hyperTRIBE assay involvesoverexpression of ADARcd and, due to the semi-indiscriminate nature of its activity, it isconceivable that editing will occur that is independent of the RBP leading to “off-target” editing. Such “off-target” editing through overexpression of deaminases has been routinely observed in the CRISPR base editing field and is a significant hindrance in the accurate interpretation of editing data and therefore, in the case of hyperTRIBE, the accurate identification of the binding sites of RBPs (Slesarenko, Y.S., Lavrov, A.V. &Smirnikhina, S.A. Off-target effects of base editors: what we know and how we can reduceit. Curr Genet 68, 39–48 (2022)). The off-target effects and hindered accuracy of TRIBE and hyperTRIBE represent significant limitations that confound the identification of bona fide RBP-RNA interactions. Accordingly, there exists a need for improved methods of identifying RBP-RNA interactions. Summary of the invention The inventors have designed methods and associated components – for example expression cassettes, vectors, cells, fusion peptides, and kits – that allow the identification of binding interactions between RNA binding proteins (RBPs) and RNA. In addition to identifying RBP-RNA interactions, the methods and associated components provided herein enable the discovery of the site on a given RNA at which a given RBP binds. As mentioned above, elucidating these processes is critical for understanding the role of RBP-RNA interactions in cellular processes and disease. The present invention enables the high-throughput and large-scale screening of an RBP (“query polypeptide”) of interest against an RNA (“first query RNA nucleic acid”) or large RNA space (“plurality of query RNA nucleic acids”), for example the whole transcriptome of a cell or a portion thereof. The methods of the invention therefore allow the identificationof RNA molecules that interact with the RBP (“query polypeptide”) of interest to beidentified or distinguished from RNA molecules that do not interact with the RBP. Conversely, the methods also allow the identification of RBPs that interact with a given query RNA nucleic acid. In addition, the methods allow the screening of a polypeptide that is suspected to be an RBP (“query polypeptide”) against an RNA or an RNA space in order to determine whether the query polypeptide does indeed interact with an RNA; and if so, to distinguish the RNAs with which the RBP interacts. For example, the identification of an interaction between a query polypeptide and a query RNA nucleic acid is assessed by contacting the query RNA nucleic acid with a test polypeptide as described herein. A test polypeptide may generally comprise: a query polypeptide or fragment thereof and an RNA modifying domain or fragment thereof that is capable of modifying RNA; a query polypeptide or fragment thereof and a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain (also known as a “split RNA modifying domain”) in which case the second portion of the RNA modifying domain isprovided as a separate polypeptide); or a query polypeptide or fragment thereof and arecruitment module comprising a first affinity domain as described herein (in which case an RNA modifying domain or fragment fused to an affinity domain is provided as a separate polypeptide). In each of these designs, binding of the query polypeptide (and thus the test polypeptide as a whole) leads to the recruitment of an RNA modifying polypeptide or fragment thereof capable of modifying RNA to a query RNA nucleic acid, either directly because the whole RNA modifying polypeptide or fragment thereof capable of modifying RNA is fused to the query polypeptide; or indirectly, because the first portion of the RNA modifying polypeptide and second portion of an RNA modifying domain are brought into proximity, forming a functional form of the “split RNA modifying domain”, or because the test polypeptide comprising a query polypeptide and recruitment module comprising a first affinity domain and RNA modifying polypeptide capable of modifying RNA comprising a second affinity domain are brought into proximity. The interaction between the test polypeptide and the query RNA nucleic acid thereby results in the modification of the RNA in a manner that may be detected, for example, by RNA sequencing. The presence of amutation and / or modification on a query RNA nucleic acid that has been contacted with atest polypeptide compared to a query RNA nucleic acid that is not contact with the test polypeptide indicates that the test and / or query polypeptide interact with the query RNA nucleic acid. By detecting portions of the query RNA nucleic acid sequence that are enriched for mutations and / or modifications, it is also possible to identify the location at which the test and / or query polypeptide interacts with the query RNA nucleic acid. Without wishing to be bound by theory, it is thought that splitting the RNA modifying domain or fragment thereof into a first and second portion – or providing the RNA modifying domain or fragment thereof as a separate polypeptide that is capable of being recruited to the test polypeptide by association of the first and second affinity domains – will prevent the RNA modifying domain or fragment thereof from modifying RNA (for example, the query RNA) unless the full RNA modifying domain or fragment thereof is associated with the test polypeptide. Similar effects have been observed in engineered CRISPR base editors (see, e.g., Berríos et al., 2021, Nat Biol. Chem., 17(12):1262-1270 doi:10.1038 / s41589-021-00880-w, herein incorporated by reference). In this way, it isexpected that off-target editing of RNAs associated with the hyperTRIBE system described in Rahman et al., 2018 will be reduced using the methods and associated components provided herein. The query polypeptide may be fused to the RNA modifying domain, fragment thereof capable of modifying RNA, first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of theRNA modifying domain or recruitment module by a polypeptide linker. The polypeptidelinker may be a flexible linker or may be a linker that is endogenous to the test polypeptide, for example as set out in the “embedded deaminase” embodiments described herein. Without wishing to be bound by theory, the inventors theorise that the incorporation of a polypeptide linker – for example a flexible linker – into the test polypeptide, or incorporating the RNA modifying domain into the existing architecture of the query polypeptide using a linker that is endogenous to the test polypeptide, will allow the RNA modifying domain, fragment thereof capable of modifying RNA, first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain or recruitment module improved access to the RNA, increase editing efficiency. Similar linker effects have been observed in engineered CRISPR base editors (see, e.g., Tan et al., 2019, Nat. Commun. 10(1):439, doi: 10.1038 / s41467-018-08034-8, herein incorporated by reference). The polypeptide linker may be tailored to each specific query polypeptide. It is expected that these factors will improve the overall performance of RBP-RNA interaction mappingcompared to existing methods such as the TRIBE and hyperTRIBE systems described inMcMahon et al., 2016 and Rahman et al., 2018. When the methods of the present invention are conducted in a cell, the test polypeptide may be expressed in the cell. Expression of the test polypeptide may be under the control of an inducible promoter, allowing temporally precise expression of the test polypeptide to be achieved. Without wishing to be bound by theory, it is anticipated that placing the test polypeptide under the control of an inducible promoter will decrease or prevent off-target editing of RNAs associated with the hyperTRIBE system described in Rahman et al., 2018. Similar effects have been observed in engineered CRISPR base editors (see, e.g., Mok et al., 2020, Nature, 583(7817):631-637 doi: 10.1038 / s41586-020-2477-4, herein incorporated by reference). The diverse arrangements of the test polypeptide provided herein allow multiplexed screening of multiple query polypeptides at the same time. For example, a test polypeptidemay comprise a first query polypeptide that may be fused to a first RNA modifying domainor fragment thereof (for example, an adenosine deaminase, which converts A to I, detectable as an A>G mutation in an RNA sequence) and a second test polypeptide may comprise a second query polypeptide that may be fused to a second RNA modifying domain or fragment thereof (for example, a cytosine deaminase, which converts C to U, detectable as a C>T or C>U mutation in an RNA sequence). In this way, it is possible to generate a distinct modification and / or mutational profile for each of the first and second test polypeptides, allowing the user to identify clearly RNAs with which each test polypeptideindependently interacts. Using this approach, it is also possible to identify sites on onequery RNA nucleic acid that interact with the first and second test polypeptides (and thus first and second query polypeptides). Similarly, a single test polypeptide comprising a first query polypeptide may be fused to recruitment module capable of recruiting first and second RNA modifying domains or fragments thereof capable of modifying RNA, where the recruitment module comprises a first affinity domain and the first and second RNA modifying domains or fragments thereof each further comprise a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain. The first RNA modifying domain or fragment thereof capable of modifying RNA may be, for example, an adenosine deaminase, which converts A to I, detectable as an A>G mutation in an RNA sequence. The second RNA modifying domain or fragment thereof capable of modifying RNA may be, for example, a cytosine deaminase, which converts C to U, detectable as a C>T or C>U mutation in an RNA sequence. In this way, the test polypeptide can recruit both an adenosine deaminaseand a cytosine deaminase to a query RNA nucleic acid, thereby generating a mutationalprofile that incorporates both A>G and C>T or C>U mutations in the test RNA nucleic acid. The incorporation of two distinct types of mutation into a query RNA nucleic acid using this arrangement allows more confident identification of RNAs with which the test polypeptide interacts. It will be appreciated that the same results may be achieved using first and second test polypeptides that respectively comprise first and second query polypeptides or fragments thereof and a first and second first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding first or second second portion of the RNA modifying domain; or first and second query polypeptides or fragments thereof and a recruitment module comprising a first or second first affinity domain as described herein (in which case the first and second RNA modifying domains or fragments thereof fused to corresponding first or second second affinity domains are provided as separate polypeptides). Finally, the methods and corresponding components provided herein may be used to produce tailored test polypeptides, for example by identifying combinations of query polypeptides, linkers, and / or RNA modifying domains or fragments thereof capable of modifying RNA, first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, and / or recruitment domains that provide optimal query RNA editing, for example optimal on-target / off-target ratios. In summary, the methods and corresponding components provided herein allow more efficient, more precise, and more controlled detection of interactions between query polypeptides (such as RBPs) and query RNA nucleic acids than extant methods such as TRIBE and hyperTRIBE. Accordingly, the present invention provides methods and corresponding components that is and are improved over existing methods of identifying interactions between a query polypeptide an a query RNA nucleic acid. Detailed description of the invention In a first aspect, the invention provides a method for identifying a binding interaction between a query polypeptide and a query RNA nucleic acid, the method comprising: a) contacting a first query RNA nucleic acid with a test polypeptide, wherein the test polypeptide comprises the query polypeptide or a fragment thereof and: i) an RNA modifying domain or fragment thereof capable of modifying RNA; or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein:the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain; or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; optionally wherein the test polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and:i. an RNA modifying polypeptide domain capable of modifying RNA; ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; wherein where said test polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a first test query RNA nucleic acid; andb) detecting the presence or absence of at least one modification in the first test query RNA nucleic acid; and c) determining that there is a binding interaction between the query polypeptide and query RNA nucleic acid when a modification is detected in the first test query RNA nucleic acid.As will be apparent to the skilled person, the RNA modifying domain is brought intoproximity with the query polynucleotide by virtue of the query polypeptide binding (if it does so) to the query polynucleotide and bringing with it the RNA modifying domain, first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, or the recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA. This applies to all aspects and embodiments described herein. It will also be clear that in step (b), where the presence or absence of at least one modification in the first test query RNA nucleic acid is detected, the modification that is detected is a modification that is capable of being induced by the RNA modifying domain. Again, this applies to all aspects and embodiments described herein. It will also be clear to the skilled person that where the test polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought intoproximity with a corresponding second portion of the RNA modifying domain, that both ofthe first portion and the corresponding second portion are not able to modify the query polynucleotide independently of one another. RNA modification will only occur when the first and second portion of the RNA modifying domain are brought into proximity with one another. This applies to all aspects and embodiments described herein. Similarly, where the test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA that comprises a second affinity domain, in preferred embodiments, the RNA modifying domain is incapable of modifying the query polynucleotide in the absence of binding to the first affinity domain on the test polypeptide. This applies to all aspects and embodiments described herein. In a related aspect, the invention provides a method for identifying one or more binding sites of a query polypeptide on a query RNA nucleic acid, the method comprising: a) contacting a first query RNA nucleic acid with a test polypeptide, wherein the test polypeptide comprises the query polypeptide or a fragment thereof and:i) an RNA modifying domain or fragment thereof capable of modifying RNA, or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein:the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain; or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain;optionally wherein the test polypeptide is a fusion protein comprising thequery polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNA; ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain;wherein where said test polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; orwherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a first test query RNA nucleic acid; b) detecting the presence or absence of at least one modification in the first test query RNA nucleic acid and generating a modification profile for the first test query RNA nucleic acid; and c) determining one or more binding sites of the query polypeptide on the query RNA nucleic acid using the modification profile.As mentioned above, the query polypeptide may be any polypeptide of interest. Accordingly, in some embodiments, the query polypeptide is an RNA binding polypeptide or an RNA binding fragment thereof, optionally an RNA binding protein (RBP) or a fragment thereof. For example, in some embodiments the query polypeptide is a polypeptide that is known to bind to RNA. In some embodiments, the query polypeptide is a polypeptide that is suspected to be an RNA binding polypeptide or an RNA binding fragment thereof. Methods of determining whether a polypeptide is suspected to be an RNA binding polypeptide or RNA binding fragment thereof are known to the person skilled in the art, and may include, for example, bioinformatic analysis of the sequence of the query polypeptide to detect the presence of a conserved RNA binding domain. Exemplary RNA binding domains include the RRM domain (RNA-recognition motif).In some embodiments the query polypeptide is an RNA binding protein that is selectedfrom the group comprising or consisting of: an RNA polymerase or a subunit thereof; a spliceosome protein or a subunit thereof; a ribosome or a subunit thereof; an RNA editing enzyme; a polyadenylase; a nuclease; a nuclear pore complex protein or subunit thereof; an RNA methyltransferase; and RNA demethylase; an RNA acetylase; an RNA deacetylase; a translational regulator; a post-transcriptional regulator; and a metabolic enzyme. In more specific embodiments, the query polypeptide is an RNA binding protein that isselected from the group comprising or consisting of: PUM2, CSDE1, NONO, MEX3A, PTBP3,IGF2BP1, ZEB1, LIN28, HNRNPNU, IRP1, IRP2, ANXA2, HuR, Musashi-1, TAF15, hnRNP H / F, FUS, EWSR1, SAMD4B, VTS1, CELF1; for example is PUM2. In some embodiments the query polypeptide is an RBP that: a) comprises or consists of an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 1, SEQ ID NO: 57, SEQ ID NO: 103, SEQ ID NO: 105, SEQ ID NO: 107, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 1, , SEQ ID NO: 57, SEQ ID NO: 103, , SEQ ID NO: 105, SEQ ID NO: 107, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is:i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 2, SEQ ID NO: 58, SEQ ID NO: 104, , SEQ ID NO: 106, SEQ ID NO: 108, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 2, , SEQ ID NO: 58, SEQ ID NO: 104, , SEQ ID NO: 106, SEQ ID NO: 108, or a subsequence thereof. The skilled person will appreciate that the RNA modifying domain can be any RNA modifying domain. Preferably the RNA modifying domain is a domain that is capable of making modifications in the RNA that are simple to detect. For example in some embodiments the RNA modifying domain modifies RNA in a manner that is detectable by sequencing. For example, adenosine deaminases cause an A to I transition in the RNA. Sequencing is therefore able to detect these A to I edits, which following RNA-seq is read as G. Similarly,cytosine deaminases cause a C to U mutation in RNA. Sequencing is therefore able todetect these C to U edits, which following RNA-seq is read as T. According, in some embodiments the RNA modifying domain is an RNA-modifying enzyme. In some embodiments the RNA modifying enzyme is an enzyme that causes a transition or mutation in the RNA which can be detected by sequencing. In some embodiments the RNA modifying enzyme is an Adenosine Deaminase acting onRNA (ADAR) enzyme or a cytosine deaminase (CBE); and / orthe first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain is a first portion of an RNA modifying enzyme, for example is a first portion of an Adenosine Deaminase acting on RNA (ADAR) enzyme or first portion of a cytosine deaminase (CBE) enzyme. In some embodiments: a) the ADAR enzyme is selected from the group comprising or consisting of: Drosophila melanogaster ADAR, Homo sapiens ADAR1, Homo sapiens ADAR2, Homo sapiens ADAR3, Homo sapiens ADAR4; or b) the CBE enzyme is APOBEC1. The skilled person will appreciate that the RNA modifying domain, for example the RNA modifying enzyme, may be wildtype RNA modifying domain or enzyme, or may be anengineered or mutated RNA modifying domain or enzyme. By engineered we include themeaning of non naturally occurring. Accordingly, in some embodiments the ADAR enzyme is a wild-type ADAR enzyme; or the CBE enzyme is a wild-type CBE enzyme. In other embodiments: a) the ADAR enzyme is a mutant ADAR enzyme comprising at least one amino acid insertion, substitution or deletion compared to wild-type ADAR enzyme; or b) the CBE enzyme is a mutant CBE enzyme comprising at least one amino acid insertion, substitution or deletion compared to wild-type CBE enzyme. In some embodiments, the engineered RNA modifying enzyme is an engineered ADAR2 enzyme that comprises a mutation at position 174 and / or 182 relative to the wild type sequence of the ADAR2 catalytic domain. In some embodiments, the wild type sequenceof the ADAR2 catalytic domain is the sequence of a wild type Drosophila ADAR2 catalyticdomain (dADARcd), for example comprising the amino acid sequence of SEQ ID NO: 109 and / or an amino acid sequence encoded by a nucleotide sequence of SEQ ID NO: 110. In some embodiments the ADAR enzyme comprises an E192Q and / or an N182F mutation relative to the wild-type sequence of SEQ ID NO: 109. In some embodiments, the wild type sequence of the ADAR2 catalytic domain is the sequence of a wild type human ADAR2 catalytic domain (hADAR2cd), for example comprising the amino acid sequence of SEQ ID NO: 111 and / or an amino acid sequence encoded by a nucleotide sequence of SEQ ID NO:112. In some embodiments the ADAR enzyme comprises an E174Q and / or an N182Fmutation relative to the wild-type sequence of SEQ ID NO: 111. In some embodiments the ADAR enzyme is hADAR2cd. In some embodiments the ADAR enzyme is dADAR2cd. In some embodiments the ADAR enzyme: a) comprises or consists an amino acid sequence that is: i) at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 111, optionally provided that residue 174 is a glutamine and residue 182 is a phenylalanine; ii) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 109, SEQ ID NO: 111, or a subsequence thereof; or iii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 109, SEQ ID NO: 111, or a subsequence thereof;and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 4, SEQ ID NO: 6, or SEQ ID NO: 112, optionally provided that residue 174 of the amino acid sequence is a glutamine and residue 182 of the amino acid sequence is a phenylalanine; ii) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 110, SEQ ID NO: 112, or a subsequence thereof; or iii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 110, SEQ ID NO: 112, or a subsequence thereof. As described above, in some instances the test polypeptide comprises a first portion of an RNA modifying polypeptide. In some instances then the test polypeptide comprises a first portion of an ADAR enzyme. In some embodiments the first portion of the ADAR enzyme that is comprised by the test polypeptide is an N-terminal fragment of the ADAR enzyme, and the corresponding second portion of the ADAR enzyme comprises a C-terminal fragment of the ADAR enzyme. In this case the first portion of the ADAR enzyme and the second portion of the ADAR fragment do not independently have adenosine deaminaseactivity; andthe first portion of the ADAR enzyme and the second portion of the ADAR enzyme form a functional ADAR enzyme having adenosine deaminase activity when brought into proximity to one another. The two portions may be brought into proximity to one another by dimerisation of dimerisation domains present on the first portion of the ADAR enzyme and the second portion of the ADAR enzyme, for example. In some embodiments the RNA modifying domain comprises: a) the first portion of the RNA modifying polypeptide domain, optionally a first portion of an ADAR enzyme; or b) the second portion of the RNA modifying polypeptide domain, optionally a second portion of an ADAR enzyme, and does not comprise both the first and the second portions of the RNA modifying polypeptide domain.It will be clear to the skilled person that in embodiments where the test polypeptidecomprises a first portion of an RNA modifying polypeptide that is capable of modifying RNA when bought into proximity with a corresponding second portion of the RNA modifying domain, the second portion of the RNA modifying domain may be expressed from an entirely separate nucleic acid to the nucleic acid from which the test polypeptide is expressed. However in some embodiments, the test polypeptide, along with the first portion of the RNA modifying domain and the second portion of the RNA modifying domain are expressed as a single transcript and are translated into a single polypeptide. In these instances, the single polypeptide is arranged so as to comprise a self-cleaving protease site between the first and second portions of the RNA modifying domain. This means that following expression, the second portion of the RNA modifying domain is cleaved away from the first portion of the RNA modifying domain (which itself is attached to the query polypeptide) so that no functional RNA modifying domain exists until such time as the two portions arebrought into proximity with one another again via binding of the query polypeptide to thequery RNA nucleic acid. Accordingly, in some embodiments the RNA modifying domain comprises: a) the first portion of the RNA modifying polypeptide domain, for example a first portion of an ADAR enzyme; or b) the second portion of the RNA modifying polypeptide domain, for example a second portion of an ADAR enzyme, wherein the first and second portions of the RNA modifying polypeptide domain areseparated by a self-cleaving protease site arranged so that following protein expression the self-cleaving protease site is cleaved, separating the first and second portions of the RNA modifying polypeptide domain onto separate polypeptide molecules. In some embodiments the test polypeptide comprises: a) the query polypeptide connected to first portion of the RNA modifying polypeptide domain, for example the first portion of an ADAR enzyme, and wherein the first portion of the RNA modifying polypeptide domain is connected to the second portion of the RNA modifying polypeptide domain via a linker comprising a self-cleaving protease site; or b) the query fusion polypeptide connected to second portion of the RNA modifying polypeptide domain, for example the second portion of an ADAR enzyme, and wherein the second portion of the RNA modifying polypeptide domain is connected to the first portion of the RNA modifying polypeptide domain via a linkercomprising a self-cleaving protease site. As described above, in some embodiments wherein the RNA modifying domain comprises both the first portion of the RNA modifying polypeptide domain and the second portion of the RNA modifying polypeptide domain, for example comprises both the first portion of a ADAR enzyme and the second portion of the ADAR enzyme. In some embodiments the first portion of the ADAR enzyme : a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 9, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 9, or a subsequence thereof;and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 10, , or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 10, , or a subsequence thereof.In some embodiments the second portion of the ADAR enzyme: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 11, SEQ ID NO: 13, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 11, SEQ ID NO: 13, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 12, SEQ ID NO: 14, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical toSEQ ID NO: 12, SEQ ID NO: 14, or a subsequence thereof. In some embodiments the first portion of the RNA modifying polypeptide domain and the second portion of the RNA modifying polypeptide domain each further comprise an inducible dimerization domain that: a) are capable of dimerising in the presence of a dimerization inducing molecule, so as to cause dimerization of the first portion of the RNA modifying polypeptide and the second portion of the RNA modifying polypeptide domain to form a functional RNA modifying polypeptide domain in the presence of a dimerization inducing molecule; and / or b) are not capable of dimerising in the absence of a dimerization inducing molecule, thereby preventing dimerization of the first portion of the RNAmodifying polypeptide and the second portion of the RNA modifying polypeptide domain. The dimerization inducing molecule may be selected from the group comprising or consisting of: rapamycin; Mandipropamid (Mandi); abscisic acid, and gibberellic acid. In some embodiments the dimerization polypeptide is selected from the group comprisingor consisting of: FRB and FKBP12.In some embodiments: a) the first portion of the RNA modifying polypeptide domain further comprises an inducible dimerization domain that is FRB and the second portion of the RNA modifying polypeptide domain further comprises an inducible dimerization domain that is FKBP12; or b) the first portion of the RNA modifying polypeptide domain further comprises an inducible dimerization domain that is FKBP12 and the second portion of the RNA modifying polypeptide domain further comprises an inducible dimerization domain that is FRB. In some embodiments the inducible dimerization domain: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO:15, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 15, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 16, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 16, or a subsequence thereof. and / or c) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO:17, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 17, or a subsequence thereof; and / or d) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO:18, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 18, or a subsequence thereof. In some embodiments: a) the first portion of the RNA modifying polypeptide domain comprises a dimerization linker connecting the inducible dimerization domain to the first portion of the RNA modifying polypeptide domain; and / or b) the second portion of the RNA modifying polypeptide domain comprises a dimerization linker connecting the inducible dimerization domain to the second portion of the RNA modifying polypeptide domain. The dimerization linker may be selected from the group comprising or consisting of: GGSGSGAGSGSPAGGGAPGSGGGS (SEQ ID NO: 19), [GGGGS]n (SEQ ID NO:121) (n canbe any whole integer, for example, 1, 2, 3., 4, 5, 6, 7, 8, 9, 10, etc); PAP[AP]n;AEAAAKEAAAKA (SEQ ID NO: 61); [XP]n; (EAAAK)n(SEQ ID NO:122) (n can be any whole integer, for example, 1, 2, 3., 4, 5, 6, 7, 8, 9, 10, etc); XTEN linker; SGGSSGGSSGSETPGTSESATPESSGGSSGGS (SEQ ID NO: 25); an endogenous linker; and any combination thereof. The dimerization linker may: a) comprise or consist an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 19, SEQ ID NO: 23,SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 59, SEQ ID NO: 61, SEQ ID NO: 63, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 19, SEQ ID NO: 23,SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 59, SEQ ID NO: 61, SEQ ID NO: 63, or a subsequence thereof; and / orb) comprise or consist an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 20, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 60, SEQ ID NO: 62, SEQ ID NO: 64, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical toSEQ ID NO: 20, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 60, SEQ ID NO: 62, SEQ ID NO: 64, or a subsequence thereof. As described above, in some embodiments the first portion of the RNA modifying polypeptide domain and the second portion of the RNA modifying polypeptide domain are connected by a self-cleavable linker. The self-cleavable linker may be selected from the group comprising or consisting of: a T2A linker; P2A linker; E2A linker; F2A linker. In some embodiments the self-cleavable linker: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 21 or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 21 or a subsequence thereof;and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 22 or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 22 or a subsequence thereof. As will be clear to the skilled person, in any of the methods described herein, the query polypeptide or a fragment thereof and the RNA modifying polypeptide or a fragment thereof may be connected by a polypeptide linker. The use of linkers between protein domains is routine in the field and the skilled personwill be able to select appropriate linkers to use.For example in some embodiments the polypeptide linker is a flexible linker. In some embodiments the polypeptide linker comprises a sequence that is: between 1 aa and 60 aa, 2 aa and 59 aa, 3 aa and 58 aa, 4aa and 57 aa, 5 aa and 56 aa, 6 aa and 55 aa, 7 aa and 54 aa, 8 aa and 53 aa, 9 aa and 52 aa, 10 aa and 51 aa, 11 aa and 40 aa, 12 aa and 49 aa, 13 aa and 48 aa, 14 aa and 47 aa, 15 aa and 46 aa, 16aa and 45 aa, 17 aa and 44 aa, 18 aa and 43 aa, 19 aa and 42 aa, 20 aa and 41 aa, 21 aaand 40 aa, 22 aa and 39 aa, 23 aa and 38 aa, 24 aa and 37 aa, 25 aa and 36 aa, 26 aa and 35 aa, 27 aa and 34 aa, 28 aa and 33 aa, 29 aa and 32 aa, 30 aa and 31 aa, 30 aa and 35 aa, 31 aa and 34 aa, 32 aa and 33 aa, or 31 aa and 33 aa in length; at least 1aa, at least 2 aa, and least 3 aa, at least 4 aa, at least 5 aa, at least 6 aa, at least 7 aa, at least 8 aa, at least 9 aa, at least 10 aa, at least 11 aa, at least 13 aa, at least 14 aa, at least 15 aa, at least 16 aa, at least 17 aa, at least 18 aa, at least 19 aa, at least 20 aa, at least 21 aa, at least 22 aa, at least 23 aa, at least 24 aa, at least 25 aa, at least 26 aa, at least 27 aa, at least 28 aa, at least 29 aa, at least 20 aa, at least 21 aa, at least 22 aa, at least 33 aa, at least 34 aa, at least 35 aa, at least 36 aa, at least 37 aa, at least 38 aa, at least 39 aa, at least 20 aa, at least 21 aa, at least 22 aa, at least 43 aa, at least 44 aa, at least 45 aa, at least 46 aa, at least 47 aa, at least 48 aa, at least 49 aa, at least 50 aa, at least 51 aa, at least 52 aa, at least 53 aa, at least 54 aa, at least 55 aa, at least 56 aa, at least 57 aa, at least 58 aa, at least 59 aa, or more in length; and / or 1 aa, 2 aa, 3 aa, 4 aa, 5 aa, 6 aa, 7 aa, 8 aa, 9 aa, 10 aa, 11 aa, 12 aa, 13 aa, 14aa, 15 aa, 16 aa, 17 aa, 18 aa, 19 aa, 20 aa, 21 aa, 22 aa, 23 aa, 24 aa, 25 aa, 26 aa, 27aa, 28 aa, 29 aa, 20 aa, 21 aa, 22 aa, 33 aa, 34 aa, 35 aa, 36 aa, 37 aa, 38 aa, 39 aa, 20 aa, 21 aa, 22 aa, 43 aa, 44 aa, 45 aa, 46 aa, 47 aa, 48 aa, 49 aa, 50 aa, 51 aa, 52 aa, 53 aa, 54 aa, 55 aa, 56 aa, 57 aa, 58 aa, 59 aa, or 60 aa in length (wherein aa means amino acid). The polypeptide linker may be selected from the group comprising or consisting of: an XTEN linker; a GGGGS (SEQ ID NO:123) linker; a (GGGGS)n (SEQ ID NO:121) linker; PAP[AP]nlinker; AEAAAKEAAAKA (SEQ ID NO: 61); [XP]n; GGSGSGAGSGSPAGGGAPGSGGGS (SEQ ID NO: 19); (EAAAK)n (SEQ ID NO: 122); SGGSSGGSSGSETPGTSESATPESSGGSSGGS (SEQ ID NO: 25); an antibody linker; an endogenous linker; or any combination thereof. In some embodiments the polypeptide linker: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%,at least 97%, at least 98%, at least 99%, or 100 % identical to 19, SEQ ID NO: 23,SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 59, SEQ ID NO: 61, SEQ ID NO: 63, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to 19, SEQ ID NO: 23, SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 59, SEQ ID NO: 61, SEQ ID NO: 63, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by anucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical SEQ ID NO: 20, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 60, SEQ ID NO: 62, SEQ ID NO: 64, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 20, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 60, SEQ ID NO: 62, SEQ ID NO: 64, or a subsequence thereof. In some embodiments the polypeptide linker is not a (GGGGS)3 linker (SEQ ID NO:27). As described above, in some embodiments the RNA modifying domain is recruited to the test polypeptide via a recruitment module that is able to recruit the RNA modifying domain to the query polypeptide. In some embodiments the recruitment module comprises a firstaffinity domain that can bind to a second affinity domain that is present on the RNAmodifying domain. The binding of the first and second affinity domains brings the query polypeptide and the RNA modifying domain together, forming the test polypeptide. Linkers may also be employed here, in the context of connecting the first and second affinity domains to the query polypeptide and the RNA modifying domain respectively. In some embodiments where the test polypeptide comprises a query polypeptide or a fragment thereof and a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA: a) the recruitment molecule and / or first affinity domain is connected to the query polypeptide or a fragment thereof by a polypeptide linker; and / or b) the second affinity domain is connected to the RNA modifying domain or fragment thereof by a polypeptide linker. In some embodiments the first affinity domain and the second affinity domain are each independently selected from the group comprising or consisting of: an SH3 domain; anSHL domain; an antibody or fragment thereof; a nanobody or fragment thereof; anantibody variable light chain or fragment thereof; an antibody variable heavy chain or fragment thereof; an antibody constant light chain or fragment thereof; an antibody constant heavy chain or fragment thereof; an antibody light chain or fragment thereof; an antibody heavy chain or fragment thereof; a Fab fragment; an Fc portion; an scFv; or any combination thereof. In some embodiments the first affinity domain and / or second affinity domain: comprise or consist an amino acid sequence that is:a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical SEQ ID NO: 99, SEQ ID NO: 101, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 99, SEQ ID NO: 101, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 100, SEQ ID NO: 102, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 100, SEQ ID NO: 102, or a subsequence thereof. In some specific embodiments, the test polypeptide: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical SEQ ID NO: 29, SEQ ID NO: 31, SEQ ID NO: 33, SEQ ID NO: 35, SEQ ID NO: 37, SEQ ID NO: 39, SEQ ID NO: 41, SEQ ID NO: 43, SEQ ID NO: 45, SEQ ID NO: 47, SEQ ID NO: 49, SEQ ID NO: 51, SEQ ID NO: 53, SEQ ID NO: 55, SEQ ID NO: 65, SEQ ID NO: 67, SEQ ID NO: 69, SEQ ID NO: 71, SEQ ID NO: 73, SEQ ID NO: 75, SEQ ID NO: 77, SEQ ID NO: 79, SEQ ID NO: 81, SEQ ID NO: 83, SEQ ID NO: 85, SEQ ID NO: 87, SEQ ID NO: 89, SEQ ID NO: 91, SEQ ID NO: 93, SEQ ID NO: 95, SEQ ID NO: 97, SEQ ID NO: 113, SEQ ID NO: 115, SEQ ID NO: 117, SEQ ID NO: 119, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 29, SEQ ID NO: 31, SEQ ID NO: 33, SEQ ID NO: 35, SEQ ID NO: 37, SEQ ID NO: 39, SEQ ID NO: 41, SEQ ID NO: 43, SEQ ID NO: 45,SEQ ID NO: 47, SEQ ID NO: 49, SEQ ID NO: 51, SEQ ID NO: 53, SEQ ID NO: 55, SEQ ID NO: 65, SEQ ID NO: 67, SEQ ID NO: 69, SEQ ID NO: 71, SEQ ID NO: 73, SEQ ID NO: 75, SEQ ID NO: 77, SEQ ID NO: 79, SEQ ID NO: 81, SEQ ID NO: 83, SEQ ID NO: 85, SEQ ID NO: 87, SEQ ID NO: 89, SEQ ID NO: 91, SEQ ID NO: 93, SEQ ID NO: 95, SEQ ID NO: 97, SEQ ID NO: 113, SEQ ID NO: 115, SEQ ID NO: 117, SEQ ID NO: 119, or a subsequence thereof; and / orb) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO: 36, SEQ ID NO: 38, SEQ ID NO: 40, SEQ ID NO: 42, SEQ ID NO: 44, SEQ ID NO: 46, SEQ ID NO: 48, SEQ ID NO: 50, SEQ ID NO:52, SEQ ID NO: 54, SEQ ID NO: 56, SEQ ID NO: 66, SEQ ID NO: 68, SEQ ID NO: 70, SEQ ID NO: 72, SEQ ID NO: 74, SEQ ID NO: 76, SEQ ID NO: 78, SEQ ID NO: 80, SEQ ID NO 82, SEQ ID NO: 84, SEQ ID NO: 86, SEQ ID NO: 88, SEQ ID NO: 90, SEQ ID NO: 92, SEQ ID NO: 94, SEQ ID NO: 96, SEQ ID NO: 98, SEQ ID NO: 114, SEQ ID NO: 116, SEQ ID NO: 118, SEQ ID NO: 120, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO: 36, SEQ ID NO: 38, SEQ ID NO: 40, SEQ ID NO: 42, SEQ ID NO: 44, SEQ ID NO: 46,SEQ ID NO: 48, SEQ ID NO: 50, SEQ ID NO:52, SEQ ID NO: 54, SEQ ID NO: 56, SEQ ID NO: 66, SEQ ID NO: 68, SEQ ID NO: 70, SEQ ID NO: 72, SEQ ID NO: 74, SEQ ID NO: 76, SEQ ID NO: 78, SEQ ID NO: 80, SEQ ID NO 82, SEQ ID NO: 84, SEQ ID NO: 86, SEQ ID NO: 88, SEQ ID NO: 90, SEQ ID NO: 92, SEQ ID NO: 94, SEQ ID NO: 96, SEQ ID NO: 98, SEQ ID NO: 114, SEQ ID NO: 116, SEQ ID NO: 118, SEQ ID NO: 120, or a subsequence thereof. Where the method comprises a test polypeptide that comprises a first portion of an RNA modifying domain, the dimerisation of the first portion and the corresponding second portion of the RNA modifying domain may be inducible. Accordingly, in some embodiments such as this, the method can further comprises in step a) contacting the test polypeptide with a dimerization molecule, thereby permitting dimerization of the first portion of the RNA modifying polypeptide domain and the second portion of the RNA modifyingpolypeptide domain to form a functional RNA modifying polypeptide domain.The methods described herein are considered to be suitable for use with any type of query RNA nucleic acid. For example in some embodiments the query RNA nucleic acid is selected from the group comprising or consisting of: mRNA, tRNA, rRNA, snRNA, snoRNA, miRNA, piRNA, siRNA. In some embodiments the query RNA nucleic acid is a natural RNA, for example an RNAisolated from a cell, a virus, or the environment, or expressed within a cell. In someembodiments the first query RNA nucleic acid is a synthetic RNA. As described elsewhere herein, preferably the RNA modification that is performed by the RNA modifying domain is a modification that can be detected by sequence. Accordingly, in some embodiments the modification in the first test query RNA nucleic acid is detectable by sequencing. For example preferred modifications are the deamination of an adenosine base present in the query RNA nucleic acid to an inosine base. In some embodiments of the methods of the invention, detecting the presence or absence of at least one modification step b) comprises: i) performing reverse transcription on at least a portion of the modified first test query RNA nucleic acid obtained in (a) to obtain a first test cDNA molecule. In some embodiments of the methods of the invention, detecting the presence or absenceof at least one modification step b) further comprises:ii) sequencing at least a portion of the first test cDNA molecule. In some embodiments of the methods of the invention, detecting the presence or absence of at least one modification step b) further comprises: iii) detecting the presence or absence of a mutation at at least one position in the sequence obtained from the first test cDNA molecule, thereby indicating the presence or absence of a modification at the at least one corresponding position of the first test query RNA nucleic acid. In preferred embodiments of the methods described herein the mutation detected at at least one position in the first test cDNA molecule is a T>C mutation, (corresponding to an A>I or A>G mutation in the first test query RNA nucleic acid), thereby indicating the presence of an inosine base at the at least one corresponding position of the first test query RNA nucleic acid. In some embodiments of the methods described herein the mutation detected at at least one position in the first test cDNA molecule is a G>A mutation (corresponding to a C>U mutation in the first test query RNA nucleic acid), thereby indicating the present of a uracil base at the at least one corresponding position of the first test query RNA nucleic acid. It will be clear to the skilled person that by determining the presence or absence ofmutations caused by the RNA modifying domain, a modification profile is generated.Accordingly, in some embodiments, generating a modification profile comprises: detecting the presence or absence of a mutation at each position in the sequence obtained from the first test cDNA molecule, thereby indicating the presence or absence of a modification at each corresponding position of the first test query RNA nucleic acid. It will be clear to the skilled person that the presence or location of one or more binding sites of the query polypeptide on the query RNA nucleic acid is indicated by the presence of a modification-enriched portion of the first query RNA nucleic acid. Such a modification- enriched portion will be identified on the modification profile. Although the methods described herein can be performed on a single query RNA nucleic acid, the methods descried herein have many advantageous properties when performedon multiple query RNA nucleic acids, such as those found within a transcriptome of a cell.Accordingly, the methods described herein are suitable for use with a single, but are also suitable for use with a plurality of different query RNA nucleic acids. For example in one embodiment the method is performed on a transcriptome to determine which RNA nucleic acids are bound by a particularly query polypeptide. Accordingly, the invention also provides a method for identifying a binding interaction between a query polypeptide and at least one query RNA nucleic acid of a plurality of query RNA nucleic acids, the method comprising: a) contacting a plurality of query RNA nucleic acids with a test polypeptide, wherein the test polypeptide comprises the query polypeptide or a fragment thereof; and i) an RNA modifying domain or fragment thereof capable of modifying RNA; or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximitywith a corresponding second portion of the RNA modifying domain, for example wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is afirst portion of an RNA modifying polypeptidedomain or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; for example wherein the test polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNAii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; wherein where said test polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA whenbrought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereofcapable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a plurality of first test query RNA nucleic acids; and b) detecting the presence or absence of at least one modification in at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids; and c) determining that there is a binding interaction between the query polypeptide and the at least one query RNA nucleic acid of the plurality of RNA nucleic acid when a modification is detected in the at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids. The invention also provides a method for identifying one or more binding sites of a querypolypeptide on at least one of a plurality of RNA nucleic acids, the method comprisinga) contacting a plurality of query RNA nucleic acids with a test polypeptide, wherein the test polypeptide comprises the query polypeptide or a fragment thereof; and i) an RNA modifying domain or fragment thereof capable of modifying RNA; or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain;or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain;optionally wherein the test polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNA; ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein thefirst affinity domain is capable of binding to the second affinity domain; wherein where said test polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitmentmodule and said RNA modifying domain or fragment thereof; thereby generating a plurality of test query RNA nucleic acid; b) detecting the presence or absence of at least one modification in at least one test query RNA nucleic acid of the plurality of first query RNA nucleic acids and generating a modification profile for said at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids; andc) determining one or more binding sites of the query polypeptide on the at least one query RNA nucleic acid of the plurality of query RNA nucleic acids using the modification profile. Preferences for features of the methods in relation to the plurality of query RNA nucleic acids are as described elsewhere herein. For example, preferences for the query polypeptide, RNA modifying domain, RNA modifying polypeptide, recruitment module and / or query RNA is the query polypeptide, fusion polypeptide, polypeptide capable of modifying RNA, recruitment module and / or query RNA as defined elsewhere herein. In some embodiments, the modification in the at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids is detectable by sequencing, as described elsewhere. For example in some embodiments detecting the presence or absence of at least one modification step b) comprises: i) performing reverse transcription on at least a portion of at least one testquery RNA nucleic acid of the plurality of test query RNA nucleic acids obtained in (a) to obtain at least one test cDNA molecule; or performing reverse transcription on at least a portion of each test query RNA nucleic acid of the plurality of test query RNA nucleic acids obtained in (a) to obtain a plurality of test cDNA molecules. In some embodiments detecting the presence or absence of at least one modification in step b) further comprises: ii) sequencing at least a portion of the at least one test cDNA molecule; or sequencing at least a portion of each test cDNA molecule of the plurality of cDNA test molecules. In some embodiments detecting the presence or absence of at least one modification in step b) further comprises: iii) detecting the presence or absence of a mutation at at least one position inthe sequence obtained from the at least one test cDNA molecule, thereby indicating the presence or absence of a modification at the at least one corresponding position of the corresponding at least one test query RNA nucleic acid; or detecting the presence or absence of a mutation at at least one position in the sequence obtained from each test cDNA molecule of the plurality of test cDNA molecules, thereby indicating the presence or absence of a modification at the at least one corresponding position of the corresponding at least one test query RNA nucleic acid.As described elsewhere, preferably the modification is deamination of an adenosine base comprised by the query RNA nucleic acid to an inosine base, and in some embodiments the mutation detected at at least one position in the first test cDNA molecule is a T>C mutation, an A>I mutation, or an A>G mutation, thereby indicating the presence of an inosine base at the at least one corresponding position of the first test query RNA nucleic acid. As described elsewhere, in some embodiments, the modification is deamination of a cytosine based comprised by the query RNA nucleic acid to a uracil base, and in some embodiments the mutation detected at at least one position in the first test cDNA molecule is a G>A mutation, C>U mutation, or C>T mutation, thereby indicating the presence of a uracil base at the at least one corresponding position of the first test query RNA nucleic acid. As also described elsewhere herein, in some embodiments generating a modification profile comprises: iii) detecting the presence or absence of a mutation at each position in the sequence obtained from the at least one test cDNA molecule of the plurality of test cDNA molecules, thereby indicating the presence or absence of a modification at each corresponding position of the at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids; or detecting the presence or absence of a mutation at each position in the sequence obtained from each test cDNA molecule of the plurality of test cDNA molecules, thereby indicating the presence or absence of a modification at each corresponding position of each test query RNA nucleic acid of the plurality of test query RNA nucleic acids. It will be clear that the presence or location on the query RNA nucleic acid of the bindinginteraction between the query polypeptide and a query RNA nucleic of the plurality of testquery RNA nucleic acids is indicated by the presence of a modification-enriched portion of the test query RNA nucleic acid of the plurality of test query RNA nucleic acids. In some embodiments each query RNA nucleic acid of the plurality of query RNA nucleic acids is identical. In some embodiments each query RNA nucleic acid of the plurality of query RNA nucleic acids is unique. In some embodiments each query RNA nucleic acid of the plurality of query RNA nucleic acids is different from at least one other query RNAnucleic acid of the plurality of first query RNA nucleic acids. In some embodiments at leastone query RNA nucleic acid of the plurality of query RNA nucleic acids is different from at least one other query RNA nucleic acid of the plurality of query RNA nucleic acids. The number of query RNA nucleic acids in the plurality may be any number. For example in some embodiments the plurality of query RNA nucleic acids comprises at least 2, 3, 4, 5, 10, 20, 30, 40, 50, 100, 200, 300, 400, 500, 600, 700, 800, 900, 1000, 1500, 2000, 2500, 3000, 3500, 4000 or more different query RNA nucleic acids. For example, in some embodiments, the plurality of query RNA nucleic acids comprises or consists of the transcriptome of a cell. Where more than one query RNA nucleic acid is present, it is necessary to determine the identity of each RNA nucleic acid. The skilled person is aware of known means to determine the identify of each of a number of nucleic acids, for example using multiplexed Illumina sequencing. In this instance, each query RNA nucleic acid may be flanked by commonprimer binding sites. Following isolation of chemically-modified RNA nucleic acids, thewhole pool(s) of RNA nucleic acids can be reverse transcribed into cDNA and then readily sequenced. In this way it is possible to determine which, if any, of the many query RNA nucleic acids the test molecule interacts with, and it is possible to look for off-target effects of a test- molecule that is known to interact with a particular target RNA nucleic acid. Accordingly, in some embodiments each query RNA nucleic acid comprises at least one adapter sequence, optionally wherein each query RNA nucleic acid comprises: a) a 5’ adapter; and or b) a 3’ adapter. In some embodiments, the adapter is a sequencing adapter.It may be useful to incorporate a distinguishing or unique sequence into a query RNAnucleic acid, such as a query RNA nucleic acid of a plurality of query RNA nucleic acids as provided herein. Such sequences are known to the person skilled in the art, and may include in some embodiments a barcode sequence, optionally wherein each barcode sequence is unique. Any suitable primer may be used to prime a reverse transcription or sequencing reactionas provided herein. Suitable primers include common primers and sequence-specificprimers, i.e., primers with a sequence that is complementary to the sequence of a query RNA as provided herein. Accordingly, in some embodiments, the or each adapter sequence is suitable for priming a sequencing reaction. As will be appreciated, the use of common primers may be advantages in some aspects of the invention, such as multiplexed assays for identifying a functional interaction between a test polypeptide and a plurality of query RNA nucleic acids. Methods of preparing sequencing libraries are known to the skilled person, and may include, for example, capturing and / or purifying an RNA or DNA nucleic acid of interest. Accordingly, in some embodiments, each adapter sequence is suitable for capturing and purifying the query RNA nucleic acid. In some embodiments, the 3’ adapter sequence is suitable for priming a reverse transcription reaction. In alternative embodiments, the RNA nucleic acid does not comprise an adapter sequence.In this embodiment, a sequence-specific primer may be used to prime reverse transcriptionat any portion of the first query RNA; sequencing adapters may suitably be ligated to the resultant cDNA before sequencing. The cell may be any cell. Accordingly, in some embodiments, the cell is a eukaryotic cell, a bacterial cell, or an archaeal cell. In preferred embodiments: a) the eukaryotic cell is a human cell or a yeast cell; and / or b) the bacterial cell is an E. coli cell. Alternatively, in some embodiments, the method is an in vitro method, optionally a cell- free method. In some embodiments, the method is an in vivo method. In some embodiments, the invivo method is performed in a cell as described herein. In some embodiments, the in vivomethod is performed in a multicellular organism, for example in an animal. Suitable model animals are known to the skilled person, and include but are not limited to – for example – Drosophila, Caenorhabditis elegans, and Mus musculus. Where the method is performed in a cell, it will be appreciated that the corresponding components must be present in the cell. Accordingly, in some embodiments, the method comprises: a) expressing:i) the test polypeptide; ii) the RNA modifying domain or fragment thereof; iii) a first portion of an RNA modifying domain and / or a corresponding second portion of the RNA modifying domain; iv) first query RNA nucleic acid; v) recruitment module comprising a first affinity domain; vi) RNA modifying domain or fragment thereof comprising an affinity domain and / or vii) plurality of first query RNA nucleic acids in the cell. and / or b) delivering: i) the test polypeptide; ii) the RNA modifying domain or fragment thereof; iii) a first portion of an RNA modifying domain and / or a correspondingsecond portion of the RNA modifying domain; iv) first query RNA nucleic acid; v) recruitment module comprising a first affinity domain; vi) RNA modifying domain or fragment thereof comprising an affinity domain and / or vii) plurality of first query RNA nucleic acids to the cell. In some embodiments, where a component i)-vii) listed above is expressed and / or delivered to the cell, the corresponding partner for each of the components i)-vii) is also expressed in the cell or delivered to the cell. 72. The method of claims 69-71, wherein where the RNA modifying domain of the test polypeptide comprises a first portion of an RNA modifying domain that is capable ofmodifying RNA when brought into proximity with a corresponding second portion of theRNA modifying domain, the method further comprises expressing the corresponding second portion of the RNA modifying domain in the same cell. In some embodiments, the first portion of an RNA modifying domain that is capable of modifying RNA and the corresponding second portion of the RNA modifying domain: a) are expressed from the same transcript; or b) are each expressed from an independent transcript. In some embodiments, the test polypeptide, first query RNA nucleic acid, recruitment module, and / or plurality of query RNA nucleic acids are each expressed from one or more expression cassettes comprising a nucleotide sequence encoding: a) the RNA modifying polypeptide or a fragment thereof, optionally wherein the RNA modifying polypeptide is a fusion polypeptide; b) the fusion polypeptide; c) the first query RNA nucleic acid; d) the recruitment module; and / or d) the plurality of first query RNA nucleic acids. As will be appreciated, the RNA may be a naturally occurring RNA present in the cell (for example, a component of the transcriptome of the cell). In these embodiments, it is not necessary to express the first query RNA nucleic acid in the cell.In some embodiments, each of the nucleotide sequences encoding:a) the RNA modifying polypeptide or a fragment thereof, optionally wherein the RNA modifying polypeptide is a fusion polypeptide; b) the fusion polypeptide; c) the first query RNA nucleic acid; d) the recruitment module; and / or d) the plurality of first query RNA nucleic acids are operably linked to a promoter in the cassette, optionally wherein the promoter is selected from the group comprising or consisting of: a CMV promoter; an EF1a promoter; an SV40 promoter; a PGK promoter; a CAG promoter; a minimal promoter; or any combination thereof. As has been described herein, it is advantageous to control the expression of thecomponents expressed in the cell. Accordingly, in some embodiments, the promoter is aninducible promoter. It is generally preferred that where the promoter is an inducible promoter, it is a tightly regulated promoter. Suitable promoters that may be tightly regulated are known to the person skilled in the art, and include – for example – the Tet-on system, the Tet-off system, the Tet-repressor system, and the cumate expression system. The Tet expression systemsare well known to the person skilled in the art, and are described – for example – in Gossenand Bujard, 2001, Tetracyclines in the control of gene expression in eukaryotes. In: Nelson M, Hillen W, Greenwald RA, Eds. Tetracyclines in biology, chemistry and medicine. Birkhäuser Verlag: Basel 2001; pp. 139; Baron and Bujard, 2000, Methods Enzymol. 327:401-421; Barens and Hillen, 2003, Eur. J. Biochem 270(15):3109-3121; and Das et al., 2016, Curr. Gene Ther. 16:156-167, each of which is herein incorporated by reference. In one embodiment, the one or more cassettes further comprises an operator sequence, optionally wherein the operator sequence is selected from the group comprising or consisting of: TetO; CuO. In one embodiment, expression from the promoter is controlled by an inducible expression system, optionally wherein the inducible expression system is selected from the group comprising or consisting of: a) a Tet-on system, wherein expression of the test polypeptide, first query RNA nucleic acid, recruitment module and / or plurality of query RNA nucleic acids isrepressed in the absence of the controller molecule and is induced in the presence of a controller molecule; b) a Tet-off system, wherein expression of the test polypeptide, first query RNA nucleic acid, recruitment module and / or plurality of query RNA nucleic acids is repressed in the presence of the controller molecule and is induced in the absence of the controller molecule; c) a tet-repressor system, wherein expression of the test polypeptide, first query RNA nucleic acid, recruitment module and / or plurality of query RNA nucleic acids repressed in the presence of the controller molecule and is induced in the absence of the controller molecule; or d) a cumate expression system, wherein expression of the test polypeptide, first query RNA nucleic acid, recruitment module and / or plurality of query RNA nucleic acids is repressed in the presence of the inducer molecule and induced in the absence of the controller molecule. Expression from the Tet-on system, Tet-off system, tet-repressor system, and cumate expression system is tightly controlled by cognate controller and / or inducer molecules. Accordingly, in one embodiment the controller and / or inducer molecule is selected from the group comprising or consisting of: tetracycline; doxycycline; cumate. In some embodiments, the one or more cassettes is encoded by a vector comprised by thecell, optionally wherein the vector is a plasmid, a lentiviral vector, or a landing pad vector.The vector may be maintained episomally, or may be incorporated into the genome of the cell. It may be desirable to effect transient expression of the components provided herein in the cell. This approach may be advantageous, for example, when seeking to minimise toxicity of a query polypeptide to a cell or model organism. Accordingly, in some embodiments: a) the test polypeptide; b) the RNA modifying domain or fragment thereof; c) a first portion of an RNA modifying domain and / or a corresponding second portion of the RNA modifying domain; and / or d) recruitment module; are delivered to the cell in protein form or RNA form, optionally as mRNA. The skilled person will appreciate that following delivery of such an mRNA, the component willbe expressed in the cell; and that the mRNA will degrade, thereby preventing furtherexpression of the component in the cell. In a cell As will be appreciated, these methods may be performed in vitro, in vivo, or in a cell, such as any cell provided or described herein. In some preferred embodiments, the methods are in vitro methods, for example cell-free methods. Accordingly, in one aspect the invention provides a method for identifying a binding interaction between a query polypeptide and a query RNA nucleic acid in a cell, the method comprising: a) expressing in the cell a first query RNA nucleic acid and a test polypeptide wherein the test polypeptide comprises the query polypeptide or a fragment thereof; and i) an RNA modifying domain or fragment thereof capableof modifying RNA, or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain isa first portion of an RNA modifying polypeptide domain; or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; optionally wherein the RNA modifying polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i) a RNA modifying polypeptide domain capable of modifying RNA;ii) a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; wherein where said RNA modifying polypeptide comprises a firstportion of an RNA modifying domain that is capable of modifying RNAwhen brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereofcapable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a first test query RNA nucleic acid in the cell; and b) detecting the presence or absence of at least one modification in the first test query RNA nucleic acid; and c) determining that there is a binding interaction between the polypeptide and first query RNA nucleic acid when a modification is detected in the first test query RNA nucleic acid. In a related aspect, the invention provides a method for identifying one or more binding sites of a query polypeptide on query RNA nucleic acid in a cell, the method comprising: a) expressing in the cell a first query RNA nucleic acid anda test polypeptide wherein the test polypeptide comprises: i) the query polypeptide or a fragment thereof; and ii) an RNA modifying domain or fragment thereof capable of modifying RNA, or a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain ora recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; optionally wherein the RNA modifying polypeptide is afusion protein comprising the query polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNA; ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the secondaffinity domain; wherein where said RNA modifying polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof;thereby generating a first test query RNA nucleic acid; b) detecting the presence or absence of at least one modification in the first test query RNA nucleic acid and generating a modification profile for the first test query RNA nucleic acid; and c) determining one or more binding sites of the query polypeptide on the first query RNA nucleic acid using the modification profile.In each of these aspects, the query polypeptide, RNA modifying polypeptide, and / or query RNA is the query polypeptide, RNA modifying polypeptide, and / or query RNA as defined herein. As already described herein, in one embodiment the modification in the at least one first test query RNA nucleic acid of the plurality of first test query RNA nucleic acid is detectable by sequencing. In one embodiment, detecting the presence or absence of at least one modification step b) comprises the additional steps as already described herein. In one embodiment, generating a modification profile comprises the additional steps described herein. As described herein, in some embodiments the presence or location on the RNA nucleic acid of the binding interaction between the query polypeptide and the first query RNAnucleic acid is indicated by the presence of a modification-enriched portion of the firstquery RNA nucleic acid. As will be appreciated, a cell may comprise a plurality of RNA nucleic acids. Accordingly, in a further aspect, the inventions provides a method for identifying a binding interaction between a query polypeptide and at least one RNA nucleic acid of a plurality of RNA nucleic acids in a cell, the method comprising: a) expressing in the cell a plurality of query RNA nucleic acids with a test polypeptide wherein the test polypeptide comprises: i) the query polypeptide or a fragment thereof; and ii) an RNA modifying domain or fragment thereof capable of modifying RNA, or a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain,optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain ora recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; optionally wherein the RNA modifying polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNA; ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when broughtinto proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; wherein where said RNA modifying polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion ofthe RNA modifying domain, said contacting is conducted underconditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitmentmodule and said RNA modifying domain or fragment thereof; thereby generating a plurality of test query RNA nucleic acids; and b) detecting the presence or absence of at least one modification in at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids; and c) determining that there is a binding interaction between the query polypeptide and the at least one RNA nucleic acid of the plurality of RNA nucleic acid when a modification is detected in the at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids. In a related aspect, the invention provides a method for identifying one or more binding sites of a query polypeptide on at least one RNA nucleic acid of a plurality of nucleic acids in a cell, the method comprising: a) expressing in the cell a plurality of query RNA nucleic acids and a test polypeptide, wherein the test polypeptide comprises the query polypeptide or afragment thereof; and i) an RNA modifying domain or fragment thereof capable of modifying RNA, or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain or iii) a recruitment module capable of recruiting an RNAmodifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; optionally wherein the RNA modifying polypeptide is a fusion proteincomprising the query polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNA or ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain;wherein where said RNA modifying polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a plurality of test query RNA nucleic acids; b) detecting the presence or absence of at least one modification in at least one first test query RNA nucleic acid of the plurality of test query RNA nucleic acids and generating a modification profile for said at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids; and c) determining one or more binding sites of a query polypeptide on at least oneRNA nucleic acid of the plurality of RNA nucleic acids using the modification profile. In some embodiments, the query polypeptide, RNA modifying polypeptide, and / or query RNA is the query polypeptide, RNA modifying polypeptide, and / or RNA as defined herein. In some embodiments, the modification in the at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acid is detectable by sequencing. In some embodiments, detecting the presence or absence of at least one modification step b) comprises the additional steps as defined herein. In some embodiments, generating a modification profile comprises the steps as described herein. As explained elsewhere, the presence or location on the RNA nucleic acid of the binding interaction between the query polypeptide and a query RNA nucleic of the plurality of test query RNA nucleic acids is indicated by the presence of a modification-enriched portion of the test query RNA nucleic acid of the plurality of test query RNA nucleic acids. As will be appreciated, the composition of a plurality of query RNA nucleic acids may be defined, designed, or may be natural. Accordingly, in some embodiments: a) each query RNA nucleic acid of the plurality of query RNA nucleic acids is identical; b) each query RNA nucleic acid of the plurality of query RNA nucleic acids is unique; or c) each query RNA nucleic acid of the plurality of query RNA nucleic acids is different from at least one other query RNA nucleic acid of the plurality of query RNA nucleic acids; or c) at least one query RNA nucleic acid of the plurality of query RNA nucleic acids is different from at least one other query RNA nucleic acid of the plurality of query RNA nucleic acids. As described elsewhere, the plurality of query RNA nucleic acids may comprise or consistof the transcriptome of a cell. The cell may be any cell, such as a eukaryotic cell, a bacterialcell, or an archaeal cell. In some embodiments the eukaryotic cell is a human cell or a yeast cell; and / or the bacterial cell is an E. coli cell. It will be clear that the where the plurality comprises a transcriptome of a cell, the cell preferably expresses the components necessary to perform the method. For example in some embodiments of the methods described herein, the cell comprises: a) a nucleotide sequence encoding the first query RNA or plurality of query RNAs;b) a nucleotide sequence encoding the test polypeptide; c) a nucleotide sequence encoding the query polypeptide; d) a nucleotide sequence encoding the RNA modifying domain or fragment thereof; e) a nucleotide sequence encoding the first portion of an RNA modifying domain and / or a corresponding second portion of the RNA modifying domain; and / or f) a nucleotide encoding a recruitment module. In some embodiments: a) the nucleotide sequence encoding the first query RNA or plurality of query RNAs; b) the nucleotide sequence encoding the test polypeptide; c) the nucleotide sequence encoding the query polypeptide; d) the nucleotide sequence encoding the RNA modifying domain or fragment thereof;e) the nucleotide sequence encoding the first portion of an RNA modifying domain and / or a corresponding second portion of the RNA modifying domain; f) a nucleotide encoding a recruitment module are each operably linked to a promoter in the expression cassette; optionally wherein the promoter is selected from the group comprising or consisting of: a CMV promoter; an EF1a promoter; an SV40 promoter; a PGK promoter; a CAG promoter; a minimal promoter; or any combination thereof. The promoter may be an inducible promoter. In any of the embodiments that comprise an expression cassette as described herein, the expression cassette may further comprise an operator sequence, for example wherein the operator sequence is selected from the group comprising or consisting of: TetO; CuO.The Tet system is well known to the skilled person. In some embodiments of the methodsdescribed herein, expression of any of the component parts of the method from the promoter is controlled by an inducible expression system, for example wherein the inducible expression system is selected from the group comprising or consisting of: a) a Tet-on system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in the absence of the controller molecule and is induced in the presence of a controller molecule; b) a Tet-off system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in thepresence of the controller molecule and is induced in the absence of the controller molecule; c) a tet-repressor system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids repressed in the presence of the controller molecule and is induced in the absence of the controller molecule; or d) a cumate expression system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in the presence of the inducer molecule and induced in the absence of the controller molecule. The controller molecule may be selected from the group comprising or consisting of: tetracycline; doxycycline; and cumate.In some embodiments, wherein expressing in a cell the first query RNA nucleic acid,plurality of query RNA nucleic acids, RNA modifying polypeptide and / or query polypeptide comprises contacting the cell with an inducer molecule selected from the group comprising or consisting of: tetracycline; doxycycline; and cumate. In some embodiments, the cell further comprises a selectable marker, optionally wherein the selectable marker is a fluorescent selectable marker, optionally wherein the fluorescent selectable marker is selected from the group comprising or consisting of: GFP, YFP, and RFP. In some embodiments of the methods described herein, the cassette and / or selectable marker are encoded by a vector, optionally wherein the vector is selected from the group comprising or consisting of: a plasmid, a lentiviral vector, and / or an mRNA vector. In any of the methods described herein, in step a) where the first query RNA nucleic acid(or plurality thereof) is contacted with a test polypeptide, the method may further compriseexposing the cell to a dimerization inducing molecule, optionally wherein the dimerization inducing molecule is selected from the group comprising or consisting of: rifampicin; Mandipropamid (Mandi); abscisic acid, and gibberellic acid. In any of the methods described herein, in step b) (detecting the presence or absence of at least one modification in the first test query RNA nucleic acid or plurality thereof) the method may further comprise isolating and / or purifying the first test query RNA nucleicacid or plurality of first test query RNA nucleic acids from the cell prior to reversetranscription. The invention also provides an engineered RNA modifying polypeptide that is capable of modifying RNA, wherein the engineered RNA modifying polypeptide has an increased RNA editing efficiency compared to an RNA modifying polypeptide that is not engineered or that is a wild-type RNA modifying polypeptide. As will be appreciated, the engineered RNA modifying polypeptide may be an engineered version of any RNA modifying polypeptide provided herein. For example, in some embodiments, the engineered RNA modifying polypeptide is an engineered Adenosine Deaminase acting on RNA (ADAR) enzyme or an engineered cytosine deaminase (CBE) as disclosed herein; and / or An engineered first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of theRNA modifying domain is a first portion of an RNA modifying enzyme, for example is anengineered first portion of an Adenosine Deaminase acting on RNA (ADAR) enzyme or an engineered first portion of a cytosine deaminase (CBE) enzyme. The term “engineered” when applied to a polypeptide is known in the art, and includes a polypeptide that is not naturally occurring. The term “engineered” polypeptide includes a polypeptide that has an amino acid sequence, structure (for example, primary structure, secondary structure, tertiary structure, and / or quaternary structure), or that is encoded by a DNA sequence, that is different from the amino acid sequence, structure, or DNA sequence of a polypeptide that has not been "engineered”, for example a polypeptide that is a wild-type polypeptide. The term “engineered” polypeptide includes a mutant polypeptide. In some embodiments, the engineered RNA modifying polypeptide: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%,at least 97%, at least 98%, at least 99%, or 100 % identical SEQ ID NO: 5, SEQ ID NO: 13, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 5, SEQ ID NO: 13, or a subsequence thereof; optionally provided that residue 174 is a glutamine and residue 182 is a phenylalanine; and / orb) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 6, SEQ ID NO: 14, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 6, SEQ ID NO: 14, or a subsequence thereof; optionally provided that residue 174 of the amino acid sequence is a glutamine and residue 182 of the amino acid sequence is a phenylalanine. In some embodiments, engineered RNA modifying polypeptide has an improved editing efficiency and / or editing frequency compared to: a) an RNA modifying polypeptide comprising or consisting an amino acid sequence that is SEQ ID NO: 3, SEQ ID NO: 7, SEQ ID NO: 11, SEQ ID NO: 109, and / or SEQ ID NO: 111;optionally compared to an RNA modifying polypeptide comprising or consisting an amino acid sequence that is SEQ ID NO: 3, SEQ ID NO: 7, SEQ ID NO: 11, SEQ ID NO: 109, and / or SEQ ID NO: 111 that does not have a glutamine at residue 174 and / or a phenylalanine at residue 182; and / or b) an RNA modifying polypeptide comprising or consisting an amino acid sequence that is encoded by a nucleotide sequence that is SEQ ID NO: 4, SEQ ID NO: 8, SEQ ID NO: 12, SEQ ID NO: 110, and / or SEQ ID NO: 112; optionally compared to an RNA modifying polypeptide comprising or consisting an amino acid sequence that is encoded by a nucleotide sequence that is SEQ ID NO: 4, SEQ ID NO: 8, SEQ ID NO: 12, SEQ ID NO: 110, and / or SEQ ID NO: 112 that does not have a glutamine at residue 174 of the amino acid sequence and / or a phenylalanine at residue 182 of the amino acid sequence.The invention also provides various nucleic acids, and vectors associated with the method,for example that express components required in the method. For example the invention provides an expression cassette comprising: a) a nucleotide sequence encoding a first query RNA or plurality of query RNAs; b) a nucleotide sequence encoding the test polypeptide; c) a nucleotide sequence encoding a query polypeptide; d) a nucleotide sequence encoding the fusion polypeptide; e) a nucleotide sequence encoding the polypeptide capable of modifying RNA or a fragment thereoff) a nucleotide encoding a recruitment module wherein the query polypeptide, test polypeptide, fusion polypeptide, polypeptide capable of modifying RNA, recruitment module and / or RNA is the query polypeptide, fusion polypeptide, polypeptide capable of modifying RNA, and / or RNA as defined elsewhere herein. The expression cassette of the invention may further comprise a promoter; optionally wherein each of: a) the nucleotide sequence encoding the first query RNA or plurality of first query RNAs; b) the nucleotide sequence encoding the fusion polypeptide; c) the nucleotide sequence encoding the query polypeptide; d) the nucleotide sequence encoding a polypeptide capable of modifying RNA or a fragment thereof;e) the nucleotide sequence encoding a recruitment module; and / or e) the nucleotide sequence encoding the test polypeptide; are operably linked to said promoter. The promoter of the expression cassette may be selected from the group comprising or consisting of: a CMV promoter; an EF1a promoter; an SV40 promoter; a PGK promoter; a CAG promoter; a minimal promoter; or any combination thereof. The expression cassette of the invention may further comprise an operator sequence, optionally wherein the operator sequence is selected from the group comprising or consisting of: TetO; and CuO. In some embodiments of the expression cassette: a) the promoter is capable of driving the transcription and / or expression of a nucleotide sequence to which the promoter is operably linked in the presence of ancontroller molecule; and / or b) the promoter is not capable of driving the transcription and / or expression of a nucleotide sequence to which the promoter is operably linked in the absence of a controller molecule.As described elsewhere herein, in any of the methods of the invention, expression fromthe promoter in the expression cassette, or expression of any of the component parts of the method, is controlled by an inducible expression system, optionally wherein the inducible expression system is selected from the group comprising or consisting of: a) a Tet-on system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in the absence of the controller molecule and is induced in the presence of a controller molecule; b) a Tet-off system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in the presence of the controller molecule and is induced in the absence of the controller molecule; c) a tet-repressor system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids repressed in the presence of the controller molecule and is induced in the absence of the controller molecule; or d) a cumate expression system, wherein expression of the test polypeptide,first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in the presence of the inducer molecule and induced in the absence of the controller molecule. In some embodiments the controller molecule selected from the group comprising or consisting of: tetracycline; doxycycline; cumate. The invention also provides a plurality of expression cassettes, wherein each expression cassette of the plurality of expression cassettes is an expression cassette of the invention, as defined elsewhere herein. The invention also provides vectors that encode the component parts of the method, or that comprise the expression cassette of the invention or plurality of expression cassettes of the invention. As is standard in the field, the vectors of the invention may further comprises a selectable marker, optionally wherein the selectable marker is a fluorescent selectable marker, optionally wherein the fluorescent selectable marker is selected from the group comprising or consisting of: GFP, YFP, and RFP. The vector of the invention may be a vector selected from the group comprising orconsisting of: a plasmid, a lentiviral vector, and / or an landing pad vector.The invention also provides a plurality of vectors, wherein each vector of the plurality of vectors is a vector of the invention, as described herein. The invention also provides a cell that comprises the expression cassette of the invention,; the plurality of expression cassettes of the invention; the vector of the invention; and / or the plurality of vectors of the invention, as described herein. The cell may be a eukaryotic cell, a bacterial cell, or an archaeal cell. The eukaryotic cell may be a human cell or a yeast cell. The bacterial cell may be an E. coli cell. The invention also provides a plurality of cells, wherein each cell of the plurality of cells is a cell of the invention, as described herein. The invention also provides a fusion protein or polypeptide as described herein. Forexample a fusion protein comprising a query polypeptide and:i) an RNA modifying domain or fragment thereof capable of modifying RNA; or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain; or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable ofmodifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain.Preferences for features of the fusion protein or fusion polypeptide are as describedelsewhere herein, for example preferences for the RNA modifying domain or RNA modifying enzyme. The invention also provides a nucleic acid encoding a fusion protein or polypeptide as described herein. The invention provides a library of fusion polypeptides or fusion proteins, wherein each fusion polypeptide is a fusion polypeptide or protein of the invention. The invention also provides a library of query RNA nucleic acids, wherein each query RNA nucleic acid is a query RNA nucleic acid as defined herein. The term “library” when applied to polypeptides and / or RNAs is known in the art, and includes a plurality of individual units of a particular entity. For example, a library of fusionpolypeptides or fusion proteins comprises a plurality of fusion polypeptides or fusionproteins of the invention; and a library of query RNA nucleic acids comprises a plurality of query RNA nucleic acids as defined herein. In one embodiment, the library of fusion polypeptides or fusion proteins comprises at least at least 2, at least 3, at least 4, at least 5, at least 6, at least 7, at least 8, at least 9, at least 10, at least 20, at least 30, at least 40, at least 50, at least 60, at least 70, at least 80, at least 90, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, or more fusion polypeptides or fusion proteins. In one embodiment, the library of fusion polypeptides or fusion proteins comprises about 2, about 3, about 4, about 5, about 6, about 7, about 8, about 9, about 10, about 20, about 30, about 40, about 50, about 60, about 70, about 80, about 90, about 100, about 200, about 300, about 400, about 500, about 600, about 700, about 800, about 900, or about 1000 fusion polypeptides or fusion proteins. In one embodiment, the library of fusion polypeptides or fusion proteins comprises 2, 3, 4, 5, 6, 7, 8, 9, 10, 20, 30, 40,50, 60, 70, 80, 90, 100, 200, 300, 400, 500, 600, 700, 800, 900, or 1000 fusionpolypeptides or fusion proteins. Each fusion polypeptide or fusion protein comprised by the library of fusion polypeptides or fusion proteins may be expressed in a cell. For example, in some embodiments, each fusion polypeptide or fusion protein comprised by the library of fusion polypeptides or fusion proteins is expressed in a different cell. In some embodiments, the cell is a human cell. In one embodiment, the library of query RNA nucleic acids comprises at least 2, at least 3,at least 4, at least 5, at least 6, at least 7, at least 8, at least 9, at least 10, at least 20, atleast 30, at least 40, at least 50, at least 60, at least 70, at least 80, at least 90, at least 100, at least 200, at least 300, at least 400, at least 500, at least 600, at least 700, at least 800, at least 900, at least 1000, at least 2000, at least 3000, at least 4000, at least 5000, at least 6000, at least 7000, at least 8000, at least 9000, at least 10,000, at least 20,000, at least 30,000, at least 40,000, at least 50,000, at least 60,000, at least 70,000, at least 80,000 at least 90,000, at least 100,000, or more query RNA nucleic acids. In some embodiments, the library of query RNA nucleic acids comprises about 2, about 3, about 4, about 5, about 6, about 7, about 8, about 9, about 10, about 20, about 30, about 40, about 50, about 60, about 70, about 80, about 90, about 100, about 200, about 300, about 400, about 500, about 600, about 700, about 800, about 900, about 1000, about 2000, about 3000, about 4000, about 5000, about 6000, about 7000, about 8000, about 9000, about 10,000, about 20,000, about 30,000, about 40,000, about 50,000, about 60,000, about 70,000, about 80,000 about 90,000, or about 100,000 query RNA nucleic acids. In some embodiments, the library of query RNA nucleic acids comprises 2, 3, 4, 5,6, 7, 8, 9, 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 200, 300, 400, 500, 600, 700, 800,900, 1000, 2000, 3000, 4000, 5000, 6000, 7000, 8000, 9000, 10,000, 20,000, 30,000, 40,000, 50,000, 60,000, 70,000, 80,00090,000, or 100,000 query RNA nucleic acids. The library of query RNA nucleic acids may be derived from any suitable source. For example, the library of query RNA nucleic acids may comprise synthetic RNA nucleic acids, RNA nucleic acids derived from a cell, extracellular RNA (eRNA), cell-free RNA (cfRNA), environmental RNA, and / or any mixture thereof. In some embodiments, the library of query RNA nucleic acids comprises the whole transcriptome of a cell. In some embodiments, the cell is a human cell. In some embodiments, the library of query RNA nucleic acids is comprised by the cell. A library of fusion polypeptides or fusion proteins, or a library of query RNA nucleic acids, may suitably be used in a multiplexed assay or an arrayed assay. In a multiplex assay, the library of fusion polypeptides or fusion proteins or library of query RNA nucleic acids are admixed together in one reaction vessel and taken through the methods providedherein. In an arrayed assay, each fusion polypeptide or fusion protein of the library offusion polypeptides or fusion proteins, or each query RNA nucleic acid of the library of query RNA nucleic acids, is assayed individually in a separate reaction vessel, for example in the separate wells of a multi-well plate. Accordingly, in some embodiments, the methods provided herein are performed as multiplex methods. In some embodiments, the methods provided herein are performed as arrayed methods. As will be appreciated, multiplex and arrayed methods may be combined. For example, in some embodiments, a multiplex library of query of RNA nucleic acids may be assayed using an arrayed library of fusionpolypeptides or fusion proteins. In this way, the binding interactions between each fusionpolypeptide or fusion protein of the library of fusion polypeptides or fusion proteins and each of the query RNA nucleic acids comprised by the library of RNA nucleic acids may be assessed. Also provided herein is a kit comprising any one or more of: a) a query polypeptide or a fragment thereof, query RNA nucleic acid, first query RNA nucleic acid, plurality of query RNA nucleic acids, test polypeptide, polypeptide capable of modifying RNA, a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, or a fragment thereof, or fusion polypeptide as provided herein; b) an expression cassette as provided herein; c) a plurality of expression cassettes as provided herein; d) a vector as provided herein; e) a plurality of vectors as provided herein;f) a cell as provided herein; g) a plurality of cells as provided herein; h) a library of fusion polypeptides as provided herein; and / or i) a library of RNA nucleic acids as provided herein. Such kits are suitable for use in the methods provided herein. Also provided herein is a method of identifying an improved test polypeptide, wherein the test polypeptide is a test polypeptide provided herein, the method comprising: a) preparing at least a reference test polypeptide and a candidate test polypeptide; b) performing the method provided herein on the reference test polypeptide and candidate test polypeptide; and c) comparing the performance of the reference test polypeptide and candidate test polypeptide; andd) determining whether the candidate test polypeptide is an improved test polypeptide. As will be understood, multiple performance characteristics of the test polypeptide may suitably be improved. For example, the editing efficiency, editing frequency, “on-target” editing, "off-target” editing, and / or the ratio of “on-target” to “off-target” editing of the test polypeptide may suitably be improved. Accordingly, in one embodiment, step b) determining the performance of the reference test polypeptide and candidate test polypeptide comprises: i) determining the editing efficiency of the reference test polypeptide and candidate test polypeptide; ii) determining the editing frequency of the reference test polypeptide and candidate test polypeptide; iii) determining the “on target” editing frequency of the reference test polypeptide and candidate test polypeptide; iv) determining the “off-target” editing frequency of the reference test polypeptide and candidate test polypeptide; and / or v) determining the ratio of “on-target” to “off-target” editing of of the reference test polypeptide and candidate test polypeptide. In one embodiment, step c) comparing the performance of the reference test polypeptideand candidate test polypeptide comprises:i) comparing the editing efficiency of the reference test polypeptide to the editing efficiency of the candidate test polypeptide; ii) comparing the editing frequency of the reference test polypeptide to the editing frequency of the candidate test polypeptide; iii) comparing the “on-target” editing frequency of the reference test polypeptide to the “on-target” editing frequency of the candidate test polypeptide; iv) comparing the “off-target” editing frequency of the reference test polypeptide to the “off-target” editing frequence of the candidate test polypeptide; and / or v) comparing the ratio of “on-target” to “off-target” editing of the reference test polypeptide to the ratio of “on-target” to “off-target” editing of candidate test polypeptide. In one embodiment, the candidate test polypeptide is determined to be an improved testpolypeptide when:a) the candidate test polypeptide has a higher editing efficiency than the reference test polypeptide; b) the candidate test polypeptide has a higher editing frequence than the reference test polypeptide; c) the candidate test polypeptide has an higher “on-target” editing frequency than the reference test polypeptide; d) the candidate test polypeptide has a lower “off-target” editing frequencythan the reference test polypeptide; and / or e) the candidate test polypeptide has higher “on-target” to “off-target” editing ratio than the reference test polypeptide. The test polypeptide provided herein may have any one of a plurality of different configurations. For example, as described herein, the test polypeptide may be a fusion protein comprising a query polypeptide and an RNA modifying domain or fragment thereof capable of modifying RNA; a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain. The RNA modifying domain or fragment thereofcapable of modifying RNA; a first portion of an RNA modifying domain that is capable ofmodifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain may be N-terminally linked to the query polypeptide, or may be C-terminally linked to the query polypeptide. A flexible linker may be present between the query polypeptide and the RNA modifying domain or fragment thereof capable of modifying RNA; a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to thesecond affinity domain. Furthermore, as described herein, any of the components of thetest polypeptide may carry one or more mutations. Accordingly, as will be appreciated, a candidate test polypeptide and / or reference test polypeptide may comprise any configuration of test polypeptide. Preferably, the configuration of the candidate test polypeptide is different in at least one way to the reference test polypeptide. Accordingly, in some embodiments: a) the candidate test polypeptide comprises a different query polypeptide to the reference test polypeptide; b) the candidate test polypeptide comprises a different: i) RNA modifying domain or fragment thereof capable of modifying RNA; ii) first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain; iii) recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitmentmodule comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; or iv) flexible linker to the reference test polypeptide; c) the candidate test polypeptide is N-terminally fused to the RNA modifying domain, first portion of an RNA modifying domain or second portion of an RNA modifying domain, or recruitment domain; and the reference test polypeptide is C- terminally fused to the RNA modifying domain, first portion of an RNA modifying domain or second portion of an RNA modifying domain, or recruitment domain; d) the candidate test polypeptide is C-terminally fused to the RNA modifying domain, first portion of an RNA modifying domain or second portion of an RNA modifying domain, or recruitment domain; and the reference test polypeptide is N- terminally fused to the RNA modifying domain, first portion of an RNA modifyingdomain or second portion of an RNA modifying domain, or recruitment domain; e) the candidate test polypeptide and reference test polypeptide are N- terminally fused to the RNA modifying domain, first portion of an RNA modifying domain or second portion of an RNA modifying domain, or recruitment domain; and / or f) the candidate test polypeptide and reference test polypeptide are N- terminally fused to the RNA modifying domain, first portion of an RNA modifying domain or second portion of an RNA modifying domain, or recruitment domain.In some embodiments, the candidate test polypeptide is mutated compared to the reference test polypeptide, optionally wherein the RNA modifying domain or fragment thereof is a mutant RNA modifying domain or fragment thereof and / or an engineered RNA modifying domain or fragment thereof. Figure Legends Figure 1 A plot mapping the frequency of A>G edited (“A2G”) sites as determined by RNA- seq in HEK293 cells in the presence of an hIREB2 or hACO1 configured hyperTRIBE assay. hIREB2 and hACO1 represent two RBPs with well characterised RNA binding motifs (Iron Response Elements – IRE) that are highlighted in the TFRC transcript by square dots beneath the x-axis. The negative control (“Ctrl”) represents cells which do not express hyperTRIBE. Figure 2 Schematic of exemplary systems according to the invention. A) In one exemplary embodiment, an RBP (“query polypeptide”) is fused to an SH3 domain (“first affinity domain”), and an ADARCD and / or CBE polypeptide (“RNA modifying domain or fragment thereof capable of modifying RNA”) is / are fused to an SHL domain (“second affinity domain”). Following association of the RBP with RNA, binding of the SH3 domainto the SHL domain recruits the ADARCD and / or CBE polypeptide to the RNA, leading toA>I or C>U deamination of RNA at or close to the RBP binding site. Co-delivery of both the ARCARcd and CBE polypeptides could enable both A>I and C>U edits by a single RBP at a single RNA locus through the transitory nature of the recruitment of either effector though the RBP fused first affinity domain (SH3). Such a process would create an on-target editing signature of both A>I and C>U transitions allowing more confident determination of tre-positive signals Alternatively b), the RBP may be fused to the ADARCD or CBE; or c) the ADARCD or CBE may be a split-ADAR or split-CBE. By way of example, the ADARCD N-terminus may be fused to the RPB, and the ADARCD C-terminus may be expressed separately. Following association of the RBP with RNA, the ADARCD C-terminus is recruited to the ADARCD N-terminus forming a functional ADARCD enzyme, leading to A>I deamination of RNA at or close to the RBP binding site. Recruitment of the ADAR C- terminus to the N-terminus may be mediated by dimerization of two dimerization domains as described herein (not shown). One dimerization domain may be fused to the ADARCD N-terminus and one dimerization domain may be fused to the ADARCD C-terminal fragment. Figure 3 Schematic showing an “embedded deaminases” according to the invention. Dueto the modular nature of RBPs, the RNA binding element or domain of the RBP may beisolated and fused with a deaminase either using a native linker or optimised linker, such as a 32 aa linker. a) Exemplary architecture of the PUM2 polypeptide, and “embedded deaminase” fusions with ADARCD fused to the RNA binding element PUM-HD by endogenous linkers (1, 2) or by an optimised 32 aa linker (3). b) Exemplary architecture of the UHMK1 polypeptide, and “embedded deaminase” fusions with ADARCD fused to the RNA binding domain RPM by an endogenous linker (1) or by an optimised 32 aa linker (2). Figure 4 Plasmid constructs encoding components of the improved RBP mapping system system provided herein. a) hADAR2CD (E174Q)_[GGGGS]3_hPUM2 - human ADAR2CD (E174Q) fused to the N terminus of PUM2. b) hPUM2_[GGGGS]3_hADAR2CD (E174Q) - human ADAR2CD (E174Q) fused to the C terminus of PUM2. c) hADAR2CD (E174Q / N182F)_[GGGGS]3_hPUM2 - hADAR2CD (E174Q + N182F) fused to the N terminus of PUM2. d) hPUM2_[GGGGS]3_hADAR2CD (E174Q / N182F) - hADAR2CD (E174Q + N182F) fused to the C terminus of PUM2. e) hADAR2CD(E174Q / N182F)_XTEN_hPUM2 - fusion of human ADAR2CD (E174Q + N182F) to the Nterminus of human PUM2 via the XTEN linker. f) hPUM2_XTEN_hADAR2CD (E174Q / N182F) - fusion of human ADAR2CD (E174Q + N182F) to the C terminus of human PUM2 via the XTEN linker. g) hADAR2CD (E174Q / N182F)_32aa_hPUM2 - fusion of human ADAR2CD (E174Q + N182F) to the N terminus of human PUM2 via the 32aa linker. h) hPUM2_32aa_hADAR2CD (E174Q / N182F) - fusion of human ADARCD (E174Q + N182F) to the C terminus of human PUM2 via the 32aa linker. i) Split deaminase design 1. The C terminal end of the split enzyme is fused to the N terminus of PUM2 via FKBP12. The N terminal end of the split enzyme is fused to FRB. j) Split deaminase design 2. The N terminal end of the split enzyme is fused to the C terminus PUM2 via FKBP12. The C terminal end of the split enzyme is fused to FRB k) Split deaminase design 3. The C terminal end of the split enzyme is fused to the N terminus of PUM2 with FKBP12 fused to the N terminus of the ADAR2 C terminal fragment. The N terminal end of the split enzyme is fused to FRB. l) Split deaminase design 4. The N terminal end of the split enzyme is fused to the C terminus of PUM2. with FKBP12 fused to the C terminus of the ADAR2 Nterminal fragment. m) TetOn_dADARCD (E192Q)_hPUM2. Fusion of Drosophila ADARCD(E192Q) to the N terminus of human PUM2. Expression is under the control of a doxycycline inducible promoter. n) TetOn_hPUM2_dADARCD (E192Q). Fusion of Drosophila ADARCD (E192Q) to the C terminus of human PUM2. Expression is under the control of a doxycycline inducible promoter. Figure 5 HEK293 cells were transfected with the indicated vector and 24 hours posttransduction the cells were collected and RNA was extracted, after which the RNA wassequenced. The data shows the overall A>G mutation frequency following transfection with the different constructs. The RBP (RNA binding protein) mapping systems introduced to the cells catalyse A>G mutations by recruiting the RNA adenine deaminase ADAR to the RNA binding site of the query protein. The RNA editing systems were configured to map the RNA binding sites of PUM2 and CSDE1. PUM2 represents an RBP with a known RNA binding motif whereas CSDE1 is a RBP with an uncharacterized RNA binding motif. Figure 6 a) Number of PUM2 binding sites. PUM2 has a known binding motif (UGUA) and so the total number of true positive editing sites can be readily identified within all edited sites identified from RNA-seq. Edited sites were defined as those that show an A>G editing frequency of at least 0.1 in one replicate and 0.05 in the other replicate. The sequence 50 bp either side of the edited site was then scanned for the PUM2 binding motif. The data shows that the introduction of hADAR2CD_N182F improves upon the original HyperTRIBE platform in terms of the total number of PUM2 binding sites identified - in the optimumconfiguration 3451 sites are identified with dADARCD, whereas 6506 are identified in thepresence of hADAR2CD_N182F. Additionally the data also demonstrates that the configuration of the platform has a critical determination on its performance. In the presence of either deaminase, fusion to the C terminus of PUM2 outperforms an N-terminal fusion (3451 versus 179 for dADARCD and 6506 versus 455 for hADAR2CD_N182F). This data suggests that for optimum results configuration of the platform needs to be customised to each individual RBP, in addition to system orientation this optimisation process is likely to include refinement of other parameters such as the length and constitution of linkers. b) Percentage enrichment of high-confidence PUM2 sites. High concordant editing sites were extracted from the optimum dADARC and hARA2CD_N182F platforms and the enrichment of PUM2 binding sites within the total number of edited sites. Data is shown for those sites that show an A>G editing frequency of at least 0.1 in one replicate and 0.05 in the other replicate (0.1), and additionally data is shown for those sites that show an A>G editing frequency of at least 0.2 in one replicate and 0.1 in the other replicate (0.2). The data demonstrates an increased enrichment of PUM2 sites whenusing the hARA2CD_N182F platform.Examples Example 1: Case study assessing the specificity of the known hyperTRIBE assay In this study hyperTRIBE was used to map the binding sites of hIREB2 and hACO1, two RNA binding proteins which are known to bind with high-affinity to RNA-stem loops referred to iron-response elements (IRE) which possess a core 6nt RNA motif (Kaptain et al., 1991, PNAS 88(22):10109-10113 doi: 10.1073 / pnas.88.22.10109; Samaniego et al., 1994, J.Biol. Chem., 269(49):30904-30910, both incorporated by reference).hREB2 and hACO1 have known binding sites they serve as an ideal target for testing the veracity of hyperTRIBE in mapping the binding sites of RBPs. This study we observed only a modest increase in the overall A>G mutation frequency for hIREB2 (0.089029) and hACO1 (0.088834) compared to the control (0.085247). Furthermore, detailed analysis of the mutational profile of a known positive control for binding of hIREB2 and hACO1 (TFRC) demonstrated poor resolution and specificity of the assay. Figure 1 maps sites within the TFRC transcript that have been determined to be edited (A>G). Based on the fundamental principle of how hyperTRIBE functions it would be expected that these edited sites would correspond to binding sites of the RBP under interrogation. As discussed above, hIREB2 and hACO1 are known to bind defined IREs within the TFRC transcript; however, as shown in the Figure 1, there is poor overlap between the purported binding sites determined by hyperTRIBE and the known binding sites (indicated by square dots). It is also apparent that the resolution of “binding” provided by hyperTRIBE is poor, with the spread of edited sites a significant hindrance to narrowing down true RNA binding sites. Further analysis of the data also revealed that the 6 nt core RNA motif of IREs was not enriched within “binding” regions reported by hyperTRIBE throughout the transcriptome. It can be therefore concluded based on this data that the ability of known hyperTRIBE assay to identify true positive binding sites is limited. This data also suggests that the known hyperTRIBE assay may incorporate false positives into the data, severely confounding interpretation of the results. Example 2: Design and construction of an improved RBP mapping system using an RBP- RNA modifying fusion polypeptide construct To assess the proposed RBP mapping assay the relevant coding sequences (SEQ ID NOs: 38 and 40, encoding test polypeptides with SEQ ID NOs: 37 and 39 respectively; and SEQ ID NOs: 2, 6, 8, 30, and 32 encoding control polypeptides with SEQ ID NO: 1, 5, 7, 29, and 31) were be cloned into the vector backbone that is depicted in Figure 4a, 4b, 4c, 4d, 4e, 4f, 4g and 4h. This vector architecture consists of driving the expression of the deaminase fused to the query RBP via an EF-1α promoter. Within this system there are 2 primary targets for optimisation; 1) The deaminase; 2) The polypeptide linker. To interrogate different modifications of the linker and / or deaminase the sequence of interest will be cloned into the vector replacing the original sequence. For example, the XTEN nucleotide would be synthesised and cloned into the vector following removal of the GGGGS3 (SEQ ID NO:27) linker. Example 3: Analysis and validation of an improved RBP mapping system using an RBP- RNA modifying fusion polypeptide construct Vectors encoding the following constructs were generated, including constructs as set out in Example : Constructs Description Control PUM2 empty Wild-type PUM2 protein with no RNA Q P ly D ly D ly D ly D 2F g 5 2F to Constructs Description PUM2 RBP protein (SEQ ID NO: SEQ 2F to Q 2F to O: O: 2F to 9 te, using the following protocol: 1. 24 hours prior to transfection seed 500,000 HEK293 cells into a well of a 6-wellplate. 2. Mix 250 µl of Opti-MEM ^ with 5µl of Lipofectamine ^ 2000 reagent in tube A 3. Mix 250 µl of Opti-MEM ^ with 2 µg of plasmid DNA in tube B. 4. Combine tube A and tube B, mix gently and incubate for 20 minutes at room temperature. Add the 500 µl DNA-lipid complex to a well of a 6-well plate andincubate for 6 hours at 37°C. 5. Aspirate medium and replace with 2 µl in DMEM + 10%FBS. 6. Live cell imaging of a fluorescent marker was used to ensure high-transfection efficiency 7. 24 hours post-transfection RNA was extracted using TRIzol extraction and mRNA next generation sequencing was performed to identify hotspots of A>G mutations. Each experiment was conducted in duplicate. As shown in Figure 5, test constructs comprising the PUM2 or CSDE1 RBP N- or C- terminally fused to dADARCD or hADAR2CD showed increased editing frequency compared to empty control constructs. Additionally, hADAR2CD comprising an N182F mutation have a higher editing frequency compared to the dADARCD constructs. These data demonstrate that the constructs provided herein, such as the fusion constructs, are capable of editing RNA transcripts; and that the N182F mutation in hADAR2CD increases the editing performance of the construct compared to dADARCD. The data also demonstrates that theRNA modifying polypeptide, such as dADARCD or hADAR2CD, retains RNA editing activitywhen fused to the N- or C-terminus of the RBP. PUM2 has a known binding motif (UGUA) and this was used to determine the number of true positive binding sites identified with the different constructs used. An edited site was determined to possess a PUM2 binding site if the UGUA motif was identified within 50 bp either side of the edited site. An edited site is defined as having an editing frequency of at least 0.1 in one replicate and at least 0.05 in the other. Figure 6 a) demonstrates that utilisation of the hADAR2CD_N182F deaminase enzyme leads to an increase in the total number of PUM2 binding sites identified. Figure 6 b) Demonstrates an enrichment of high- confidence PUM2 binding sites within the total number of edited sites when the hADAR2CD_N182F deaminase is integrated into the platform. High-confidence edited sites were defined as those that occur within overlapping genes between different constructs. Additionally, edited sites were segregated into low (0.1) and high (0.2) frequency sites. High frequency sites were defined as having an editing frequency of at least 0.2 in onereplicate and at least 0.1 in the other.Prophetic Example 4: Design and construction of an improved RBP mapping system using an RBP-split RNA modifying polypeptide fusion construct and / or RBP-inducible RNA modifying polypeptide fusion construct In addition to the fusion protein configuration set out in Example 2 above, an RBP-split RNA modifying polypeptide fusion construct and an RBP-inducible RNA modifying construct are provided herein. Accordingly, a second configuration of the backbone is represented in figure 4i, 4j, 4k and 4l. In this set-up the deaminase is split into two terminal domains that are tethered to dimerization domains, in this case FRB and FKP12 (Figure 2c). The coding sequences are expressed as a single transcript driven by an EF-1α promoter and translated into a single prolylpeptide. Critically, a T2A self-cleavage peptide is encoded that within the sequence that enables separation of the two halves of the deaminase into two distinct recombinant proteins – one half of the deaminase fused to a dimerization domain and a second recombinant protein that consists of the second half of the deaminase fused to the query RBP and corresponding dimerization domain to that encoded within the first recombinant protein. The utilisation of a self-cleavage peptide will also be sued to generate a non- covalent system that used affinity domains for recruitment. The third configuration of the system is depicted in figure 4n and 4m. In this vectorbackbone the expression of the coding sequence is dependent on an inducible promotersystem rather than the constitutively active EF-1α promoter. Utilising the above backbones different iterations of the system can be generated and interrogated. To interrogate different designs, such as linkers and deaminases, the sequence of interest will be cloned into the vector replacing the original sequence. For example, the XTEN nucleotide would be synthesised and cloned into the vector following removal of the GGGGS3 (SEQ ID NO:27) linker. Cloning would be carried out by traditional restriction cloning, golden gate cloning or Gibson assembly. Successful cloning would be determined by Sanger sequencing to confirm the presence of the correct insert into the vector backbone. To achieve the best balance of on-target editing whilst minimising off-target editing, different combinations of inserts and vector architectures will be utilised. For example, combinations of linkers of deaminase will be cloned into the vectors depicted in figures 4mand 4n to enable assessment of these modifications in a system that minimised off-targeteffects. The vectors encoding the RBP mapping system as set out in Figures 2 a), 2 c), and Figures 4i-4m will be delivered into HEK 293 cells via transient reverse transfection in a 96 well plate. Initially the success of the various designs will be determined at candidate positive and negative loci, the known binding motif can be used to identify positive control sites which can be used to ascertain the efficacy of the assay: 1. Mix 25 µl of Opti-MEM ^ with 0.5µl of Lipofectamine ^ 2000 reagent in tube A 2. Mix 25 µl of Opti-MEM ^ with 200 ng of plasmid DNA in tube B. 3. Combine tube A and tube B, mix gently and incubate for 20 minutes at room temperature. Add the 50 µl DNA-lipid complex to a well of a 96-well plate. 4. Add 10,000 cells suspended in 50 µl in DMEM + 10%FBS to the well, and rock the plate gently to disperse the cells homogenously. Incubate the cells at 37°C for 6 hours. 5. Aspirate medium and replace with 200 µl in DMEM + 10%FBS. 6. RNA will be collected at 6h, 24h and 48h post transfection. 7. RNA extracted using the RNeasy ^ kit and 500 ng of RNA will be converted to cDNA using the SuperScript™ II Reverse Transcriptase kit. 8. Target regions will be amplified by PCR and sequenced via Sanger sequencing. PCR will be performed as follows: Reagent Quantity DreamTaq Buffer 5 µl Step Temperature Time Cycles 9. e eve o ed t ng w be determ ned by Sanger sequencing. As the Sanger sequencing will represent a mixed population of edited and non-edited samples there will be a mixture of A and G (or T and C) bases at the target residues. Therefore, quantification of the relevant base peak area (G or C) relative to thetotal peak area (A + G or T + C) will give an approximation of the percentage of editing at the residue. These values will be used to determine the level of editing at the positive and negative control loci. Success will be determined by identifying those designs that increase the ratio of on-target to off-targeting editing at these loci 10. Those designs that demonstrate improved functionality will assessed at a transcriptome-wide level through RNA-seq Equivalents Those skilled in the art will recognize, or be able to ascertain using no more than routine experimentation, many equivalents to the specific embodiments of the invention described herein. The scope of the present invention is not intended to be limited to the above Description. Sequences >SEQ_ID_NO:_1_hPUM2_AA MSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGD DDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQV PMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGP AVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGY QVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGS SSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLAL QMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLP ILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKD QYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGML >SEQ_ID_NO:_2_hPUM2_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagat gatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcct ctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgt tgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggta ccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagt taactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatttgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtccagcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacag ccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtca gcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctat caagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaa tggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcac aaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagc agttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaact ctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagtccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatt tagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttc agaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagc aaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaactatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttgcagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgc tcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctg aagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttac tcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggac cagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattacta ctttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggacc accaaatggaatgctg >SEQ_ID_NO:_3_Human_ADAR2_catalytic_domain_(hADAR2cd)_E174Q_AA MQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLY TQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSNASIQTW DGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAP NFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEK PTEQDQFSLTP >SEQ_ID_NO:_4_Human_ADAR2_catalytic_domain_(hADAR2cd)_E174Q_DNA atgcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctcatgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctac actcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacg ttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagaca tcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccAACgctagtattcaaacgtgg gacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttga gcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcctaacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgt gtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatca tgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaag ccgaccgagcaggaccaattctctctgacgccc >SEQ_ID_NO:_5_Human_ADAR2_catalytic_domain_(hADAR2cd)_E174Q / N182F_AA MQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLY TQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSFASIQTW DGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAP NFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEK PTEQDQFSLTP >SEQ_ID_NO:_6_Human_ADAR2_catalytic_domain_(hADAR2cd)_E174Q / N182F_AA _DNA atgcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctcatgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctac actcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacg ttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagaca tcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccTTCgctagtattcaaacgtgg gacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttga gcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttc taatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcct aacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgt gtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatcatgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaagccgaccgagcaggaccaattctctctgacgccc >SEQ_ID_NO:_7_Drosophila_ADAR_catalytic_domain_(dADARcd)_E192Q_AA MYSPMVVPQKNVPLPIDDKSSSMELPQIHADTIGRLVLEKFMEVIKGQEAYSRRKVLAGIVMTENMNFCEAKVISVSTGTKCVSGEHMSVNGAV LNDSHAEIVSRRCLLKYLYAQLDLQCNQATAYQSIFVRNTDGQYPYKLKSGVHFHLYINTAPCGDARIFSPHENDTGVDKHPNRKARGQLRTKI ESGQGTIPVKSSDGIQTWDGVLQGQRLLTMSCSDKIARWNIVGIQGSLLSSIIEPVYLHSIVLGSLLHPEHMYRAVCGRIEKSIQGLPPPYHLN KPRLALVTSAEPRNQAKAPNFGINWTIGDTELEVVNSLTGRTIGGQVSRITKQAFFVKYGFLMANLPGILVRKVTTDYGQTKANVKDYQIAKLE LFSAFKREDLGSWLKKPIEQDEFGLAE >SEQ_ID_NO:_8__Drosophila_ADAR_catalytic_domain_(dADARcd)_E192Q _DNA atgtattcccccatggtggtgccccagaagaacgtccccctccccattgacgacaaaagcagcagcatggagctcccccagatccacgctgaca caattggcaggctggtgctggaaaaattcatggaggtgatcaaaggacaagaggcctacagcaggaggaaagtgctggctggcattgtgatgac cgagaatatgaacttctgcgaggccaaggtgatcagcgtgtccaccggcaccaaatgcgtctccggcgaacacatgagcgtcaacggcgccgtg ctgaatgattcccacgccgagattgtctccagaaggtgcctcctcaagtacctctacgcccagctggacctgcagtgcaaccaagctaccgcctaccagagcatcttcgtcagaaacaccgatggccagtacccctataagctgaagagcggagtgcacttccacctctatatcaataccgctccttgcggcgacgctaggatcttcagccctcacgagaacgacacaggcgtggacaagcatcccaacaggaaagccaggggccagctgaggaccaagatc gagagcggccagggaaccatccccgtgaagagcagcgatggcatccagacctgggatggagtcctccagggccagagactgctgaccatgtcct gtagcgacaagatcgccaggtggaatatcgtgggcattcaaggctccctcctgtccagcatcattgaacccgtgtacctgcactccatcgtgct gggctccctgctgcaccccgaacacatgtatagggctgtgtgcggcagaattgagaagagcatccagggcctccctcccccctaccacctcaac aaacccaggctggccctcgtcaccagcgccgagcccagaaaccaggccaaagcccccaacttcggcatcaactggaccatcggagataccgagc tggaggtggtgaacagcctcaccggaaggaccattggcggccaggtgtccaggatcacaaagcaggccttcttcgtgaaatacggcttcctcat ggccaacctgcctggcatcctggtgagaaaagtcaccacagattacggccagacaaaagccaacgtgaaggactaccagattgccaagctggaa ctgttcagcgctttcaagagagaagacctgggcagctggctgaagaaacccatcgaacaggatgagttcggactggctgag>SEQ_ID_NO:_9_Human_ADAR2_catalytic_domain_N-terminus_split__(NtermADAR2)_AAMQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLY TQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPA >SEQ_ID_NO:_10_Human_ADAR2_catalytic_domain_N-terminus_split_(NtermADAR2)_DNA atgcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctc atgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtg cataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctac actcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacg ttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcg >SEQ_ID_NO:_11_Human_ADAR2_catalytic_domain_C-terminus_split_E174Q_(CtermADAR2)_AA DRHPNRKARGQLRTKIESGQGTIPVRSNASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQ RISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPN VYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTP >SEQ_ID_NO:_12_Human_ADAR2_catalytic_domain_C-terminus_split_E174Q_(CtermADAR2)_DNA gacagacatcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccaacgctagtattc aaacgtgggacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcag cctcttgagcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaa cgaatttctaatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccagccaggga aagctcctaacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctc acgcctgtgtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaat gtgtatcatgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatggg tcgagaagccgaccgagcaggaccaattctctctgacgccc >SEQ_ID_NO:_13_ Human_ADAR2_catalytic_domain_C-terminus_split_E174Q / N182F_AADRHPNRKARGQLRTKIESGQGTIPVRSFASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPN VYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTP >SEQ_ID_NO:_14_Human_ADAR2_catalytic_domain_C-Terminus_split_E174Q / N182F_DNA gacagacatcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccttcgctagtattc aaacgtgggacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcag cctcttgagcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaa cgaatttctaatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccagccaggga aagctcctaacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctc acgcctgtgtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaat gtgtatcatgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatggg tcgagaagccgaccgagcaggaccaattctctctgacgccc >SEQ_ID_NO:_15_FRB_AAMILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISK>SEQ_ID_NO:_16_FRB_DNA ATGATTTTATGGCATGAGATGTGGCATGAGGGTTTGGAAGAGGCATCTAGATTGTATTTCGGTGAAAGAAATGTCAAGGGAATGTTCGAAGTTT TAGAACCGTTGCACGCTATGATGGAGAGAGGTCCACAGACTCTAAAGGAGACTTCCTTCAACCAAGCTTATGGAAGGGACCTAATGGAGGCTCA AGAATGGTGTAGAAAATACATGAAAAGTGGAAATGTAAAGGACCTTACACAAGCTTGGGATCTCTACTACCATGTTTTTAGGAGAATATCTAAA >SEQ_ID_NO:_17_FKBP12_AA MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPP HATLVFDVELLKLE >SEQ_ID_NO:_18_FKBP12_DNA ATGGGCGTACAAGTTGAAACTATCAGCCCTGGGGACGGCAGAACCTTTCCGAAGAGGGGACAGACATGTGTTGTTCACTATACTGGAATGTTGG AAGATGGTAAGAAGTTCGATAGCAGCAGAGATAGGAATAAACCATTTAAATTCATGCTTGGCAAGCAAGAAGTGATTAGGGGTTGGGAAGAAGG TGTCGCTCAAATGAGTGTAGGTCAGAGGGCTAAGTTAACAATTAGTCCTGATTATGCTTATGGCGCTACAGGTCATCCAGGAATCATTCCCCCA CATGCTACTCTTGTTTTCGACGTTGAATTGCTTAAGCTTGAA >SEQ_ID_NO:_19_dimerisation_linker_AA GGSGSGAGSGSPAGGGAPGSGGGS >SEQ_ID_NO:_20_dimerisation_linker_DNA gggggcagtgggagcggtgcaggatctggtagtccagctgggggaggagcaccgggtagcggtggggggagc >SEQ_ID_NO:_21_T2A_linker_AA GSGEGRGSLLTCGDVEENPGP >SEQ_ID_NO:_22_T2A_linker_DNA GGAAGTGGTGAGGGTAGGGGAAGTTTATTAACCTGTGGGGATGTTGAAGAAAATCCAGGTCCT >SEQ_ID_NO:_23_XTEN_linker_AA SGSETPGTSESATPES >SEQ_ID_NO:_24_XTEN__linker_DNA agcggcagcgagactcccgggacctcagagtccgccacacccgaaagt>SEQ_ID_NO:_25_32aa_linker_AASGGSSGGSSGSETPGTSESATPESSGGSSGGS >SEQ_ID_NO:_26_32aa_linker_DNA tctggtggttcttctggtggttctagcggcagcgagactcccgggacctcagagtccgccacacccgaaagttctggtggttcttctggtggtt ct >SEQ_ID_NO:_27_GGGGS_linker_AA GGGGSGGGGSGGGGS >SEQ_ID_NO:_28_GGGGS_linker_DNA GGCGGAGGTGGTTCTGGCGGTGGAGGTTCAGGCGGTGGTGGAAGT >SEQ_ID_NO:_29_dADARcd(E192Q)_GGGGS_hPUM2_AA MYSPMVVPQKNVPLPIDDKSSSMELPQIHADTIGRLVLEKFMEVIKGQEAYSRRKVLAGIVMTENMNFCEAKVISVSTGTKCVSGEHMSVNGAVLNDSHAEIVSRRCLLKYLYAQLDLQCNQATAYQSIFVRNTDGQYPYKLKSGVHFHLYINTAPCGDARIFSPHENDTGVDKHPNRKARGQLRTKIESGQGTIPVKSSDGIQTWDGVLQGQRLLTMSCSDKIARWNIVGIQGSLLSSIIEPVYLHSIVLGSLLHPEHMYRAVCGRIEKSIQGLPPPYHLN KPRLALVTSAEPRNQAKAPNFGINWTIGDTELEVVNSLTGRTIGGQVSRITKQAFFVKYGFLMANLPGILVRKVTTDYGQTKANVKDYQIAKLE LFSAFKREDLGSWLKKPIEQDEFGLAEGGGGSGGGGSGGGGSSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDS RFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPL PNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGV FSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAG QRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAG GTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSAS SSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKY RSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAA YQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKN SPDLGPIGGPPNGML >SEQ_ID_NO:_30_dADARcd(E192Q)_GGGGS_hPUM2_DNA atgtattcccccatggtggtgccccagaagaacgtccccctccccattgacgacaaaagcagcagcatggagctcccccagatccacgctgaca caattggcaggctggtgctggaaaaattcatggaggtgatcaaaggacaagaggcctacagcaggaggaaagtgctggctggcattgtgatgac cgagaatatgaacttctgcgaggccaaggtgatcagcgtgtccaccggcaccaaatgcgtctccggcgaacacatgagcgtcaacggcgccgtg ctgaatgattcccacgccgagattgtctccagaaggtgcctcctcaagtacctctacgcccagctggacctgcagtgcaaccaagctaccgcct accagagcatcttcgtcagaaacaccgatggccagtacccctataagctgaagagcggagtgcacttccacctctatatcaataccgctccttg cggcgacgctaggatcttcagccctcacgagaacgacacaggcgtggacaagcatcccaacaggaaagccaggggccagctgaggaccaagatc gagagcggccagggaaccatccccgtgaagagcagcgatggcatccagacctgggatggagtcctccagggccagagactgctgaccatgtcct gtagcgacaagatcgccaggtggaatatcgtgggcattcaaggctccctcctgtccagcatcattgaacccgtgtacctgcactccatcgtgct gggctccctgctgcaccccgaacacatgtatagggctgtgtgcggcagaattgagaagagcatccagggcctccctcccccctaccacctcaac aaacccaggctggccctcgtcaccagcgccgagcccagaaaccaggccaaagcccccaacttcggcatcaactggaccatcggagataccgagctggaggtggtgaacagcctcaccggaaggaccattggcggccaggtgtccaggatcacaaagcaggccttcttcgtgaaatacggcttcctcatggccaacctgcctggcatcctggtgagaaaagtcaccacagattacggccagacaaaagccaacgtgaaggactaccagattgccaagctggaa ctgttcagcgctttcaagagagaagacctgggcagctggctgaagaaacccatcgaacaggatgagttcggactggctgagGGCGGAGGTGGTT CTGGCGGTGGAGGTTCAGGCGGTGGTGGAAGTtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaa tgcaatactgtctccgcgatcagaaagtggaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattct cgatttaggaagggaaattttggcactagagatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggagg accaaaacagagatcttaaacaaggagatgatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattt taatcgtactcctggaagtcgtcaagcctctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctctt cctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatcct tacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagttaactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatttgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggat tggctgcagcagctacattagcaggtccagcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagca gcaagctgcagctgcggcaaataacacagccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggt cagcgtcctcttactcccaatcagggtcagcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtc agggtcttgctactggcatgccaggctatcaagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaag gactggccttggagctccagttcggttaatggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctgga ggaactgcaagtagccttacaggcagcacaaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcacta atctgcaatctaattcattttatggaagcagttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaag tacatctcttggctttggaagtggtaactctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagt agtagtgccacaaggagagagtctctatctactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttaca atagtctgggattttcctcctctccaagtccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttc atcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatat cgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgcctt ctggccgcagtagattattggaagatttcagaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagcaaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaactatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgta ttcgtggtcatgttctacccttagccttgcagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtga aatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagcca cagtcactacagttcatcattgatgctttcaagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctag agcattgcactgcagaacagaccttacctatcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttat tcagcatgtactggaacacggtcgacctgaagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaattt gccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctc acagtgccttatacaccatgatgaaggaccagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataat catgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggaccaccaaatggaatgctg>SEQ_ID_NO:_31_hPUM2_GGGGS_dADARcd(E192Q)_AA MSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGD DDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQV PMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGP AVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGY QVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGS SSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPS PIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDF RNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLAL QMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLP ILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKD QYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLGGGGSGGGGSGGGGSYSPMVVPQKNV PLPIDDKSSSMELPQIHADTIGRLVLEKFMEVIKGQEAYSRRKVLAGIVMTENMNFCEAKVISVSTGTKCVSGEHMSVNGAVLNDSHAEIVSRRCLLKYLYAQLDLQCNQATAYQSIFVRNTDGQYPYKLKSGVHFHLYINTAPCGDARIFSPHENDTGVDKHPNRKARGQLRTKIESGQGTIPVKSSDGIQTWDGVLQGQRLLTMSCSDKIARWNIVGIQGSLLSSIIEPVYLHSIVLGSLLHPEHMYRAVCGRIEKSIQGLPPPYHLNKPRLALVTSAEP RNQAKAPNFGINWTIGDTELEVVNSLTGRTIGGQVSRITKQAFFVKYGFLMANLPGILVRKVTTDYGQTKANVKDYQIAKLELFSAFKREDLGS WLKKPIEQDEFGLAE >SEQ_ID_NO:_32_hPUM2_GGGGS_dADARcd(E192Q)_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagat gatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcct ctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgt tgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagttaactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatt tgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtcca gcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacag ccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtca gcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctat caagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaa tggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcac aaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagc agttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaact ctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagt ccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatt taggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatt tagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttcagaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagcaaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaa ctatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttg cagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgc tcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctg aagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttac tcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggac cagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggaccaccaaatggaatgctgGGCGGAGGTGGTTCTGGCGGTGGAGGTTCAGGCGGTGGTGGAAGTtattcccccatggtggtgccccagaagaacgtc cccctccccattgacgacaaaagcagcagcatggagctcccccagatccacgctgacacaattggcaggctggtgctggaaaaattcatggagg tgatcaaaggacaagaggcctacagcaggaggaaagtgctggctggcattgtgatgaccgagaatatgaacttctgcgaggccaaggtgatcag cgtgtccaccggcaccaaatgcgtctccggcgaacacatgagcgtcaacggcgccgtgctgaatgattcccacgccgagattgtctccagaagg tgcctcctcaagtacctctacgcccagctggacctgcagtgcaaccaagctaccgcctaccagagcatcttcgtcagaaacaccgatggccagt acccctataagctgaagagcggagtgcacttccacctctatatcaataccgctccttgcggcgacgctaggatcttcagccctcacgagaacga cacaggcgtggacaagcatcccaacaggaaagccaggggccagctgaggaccaagatcgagagcggccagggaaccatccccgtgaagagcagc gatggcatccagacctgggatggagtcctccagggccagagactgctgaccatgtcctgtagcgacaagatcgccaggtggaatatcgtgggca ttcaaggctccctcctgtccagcatcattgaacccgtgtacctgcactccatcgtgctgggctccctgctgcaccccgaacacatgtatagggc tgtgtgcggcagaattgagaagagcatccagggcctccctcccccctaccacctcaacaaacccaggctggccctcgtcaccagcgccgagccc agaaaccaggccaaagcccccaacttcggcatcaactggaccatcggagataccgagctggaggtggtgaacagcctcaccggaaggaccattg gcggccaggtgtccaggatcacaaagcaggccttcttcgtgaaatacggcttcctcatggccaacctgcctggcatcctggtgagaaaagtcac cacagattacggccagacaaaagccaacgtgaaggactaccagattgccaagctggaactgttcagcgctttcaagagagaagacctgggcagc tggctgaagaaacccatcgaacaggatgagttcggactggctgagtga >SEQ_ID_NO:_33_ hADAR2cd(E174Q)_GGGGS_hPUM2_AA MQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLY TQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSNASIQTW DGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAP NFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEK PTEQDQFSLTPGGGGSGGGGSGGGGSSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDG PEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNP ETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYI ISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLY KRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQL FPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKF FEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFV LSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAE RALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGML >SEQ_ID_NO:_34_hADAR2cd(E174Q)_GGGGS_hPUM2_DNA atgcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctc atgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtg cataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctac actcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacg ttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagaca tcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccaacgctagtattcaaacgtgggacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttc taatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcct aacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgt gtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatca tgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaag ccgaccgagcaggaccaattctctctgacgcccGGCGGAGGTGGTTCTGGCGGTGGAGGTTCAGGCGGTGGTGGAAGTtcccagcctattatgg tacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtggaggccttggtgtgagcat ggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactagagatgctgaaacagatgga cctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagatgatgatgattctaaaataa atggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagttga gcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagttaactgcagctcaacagca gcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatttgtgccaaatccatacatt attagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtccagcagtggttccacctcagt attacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacagccagtcagcaagcagcatc acaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaagcagaa tcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctatcaagtactagctccaactg cctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaatggctccaacacctgtttt aattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcacaaatggtctgtttcggcca attggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagcagttctttgactaatagct cccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaactctttgggtgctgctatagg ctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatctactagctctgacttgtac aaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagtccaataggcatgcctctgc caagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatgg tagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttcagaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagcaaaaactagagagagctac tccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaactatgttatacagaagttt tttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttgcagatgtatggctgccgcg ttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaagatca gaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgctttcaagggacaagtatttgtg ctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacctatcttagaagaactccacc aacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctgaagacaagagcaaaattgt ttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgctgag agagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggaccagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggaccaccaaatggaatgctg >SEQ_ID_NO:_35_hPUM2_GGGGS_hADAR2cd(E174Q)_AA MSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGD DDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQV PMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGP AVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGY QVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGS SSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPS PIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDF RNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLAL QMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLP ILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKD QYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLGGGGSGGGGSGGGGSQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYTQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSNASIQTWDGVLQGERLLTM SCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDSA IEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTP >SEQ_ID_NO:_36_hPUM2_GGGGS_hADAR2cd(E174Q)_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagat gatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggta ccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagt taactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatt tgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtcca gcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacag ccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtca gcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctat caagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaa tggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcac aaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagc agttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaact ctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagt ccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttc agaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagc aaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaa ctatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttg cagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgc tcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctg aagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttac tcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggac cagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggaccaccaaatggaatgctgGGCGGAGGTGGTTCTGGCGGTGGAGGTTCAGGCGGTGGTGGAAGTcagctgcacctgccccaggttctcgcagacgcc gtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctcatgcgaggcggaaagtactcgcaggcgtcgtcatga cgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatgagcgaccgggggctggc actgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctacactcaactcgaattgtaccttaacaacaaagatgac cagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacgttcagttccacttgtatatcagcacatccccttgcg gtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagacatcctaataggaaggctagaggccaacttcggacgaa gattgaaagtggccagggtactatcccggtgcggtccaacgctagtattcaaacgtgggacggagtccttcaaggtgaacggctgttgacaatg agctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatccatta ttttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaa taagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcctaacttcagtgttaactggaccgttggtgattctgcg atagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgtgtaaacacgcgttgtattgtagatggatgagagtac atgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatcatgagtcaaaactcgcggctaaagaataccaggcagc caaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaagccgaccgagcaggaccaattctctctgacgccc>SEQ_ID_NO:_37_hADAR2cd(E174Q / N182F)_GGGGS _hPUM2_AAMQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLY TQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSFASIQTW DGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAP NFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEK PTEQDQFSLTPGGGGSGGGGSGGGGSSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDG PEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNP ETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYI ISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAE SLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQL FPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKF FEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFV LSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAE RALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGML >SEQ_ID_NO:_38_hADAR2cd(E174Q / N182F)_GGGGS_hPUM2_DNA atgcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctc atgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtg cataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctac actcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacg ttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagaca tcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccTTCgctagtattcaaacgtgg gacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcct aacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgt gtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatca tgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaag ccgaccgagcaggaccaattctctctgacgcccGGCGGAGGTGGTTCTGGCGGTGGAGGTTCAGGCGGTGGTGGAAGTtcccagcctattatgg tacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtggaggccttggtgtgagcat ggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactagagatgctgaaacagatgga cctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagatgatgatgattctaaaataa atggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggag ctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagttaactgcagctcaacagca gcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatttgtgccaaatccatacatt attagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtccagcagtggttccacctcagt attacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacagccagtcagcaagcagcatc acaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaagcagaa tcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctatcaagtactagctccaactg cctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaatggctccaacacctgtttt aattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcacaaatggtctgtttcggcca attggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagcagttctttgactaatagct cccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaactctttgggtgctgctatagg ctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatctactagctctgacttgtac aaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagtccaataggcatgcctctgc caagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttcagaaacaaccgcttcccaa accttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagcaaaaactagagagagctac tccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaactatgttatacagaagttt tttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttgcagatgtatggctgccgcg ttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaagatca gaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgctttcaagggacaagtatttgtg ctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacctatcttagaagaactccacc aacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctgaagacaagagcaaaattgt ttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgctgag agagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggaccagtatgccaattacgtgg ttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggaccaccaaatggaatgctg>SEQ_ID_NO:_39_hPUM2_GGGGS_hADAR2cd(E174Q / N182F)_AA MSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGD DDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQV PMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGP AVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGY QVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGS SSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPS PIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDF RNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLAL QMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLP ILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKD QYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLGGGGSGGGGSGGGGSQLHLPQVLADA VSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYTQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSFASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDSA IEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTP >SEQ_ID_NO:_40_hPUM2_GGGGS_hADAR2cd(E174Q / N182F)_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagat gatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcct ctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagt taactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatt tgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtcca gcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacag ccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtca gcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctat caagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaa tggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcac aaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagc agttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaact ctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagt ccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatt taggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttcagaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagc aaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaa ctatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttg cagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgc tcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctg aagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttac tcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggaccagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggacc accaaatggaatgctgGGCGGAGGTGGTTCTGGCGGTGGAGGTTCAGGCGGTGGTGGAAGTcagctgcacctgccccaggttctcgcagacgcc gtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctcatgcgaggcggaaagtactcgcaggcgtcgtcatga cgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatgagcgaccgggggctggc actgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctacactcaactcgaattgtaccttaacaacaaagatgac cagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacgttcagttccacttgtatatcagcacatccccttgcg gtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagacatcctaataggaaggctagaggccaacttcggacgaa gattgaaagtggccagggtactatcccggtgcggtccTTCgctagtattcaaacgtgggacggagtccttcaaggtgaacggctgttgacaatg agctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatccatta ttttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaa taagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcctaacttcagtgttaactggaccgttggtgattctgcg atagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgtgtaaacacgcgttgtattgtagatggatgagagtac atgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatcatgagtcaaaactcgcggctaaagaataccaggcagc caaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaagccgaccgagcaggaccaattctctctgacgccc >SEQ_ID_NO:_41_dADARcd(E192Q)_XTEN_hPUM2_AA MYSPMVVPQKNVPLPIDDKSSSMELPQIHADTIGRLVLEKFMEVIKGQEAYSRRKVLAGIVMTENMNFCEAKVISVSTGTKCVSGEHMSVNGAV LNDSHAEIVSRRCLLKYLYAQLDLQCNQATAYQSIFVRNTDGQYPYKLKSGVHFHLYINTAPCGDARIFSPHENDTGVDKHPNRKARGQLRTKI ESGQGTIPVKSSDGIQTWDGVLQGQRLLTMSCSDKIARWNIVGIQGSLLSSIIEPVYLHSIVLGSLLHPEHMYRAVCGRIEKSIQGLPPPYHLN KPRLALVTSAEPRNQAKAPNFGINWTIGDTELEVVNSLTGRTIGGQVSRITKQAFFVKYGFLMANLPGILVRKVTTDYGQTKANVKDYQIAKLE LFSAFKREDLGSWLKKPIEQDEFGLAESGSETPGTSESATPESSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLD SRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGP LPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAG VFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGA GQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAA GGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQA AYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQ PQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHK FASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLK NSPDLGPIGGPPNGML >SEQ_ID_NO:_42_dADARcd(E192Q)_XTEN_hPUM2_DNA atgtattcccccatggtggtgccccagaagaacgtccccctccccattgacgacaaaagcagcagcatggagctcccccagatccacgctgaca caattggcaggctggtgctggaaaaattcatggaggtgatcaaaggacaagaggcctacagcaggaggaaagtgctggctggcattgtgatgac cgagaatatgaacttctgcgaggccaaggtgatcagcgtgtccaccggcaccaaatgcgtctccggcgaacacatgagcgtcaacggcgccgtg ctgaatgattcccacgccgagattgtctccagaaggtgcctcctcaagtacctctacgcccagctggacctgcagtgcaaccaagctaccgcct accagagcatcttcgtcagaaacaccgatggccagtacccctataagctgaagagcggagtgcacttccacctctatatcaataccgctccttg cggcgacgctaggatcttcagccctcacgagaacgacacaggcgtggacaagcatcccaacaggaaagccaggggccagctgaggaccaagatc gagagcggccagggaaccatccccgtgaagagcagcgatggcatccagacctgggatggagtcctccagggccagagactgctgaccatgtcctgtagcgacaagatcgccaggtggaatatcgtgggcattcaaggctccctcctgtccagcatcattgaacccgtgtacctgcactccatcgtgctgggctccctgctgcaccccgaacacatgtatagggctgtgtgcggcagaattgagaagagcatccagggcctccctcccccctaccacctcaac aaacccaggctggccctcgtcaccagcgccgagcccagaaaccaggccaaagcccccaacttcggcatcaactggaccatcggagataccgagc tggaggtggtgaacagcctcaccggaaggaccattggcggccaggtgtccaggatcacaaagcaggccttcttcgtgaaatacggcttcctcat ggccaacctgcctggcatcctggtgagaaaagtcaccacagattacggccagacaaaagccaacgtgaaggactaccagattgccaagctggaa ctgttcagcgctttcaagagagaagacctgggcagctggctgaagaaacccatcgaacaggatgagttcggactggctgagagcggcagcgaga ctcccgggacctcagagtccgccacacccgaaagttcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagt aaatgcaatactgtctccgcgatcagaaagtggaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggat tctcgatttaggaagggaaattttggcactagagatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgagg aggaccaaaacagagatcttaaacaaggagatgatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaat ccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctt tcagaggactaatgcactaacagttcaacagttaactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggt gtattctcagcaggccttgctccagctgcatttgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcag gattggctgcagcagctacattagcaggtccagcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttca gcagcaagctgcagctgcggcaaataacacagccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagca ggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttg gtcagggtcttgctactggcatgccaggctatcaagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagc aaggactggccttggagctccagttcggttaatggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagct ggaggaactgcaagtagccttacaggcagcacaaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagca ctaatctgcaatctaattcattttatggaagcagttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctgg aagtacatctcttggctttggaagtggtaactctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgca agtagtagtgccacaaggagagagtctctatctactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccatttt acaatagtctgggattttcctcctctccaagtccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgc cttctggccgcagtagattattggaagatttcagaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttc tcaagaccagcatggttctagattcatacagcaaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagca gcctatcaattaatgactgatgtttttggcaactatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactc gtattcgtggtcatgttctacccttagccttgcagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagag tgaaatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcag ccacagtcactacagttcatcattgatgctttcaagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcc tagagcattgcactgcagaacagaccttacctatcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgt tattcagcatgtactggaacacggtcgacctgaagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggaccagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagat aatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaag aatagcccggacctaggacctattggaggaccaccaaatggaatgctg >SEQ_ID_NO:_43_hPUM2_XTEN_dADARcd(E192Q)_AA MSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGD DDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQV PMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGP AVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGY QVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGS SSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPS PIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDF RNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLAL QMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLSGSETPGTSESATPESYSPMVVPQKN VPLPIDDKSSSMELPQIHADTIGRLVLEKFMEVIKGQEAYSRRKVLAGIVMTENMNFCEAKVISVSTGTKCVSGEHMSVNGAVLNDSHAEIVSR RCLLKYLYAQLDLQCNQATAYQSIFVRNTDGQYPYKLKSGVHFHLYINTAPCGDARIFSPHENDTGVDKHPNRKARGQLRTKIESGQGTIPVKS SDGIQTWDGVLQGQRLLTMSCSDKIARWNIVGIQGSLLSSIIEPVYLHSIVLGSLLHPEHMYRAVCGRIEKSIQGLPPPYHLNKPRLALVTSAE PRNQAKAPNFGINWTIGDTELEVVNSLTGRTIGGQVSRITKQAFFVKYGFLMANLPGILVRKVTTDYGQTKANVKDYQIAKLELFSAFKREDLG SWLKKPIEQDEFGLAE >SEQ_ID_NO:_44_hPUM2_XTEN_dADARcd(E192Q)_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagatgatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgt tgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggta ccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagt taactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatt tgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtcca gcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacag ccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtca gcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctat caagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaa tggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcac aaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagc agttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaact ctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagtccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatt tagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttc agaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagc aaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaa ctatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttg cagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgc tcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctgaagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggac cagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattacta ctttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggacc accaaatggaatgctgagcggcagcgagactcccgggacctcagagtccgccacacccgaaagttattcccccatggtggtgccccagaagaac gtccccctccccattgacgacaaaagcagcagcatggagctcccccagatccacgctgacacaattggcaggctggtgctggaaaaattcatgg aggtgatcaaaggacaagaggcctacagcaggaggaaagtgctggctggcattgtgatgaccgagaatatgaacttctgcgaggccaaggtgat cagcgtgtccaccggcaccaaatgcgtctccggcgaacacatgagcgtcaacggcgccgtgctgaatgattcccacgccgagattgtctccaga aggtgcctcctcaagtacctctacgcccagctggacctgcagtgcaaccaagctaccgcctaccagagcatcttcgtcagaaacaccgatggcc agtacccctataagctgaagagcggagtgcacttccacctctatatcaataccgctccttgcggcgacgctaggatcttcagccctcacgagaa cgacacaggcgtggacaagcatcccaacaggaaagccaggggccagctgaggaccaagatcgagagcggccagggaaccatccccgtgaagagc agcgatggcatccagacctgggatggagtcctccagggccagagactgctgaccatgtcctgtagcgacaagatcgccaggtggaatatcgtgg gcattcaaggctccctcctgtccagcatcattgaacccgtgtacctgcactccatcgtgctgggctccctgctgcaccccgaacacatgtatag ggctgtgtgcggcagaattgagaagagcatccagggcctccctcccccctaccacctcaacaaacccaggctggccctcgtcaccagcgccgag cccagaaaccaggccaaagcccccaacttcggcatcaactggaccatcggagataccgagctggaggtggtgaacagcctcaccggaaggaccattggcggccaggtgtccaggatcacaaagcaggccttcttcgtgaaatacggcttcctcatggccaacctgcctggcatcctggtgagaaaagtcaccacagattacggccagacaaaagccaacgtgaaggactaccagattgccaagctggaactgttcagcgctttcaagagagaagacctgggc agctggctgaagaaacccatcgaacaggatgagttcggactggctgag >SEQ_ID_NO:_45_dADARcd(E192Q)_32aa-linker_hPUM2_AA MYSPMVVPQKNVPLPIDDKSSSMELPQIHADTIGRLVLEKFMEVIKGQEAYSRRKVLAGIVMTENMNFCEAKVISVSTGTKCVSGEHMSVNGAV LNDSHAEIVSRRCLLKYLYAQLDLQCNQATAYQSIFVRNTDGQYPYKLKSGVHFHLYINTAPCGDARIFSPHENDTGVDKHPNRKARGQLRTKI ESGQGTIPVKSSDGIQTWDGVLQGQRLLTMSCSDKIARWNIVGIQGSLLSSIIEPVYLHSIVLGSLLHPEHMYRAVCGRIEKSIQGLPPPYHLN KPRLALVTSAEPRNQAKAPNFGINWTIGDTELEVVNSLTGRTIGGQVSRITKQAFFVKYGFLMANLPGILVRKVTTDYGQTKANVKDYQIAKLE LFSAFKREDLGSWLKKPIEQDEFGLAESGGSSGGSSGSETPGTSESATPESSGGSSGGSSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQ QQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQA ASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTP VLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAA IGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLT NGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLER ATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVK DQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSK IVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKY TYGKHILAKLEKYYLKNSPDLGPIGGPPNGML >SEQ_ID_NO:_46_dADARcd(E192Q)_32aa-linker_hPUM2_DNA atgtattcccccatggtggtgccccagaagaacgtccccctccccattgacgacaaaagcagcagcatggagctcccccagatccacgctgaca caattggcaggctggtgctggaaaaattcatggaggtgatcaaaggacaagaggcctacagcaggaggaaagtgctggctggcattgtgatgaccgagaatatgaacttctgcgaggccaaggtgatcagcgtgtccaccggcaccaaatgcgtctccggcgaacacatgagcgtcaacggcgccgtgctgaatgattcccacgccgagattgtctccagaaggtgcctcctcaagtacctctacgcccagctggacctgcagtgcaaccaagctaccgcct accagagcatcttcgtcagaaacaccgatggccagtacccctataagctgaagagcggagtgcacttccacctctatatcaataccgctccttg cggcgacgctaggatcttcagccctcacgagaacgacacaggcgtggacaagcatcccaacaggaaagccaggggccagctgaggaccaagatc gagagcggccagggaaccatccccgtgaagagcagcgatggcatccagacctgggatggagtcctccagggccagagactgctgaccatgtcct gtagcgacaagatcgccaggtggaatatcgtgggcattcaaggctccctcctgtccagcatcattgaacccgtgtacctgcactccatcgtgct gggctccctgctgcaccccgaacacatgtatagggctgtgtgcggcagaattgagaagagcatccagggcctccctcccccctaccacctcaac aaacccaggctggccctcgtcaccagcgccgagcccagaaaccaggccaaagcccccaacttcggcatcaactggaccatcggagataccgagc tggaggtggtgaacagcctcaccggaaggaccattggcggccaggtgtccaggatcacaaagcaggccttcttcgtgaaatacggcttcctcat ggccaacctgcctggcatcctggtgagaaaagtcaccacagattacggccagacaaaagccaacgtgaaggactaccagattgccaagctggaa ctgttcagcgctttcaagagagaagacctgggcagctggctgaagaaacccatcgaacaggatgagttcggactggctgagtctggtggttctt ctggtggttctagcggcagcgagactcccgggacctcagagtccgccacacccgaaagttctggtggttcttctggtggttcttcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtggaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactagagatgctgaaacag atggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagatgatgatgattctaa aataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagta gttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaa atcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggtaccaatggactcttc aggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagttaactgcagctcaa cagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatttgtgccaaatccat acattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtccagcagtggttccacc tcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacagccagtcagcaagca gcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaag cagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctatcaagtactagctcc aactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaatggctccaacacct gttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcacaaatggtctgtttc ggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagcagttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaactctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatctactagctctgact tgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagtccaataggcatgcc tctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgaca aatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagcc agctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttcagaaacaaccgctt cccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagcaaaaactagagaga gctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaactatgttatacaga agttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttgcagatgtatggctg ccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgctttcaagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacctatcttagaagaact ccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctgaagacaagagcaaa attgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtg ctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggaccagtatgccaatta cgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattactactttgcgcaaatac acatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggaccaccaaatggaatgc tg >SEQ_ID_NO:_47_hPUM2_32aa-linker_dADARcd(E192Q)_AA MSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGD DDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQV PMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGP AVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGY QVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDF RNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLAL QMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLP ILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKD QYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLSGGSSGGSSGSETPGTSESATPESSG GSSGGSYSPMVVPQKNVPLPIDDKSSSMELPQIHADTIGRLVLEKFMEVIKGQEAYSRRKVLAGIVMTENMNFCEAKVISVSTGTKCVSGEHMS VNGAVLNDSHAEIVSRRCLLKYLYAQLDLQCNQATAYQSIFVRNTDGQYPYKLKSGVHFHLYINTAPCGDARIFSPHENDTGVDKHPNRKARGQ LRTKIESGQGTIPVKSSDGIQTWDGVLQGQRLLTMSCSDKIARWNIVGIQGSLLSSIIEPVYLHSIVLGSLLHPEHMYRAVCGRIEKSIQGLPP PYHLNKPRLALVTSAEPRNQAKAPNFGINWTIGDTELEVVNSLTGRTIGGQVSRITKQAFFVKYGFLMANLPGILVRKVTTDYGQTKANVKDYQIAKLELFSAFKREDLGSWLKKPIEQDEFGLAE>SEQ_ID_NO:_48_hPUM2_32aa-linker_dADARcd(E192Q)_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagat gatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcct ctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgt tgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggta ccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagt taactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatt tgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtcca gcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacag ccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtca gcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctatcaagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaatggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcac aaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagc agttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaact ctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagt ccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatt taggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatt tagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttc agaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagc aaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaa ctatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttgcagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctg aagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttac tcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggac cagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattacta ctttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggacc accaaatggaatgctgtctggtggttcttctggtggttctagcggcagcgagactcccgggacctcagagtccgccacacccgaaagttctggt ggttcttctggtggttcttattcccccatggtggtgccccagaagaacgtccccctccccattgacgacaaaagcagcagcatggagctccccc agatccacgctgacacaattggcaggctggtgctggaaaaattcatggaggtgatcaaaggacaagaggcctacagcaggaggaaagtgctggc tggcattgtgatgaccgagaatatgaacttctgcgaggccaaggtgatcagcgtgtccaccggcaccaaatgcgtctccggcgaacacatgagc gtcaacggcgccgtgctgaatgattcccacgccgagattgtctccagaaggtgcctcctcaagtacctctacgcccagctggacctgcagtgca accaagctaccgcctaccagagcatcttcgtcagaaacaccgatggccagtacccctataagctgaagagcggagtgcacttccacctctatat caataccgctccttgcggcgacgctaggatcttcagccctcacgagaacgacacaggcgtggacaagcatcccaacaggaaagccaggggccagctgaggaccaagatcgagagcggccagggaaccatccccgtgaagagcagcgatggcatccagacctgggatggagtcctccagggccagagactgctgaccatgtcctgtagcgacaagatcgccaggtggaatatcgtgggcattcaaggctccctcctgtccagcatcattgaacccgtgtacct gcactccatcgtgctgggctccctgctgcaccccgaacacatgtatagggctgtgtgcggcagaattgagaagagcatccagggcctccctccc ccctaccacctcaacaaacccaggctggccctcgtcaccagcgccgagcccagaaaccaggccaaagcccccaacttcggcatcaactggacca tcggagataccgagctggaggtggtgaacagcctcaccggaaggaccattggcggccaggtgtccaggatcacaaagcaggccttcttcgtgaa atacggcttcctcatggccaacctgcctggcatcctggtgagaaaagtcaccacagattacggccagacaaaagccaacgtgaaggactaccag attgccaagctggaactgttcagcgctttcaagagagaagacctgggcagctggctgaagaaacccatcgaacaggatgagttcggactggctg ag >SEQ_ID_NO:_49_FRB_linker_NtermADAR2_T2A_CtermADAR2(E174Q)_linker_FKBP12_GGGGS_hPUM2_AAMILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKGGSGSGAGSGSPAGGGAPGSGGGSQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSD RGLALNDCHAEIISRRSLLRFLYTQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPAGSGEGRGSLLT CGDVEENPGPDRHPNRKARGQLRTKIESGQGTIPVRSNASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYH GDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSH LLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTPGGSGSGAGSGSPAGGGAPGSGGGSGVQVETISPGDGRTF PKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLEGG GGSGGGGSGGGGSSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPF EEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGL ESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTA AGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLA FGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQP STNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQP FYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDI MPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQND GPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGML >SEQ_ID_NO:_50_FRB_linker_NtermADAR2_T2A_CtermADAR2(E174Q)_linker_FKBP12_GGGGS_hPUM2_AA ATGATTTTATGGCATGAGATGTGGCATGAGGGTTTGGAAGAGGCATCTAGATTGTATTTCGGTGAAAGAAATGTCAAGGGAATGTTCGAAGTTT TAGAACCGTTGCACGCTATGATGGAGAGAGGTCCACAGACTCTAAAGGAGACTTCCTTCAACCAAGCTTATGGAAGGGACCTAATGGAGGCTCA AGAATGGTGTAGAAAATACATGAAAAGTGGAAATGTAAAGGACCTTACACAAGCTTGGGATCTCTACTACCATGTTTTTAGGAGAATATCTAAA gggggcagtgggagcggtgcaggatctggtagtccagctgggggaggagcaccgggtagcggtggggggagccagctgcacctgccccaggttc tcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctcatgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctacactcaactcgaattgtaccttaaca acaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacgttcagttccacttgtatatcagcac atccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcgGGAAGTGGTGAGGGTAGGGGAAGTTTATTAACC TGTGGGGATGTTGAAGAAAATCCAGGTCCTgacagacatcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggta ctatcccggtgcggtccaacgctagtattcaaacgtgggacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgc gcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcat ggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaataagcctctcttgtccggga tatcaaacgctgaggcccgccagccagggaaagctcctaacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccac gacaggtaaggatgagctcggtagagcctcacgcctgtgtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcac ttgctccgaagcaagatcactaagcctaatgtgtatcatgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacag cttttattaaggcagggctcggggcatgggtcgagaagccgaccgagcaggaccaattctctctgacgcccgggggcagtgggagcggtgcagg atctggtagtccagctgggggaggagcaccgggtagcggtggggggagcGGCGTACAAGTTGAAACTATCAGCCCTGGGGACGGCAGAACCTTT CCGAAGAGGGGACAGACATGTGTTGTTCACTATACTGGAATGTTGGAAGATGGTAAGAAGTTCGATAGCAGCAGAGATAGGAATAAACCATTTA AATTCATGCTTGGCAAGCAAGAAGTGATTAGGGGTTGGGAAGAAGGTGTCGCTCAAATGAGTGTAGGTCAGAGGGCTAAGTTAACAATTAGTCCTGATTATGCTTATGGCGCTACAGGTCATCCAGGAATCATTCCCCCACATGCTACTCTTGTTTTCGACGTTGAATTGCTTAAGCTTGAAGGCGGAGGTGGTTCTGGCGGTGGAGGTTCAGGCGGTGGTGGAAGTtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtg aagtaaatgcaatactgtctccgcgatcagaaagtggaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaatt ggattctcgatttaggaagggaaattttggcactagagatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccattt gaggaggaccaaaacagagatcttaaacaaggagatgatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgca aagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggg gcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctg gaatccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagc tctttcagaggactaatgcactaacagttcaacagttaactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagc tggtgtattctcagcaggccttgctccagctgcatttgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgca gcaggattggctgcagcagctacattagcaggtccagcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttat ttcagcagcaagctgcagctgcggcaaataacacagccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctatcaagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctg gagcaaggactggccttggagctccagttcggttaatggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagc agctggaggaactgcaagtagccttacaggcagcacaaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagcca agcactaatctgcaatctaattcattttatggaagcagttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaac ctggaagtacatctcttggctttggaagtggtaactctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttc tgcaagtagtagtgccacaaggagagagtctctatctactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaacca ttttacaatagtctgggattttcctcctctccaagtccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccat cactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagc aaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatatt atgccttctggccgcagtagattattggaagatttcagaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagt tttctcaagaccagcatggttctagattcatacagcaaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgca agcagcctatcaattaatgactgatgtttttggcaactatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggct actcgtattcgtggtcatgttctacccttagccttgcagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagc agagtgaaatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgctttcaagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacctatcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaatt atgttattcagcatgtactggaacacggtcgacctgaagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaaca caaatttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgat ggtcctcacagtgccttatacaccatgatgaaggaccagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaa agataatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattattt gaagaatagcccggacctaggacctattggaggaccaccaaatggaatgctg >SEQ_ID_NO:51_hPUM2_GGGGS_FKBP12_linker_NtermADAR2_T2A_CtermADAR2(E174Q) _linker_FRB_AA MSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGP AVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGY QVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGS SSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPS PIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDF RNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLAL QMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLP ILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKD QYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLGGGGSGGGGSGGGGSGVQVETISPGD GRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLK LEGGSGSGAGSGSPAGGGAPGSGGGSQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYM SDRGLALNDCHAEIISRRSLLRFLYTQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPAGSGEGRGSL LTCGDVEENPGPDRHPNRKARGQLRTKIESGQGTIPVRSNASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSL YHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTPGGSGSGAGSGSPAGGGAPGSGGGSILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISK >SEQ_ID_NO:_52_hPUM2_GGGGS_FKBP12_linker_NtermADAR2_T2A_CtermADAR2(E174Q)_linker_FRB_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagat gatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcct ctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgt tgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagttaactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatt tgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtcca gcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacag ccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtca gcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctat caagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaa tggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcac aaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagc agttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaact ctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagt ccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatt taggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatt tagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttcagaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagcaaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaa ctatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttg cagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgc tcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctg aagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttac tcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggac cagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattacta ctttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggacc accaaatggaatgctgGGCGGAGGTGGTTCTGGCGGTGGAGGTTCAGGCGGTGGTGGAAGTGGCGTACAAGTTGAAACTATCAGCCCTGGGGACGGCAGAACCTTTCCGAAGAGGGGACAGACATGTGTTGTTCACTATACTGGAATGTTGGAAGATGGTAAGAAGTTCGATAGCAGCAGAGATAGGAATAAACCATTTAAATTCATGCTTGGCAAGCAAGAAGTGATTAGGGGTTGGGAAGAAGGTGTCGCTCAAATGAGTGTAGGTCAGAGGGCTAAGTT AACAATTAGTCCTGATTATGCTTATGGCGCTACAGGTCATCCAGGAATCATTCCCCCACATGCTACTCTTGTTTTCGACGTTGAATTGCTTAAG CTTGAAgggggcagtgggagcggtgcaggatctggtagtccagctgggggaggagcaccgggtagcggtggggggagccagctgcacctgcccc aggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctcatgcgaggcggaaagtact cgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatg agcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctacactcaactcgaattgtacc ttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacgttcagttccacttgtatat cagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcgGGAAGTGGTGAGGGTAGGGGAAGTTTA TTAACCTGTGGGGATGTTGAAGAAAATCCAGGTCCTgacagacatcctaataggaaggctagaggccaacttcggacgaagattgaaagtggcc agggtactatcccggtgcggtccaacgctagtattcaaacgtgggacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaa aatcgcgcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatccattattttgggctctctg tatcatggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaataagcctctcttgt ccgggatatcaaacgctgaggcccgccagccagggaaagctcctaacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaa cgccacgacaggtaaggatgagctcggtagagcctcacgcctgtgtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatcatgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaagccgaccgagcaggaccaattctctctgacgcccgggggcagtgggagcgg tgcaggatctggtagtccagctgggggaggagcaccgggtagcggtggggggagcATTTTATGGCATGAGATGTGGCATGAGGGTTTGGAAGAG GCATCTAGATTGTATTTCGGTGAAAGAAATGTCAAGGGAATGTTCGAAGTTTTAGAACCGTTGCACGCTATGATGGAGAGAGGTCCACAGACTC TAAAGGAGACTTCCTTCAACCAAGCTTATGGAAGGGACCTAATGGAGGCTCAAGAATGGTGTAGAAAATACATGAAAAGTGGAAATGTAAAGGA CCTTACACAAGCTTGGGATCTCTACTACCATGTTTTTAGGAGAATATCTAAA >SEQ_ID_NO:_53_FRB_linker_NtermADAR2_T2A_FKBP12_linker_CtermADAR2(E174Q)_GGGGS_hPUM2_AA MILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISK GGSGSGAGSGSPAGGGAPGSGGGSQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYTQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPAGSGEGRGSLLTCGDVEENPGPGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGA TGHPGIIPPHATLVFDVELLKLEGGSGSGAGSGSPAGGGAPGSGGGSDRHPNRKARGQLRTKIESGQGTIPVRSNASIQTWDGVLQGERLLTMS CSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDSAI EVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTPGG GGSGGGGSGGGGSSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPF EEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGL ESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTA AGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLA FGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQP STNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQP FYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDI MPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALA TRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQR ILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGML>SEQ_ID_NO:_54_FRB_linker_NtermADAR2_T2A_FKBP12_linker_CtermADAR2(E174Q)_GGGGS_hPUM2_DNA ATGATTTTATGGCATGAGATGTGGCATGAGGGTTTGGAAGAGGCATCTAGATTGTATTTCGGTGAAAGAAATGTCAAGGGAATGTTCGAAGTTT TAGAACCGTTGCACGCTATGATGGAGAGAGGTCCACAGACTCTAAAGGAGACTTCCTTCAACCAAGCTTATGGAAGGGACCTAATGGAGGCTCA AGAATGGTGTAGAAAATACATGAAAAGTGGAAATGTAAAGGACCTTACACAAGCTTGGGATCTCTACTACCATGTTTTTAGGAGAATATCTAAA gggggcagtgggagcggtgcaggatctggtagtccagctgggggaggagcaccgggtagcggtggggggagccagctgcacctgccccaggttc tcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctcatgcgaggcggaaagtactcgcagg cgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatgagcgac cgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctacactcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacgttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcgGGAAGTGGTGAGGGTAGGGGAAGTTTATTAACC TGTGGGGATGTTGAAGAAAATCCAGGTCCTGGCGTACAAGTTGAAACTATCAGCCCTGGGGACGGCAGAACCTTTCCGAAGAGGGGACAGACAT GTGTTGTTCACTATACTGGAATGTTGGAAGATGGTAAGAAGTTCGATAGCAGCAGAGATAGGAATAAACCATTTAAATTCATGCTTGGCAAGCA AGAAGTGATTAGGGGTTGGGAAGAAGGTGTCGCTCAAATGAGTGTAGGTCAGAGGGCTAAGTTAACAATTAGTCCTGATTATGCTTATGGCGCT ACAGGTCATCCAGGAATCATTCCCCCACATGCTACTCTTGTTTTCGACGTTGAATTGCTTAAGCTTGAAgggggcagtgggagcggtgcaggat ctggtagtccagctgggggaggagcaccgggtagcggtggggggagcgacagacatcctaataggaaggctagaggccaacttcggacgaagat tgaaagtggccagggtactatcccggtgcggtccaacgctagtattcaaacgtgggacggagtccttcaaggtgaacggctgttgacaatgagc tgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatccattattt tgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaataa gcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcctaacttcagtgttaactggaccgttggtgattctgcgata gaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgtgtaaacacgcgttgtattgtagatggatgagagtacatg ggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatcatgagtcaaaactcgcggctaaagaataccaggcagccaa agctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaagccgaccgagcaggaccaattctctctgacgcccGGCGGA GGTGGTTCTGGCGGTGGAGGTTCAGGCGGTGGTGGAAGTtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtggaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactagagatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccattt gaggaggaccaaaacagagatcttaaacaaggagatgatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgca aagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggg gcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctg gaatccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagc tctttcagaggactaatgcactaacagttcaacagttaactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagc tggtgtattctcagcaggccttgctccagctgcatttgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgca gcaggattggctgcagcagctacattagcaggtccagcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttat ttcagcagcaagctgcagctgcggcaaataacacagccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctgg agcaggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggct tttggtcagggtcttgctactggcatgccaggctatcaagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaatggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcacaaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagcca agcactaatctgcaatctaattcattttatggaagcagttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaac ctggaagtacatctcttggctttggaagtggtaactctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttc tgcaagtagtagtgccacaaggagagagtctctatctactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaacca ttttacaatagtctgggattttcctcctctccaagtccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccat cactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagc aaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatatt atgccttctggccgcagtagattattggaagatttcagaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagt tttctcaagaccagcatggttctagattcatacagcaaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgca agcagcctatcaattaatgactgatgtttttggcaactatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggct actcgtattcgtggtcatgttctacccttagccttgcagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagc agagtgaaatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgt tcagccacagtcactacagttcatcattgatgctttcaagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgc atcctagagcattgcactgcagaacagaccttacctatcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctgaagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgat ggtcctcacagtgccttatacaccatgatgaaggaccagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaa agataatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattattt gaagaatagcccggacctaggacctattggaggaccaccaaatggaatgctg >SEQ_ID_NO:_55_hPUM2_GGGGS_NtermADAR2_linker_FKBP12_T2A_CtermADAR2(E174Q)_linker_FRB_AA MSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGD DDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQV PMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGS SSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPS PIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDF RNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLAL QMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLP ILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKD QYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLGGGGSGGGGSGGGGSQLHLPQVLADA VSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYTQLELYLNNKDD QKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPAGGSGSGAGSGSPAGGGAPGSGGGSGVQVETISPGDGRTFPKRGQTC VVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLEGSGEGRGSL LTCGDVEENPGPDRHPNRKARGQLRTKIESGQGTIPVRSNASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSL YHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVP SHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTPGGSGSGAGSGSPAGGGAPGSGGGSILWHEMWHEGLEE ASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISK >SEQ_ID_NO:_56_hPUM2_GGGGS_NtermADAR2_linker_FKBP12_T2A_CtermADAR2(E174Q)_linker_FRB_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagat gatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcct ctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgt tgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggta ccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagt taactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatttgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtccagcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacag ccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtca gcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctat caagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaa tggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcac aaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagc agttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaact ctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagt ccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatt taggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatt tagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttc agaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagc aaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaactatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttgcagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgc tcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctg aagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttac tcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggac cagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattacta ctttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggacc accaaatggaatgctgGGCGGAGGTGGTTCTGGCGGTGGAGGTTCAGGCGGTGGTGGAAGTcagctgcacctgccccaggttctcgcagacgcc gtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctcatgcgaggcggaaagtactcgcaggcgtcgtcatga cgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatgagcgaccgggggctggc actgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctacactcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacgttcagttccacttgtatatcagcacatccccttgcg gtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggggggcagtgggagcggtgcaggatctggtagtccagctggggg aggagcaccgggtagcggtggggggagcGGCGTACAAGTTGAAACTATCAGCCCTGGGGACGGCAGAACCTTTCCGAAGAGGGGACAGACATGT GTTGTTCACTATACTGGAATGTTGGAAGATGGTAAGAAGTTCGATAGCAGCAGAGATAGGAATAAACCATTTAAATTCATGCTTGGCAAGCAAG AAGTGATTAGGGGTTGGGAAGAAGGTGTCGCTCAAATGAGTGTAGGTCAGAGGGCTAAGTTAACAATTAGTCCTGATTATGCTTATGGCGCTAC AGGTCATCCAGGAATCATTCCCCCACATGCTACTCTTGTTTTCGACGTTGAATTGCTTAAGCTTGAAGGAAGTGGTGAGGGTAGGGGAAGTTTA TTAACCTGTGGGGATGTTGAAGAAAATCCAGGTCCTgacagacatcctaataggaaggctagaggccaacttcggacgaagattgaaagtggcc agggtactatcccggtgcggtccaacgctagtattcaaacgtgggacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaa aatcgcgcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatccattattttgggctctctg tatcatggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaataagcctctcttgt ccgggatatcaaacgctgaggcccgccagccagggaaagctcctaacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaa cgccacgacaggtaaggatgagctcggtagagcctcacgcctgtgtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtccca tctcacttgctccgaagcaagatcactaagcctaatgtgtatcatgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgacttt ttacagcttttattaaggcagggctcggggcatgggtcgagaagccgaccgagcaggaccaattctctctgacgcccgggggcagtgggagcgg tgcaggatctggtagtccagctgggggaggagcaccgggtagcggtggggggagcATTTTATGGCATGAGATGTGGCATGAGGGTTTGGAAGAGGCATCTAGATTGTATTTCGGTGAAAGAAATGTCAAGGGAATGTTCGAAGTTTTAGAACCGTTGCACGCTATGATGGAGAGAGGTCCACAGACTC TAAAGGAGACTTCCTTCAACCAAGCTTATGGAAGGGACCTAATGGAGGCTCAAGAATGGTGTAGAAAATACATGAAAAGTGGAAATGTAAAGGA CCTTACACAAGCTTGGGATCTCTACTACCATGTTTTTAGGAGAATATCTAAA >SEQ_ID_NO:_57_CSDE1_AA MSFDPNLLHNNGHNGYPNGTSAALRETGVIEKLLTSYGFIQCSERQARLFFHCSQYNGNLQDLKVGDDVEFEVSSDRRTGKPIAVKLVKIKQEI LPEERMNGQVVCAVPHNLESKSPAAPGQSPTGSVCYERNGEVFYLTYTPEDVEGNVQLETGDKINFVIDNNKHTGAVSARNIMLLKKKQARCQG VVCAMKEAFGFIERGDVVKEIFFHYSEFKGDLETLQPGDDVEFTIKDRNGKEVATDVRLLPQGTVIFEDISIEHFEGTVTKVIPKVPSKNQNDP LPGRIKVDFVIPKELPFGDKDTKSKVTLLEGDHVRFNISTDRRDKLERATNIEVLSNTFQFTNEAREMGVIAAMRDGFGFIKCVDRDVRMFFHF SEILDGNQLHIADEVEFTVVPDMLSAQRNHAIRIKKLPKGTVSFHSHSDHRFLGTVEKEATFSNPKTTSPNKGKEKEAEDGIIAYDDCGVKLTIAFQAKDVEGSTSPQIGDKVEFSISDKQRPGQQVATCVRLLGRNSNSKRLLGYVATLKDNFGFIETANHDKEIFFHYSEFSGDVDSLELGDMVEY SLSKGKGNKVSAEKVNKTHSVNGITEEADPTIYSGKVIRPLRSVDPTQTEYQGMIEIVEEGDMKGEVYPFGIVGMANKGDCLQKGESVKFQLCV LGQNAQTMAYNITPLRRATVECVKDQFGFINYEVGDSKKLFFHVKEVQDGIELQAGDEVEFSVILNQRTGKCSACNVWRVCEGPKAVAAPRPDR LVNRLKNITLDDASAPRLMVLRQPRGPDNSMGFGAERKIRQAGVID >SEQ_ID_NO:_58_CSDE1_DNA atgagctttgatccaaaccttctccacaacaatggacataatgggtaccctaatggtacttcagcagcactgcgtgaaactggggttattgaaa aactgttaacctcttacggatttattcagtgttcagaacgtcaagctagacttttcttccactgttcacagtataatggcaacctgcaagactt aaaagtaggagatgatgttgaatttgaagtatcatcggaccgacggactgggaaacccattgctgttaaactggtgaagataaaacaagaaatc ctccctgaagaacgaatgaatggacaagttgtgtgcgctgttcctcacaacttagagagtaaatctccagctgccccgggtcagagtccaacag ggagtgtatgctacgaacgtaatggggaagtgttttatctgacttacacccctgaagatgtcgaagggaacgttcagctggaaactggagataa aataaactttgtaattgataacaataaacatactggtgctgtaagtgctcgcaacattatgctgttgaaaaagaaacaagcccgctgtcaggga gtagtttgtgccatgaaggaggcatttggctttattgaaagaggtgatgttgtaaaagagatattctttcactatagtgaatttaagggtgact tagaaaccttacagcctggcgatgatgtggaattcacaatcaaggacagaaatggtaaagaagttgcaacagatgtcagactattgcctcaagg aacagtcatttttgaagatatcagcattgaacattttgaaggaactgtaaccaaagttatcccaaaagtacccagtaaaaaccagaatgacccattgccaggacgcatcaaagttgactttgtgatccctaaagaacttccctttggagacaaagatacgaaatccaaggtgaccctgctggaaggtg accatgttaggtttaatatttcaacagaccgacgtgacaaattagagcgagcaaccaatatagaagttctgtcaaatacatttcagttcactaa tgaagcccgagaaatgggtgtgattgctgccatgagagatggttttggtttcatcaagtgtgtggatcgtgatgttcgtatgttcttccacttc agtgaaattctggatgggaaccagctccatattgcagatgaagtagagtttactgtggttcctgatatgctctctgctcaaagaaatcatgcta ttaggattaaaaaacttcccaagggcacggtttcatttcattcccattcagatcaccgttttctgggcacggtagaaaaagaagccactttttc caatcctaaaaccactagcccaaataaaggcaaagagaaggaggctgaggatggcattattgcttatgatgactgtggggtgaaactgactatt gcttttcaagccaaggatgtggaaggatctacttctcctcaaataggagataaggttgaatttagtattagtgacaaacagaggcctggacagc aggttgcaacttgtgtgcgacttttaggtcgtaattctaactccaagaggctcttgggttatgtggcaactctgaaggataattttggatttat tgaaacagccaatcatgataaggaaatctttttccattacagtgagttctctggtgatgttgatagcctggaactgggggacatggtcgagtat agcttgtccaaaggcaaaggcaacaaagtcagtgcagaaaaagtgaacaaaacacactcagtgaatggcattactgaggaagctgatcccaccatttactctggcaaagtaattcgccccctgaggagtgttgatccaacacagactgagtaccaaggaatgattgagattgtggaggagggcgatat gaaaggtgaggtctatccatttggcatcgttgggatggccaacaaaggggattgcctgcagaaaggggagagcgtcaagttccaattgtgtgtc ctgggccaaaatgcacaaactatggcttacaacatcacacccctgcgcagggccacagtggaatgtgtgaaagatcagtttggcttcattaact atgaagtaggagatagcaagaagctctttttccatgtgaaagaagttcaggatggcattgagctacaggcaggagatgaggtggagttctcagt gattcttaatcagcgcactggcaagtgcagcgcctgtaatgtttggcgagtctgtgagggccccaaggctgttgcagctcctcgacctgatcgg ttggtcaatcgcttgaagaatatcactctggatgatgccagtgctcctcgcctaatggttcttcgtcagccaaggggaccagataactcaatgg ggtttggtgcagaaagaaagatccgtcaagctggtgtcattgac >SEQ_ID_NO:_59_PAP[AP]_linker_AA PAPAP >SEQ_ID_NO:_64_(EAAAK)n_linker_DNA GAAGCAGCAGCGAAA>SEQ_ID_NO:_65_hADAR2cd(E174Q)_XTEN_hPUM2_AAMQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLY TQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSNASIQTW DGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAP NFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEK PTEQDQFSLTPSGSETPGTSESATPESSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETD GPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSN PETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPY IISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQA ESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFR PIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDL YKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQ LFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQK FFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVF VLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGML>SEQ_ID_NO:_66_hADAR2cd(E174Q)_XTEN_hPUM2_DNA atgcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctc atgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtg cataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctac actcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacg ttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagaca tcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccAACgctagtattcaaacgtgg gacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcct aacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgt gtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatca tgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaag ccgaccgagcaggaccaattctctctgacgcccagcggcagcgagactcccgggacctcagagtccgccacacccgaaagttcccagcctatta tggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtggaggccttggtgtgag catggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactagagatgctgaaacagat ggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagatgatgatgattctaaaa taaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagt tgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaaat cctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggtaccaatggactcttcag gagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagttaactgcagctcaaca gcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatttgtgccaaatccatac attattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtccagcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacagccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaagca gaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctatcaagtactagctccaa ctgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaatggctccaacacctgt tttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcacaaatggtctgtttcgg ccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagcagttctttgactaata gctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaactctttgggtgctgctat aggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatctactagctctgacttg tacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagtccaataggcatgcctc tgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttcagaaacaaccgcttcc caaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagcaaaaactagagagagc tactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaactatgttatacagaag ttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttgcagatgtatggctgcc gcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaaga tcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgctttcaagggacaagtattt gtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacctatcttagaagaactcc accaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctgaagacaagagcaaaat tgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgct gagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggaccagtatgccaattacg tggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattactactttgcgcaaatacac atacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggaccaccaaatggaatgctg >SEQ_ID_NO:_67_hPUM2_XTEN_hADARcd(E174Q)_AAMSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQV PMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGP AVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGY QVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGS SSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPS PIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDF RNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLAL QMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLP ILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKD QYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLSGSETPGTSESATPESQLHLPQVLAD AVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYTQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSNASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDS AIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTP >SEQ_ID_NO:_68_hPUM2_XTEN_hADARcd(E174Q)_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagat gatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcct ctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgt tgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggta ccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagt taactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatt tgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtcca gcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacagccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctat caagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaa tggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcac aaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagc agttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaact ctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagt ccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatt taggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttcagaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagc aaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaa ctatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttg cagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgc tcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctg aagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttac tcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggac cagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattacta ctttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggacc accaaatggaatgctgagcggcagcgagactcccgggacctcagagtccgccacacccgaaagtcagctgcacctgccccaggttctcgcagac gccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctcatgcgaggcggaaagtactcgcaggcgtcgtca tgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctacactcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacgttcagttccacttgtatatcagcacatcccctt gcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagacatcctaataggaaggctagaggccaacttcggac gaagattgaaagtggccagggtactatcccggtgcggtccAACgctagtattcaaacgtgggacggagtccttcaaggtgaacggctgttgaca atgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatcca ttattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacact caataagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcctaacttcagtgttaactggaccgttggtgattct gcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgtgtaaacacgcgttgtattgtagatggatgagag tacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatcatgagtcaaaactcgcggctaaagaataccaggc agccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaagccgaccgagcaggaccaattctctctgacgccc >SEQ_ID_NO:_69_hADAR2cd(E174Q)_32aa-linker_hPUM2_AA MQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLY TQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSNASIQTW DGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAP NFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEK PTEQDQFSLTPSGGSSGGSSGSETPGTSESATPESSGGSSGGSSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLD SRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGP LPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAG VFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGA GQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAA GGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSA SSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAK YRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQA AYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLK NSPDLGPIGGPPNGML >SEQ_ID_NO:_70_hADAR2cd(E174Q)_32aa-linker_hPUM2_DNA atgcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctc atgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtg cataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctac actcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacg ttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagaca tcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccAACgctagtattcaaacgtgg gacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcct aacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgt gtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatca tgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaag ccgaccgagcaggaccaattctctctgacgccctctggtggttcttctggtggttctagcggcagcgagactcccgggacctcagagtccgcca cacccgaaagttctggtggttcttctggtggttcttcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagt aaatgcaatactgtctccgcgatcagaaagtggaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggat tctcgatttaggaagggaaattttggcactagagatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgagg aggaccaaaacagagatcttaaacaaggagatgatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaaga ttttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcct cttcctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaat ccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctt tcagaggactaatgcactaacagttcaacagttaactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggt gtattctcagcaggccttgctccagctgcatttgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtccagcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacagccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagca ggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttg gtcagggtcttgctactggcatgccaggctatcaagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagc aaggactggccttggagctccagttcggttaatggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagct ggaggaactgcaagtagccttacaggcagcacaaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagca ctaatctgcaatctaattcattttatggaagcagttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctgg aagtacatctcttggctttggaagtggtaactctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgca agtagtagtgccacaaggagagagtctctatctactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccatttt acaatagtctgggattttcctcctctccaagtccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgc cttctggccgcagtagattattggaagatttcagaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttc tcaagaccagcatggttctagattcatacagcaaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagca gcctatcaattaatgactgatgtttttggcaactatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactc gtattcgtggtcatgttctacccttagccttgcagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagag tgaaatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcag ccacagtcactacagttcatcattgatgctttcaagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcc tagagcattgcactgcagaacagaccttacctatcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgt tattcagcatgtactggaacacggtcgacctgaagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaa tttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtc ctcacagtgccttatacaccatgatgaaggaccagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagat aatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaag aatagcccggacctaggacctattggaggaccaccaaatggaatgctg>SEQ_ID_NO:_71_hPUM2_32aa-linker_hADARcd(E174Q)_AAMSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGD DDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQV PMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGP AVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGY QVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGS SSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPS PIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDF RNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLAL QMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLSGGSSGGSSGSETPGTSESATPESSG GSSGGSQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSL LRFLYTQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSNA SIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQ PGKAPNFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLG AWVEKPTEQDQFSLTP >SEQ_ID_NO:_72_hPUM2_32aa-linker_hADARcd(E174Q)_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagat gatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcct ctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgt tgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagttaactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatt tgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtcca gcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacag ccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtca gcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctat caagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaa tggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcac aaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagc agttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaact ctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagtccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatt tagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttc agaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagc aaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaa ctatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttg cagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgc tcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctg aagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttac tcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggac cagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattacta ctttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggacc accaaatggaatgctgtctggtggttcttctggtggttctagcggcagcgagactcccgggacctcagagtccgccacacccgaaagttctggtggttcttctggtggttctcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctcatgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctc cacgggcacaaagtgcataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctg cttagatttctctacactcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttc gacttaaggaaaacgttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggagga gcccgcggacagacatcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccAACgct agtattcaaacgtgggacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatcc aaggcagcctcttgagcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctat gtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccag ccagggaaagctcctaacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgtgtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatcatgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggg gcatgggtcgagaagccgaccgagcaggaccaattctctctgacgccc >SEQ_ID_NO:_73_hADAR2cd(E174Q / N182F)_XTEN_hPUM2_AA MQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLY TQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSFASIQTW DGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAP NFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEK PTEQDQFSLTPSGSETPGTSESATPESSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETD GPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSN PETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPY IISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQA ESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFR PIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQK FFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVF VLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRA ERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGML >SEQ_ID_NO:_74_hADAR2cd(E174Q / N182F)_XTEN_hPUM2_DNA atgcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctc atgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctacactcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacg ttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagaca tcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccTTCgctagtattcaaacgtgg gacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttga gcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttc taatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcct aacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgt gtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatca tgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaag ccgaccgagcaggaccaattctctctgacgcccagcggcagcgagactcccgggacctcagagtccgccacacccgaaagttcccagcctatta tggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtggaggccttggtgtgag catggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactagagatgctgaaacagat ggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagatgatgatgattctaaaa taaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggtaccaatggactcttcag gagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagttaactgcagctcaaca gcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatttgtgccaaatccatac attattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtccagcagtggttccacctc agtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacagccagtcagcaagcagc atcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaagca gaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctatcaagtactagctccaa ctgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaatggctccaacacctgt tttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcacaaatggtctgtttcgg ccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagcagttctttgactaata gctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaactctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatctactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagtccaataggcatgcctc tgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgacaaa tggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagccag ctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttcagaaacaaccgcttcc caaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagcaaaaactagagagagc tactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaactatgttatacagaag ttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttgcagatgtatggctgcc gcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaaga tcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgctttcaagggacaagtattt gtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacctatcttagaagaactcc accaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctgaagacaagagcaaaat tgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgct gagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggaccagtatgccaattacg tggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggaccaccaaatggaatgctg>SEQ_ID_NO:_75_hPUM2_XTEN_hADARcd(E174Q / N182F)_AA MSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGD DDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQV PMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGP AVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGY QVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGS SSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPS PIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLP ILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKD QYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLSGSETPGTSESATPESQLHLPQVLAD AVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYTQLELYLNNKD DQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSFASIQTWDGVLQGERLLT MSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDS AIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTP >SEQ_ID_NO:_76_hPUM2_XTEN_hADARcd(E174Q / N182F)_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagat gatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcct ctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagt taactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatt tgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtcca gcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacag ccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtca gcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctat caagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaa tggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcac aaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagcagttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaactctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagt ccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatt taggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatt tagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttc agaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagc aaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaa ctatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttg cagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgc tcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctg aagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttac tcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggaccagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggacc accaaatggaatgctgagcggcagcgagactcccgggacctcagagtccgccacacccgaaagtcagctgcacctgccccaggttctcgcagac gccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctcatgcgaggcggaaagtactcgcaggcgtcgtca tgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatgagcgaccgggggct ggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctacactcaactcgaattgtaccttaacaacaaagat gaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacgttcagttccacttgtatatcagcacatcccctt gcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagacatcctaataggaaggctagaggccaacttcggac gaagattgaaagtggccagggtactatcccggtgcggtccTTCgctagtattcaaacgtgggacggagtccttcaaggtgaacggctgttgaca atgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttgagcatattcgtagaacccatatatttctcatcca ttattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttctaatatcgaggatcttcctccactctatacact caataagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcctaacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgtgtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatcatgagtcaaaactcgcggctaaagaataccaggc agccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaagccgaccgagcaggaccaattctctctgacgccc >SEQ_ID_NO:_77_hADAR2cd(E174Q / N182F)_32aa-linker_hPUM2_AA MQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLY TQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSFASIQTW DGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAP NFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEK PTEQDQFSLTPSGGSSGGSSGSETPGTSESATPESSGGSSGGSSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLD SRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGP LPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAG VFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGA GQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAA GGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQA AYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQ PQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHK FASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLK NSPDLGPIGGPPNGML >SEQ_ID_NO:_78_hADAR2cd(E174Q / N182F)_32aa-linker_hPUM2_DNA atgcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctc atgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtgcataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctacactcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacg ttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagaca tcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccTTCgctagtattcaaacgtgg gacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttga gcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttc taatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcct aacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgt gtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatca tgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaag ccgaccgagcaggaccaattctctctgacgccctctggtggttcttctggtggttctagcggcagcgagactcccgggacctcagagtccgcca cacccgaaagttctggtggttcttctggtggttcttcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagt aaatgcaatactgtctccgcgatcagaaagtggaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggat tctcgatttaggaagggaaattttggcactagagatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgagg aggaccaaaacagagatcttaaacaaggagatgatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaat ccttacagtttgactatcctggtaatcaggtaccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctt tcagaggactaatgcactaacagttcaacagttaactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggt gtattctcagcaggccttgctccagctgcatttgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcag gattggctgcagcagctacattagcaggtccagcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttca gcagcaagctgcagctgcggcaaataacacagccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagca ggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttg gtcagggtcttgctactggcatgccaggctatcaagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagc aaggactggccttggagctccagttcggttaatggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcacaaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagcagttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctgg aagtacatctcttggctttggaagtggtaactctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgca agtagtagtgccacaaggagagagtctctatctactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccatttt acaatagtctgggattttcctcctctccaagtccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcact ttcatcacatggatcctcatccagtttgcatttaggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaa tatcgaagtgcttcaagcacttccagtctatttagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgc cttctggccgcagtagattattggaagatttcagaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttc tcaagaccagcatggttctagattcatacagcaaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagca gcctatcaattaatgactgatgtttttggcaactatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactc gtattcgtggtcatgttctacccttagccttgcagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagag tgaaatggtaaaggagctggatggtcatgtgctcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcag ccacagtcactacagttcatcattgatgctttcaagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcc tagagcattgcactgcagaacagaccttacctatcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgt tattcagcatgtactggaacacggtcgacctgaagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggaccagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagat aatcatgcacaagattcgacctcacattactactttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaag aatagcccggacctaggacctattggaggaccaccaaatggaatgctg >SEQ_ID_NO:_79_hPUM2_32aa-linker_hADARcd(E174Q / N182F)_AA MSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGD DDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQV PMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQQQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGP AVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQAASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGY QVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTPVLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGS SSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAAIGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLTNGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLERATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLAL QMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLP ILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKD QYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKYTYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLSGGSSGGSSGSETPGTSESATPESSG GSSGGSQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSL LRFLYTQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSFA SIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQ PGKAPNFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLG AWVEKPTEQDQFSLTP >SEQ_ID_NO:_80_hPUM2_32aa-linker_hADARcd(E174Q / N182F)_DNA atgtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtg gaggccttggtgtgagcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactag agatgctgaaacagatggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagatgatgatgattctaaaataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagtagttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgt tgaagaattttcaaatcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggta ccaatggactcttcaggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagt taactgcagctcaacagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatt tgtgccaaatccatacattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtcca gcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacag ccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtca gcaagggcagcaagcagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctat caagtactagctccaactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaatggctccaacacctgttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcacaaatggtctgtttcggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagc agttctttgactaatagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaact ctttgggtgctgctataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatc tactagctctgacttgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagt ccaataggcatgcctctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatt taggaggactgacaaatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatt tagctccagcagccagctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttc agaaacaaccgcttcccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagc aaaaactagagagagctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgatgtttttggcaa ctatgttatacagaagttttttgagtttgggagtctggatcaaaaattagccctggctactcgtattcgtggtcatgttctacccttagccttg cagatgtatggctgccgcgttattcagaaagcattagaatctatttcttctgaccagcagagtgaaatggtaaaggagctggatggtcatgtgc tcaaatgtgtgaaagatcagaatggaaaccatgttgtacaaaaatgtatcgaatgtgttcagccacagtcactacagttcatcattgatgcttt caagggacaagtatttgtgctttcaactcatccttatggctgcagagtaattcagcgcatcctagagcattgcactgcagaacagaccttacct atcttagaagaactccaccaacatacagagcagttggtacaggatcagtatggcaattatgttattcagcatgtactggaacacggtcgacctgaagacaagagcaaaattgtttccgaaatcaggggaaaggttttagccctgagtcaacacaaatttgccagcaatgtagtagaaaagtgtgttactcatgcctcccgtgctgagagagctttactgattgacgaggtttgctgccagaatgatggtcctcacagtgccttatacaccatgatgaaggac cagtatgccaattacgtggttcaaaagatgattgatatggctgaacctgctcagagaaagataatcatgcacaagattcgacctcacattacta ctttgcgcaaatacacatacgggaagcatatactggccaagttggaaaagtattatttgaagaatagcccggacctaggacctattggaggacc accaaatggaatgctgtctggtggttcttctggtggttctagcggcagcgagactcccgggacctcagagtccgccacacccgaaagttctggt ggttcttctggtggttctatgcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactg acaatttttcatctcctcatgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgt ctccacgggcacaaagtgcataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatct ctgcttagatttctctacactcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggat ttcgacttaaggaaaacgttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagacatcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccTTCgctagtattcaaacgtgggacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaa tccaaggcagcctcttgagcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggc tatgtaccaacgaatttctaatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgc cagccagggaaagctcctaacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcg gtagagcctcacgcctgtgtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcac taagcctaatgtgtatcatgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctc ggggcatgggtcgagaagccgaccgagcaggaccaattctctctgacgccc >SEQ_ID_NO:_81_hADAR2CD(E174Q / N182F)_SHL_T2A_hPUM2_SH3_AA MQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLY TQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEEPADRHPNRKARGQLRTKIESGQGTIPVRSFASIQTW DGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAP NFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEK PTEQDQFSLTPSSMVDPPPALPPKRRREFGPGTSFCSLGSGEGRGSLLTCGDVEENPGPSQPIMVQRRSGQGFHGNSEVNAILSPRSESGGLGVSMVEYVLSSSPADKLDSRFRKGNFGTRDAETDGPEKGDQKGKASPFEEDQNRDLKQGDDDDSKINGRGLPNGMDADCKDFNRTPGSRQASPTEVVERLGPNTNPSEGLGPLPNPTANKPLVEEFSNPETQNLDAMEQVGLESLQFDYPGNQVPMDSSGATVGLFDYNSQQQLFQRTNALTVQQLTAAQ QQQYALAAAQQPHIAGVFSAGLAPAAFVPNPYIISAAPPGTDPYTAAGLAAAATLAGPAVVPPQYYGVPWGVYPANLFQQQAAAAANNTASQQA ASQAQPGQQQVLRAGAGQRPLTPNQGQQGQQAESLAAAAAANPTLAFGQGLATGMPGYQVLAPTAYYDQTGALVVGPGARTGLGAPVRLMAPTP VLISSAAAQAAAAAAAGGTASSLTGSTNGLFRPIGTQPPQQQQQQPSTNLQSNSFYGSSSLTNSSQSSSLFSHGPGQPGSTSLGFGSGNSLGAA IGSALSGFGSSVGSSASSSATRRESLSTSSDLYKRSSSSLAPIGQPFYNSLGFSSSPSPIGMPLPSQTPGHSLTPPPSLSSHGSSSSLHLGGLT NGSGRYISAAPGAEAKYRSASSTSSLFSSSSQLFPPSRLRYNRSDIMPSGRSRLLEDFRNNRFPNLQLRDLIGHIVEFSQDQHGSRFIQQKLER ATPAERQMVFNEILQAAYQLMTDVFGNYVIQKFFEFGSLDQKLALATRIRGHVLPLALQMYGCRVIQKALESISSDQQSEMVKELDGHVLKCVK DQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFVLSTHPYGCRVIQRILEHCTAEQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSK IVSEIRGKVLALSQHKFASNVVEKCVTHASRAERALLIDEVCCQNDGPHSALYTMMKDQYANYVVQKMIDMAEPAQRKIIMHKIRPHITTLRKY TYGKHILAKLEKYYLKNSPDLGPIGGPPNGMLGGGGSGGGGSAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVP YVEKYSG >SEQ_ID_NO:_82_hADAR2CD(E174Q / N182F)_SHL_T2A_hPUM2_SH3_DNA atgcagctgcacctgccccaggttctcgcagacgccgtatcccgccttgtactgggcaagtttggtgatcttactgacaatttttcatctcctc atgcgaggcggaaagtactcgcaggcgtcgtcatgacgaccggaactgacgtgaaagacgccaaagtcatctctgtctccacgggcacaaagtg cataaacggggagtacatgagcgaccgggggctggcactgaatgattgtcacgctgaaataatatctaggcgatctctgcttagatttctctac actcaactcgaattgtaccttaacaacaaagatgaccagaaacgcagtatatttcagaaatcagaacgcggcggatttcgacttaaggaaaacg ttcagttccacttgtatatcagcacatccccttgcggtgacgcccgaatcttttccccgcacgagccgatattggaggagcccgcggacagaca tcctaataggaaggctagaggccaacttcggacgaagattgaaagtggccagggtactatcccggtgcggtccTTCgctagtattcaaacgtgg gacggagtccttcaaggtgaacggctgttgacaatgagctgctcagacaaaatcgcgcgctggaatgtagtgggaatccaaggcagcctcttga gcatattcgtagaacccatatatttctcatccattattttgggctctctgtatcatggtgaccatctgtcaagggctatgtaccaacgaatttc taatatcgaggatcttcctccactctatacactcaataagcctctcttgtccgggatatcaaacgctgaggcccgccagccagggaaagctcct aacttcagtgttaactggaccgttggtgattctgcgatagaggtcatcaacgccacgacaggtaaggatgagctcggtagagcctcacgcctgt gtaaacacgcgttgtattgtagatggatgagagtacatgggaaggtcccatctcacttgctccgaagcaagatcactaagcctaatgtgtatca tgagtcaaaactcgcggctaaagaataccaggcagccaaagctcgactttttacagcttttattaaggcagggctcggggcatgggtcgagaag ccgaccgagcaggaccaattctctctgacgccctctagtatggtcgaccctccacctgctctgccacctaagagaaggagagaattcgggcccggtaccagcttttgttcccttGGAAGTGGTGAGGGTAGGGGAAGTTTATTAACCTGTGGGGATGTTGAAGAAAATCCAGGTCCTtcccagcctattatggtacagagaagatctggacagggttttcatggaaacagtgaagtaaatgcaatactgtctccgcgatcagaaagtggaggccttggtgtg agcatggtagaatatgtattaagttcttctcctgctgataaattggattctcgatttaggaagggaaattttggcactagagatgctgaaacag atggacctgagaaaggagatcaaaaaggcaaggcttctccatttgaggaggaccaaaacagagatcttaaacaaggagatgatgatgattctaa aataaatggcagaggtttgccaaatggaatggatgccgattgcaaagattttaatcgtactcctggaagtcgtcaagcctctccaactgaagta gttgagcgcttgggccccaatactaatccctcagaaggactggggcctcttcctaatcctacagctaataaaccacttgttgaagaattttcaa atcctgaaactcagaatctggatgccatggaacaagttggtctggaatccttacagtttgactatcctggtaatcaggtaccaatggactcttc aggagctactgtaggcctttttgactacaattcccagcagcagctctttcagaggactaatgcactaacagttcaacagttaactgcagctcaa cagcagcaatatgcattagcagcagctcagcagccacatatagctggtgtattctcagcaggccttgctccagctgcatttgtgccaaatccat acattattagtgctgctcctccagggaccgatccgtatactgcagcaggattggctgcagcagctacattagcaggtccagcagtggttccacctcagtattacggcgttccatggggggtgtatccagccaacttatttcagcagcaagctgcagctgcggcaaataacacagccagtcagcaagcagcatcacaagctcagcctggacagcaacaggttctccgtgctggagcaggtcagcgtcctcttactcccaatcagggtcagcaagggcagcaag cagaatcacttgcggcagctgcagcagcaaatccaacattggcttttggtcagggtcttgctactggcatgccaggctatcaagtactagctcc aactgcctattatgatcagactggtgccttagtggttggccctggagcaaggactggccttggagctccagttcggttaatggctccaacacct gttttaattagttcagcagcagcacaagctgcagcagcagcagcagctggaggaactgcaagtagccttacaggcagcacaaatggtctgtttc ggccaattggcactcagccaccacagcagcagcaacagcagccaagcactaatctgcaatctaattcattttatggaagcagttctttgactaa tagctcccagagtagttctttattttctcatggacctggtcaacctggaagtacatctcttggctttggaagtggtaactctttgggtgctgct ataggctcagccctcagtggatttggttcatcagttggcagttctgcaagtagtagtgccacaaggagagagtctctatctactagctctgact tgtacaaaagatctagtagcagcctagcacccatagggcaaccattttacaatagtctgggattttcctcctctccaagtccaataggcatgcc tctgccaagccaaactccaggacattcacttacgccaccgccatcactttcatcacatggatcctcatccagtttgcatttaggaggactgaca aatggtagtggtcgatatatctctgcagcacctggagcagaagcaaaatatcgaagtgcttcaagcacttccagtctatttagctccagcagcc agctctttcctccttcccggcttcggtataataggtctgatattatgccttctggccgcagtagattattggaagatttcagaaacaaccgctt cccaaaccttcagcttagagacttgattggacatatagttgagttttctcaagaccagcatggttctagattcatacagcaaaaactagagaga gctactccagctgagcgacagatggtatttaatgaaattctgcaagcagcctatcaattaatgactgat...

Claims

Claims 1. A method for identifying a binding interaction between a query polypeptide and a query RNA nucleic acid, the method comprising: a) contacting a first query RNA nucleic acid with a test polypeptide, wherein the test polypeptide comprises the query polypeptide or a fragment thereof and: i) an RNA modifying domain or fragment thereof capable of modifying RNA; or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain; or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; optionally wherein the test polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i. an RNA modifying polypeptide domain capable of modifying RNA; ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; oriii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; wherein where said test polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a first test query RNA nucleic acid; and b) detecting the presence or absence of at least one modification in the first test query RNA nucleic acid; and c) determining that there is a binding interaction between the query polypeptide and query RNA nucleic acid when a modification is detected in the first test query RNA nucleic acid.

2. A method for identifying one or more binding sites of a query polypeptide on a query RNA nucleic acid, the method comprising: a) contacting a first query RNA nucleic acid with a test polypeptide, wherein the test polypeptide comprises the query polypeptide or a fragment thereof and: i) an RNA modifying domain or fragment thereof capable of modifying RNA, orii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain; or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; optionally wherein the test polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNA; ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; wherein where said test polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA whenbrought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a first test query RNA nucleic acid; b) detecting the presence or absence of at least one modification in the first test query RNA nucleic acid and generating a modification profile for the first test query RNA nucleic acid; and c) determining one or more binding sites of the query polypeptide on the query RNA nucleic acid using the modification profile.

3. The method of claim 1 or 2, wherein the query polypeptide is an RNA binding polypeptide or an RNA binding fragment thereof, optionally an RNA binding protein (RBP) or a fragment thereof.

4. The method of claim 3, wherein the RNA binding protein is selected from the group comprising or consisting of: an RNA polymerase or a subunit thereof; a DNA polymerase or a subunit thereof; a spliceosome protein or a subunit thereof; a ribosome or a subunit thereof; an RNA editing enzyme; a polyadenylase; a nuclease; a nuclear pore complex protein or subunit thereof; an RNA methyltransferase; and RNA demethylase; an RNA acetylase; an RNA deacetylase; a translational regulator; a post-transcriptional regulator; and a metabolic enzyme.

5. The method of any of claims 3-4, wherein the RBP is selected from the group comprising or consisting of: PUM2, CSDE1, NONO, MEX3A, PTBP3, IGF2BP1, ZEB1, LIN28, HNRNPNU, IRP1, IRP2, ANXA2, HuR, Musashi-1, TAF15, hnRNP H / F, FUS, EWSR1, SAMD4B, VTS1, CELF1; optionally wherein the RBP is PUM2.

6. The method of claims 3-5, wherein the RBP: a) comprises or consists of an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 1, SEQ ID NO: 57, SEQ ID NO: 103, SEQ ID NO: 105, SEQ ID NO: 107, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 1, , SEQ ID NO: 57, SEQ ID NO: 103, , SEQ ID NO: 105, SEQ ID NO: 107, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 2, SEQ ID NO: 58, SEQ ID NO: 104, , SEQ ID NO: 106, SEQ ID NO: 108, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 2, , SEQ ID NO: 58, SEQ ID NO: 104, , SEQ ID NO: 106, SEQ ID NO: 108, or a subsequence thereof.

7. The method of any of the preceding claims, wherein the RNA modifying domain is an RNA-modifying enzyme, wherein the RNA-modifying enzyme is: a) a Homo sapiens ADAR2 that has at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100% sequence identity to SEQ ID NO: 111, provided that provided that residue 174 is a glutamine and residue 182 is a phenylalanine; b) an Adenosine Deaminase acting on RNA (ADAR) enzyme or a cytosine deaminase (CBE); and / or c) the first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain is a first portion of an RNA modifying enzyme, optionally is a first portion of an Adenosine Deaminase acting on RNA (ADAR) enzyme or first portion of a cytosine deaminase (CBE) enzyme.

8. The method of claim 7, wherein:a) the ADAR enzyme is selected from the group comprising or consisting of: Drosophila melanogaster ADAR, Homo sapiens ADAR1, Homo sapiens ADAR2, Homo sapiens ADAR3, Homo sapiens ADAR4; or b) the CBE enzyme is APOBEC1.

9. The method of claim 7 or 8, wherein: a) the ADAR enzyme is a wild-type ADAR enzyme; or b) the CBE enzyme is a wild-type CBE enzyme.

10. The method of claim 7 or 8, wherein: a) the ADAR enzyme is a mutant ADAR enzyme comprising at least one amino acid insertion, substitution or deletion compared to wild-type ADAR enzyme; or b) the CBE enzyme is a mutant CBE enzyme comprising at least one amino acid insertion, substitution or deletion compared to wild-type CBE enzyme.

11. The method of claim 10, wherein the ADAR2 enzyme comprises a mutation at position 174, 182 of SEQ ID NO: 111; optionally wherein the ADAR enzyme comprises an E174Q and / or an N182F mutation of SEQ ID NO: 111; optionally wherein the ADAR enzyme is hADAR2cd.

12. The method of claims 7-11, wherein the ADAR enzyme: a) comprises or consists an amino acid sequence that is: i) at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 3, SEQ ID NO: 5, or SEQ ID NO: 111, provided that residue 174 is a glutamine and residue 182 is a phenylalanine; ii) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 109, SEQ ID NO: 111, or a subsequence thereof; or iii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 7, SEQ ID NO: 109, SEQ ID NO: 111, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 4, SEQ ID NO: 6, or SEQ ID NO: 112, provided thatresidue 174 of the amino acid sequence is a glutamine and residue 182 of the amino acid sequence is a phenylalanine; ii) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 110, SEQ ID NO: 112, or a subsequence thereof; or iii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 110, SEQ ID NO: 112, or a subsequence thereof.

13. The method of any of claims 7-12, wherein the first portion of the ADAR enzyme comprises an N-terminal fragment of the ADAR enzyme and the second portion of the ADAR enzyme comprises a C-terminal fragment of the ADAR enzyme, and wherein: the first portion of the ADAR enzyme and the second portion of the ADAR fragment do not independently have adenosine deaminase activity; and the first portion of the ADAR enzyme and the second portion of the ADAR enzyme form a functional ADAR enzyme having adenosine deaminase activity when brought into proximity to one another, optionally brought into proximity to one another via dimerisation of dimerisation domains present on the first portion of the ADAR enzyme and the second portion of the ADAR enzyme.

14. The method of claims 1-13, wherein the RNA modifying domain comprises: a) the first portion of the RNA modifying polypeptide domain, optionally a first portion of an ADAR enzyme; or b) the second portion of the RNA modifying polypeptide domain, optionally a second portion of an ADAR enzyme, and does not comprise both the first and the second portions of the RNA modifying polypeptide domain.

15. The method of claims 1-14 wherein the RNA modifying domain comprises: a) the first portion of the RNA modifying polypeptide domain, optionally a first portion of an ADAR enzyme; or b) the second portion of the RNA modifying polypeptide domain, optionally a second portion of an ADAR enzyme, wherein the first and second portions of the RNA modifying polypeptide domain are separated by a self-cleaving protease site arranged so that following protein expression the self-cleaving protease site is cleaved, separating the first and second portions of the RNA modifying polypeptide domain onto separate polypeptide molecules.

16. The method of claims 1-15 wherein the test polypeptide comprises: a) the query fusion polypeptide connected to first portion of the RNA modifying polypeptide domain, optionally the first portion of an ADAR enzyme, and wherein the first portion of the RNA modifying polypeptide domain is connected to the second portion of the RNA modifying polypeptide domain via a linker comprising a self- cleaving protease site; or b) the query fusion polypeptide connected to second portion of the RNA modifying polypeptide domain, optionally the second portion of an ADAR enzyme, and wherein the second portion of the RNA modifying polypeptide domain is connected to the first portion of the RNA modifying polypeptide domain via a linker comprising a self-cleaving protease site.

17. The method of claim 1-13, 15-16, wherein the RNA modifying domain comprises both the first portion of the RNA modifying polypeptide domain and the second portion of the RNA modifying polypeptide domain, optionally comprises both the first portion of a ADAR enzyme and the second portion of the ADAR enzyme.

18. The method of claims 13-17, wherein the first portion of the ADAR enzyme : a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 9, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 9, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 10, , or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 10, or a subsequence thereof.

19. The method of claims 13-18, wherein the second portion of the ADAR enzyme: a) comprises or consists an amino acid sequence that is:i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 11, SEQ ID NO: 13, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 11, SEQ ID NO: 13, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 12, SEQ ID NO: 14, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 12, SEQ ID NO: 14, or a subsequence thereof.

20. The method of claims 13-19, wherein the first portion of the RNA modifying polypeptide domain and the second portion of the RNA modifying polypeptide domain each further comprise an inducible dimerization domain that: a) are capable of dimerising in the presence of a dimerization inducing molecule, so as to cause dimerization of the first portion of the RNA modifying polypeptide and the second portion of the RNA modifying polypeptide domain to form a functional RNA modifying polypeptide domain in the presence of a dimerization inducing molecule; and / or b) are not capable of dimerising in the absence of a dimerization inducing molecule, thereby preventing dimerization of the first portion of the RNA modifying polypeptide and the second portion of the RNA modifying polypeptide domain.

21. The method of claim 20, wherein the dimerization inducing molecule is selected from the group comprising or consisting of: rapamycin; Mandipropamid (Mandi); abscisic acid, and gibberellic acid.

22. The method of claims 20-21, wherein the dimerization polypeptide is selected from the group comprising or consisting of: FRB and FKBP12.

23. The method of claim 20-22, wherein:a) the first portion of the RNA modifying polypeptide domain further comprises an inducible dimerization domain that is FRB and the second portion of the RNA modifying polypeptide domain further comprises an inducible dimerization domain that is FKBP12; or b) the first portion of the RNA modifying polypeptide domain further comprises an inducible dimerization domain that is FKBP12 and the second portion of the RNA modifying polypeptide domain further comprises an inducible dimerization domain that is FRB.

24. The method of claims 20-23, wherein the inducible dimerization domain: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 15, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 15, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 16, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 16, or a subsequence thereof. and / or c) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 17, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 17, or a subsequence thereof; and / or d) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 18, or a subsequence thereof; orii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 18, or a subsequence thereof.

25. The method of claims 20-24, wherein: a) the first portion of the RNA modifying polypeptide domain comprises a dimerization linker connecting the inducible dimerization domain to the first portion of the RNA modifying polypeptide domain; and / or b) the second portion of the RNA modifying polypeptide domain comprises a dimerization linker connecting the inducible dimerization domain to the second portion of the RNA modifying polypeptide domain.

26. The method of claim 25, wherein the dimerization linker is selected from the group comprising or consisting of: GGSGSGAGSGSPAGGGAPGSGGGS (SEQ ID NO: 19), [GGGGS]n (SEQ ID NO: 121); PAP[AP]n; AEAAAKEAAAKA (SEQ ID NO: 61); [XP]n; (EAAAK)n (SEQ ID NO: 122); XTEN linker; SGGSSGGSSGSETPGTSESATPESSGGSSGGS (SEQ ID NO: 25); an endogenous linker; and any combination thereof.

27. The method of claims 25-26, wherein the dimerization linker: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 19, SEQ ID NO: 23,SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 59, SEQ ID NO: 61, SEQ ID NO: 63, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 19, SEQ ID NO: 23,SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 59, SEQ ID NO: 61, SEQ ID NO: 63, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 20, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 60, SEQ ID NO: 62, SEQ ID NO: 64, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 20, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 60, SEQ ID NO: 62, SEQ ID NO: 64, or a subsequence thereof.

28. The method of claims 13-27, wherein where the first portion of the RNA modifying polypeptide domain and the second portion of the RNA modifying polypeptide domain are connected by a self-cleavable linker.

29. The method of claim 28, wherein the self-cleavable linker is selected from the group comprising or consisting of: a T2A linker; P2A linker; E2A linker; F2A linker.

30. The method of claims 28-29, wherein the self-cleavable linker: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 21 or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 21 or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 22 or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 22 or a subsequence thereof.

31. The method of any of the preceding claims, wherein the query polypeptide or a fragment thereof and the RNA modifying polypeptide or a fragment thereof are connected by a polypeptide linker.

32. The method of claim 31, wherein the polypeptide linker is a flexible linker.

33. The method of claim 32, wherein the polypeptide linker comprises a sequence that is: between 1 aa and 60 aa, 2 aa and 59 aa, 3 aa and 58 aa, 4aa and 57 aa, 5 aa and 56 aa, 6 aa and 55 aa, 7 aa and 54 aa, 8 aa and 53 aa, 9 aa and 52 aa, 10 aa and 51 aa, 11 aa and 40 aa, 12 aa and 49 aa, 13 aa and 48 aa, 14 aa and 47 aa, 15 aa and 46 aa, 16 aa and 45 aa, 17 aa and 44 aa, 18 aa and 43 aa, 19 aa and 42 aa, 20 aa and 41 aa, 21 aa and 40 aa, 22 aa and 39 aa, 23 aa and 38 aa, 24 aa and 37 aa, 25 aa and 36 aa, 26 aa and 35 aa, 27 aa and 34 aa, 28 aa and 33 aa, 29 aa and 32 aa, 30 aa and 31 aa, 30 aa and 35 aa, 31 aa and 34 aa, 32 aa and 33 aa, or 31 aa and 33 aa in length;at least 1aa, at least 2 aa, and least 3 aa, at least 4 aa, at least 5 aa, at least 6 aa, at least 7 aa, at least 8 aa, at least 9 aa, at least 10 aa, at least 11 aa, at least 13 aa, at least 14 aa, at least 15 aa, at least 16 aa, at least 17 aa, at least 18 aa, at least 19 aa, at least 20 aa, at least 21 aa, at least 22 aa, at least 23 aa, at least 24 aa, at least 25 aa, at least 26 aa, at least 27 aa, at least 28 aa, at least 29 aa, at least 20 aa, at least 21 aa, at least 22 aa, at least 33 aa, at least 34 aa, at least 35 aa, at least 36 aa, at least 37 aa, at least 38 aa, at least 39 aa, at least 20 aa, at least 21 aa, at least 22 aa, at least 43 aa, at least 44 aa, at least 45 aa, at least 46 aa, at least 47 aa, at least 48 aa, at least 49 aa, at least 50 aa, at least 51 aa, at least 52 aa, at least 53 aa, at least 54 aa, at least 55 aa, at least 56 aa, at least 57 aa, at least 58 aa, at least 59 aa, or more in length; and / or 1 aa, 2 aa, 3 aa, 4 aa, 5 aa, 6 aa, 7 aa, 8 aa, 9 aa, 10 aa, 11 aa, 12 aa, 13 aa, 14 aa, 15 aa, 16 aa, 17 aa, 18 aa, 19 aa, 20 aa, 21 aa, 22 aa, 23 aa, 24 aa, 25 aa, 26 aa, 27 aa, 28 aa, 29 aa, 20 aa, 21 aa, 22 aa, 33 aa, 34 aa, 35 aa, 36 aa, 37 aa, 38 aa, 39 aa, 20 aa, 21 aa, 22 aa, 43 aa, 44 aa, 45 aa, 46 aa, 47 aa, 48 aa, 49 aa, 50 aa, 51 aa, 52 aa, 53 aa, 54 aa, 55 aa, 56 aa, 57 aa, 58 aa, 59 aa, or 60 aa in length.

34. The method of any of claims 31-33, wherein the polypeptide linker is selected from the group comprising or consisting of: an XTEN linker; a GGGGS (SEQ ID NO: 123) linker; a (GGGGS)n (SEQ ID NO: 121) linker; PAP[AP]n linker; AEAAAKEAAAKA (SEQ ID NO: 61); [XP]n; GGSGSGAGSGSPAGGGAPGSGGGS (SEQ ID NO: 19); (EAAAK)n (SEQ ID NO: 122); SGGSSGGSSGSETPGTSESATPESSGGSSGGS (SEQ ID NO: 25); an antibody linker; an endogenous linker; or any combination thereof.

35. The method of any of claims 31-34, wherein the polypeptide linker: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to 19, SEQ ID NO: 23,SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 59, SEQ ID NO: 61, SEQ ID NO: 63, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to 19, SEQ ID NO: 23,SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 59, SEQ ID NO: 61, SEQ ID NO: 63, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical SEQ ID NO:20, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 60, SEQ ID NO: 62, SEQ ID NO: 64, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 20, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, SEQ ID NO: 60, SEQ ID NO: 62, SEQ ID NO: 64, or a subsequence thereof.

36. The method of any of claims 31-35, wherein the polypeptide linker is not a (GGGGS)3 (SEQ ID NO: 27) linker.

37. The method of any of the preceding claims 1-12, wherein where the test polypeptide comprises a query polypeptide or a fragment thereof and a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA: a) the recruitment molecule and / or first affinity domain is connected to the query polypeptide or a fragment thereof by a polypeptide linker; and / or b) the second affinity domain is connected to the RNA modifying domain or fragment thereof by a polypeptide linker.

38. The method of any of claims 1-12 and 37, wherein the first affinity domain and the second affinity domain are each independently selected from the group comprising or consisting of: an SH3 domain; an SHL domain; an antibody or fragment thereof; a nanobody or fragment thereof; an antibody variable light chain or fragment thereof; an antibody variable heavy chain or fragment thereof; an antibody constant light chain or fragment thereof; an antibody constant heavy chain or fragment thereof; an antibody light chain or fragment thereof; an antibody heavy chain or fragment thereof; a Fab fragment; an Fc portion; an scFv; or any combination thereof.

39. The method of any of any of claims 1-12 and 37-38 wherein the first affinity domain and / or second affinity domain: comprise or consist an amino acid sequence that is: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical SEQ ID NO: 99, SEQ ID NO: 101, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 99, SEQ ID NO: 101, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is:i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 100, SEQ ID NO: 102, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 100, SEQ ID NO: 102, or a subsequence thereof.

40. The method of any of claims 1-12, 37-39 wherein the polypeptide linker is a flexible linker; and / or wherein the linker is a linker as defined in any one of claims 25-36.

41. The method of any of the claims 1-40, wherein the test polypeptide: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, act least 99%, or 100 % identical SEQ ID NO: 29, SEQ ID NO: 31, SEQ ID NO: 33, SEQ ID NO: 35, SEQ ID NO: 37, SEQ ID NO: 39, SEQ ID NO: 41, SEQ ID NO: 43, SEQ ID NO: 45, SEQ ID NO: 47, SEQ ID NO: 49, SEQ ID NO: 51, SEQ ID NO: 53, SEQ ID NO: 55, SEQ ID NO: 65, SEQ ID NO: 67, SEQ ID NO: 69, SEQ ID NO: 71, SEQ ID NO: 73, SEQ ID NO: 75, SEQ ID NO: 77, SEQ ID NO: 79, SEQ ID NO: 81, SEQ ID NO: 83, SEQ ID NO: 85, SEQ ID NO: 87, SEQ ID NO: 89, SEQ ID NO: 91, SEQ ID NO: 93, SEQ ID NO: 95, SEQ ID NO: 97, SEQ ID NO 113, SEQ ID NO: 115, SEQ ID NO: 117, SEQ ID NO: 119, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 29, SEQ ID NO: 31, SEQ ID NO: 33, SEQ ID NO: 35, SEQ ID NO: 37, SEQ ID NO: 39, SEQ ID NO: 41, SEQ ID NO: 43, SEQ ID NO: 45, SEQ ID NO: 47, SEQ ID NO: 49, SEQ ID NO: 51, SEQ ID NO: 53, SEQ ID NO: 55, SEQ ID NO: 65, SEQ ID NO: 67, SEQ ID NO: 69, SEQ ID NO: 71, SEQ ID NO: 73, SEQ ID NO: 75, SEQ ID NO: 77, SEQ ID NO: 79, SEQ ID NO: 81, SEQ ID NO: 83, SEQ ID NO: 85, SEQ ID NO: 87, SEQ ID NO: 89, SEQ ID NO: 91, SEQ ID NO: 93, SEQ ID NO: 95, SEQ ID NO: 97, SEQ ID NO: 113, SEQ ID NO: 115, SEQ ID NO: 117, SEQ ID NO 177, or a subsequence thereof; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO: 36, SEQ ID NO: 38, SEQ ID NO: 40, SEQ ID NO: 42, SEQ ID NO: 44, SEQ ID NO: 46, SEQ ID NO: 48,SEQ ID NO: 50, SEQ ID NO:52, SEQ ID NO: 54, SEQ ID NO: 56, SEQ ID NO: 66, SEQ ID NO: 68, SEQ ID NO: 70, SEQ ID NO: 72, SEQ ID NO: 74, SEQ ID NO: 76, SEQ ID NO: 78, SEQ ID NO: 80, SEQ ID NO 82, SEQ ID NO: 84, SEQ ID NO: 86, SEQ ID NO: 88, SEQ ID NO: 90, SEQ ID NO: 92, SEQ ID NO: 94, SEQ ID NO: 96, SEQ ID NO: 98, SEQ ID NO: 114, SEQ ID NO: 116, SEQ ID NO: 118, SEQ ID NO: 120 or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 30, SEQ ID NO: 32, SEQ ID NO: 34, SEQ ID NO: 36, SEQ ID NO: 38, SEQ ID NO: 40, SEQ ID NO: 42, SEQ ID NO: 44, SEQ ID NO: 46, SEQ ID NO: 48, SEQ ID NO: 50, SEQ ID NO:52, SEQ ID NO: 54, SEQ ID NO: 56, SEQ ID NO: 66, SEQ ID NO: 68, SEQ ID NO: 70, SEQ ID NO: 72, SEQ ID NO: 74, SEQ ID NO: 76, SEQ ID NO: 78, SEQ ID NO: 80, SEQ ID NO 82, SEQ ID NO: 84, SEQ ID NO: 86, SEQ ID NO: 88, SEQ ID NO: 90, SEQ ID NO: 92, SEQ ID NO: 94, SEQ ID NO: 96, SEQ ID NO: 98, SEQ ID NO: 114, SEQ ID NO: 116 , SEQ ID NO: 118, SEQ ID NO: 120, or a subsequence thereof.

42. The method of any of claims 1-41, wherein the method further comprises in step a) contacting the test polypeptide with a dimerization molecule, thereby permitting dimerization of the first portion of the RNA modifying polypeptide domain and the second portion of the RNA modifying polypeptide domain to form a functional RNA modifying polypeptide domain.

43. The method of any of the preceding claims, wherein the RNA is selected from the group comprising or consisting of: mRNA, tRNA, rRNA, snRNA, snoRNA, miRNA, piRNA, siRNA.

44. The method of any of the preceding claims, wherein: a) the first query RNA is a natural RNA, optionally an RNA isolated from a cell, a virus, or the environment; or b) the first query RNA is a synthetic RNA.

45. The method of any of the preceding claims, wherein the modification in the first test query RNA nucleic acid is detectable by sequencing.

46. The method of any of the preceding claims, wherein detecting the presence or absence of at least one modification step b) comprises:i) performing reverse transcription on at least a portion of the modified first test query RNA nucleic acid obtained in (a) to obtain a first test cDNA molecule.

47. The method of claim 46, wherein detecting the presence or absence of at least one modification in step b) further comprises: ii) sequencing at least a portion of the first test cDNA molecule.

48. The method of claim 47, wherein detecting the presence or absence of at least one modification in step b) further comprises: iii) detecting the presence or absence of a mutation at at least one position in the sequence obtained from the first test cDNA molecule, thereby indicating the presence or absence of a modification at the at least one corresponding position of the first test query RNA nucleic acid.

49. The method of any of the preceding claims, where the modification is deamination of an adenosine base present in the query RNA nucleic acid to an inosine base.

50. The method of claims 48-49, wherein the mutation detected at at least one position in the first test cDNA molecule is a T>C transition mutation, thereby indicating the presence of an inosine base at the at least one corresponding position of the first test query RNA nucleic acid.

51. The method of claims 2-50, wherein generating a modification profile comprises: iii) detecting the presence or absence of a mutation at each position in the sequence obtained from the first test cDNA molecule, thereby indicating the presence or absence of a modification at each corresponding position of the first test query RNA nucleic acid.

52. The method of claims 2-51, wherein the presence or location of one or more binding sites of the query polypeptide on the query RNA nucleic acid is indicated by the presence of a modification-enriched portion of the first query RNA nucleic acid.

53. A method for identifying a binding interaction between a query polypeptide and at least one query RNA nucleic acid of a plurality of query RNA nucleic acids, the method comprising: a) contacting a plurality of query RNA nucleic acids with a test polypeptide, wherein the test polypeptide comprises the query polypeptide or a fragment thereof; andi) an RNA modifying domain or fragment thereof capable of modifying RNA; or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; optionally wherein the test polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNA ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein thefirst affinity domain is capable of binding to the second affinity domain; wherein where said test polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a plurality of first test query RNA nucleic acids; and b) detecting the presence or absence of at least one modification in at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids; and c) determining that there is a binding interaction between the query polypeptide and the at least one query RNA nucleic acid of the plurality of RNA nucleic acid when a modification is detected in the at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids.

54. A method for identifying one or more binding sites of a query polypeptide on at least one of a plurality of RNA nucleic acids, the method comprising a) contacting a plurality of query RNA nucleic acids with a test polypeptide, wherein the test polypeptide comprises the query polypeptide or a fragment thereof; and i) an RNA modifying domain or fragment thereof capable of modifying RNA; or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein:the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain; or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; optionally wherein the test polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNA; ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; wherein where said test polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; orwherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a plurality of test query RNA nucleic acid; b) detecting the presence or absence of at least one modification in at least one test query RNA nucleic acid of the plurality of first query RNA nucleic acids and generating a modification profile for said at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids; and c) determining one or more binding sites of the query polypeptide on the at least one query RNA nucleic acid of the plurality of query RNA nucleic acids using the modification profile.

55. The method of claims 53-54, wherein the query polypeptide, RNA modifying polypeptide, recruitment module and / or query RNA is the query polypeptide, fusion polypeptide, polypeptide capable of modifying RNA, recruitment module and / or query RNA as defined in any of claims 3-44.

56. The method of any of claims 53-55, wherein the modification in the at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids is detectable by sequencing.

57. The method of claims 53-56, wherein detecting the presence or absence of at least one modification step b) comprises: i) performing reverse transcription on at least a portion of at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids obtained in (a) to obtain at least one test cDNA molecule; or performing reverse transcription on at least a portion of each test query RNA nucleic acid of the plurality of test query RNA nucleic acids obtained in (a) to obtain a plurality of test cDNA molecules.

58. The method of claim 57, wherein detecting the presence or absence of at least one modification in step b) further comprises: ii) sequencing at least a portion of the at least one test cDNA molecule; orsequencing at least a portion of each test cDNA molecule of the plurality of cDNA test molecules.

59. The method of claim 58, wherein detecting the presence or absence of at least one modification in step b) further comprises: iii) detecting the presence or absence of a mutation at at least one position in the sequence obtained from the at least one test cDNA molecule, thereby indicating the presence or absence of a modification at the at least one corresponding position of the corresponding at least one test query RNA nucleic acid; or detecting the presence or absence of a mutation at at least one position in the sequence obtained from each test cDNA molecule of the plurality of test cDNA molecules, thereby indicating the presence or absence of a modification at the at least one corresponding position of the corresponding at least one test query RNA nucleic acid.

60. The method of claims 53-59, where the modification is deamination of an adenosine base comprised by the query RNA nucleic acid to an inosine base.

61. The method of claims 7-60, wherein the mutation detected at at least one position in the first test cDNA molecule is a T>C transition mutation, thereby indicating the presence of an inosine base at the at least one corresponding position of the first test query RNA nucleic acid.

62. The method of claims 53-61, wherein generating a modification profile comprises: iii) detecting the presence or absence of a mutation at each position in the sequence obtained from the at least one test cDNA molecule of the plurality of test cDNA molecules, thereby indicating the presence or absence of a modification at each corresponding position of the at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids; or detecting the presence or absence of a mutation at each position in the sequence obtained from each test cDNA molecule of the plurality of test cDNA molecules, thereby indicating the presence or absence of a modification at each corresponding position of each test query RNA nucleic acid of the plurality of test query RNA nucleic acids.

63. The method of claims 53-62, wherein the presence or location on the query RNA nucleic acid of the binding interaction between the query polypeptide and a query RNA nucleic of the plurality of test query RNA nucleic acids is indicated by the presence of amodification-enriched portion of the test query RNA nucleic acid of the plurality of test query RNA nucleic acids.

64. The method of claims 52-63, wherein: a) each query RNA nucleic acid of the plurality of query RNA nucleic acids is identical; b) each query RNA nucleic acid of the plurality of query RNA nucleic acids is unique; or c) each query RNA nucleic acid of the plurality of query RNA nucleic acids is different from at least one other query RNA nucleic acid of the plurality of first query RNA nucleic acids; or c) at least one query RNA nucleic acid of the plurality of query RNA nucleic acids is different from at least one other query RNA nucleic acid of the plurality of query RNA nucleic acids.

65. The method of claims 52-64, wherein the plurality of query RNA nucleic acids comprises or consists the transcriptome of a cell.

66. The method of claim 65, wherein the cell is a eukaryotic cell, a bacterial cell, or an archaeal cell.

67. The method of claim 66, wherein: a) the eukaryotic cell is a human cell or a yeast cell; and / or b) the bacterial cell is an E. coli cell.

68. The method of any of the preceding claims, wherein the method is an in vitro method, optionally a cell-free method.

69. The method of any of the preceding claims, wherein the method is an in vivo method.

70. The method of claim 69, wherein the in vivo method is performed in a cell.

71. The method of claim 70, wherein the method comprises: a) expressing: i) the test polypeptide; ii) the RNA modifying domain or fragment thereof;iii) a first portion of an RNA modifying domain and / or a corresponding second portion of the RNA modifying domain; iv) first query RNA nucleic acid; v) recruitment module comprising a first affinity domain; vi) RNA modifying domain or fragment thereof comprising an affinity domain and / or vii) plurality of first query RNA nucleic acids in the cell; and / or b) delivering: i) the test polypeptide; ii) the RNA modifying domain or fragment thereof; iii) a first portion of an RNA modifying domain and / or a corresponding second portion of the RNA modifying domain; iv) first query RNA nucleic acid; v) recruitment module comprising a first affinity domain; vi) RNA modifying domain or fragment thereof comprising an affinity domain and / or vii) plurality of first query RNA nucleic acids v) plurality of first query RNA nucleic acids to the cell.

72. The method of claims 69-71, wherein where the RNA modifying domain of the test polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, the method further comprises expressing the corresponding second portion of the RNA modifying domain in the same cell.

73. The method of claim 72, wherein the first portion of an RNA modifying domain that is capable of modifying RNA and the corresponding second portion of the RNA modifying domain: a) are expressed from the same transcript; or b) are each expressed from an independent transcript.

74. The method of claims 71-73, wherein the test polypeptide, first query RNA nucleic acid, recruitment module, and / or plurality of query RNA nucleic acids are each expressed from one or more expression cassettes comprising a nucleotide sequence encoding: a) the RNA modifying polypeptide or a fragment thereof, optionally wherein the RNA modifying polypeptide is a fusion polypeptide;b) the fusion polypeptide; c) the first query RNA nucleic acid; d) the recruitment module; and / or d) the plurality of first query RNA nucleic acids.

75. The method of claim 74, wherein each of the nucleotide sequences encoding: a) the RNA modifying polypeptide or a fragment thereof, optionally wherein the RNA modifying polypeptide is a fusion polypeptide; b) the fusion polypeptide; c) the first query RNA nucleic acid; d) the recruitment module; and / or d) the plurality of first query RNA nucleic acids are operably linked to a promoter in the cassette, optionally wherein the promoter is selected from the group comprising or consisting of: a CMV promoter; an EF1a promoter; an SV40 promoter; a PGK promoter; a CAG promoter; a minimal promoter; or any combination thereof.

76. The method of claim 75, wherein the promoter is an inducible promoter.

77. The method of any of claims 75-76, wherein the one or more cassettes further comprises an operator sequence, optionally wherein the operator sequence is selected from the group comprising or consisting of: TetO; CuO.

78. The method of any of claims 75-77, wherein expression from the promoter is controlled by an inducible expression system, optionally wherein the inducible expression system is selected from the group comprising or consisting of: a) a Tet-on system, wherein expression of the test polypeptide, first query RNA nucleic acid, recruitment module and / or plurality of query RNA nucleic acids is repressed in the absence of the controller molecule and is induced in the presence of a controller molecule; b) a Tet-off system, wherein expression of the test polypeptide, first query RNA nucleic acid, recruitment module and / or plurality of query RNA nucleic acids is repressed in the presence of the controller molecule and is induced in the absence of the controller molecule; c) a tet-repressor system, wherein expression of the test polypeptide, first query RNA nucleic acid, recruitment module and / or plurality of query RNA nucleicacids repressed in the presence of the controller molecule and is induced in the absence of the controller molecule; or d) a cumate expression system, wherein expression of the test polypeptide, first query RNA nucleic acid, recruitment module and / or plurality of query RNA nucleic acids is repressed in the presence of the inducer molecule and induced in the absence of the controller molecule.

79. The method of any of claims 74-78, wherein the controller molecule is selected from the group comprising or consisting of: tetracycline; doxycycline; cumate.

80. The method of any of claims 74-79, wherein the one or more cassettes is encoded by a vector comprised by the cell, optionally wherein the vector is a plasmid, a lentiviral vector, a landing pad vector.

81. The method of claims 69-80, wherein: a) the test polypeptide; b) the RNA modifying domain or fragment thereof; c) a first portion of an RNA modifying domain and / or a corresponding second portion of the RNA modifying domain; and / or d) recruitment module; are delivered to the cell in protein form or RNA form, optionally as mRNA.

82. A method for identifying a binding interaction between a query polypeptide and a query RNA nucleic acid in a cell, the method comprising: a) expressing in the cell a first query RNA nucleic acid and a test polypeptide wherein the test polypeptide comprises the query polypeptide or a fragment thereof; and i) an RNA modifying domain or fragment thereof capable of modifying RNA, or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain;or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; optionally wherein the RNA modifying polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i) a RNA modifying polypeptide domain capable of modifying RNA; ii) a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; wherein where said RNA modifying polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted underconditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a first test query RNA nucleic acid in the cell; and b) detecting the presence or absence of at least one modification in the first test query RNA nucleic acid; and c) determining that there is a binding interaction between the polypeptide and first query RNA nucleic acid when a modification is detected in the first test query RNA nucleic acid.

83. A method for identifying one or more binding sites of a query polypeptide on query RNA nucleic acid in a cell, the method comprising: a) expressing in the cell a first query RNA nucleic acid and a test polypeptide wherein the test polypeptide comprises: i) the query polypeptide or a fragment thereof; and ii) an RNA modifying domain or fragment thereof capable of modifying RNA, or a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain or a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain;optionally wherein the RNA modifying polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNA; ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; wherein where said RNA modifying polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a first test query RNA nucleic acid; b) detecting the presence or absence of at least one modification in the first test query RNA nucleic acid and generating a modification profile for the first test query RNA nucleic acid; and c) determining one or more binding sites of the query polypeptide on the first query RNA nucleic acid using the modification profile.

84. The method of claims 82-83, wherein the query polypeptide, RNA modifying polypeptide, and / or query RNA is the query polypeptide, RNA modifying polypeptide, and / or query RNA as defined in any of claims 3-44.

85. The method of any of claims 82-84, wherein the modification in the at least one first test query RNA nucleic acid of the plurality of first test query RNA nucleic acid is detectable by sequencing.

86. The method of any of claims 82-85, wherein detecting the presence or absence of at least one modification step b) comprises the steps as defined in any of claims 43-50.

87. The method of any of claims 82-86, wherein generating a modification profile comprises the steps as defined in any of claims 51-52.

88. The method of claims 82-87, wherein the presence or location on the RNA nucleic acid of the binding interaction between the query polypeptide and the first query RNA nucleic acid is indicated by the presence of a modification-enriched portion of the first query RNA nucleic acid.

89. A method for identifying a binding interaction between a query polypeptide and at least one RNA nucleic acid of a plurality of RNA nucleic acids in a cell, the method comprising: a) expressing in the cell a plurality of query RNA nucleic acids with a test polypeptide wherein the test polypeptide comprises: i) the query polypeptide or a fragment thereof; and ii) an RNA modifying domain or fragment thereof capable of modifying RNA, or a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domainor a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; optionally wherein the RNA modifying polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNA; ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; wherein where said RNA modifying polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted underconditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a plurality of test query RNA nucleic acids; and b) detecting the presence or absence of at least one modification in at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids; and c) determining that there is a binding interaction between the query polypeptide and the at least one RNA nucleic acid of the plurality of RNA nucleic acid when a modification is detected in the at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids.

90. A method for identifying one or more binding sites of a query polypeptide on at least one RNA nucleic acid of a plurality of nucleic acids in a cell, the method comprising: a) expressing in the cell a plurality of query RNA nucleic acids and a test polypeptide, wherein the test polypeptide comprises the query polypeptide or a fragment thereof; and i) an RNA modifying domain or fragment thereof capable of modifying RNA, or ii) a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain or iii) a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain;optionally wherein the RNA modifying polypeptide is a fusion protein comprising the query polypeptide or a fragment thereof and: i. a RNA modifying polypeptide domain capable of modifying RNA or ii. a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain; or iii. a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; wherein where said RNA modifying polypeptide comprises a first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, said contacting is conducted under conditions where said first portion and said corresponding second portion are brought into proximity with one another to form a functional RNA modifying domain; or wherein where said test polypeptide comprises a recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, said contacting is conducted under conditions where a complex is formed between said recruitment module and said RNA modifying domain or fragment thereof; thereby generating a plurality of test query RNA nucleic acids; b) detecting the presence or absence of at least one modification in at least one first test query RNA nucleic acid of the plurality of test query RNA nucleic acids and generating a modification profile for said at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acids; andc) determining one or more binding sites of a query polypeptide on at least one RNA nucleic acid of the plurality of RNA nucleic acids using the modification profile.

91. The method of claims 89-90, wherein the query polypeptide, RNA modifying polypeptide, and / or query RNA is the query polypeptide, RNA modifying polypeptide, and / or RNA as defined in any of claims 3-44.

92. The method of any of claims 89-91, wherein the modification in the at least one test query RNA nucleic acid of the plurality of test query RNA nucleic acid is detectable by sequencing.

93. The method of any of claims 89-92, wherein detecting the presence or absence of at least one modification step b) comprises the steps as defined in any of claims 59-63.

94. The method of any of claims 90-93, wherein generating a modification profile comprises the steps as defined in any of claims 63-64.

95. The method of claims 90-94, wherein the presence or location on the RNA nucleic acid of the binding interaction between the query polypeptide and a query RNA nucleic of the plurality of test query RNA nucleic acids is indicated by the presence of a modification- enriched portion of the test query RNA nucleic acid of the plurality of test query RNA nucleic acids.

96. The method of claims 92-95, wherein: a) each query RNA nucleic acid of the plurality of query RNA nucleic acids is identical; b) each query RNA nucleic acid of the plurality of query RNA nucleic acids is unique; or c) each query RNA nucleic acid of the plurality of query RNA nucleic acids is different from at least one other query RNA nucleic acid of the plurality of query RNA nucleic acids; or c) at least one query RNA nucleic acid of the plurality of query RNA nucleic acids is different from at least one other query RNA nucleic acid of the plurality of query RNA nucleic acids.

97. The method of claims 90-96, wherein the plurality of query RNA nucleic acids comprises or consists the transcriptome of a cell.

98. The method of claims 83-97, wherein the cell is a eukaryotic cell, a bacterial cell, or an archaeal cell.

99. The method of claim 98, wherein: a) the eukaryotic cell is a human cell or a yeast cell; and / or b) the bacterial cell is an E. coli cell.

100. The method of any of claims 83-99, wherein the cell comprises: a) a nucleotide sequence encoding the first query RNA or plurality of query RNAs; b) a nucleotide sequence encoding the test polypeptide; c) a nucleotide sequence encoding the query polypeptide; d) a nucleotide sequence encoding the RNA modifying domain or fragment thereof; e) a nucleotide sequence encoding the first portion of an RNA modifying domain and / or a corresponding second portion of the RNA modifying domain; and / or f) a nucleotide encoding a recruitment module.

101. The method of claim 100, wherein: a) the nucleotide sequence encoding the first query RNA or plurality of query RNAs; b) the nucleotide sequence encoding the test polypeptide; c) the nucleotide sequence encoding the query polypeptide; d) the nucleotide sequence encoding the RNA modifying domain or fragment thereof; e) the nucleotide sequence encoding the first portion of an RNA modifying domain and / or a corresponding second portion of the RNA modifying domain; f) a nucleotide encoding a recruitment module are each operably linked to a promoter in the expression cassette; optionally wherein the promoter is selected from the group comprising or consisting of: a CMV promoter; an EF1a promoter; an SV40 promoter; a PGK promoter; a CAG promoter; a minimal promoter; or any combination thereof.

102. The method of claim 101, wherein the promoter is an inducible promoter.

103. The method of claims 100-102, wherein the cassette further comprises an operator sequence, optionally wherein the operator sequence is selected from the group comprising or consisting of: TetO; CuO.

104. The method of any of claims 100-103, wherein expression from the promoter is controlled by an inducible expression system, optionally wherein the inducible expression system is selected from the group comprising or consisting of: a) a Tet-on system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in the absence of the controller molecule and is induced in the presence of a controller molecule; b) a Tet-off system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in the presence of the controller molecule and is induced in the absence of the controller molecule; c) a tet-repressor system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids repressed in the presence of the controller molecule and is induced in the absence of the controller molecule; or d) a cumate expression system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in the presence of the inducer molecule and induced in the absence of the controller molecule..

105. The method of any of claims 100-104, wherein the controller molecule is selected from the group comprising or consisting of: tetracycline; doxycycline; and cumate.

106. The method of any of claims 83-105, wherein expressing in a cell the first query RNA nucleic acid, plurality of query RNA nucleic acids, RNA modifying polypeptide and / or query polypeptide comprises contacting the cell with an inducer molecule selected from the group comprising or consisting of: tetracycline; doxycycline; and cumate.

107. The method of any of claims 83-106, wherein the cell further comprises a selectable marker, optionally wherein the selectable marker is a fluorescent selectable marker, optionally wherein the fluorescent selectable marker is selected from the group comprising or consisting of: GFP, YFP, and RFP.

108. The method of any of claims 100-107, wherein the cassette and / or selectable marker are encoded by a vector, optionally wherein the vector is selected from the group comprising or consisting of: a plasmid, a lentiviral vector, and / or an mRNA vector.

109. The method of any of claims 83-108, wherein the method further comprises in step a) exposing the cell to a dimerization inducing molecule, optionally wherein the dimerization inducing molecule is selected from the group comprising or consisting of: rifampicin; Mandipropamid (Mandi); abscisic acid, and gibberellic acid.

110. The method of any of claims 83-109, wherein the method further comprises in step b) isolating and / or purifying the first test query RNA nucleic acid or plurality of first test query RNA nucleic acids from the cell prior to reverse transcription.

111. An engineered RNA modifying polypeptide that is capable of modifying RNA, wherein the engineered RNA modifying polypeptide has an increased RNA editing efficiency and / or editing frequency compared to an RNA modifying polypeptide that is not engineered or that is a wild-type RNA modifying polypeptide.

112. The engineered RNA modifying polypeptide of claim 111, wherein the engineered RNA modifying polypeptide: a) comprises or consists an amino acid sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical SEQ ID NO: 5, SEQ ID NO: 13, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 5, SEQ ID NO: 13, or a subsequence thereof; optionally provided that residue 174 is a glutamine and residue 182 is a phenylalanine; and / or b) comprises or consists an amino acid sequence that is encoded by a nucleotide sequence that is: i) at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100 % identical to SEQ ID NO: 6, SEQ ID NO: 14, or a subsequence thereof; or ii) 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, or 100% identical to SEQ ID NO: 6, SEQ ID NO: 14, or a subsequence thereof; optionally provided that residue 174 of the amino acid sequence is a glutamine and residue 182 of the amino acid sequence is a phenylalanine.

113. The engineered RNA modifying polypeptide of any one of claim 111 or 112, wherein the engineered RNA modifying polypeptide has an improved editing efficiency and / or editing frequency compared to:a) an RNA modifying polypeptide comprising or consisting an amino acid sequence that is SEQ ID NO: 3, SEQ ID NO: 7, SEQ ID NO: 11, SEQ ID NO: 109, and / or SEQ ID NO: 111; optionally compared to an RNA modifying polypeptide comprising or consisting an amino acid sequence that is SEQ ID NO: 3, SEQ ID NO: 7, SEQ ID NO: 11, SEQ ID NO: 109, and / or SEQ ID NO: 111 that does not have a glutamine at residue 174 and / or a phenylalanine at residue 182; and / or b) an RNA modifying polypeptide comprising or consisting an amino acid sequence that is encoded by a nucleotide sequence that is SEQ ID NO: 4, SEQ ID NO: 8, SEQ ID NO: 12, SEQ ID NO: 110, and / or SEQ ID NO: 112; optionally compared to an RNA modifying polypeptide comprising or consisting an amino acid sequence that is encoded by a nucleotide sequence that is SEQ ID NO: 4, SEQ ID NO: 8, SEQ ID NO: 12, SEQ ID NO: 110, and / or SEQ ID NO: 112 that does not have a glutamine at residue 174 of the amino acid sequence and / or a phenylalanine at residue 182 of the amino acid sequence.

114. An expression cassette comprising: a) a nucleotide sequence encoding a first query RNA or plurality of query RNAs; b) a nucleotide sequence encoding the test polypeptide; c) a nucleotide sequence encoding a query polypeptide; d) a nucleotide sequence encoding the fusion polypeptide; e) a nucleotide sequence encoding the polypeptide capable of modifying RNA or a fragment thereof; and / or f) a nucleotide encoding a recruitment module wherein the query polypeptide, test polypeptide, fusion polypeptide, polypeptide capable of modifying RNA, recruitment module and / or RNA is the query polypeptide, fusion polypeptide, polypeptide capable of modifying RNA, and / or RNA as defined in any of claims 1-44; and / or g) a nucleotide sequence encoding an engineered RNA modifying polypeptide, wherein the engineered RNA modifying polypeptide is the RNA modifying polypeptide of any one of claims 111-113.

115. An expression cassette of claim 114, wherein the expression cassette further comprises a promoter; optionally wherein each of:a) the nucleotide sequence encoding the first query RNA or plurality of first query RNAs; b) the nucleotide sequence encoding the fusion polypeptide; c) the nucleotide sequence encoding the query polypeptide; d) the nucleotide sequence encoding a polypeptide capable of modifying RNA or a fragment thereof; e) the nucleotide sequence encoding a recruitment module; f) the nucleotide sequence encoding the test polypeptide; and / or g) the nucleotide sequence encoding the engineered RNA modifying polypeptide; are operably linked to said promoter.

116. The expression cassette of claims 114-115, wherein the promoter is selected from the group comprising or consisting of: a CMV promoter; an EF1a promoter; an SV40 promoter; a PGK promoter; a CAG promoter; a minimal promoter; or any combination thereof.

117. The expression cassette of claims 114-116, wherein the cassette further comprises an operator sequence, optionally wherein the operator sequence is selected from the group comprising or consisting of: TetO; and CuO.

118. The expression cassette of any of claims 114-117, wherein: a) the promoter is capable of driving the transcription and / or expression of a nucleotide sequence to which the promoter is operably linked in the presence of an controller molecule; and / or b) the promoter is not capable of driving the transcription and / or expression of a nucleotide sequence to which the promoter is operably linked in the absence of an controller molecule.

119. The method of any of claims 116-118, wherein expression from the promoter is controlled by an inducible expression system, optionally wherein the inducible expression system is selected from the group comprising or consisting of: a) a Tet-on system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in the absence of the controller molecule and is induced in the presence of a controller molecule; b) a Tet-off system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in thepresence of the controller molecule and is induced in the absence of the controller molecule; c) a tet-repressor system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids repressed in the presence of the controller molecule and is induced in the absence of the controller molecule; or d) a cumate expression system, wherein expression of the test polypeptide, first query RNA nucleic acid and / or plurality of query RNA nucleic acids is repressed in the presence of the inducer molecule and induced in the absence of the controller molecule..

120. The expression cassette of any of claims 114-119, wherein the controller molecule selected from the group comprising or consisting of: tetracycline; doxycycline; cumate .

121. A plurality of expression cassettes, wherein each expression cassette of the plurality of expression cassettes is an expression cassette as defined in any of claims 114-120.

122. A vector comprising the expression cassette of any of claims 114-120 or the plurality of expression cassettes of claim 121.

123. The vector of claim 122, wherein the vector further comprises a selectable marker, optionally wherein the selectable marker is a fluorescent selectable marker, optionally wherein the fluorescent selectable marker is selected from the group comprising or consisting of: GFP, YFP, and RFP.

124. The vector of claims 122-123, wherein the vector is a vector selected from the group comprising or consisting of: a plasmid, a lentiviral vector, and / or an mRNA vector.

125. A plurality of vectors, wherein each vector of the plurality of vectors is a vector as defined in any of claims 112-124.

126. A cell comprising the expression cassette of any of claims 114-120; the plurality of expression cassettes of claim 121; the vector of claims 122-124; and / or the plurality of vectors of claim 125.

127. The cell of claim 126, wherein the cell is a eukaryotic cell, a bacterial cell, or an archaeal cell.

128. The cell claim 127, wherein: a) the eukaryotic cell is a human cell or a yeast cell; and / or b) the bacterial cell is an E. coli cell.

129. A plurality of cells, wherein each cell of the plurality of cells is a cell as defined in any of claims 126-128.

130. A fusion polypeptide, wherein the fusion polypeptide is a fusion polypeptide as defined in any of claims 1-44.

131. A library of fusion polypeptides, wherein each fusion polypeptide is as defined in claim 130.

132. A library of RNA nucleic acids, wherein each RNA nucleic acid is as defined in any of claims 1-44.

133. A kit comprising any one or more of: a) a query polypeptide or a fragment thereof, query RNA nucleic acid, first query RNA nucleic acid, plurality of query RNA nucleic acids, test polypeptide, polypeptide capable of modifying RNA, a first portion of an RNA modifying polypeptide domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, or a fragment thereof, or fusion polypeptide as defined in any of claims 1-110 and 130; b) an engineered RNA modifying polypeptide as defined in any of claims 111- 113; c) an expression cassette as defined in any of claims 114-120; d) a plurality of expression cassettes as defined in claim 121; e) a vector as defined in any of claims 122-124; f) a plurality of vectors as defined in claim 125; g) a cell as defined in any of claims 126-128; h) a plurality of cells as defined in claim 129; i) a library of fusion polypeptides as defined in claim 131; and / or j) a library of RNA nucleic acids as defined in claim 132.

134. A method of identifying an improved test polypeptide, wherein the test polypeptide is a test polypeptide as defined in any of the preceding claims, the method comprising: a) preparing at least a reference test polypeptide and a candidate test polypeptide;b) performing the method of any of claims 1-110 on the reference test polypeptide and candidate test polypeptide; and c) comparing the performance of the reference test polypeptide and candidate test polypeptide; and d) determining whether the candidate test polypeptide is an improved test polypeptide.

135. The method of claim 134, wherein b) determining the performance of the reference test polypeptide and candidate test polypeptide comprises: i) determining the editing efficiency of the reference test polypeptide and candidate test polypeptide; ii) determining the editing frequency of the reference test polypeptide and candidate test polypeptide; iii) determining the “on target” editing frequency of the reference test polypeptide and candidate test polypeptide; iv) determining the “off-target” editing frequency of the reference test polypeptide and candidate test polypeptide; and / or v) determining the ratio of “on-target” to “off-target” editing of of the reference test polypeptide and candidate test polypeptide.

136. The method of claim 134 or 135, where c) comparing the performance of the reference test polypeptide and candidate test polypeptide comprises: i) comparing the editing efficiency of the reference test polypeptide to the editing efficiency of the candidate test polypeptide; ii) comparing the editing frequency of the reference test polypeptide to the editing frequency of the candidate test polypeptide; iii) comparing the “on-target” editing frequency of the reference test polypeptide to the “on-target” editing frequency of the candidate test polypeptide; iv) comparing the “off-target” editing frequency of the reference test polypeptide to the “off-target” editing frequence of the candidate test polypeptide; and / or v) comparing the ratio of “on-target” to “off-target” editing of the reference test polypeptide to the ratio of “on-target” to “off-target” editing of candidate test polypeptide.

137. The method of any one of claims 134-136, wherein the candidate test polypeptide is determined to be an improved test polypeptide when:a) the candidate test polypeptide has a higher editing efficiency than the reference test polypeptide; b) the candidate test polypeptide has a higher editing frequence than the reference test polypeptide; c) the candidate test polypeptide has an higher “on-target” editing frequency than the reference test polypeptide; d) the candidate test polypeptide has a lower “off-target” editing frequency than the reference test polypeptide; and / or e) the candidate test polypeptide has higher “on-target” to “off-target” editing ratio than the reference test polypeptide.

138. The method of any one of claims 134-137, wherein: a) the candidate test polypeptide comprises a different query polypeptide to the reference test polypeptide; b) the candidate test polypeptide comprises a different: i) RNA modifying domain or fragment thereof capable of modifying RNA; ii) first portion of an RNA modifying domain that is capable of modifying RNA when brought into proximity with a corresponding second portion of the RNA modifying domain, optionally wherein: the RNA modifying domain or fragment thereof is an RNA modifying polypeptide domain; and the first portion of an RNA modifying domain is a first portion of an RNA modifying polypeptide domain; iii) recruitment module capable of recruiting an RNA modifying domain or fragment thereof capable of modifying RNA, wherein the recruitment module comprises a first affinity domain and the RNA modifying domain or fragment thereof further comprises a second affinity domain, and wherein the first affinity domain is capable of binding to the second affinity domain; or iv) flexible linker to the reference test polypeptide; c) the candidate test polypeptide is N-terminally fused to the RNA modifying domain, first portion of an RNA modifying domain or second portion of an RNA modifying domain, or recruitment domain; and the reference test polypeptide is C- terminally fused to the RNA modifying domain, first portion of an RNA modifying domain or second portion of an RNA modifying domain, or recruitment domain;d) the candidate test polypeptide is C-terminally fused to the RNA modifying domain, first portion of an RNA modifying domain or second portion of an RNA modifying domain, or recruitment domain; and the reference test polypeptide is N- terminally fused to the RNA modifying domain, first portion of an RNA modifying domain or second portion of an RNA modifying domain, or recruitment domain; e) the candidate test polypeptide and reference test polypeptide are N- terminally fused to the RNA modifying domain, first portion of an RNA modifying domain or second portion of an RNA modifying domain, or recruitment domain; and / or f) the candidate test polypeptide and reference test polypeptide are N- terminally fused to the RNA modifying domain, first portion of an RNA modifying domain or second portion of an RNA modifying domain, or recruitment domain.

139. The method of any one of claims 134-138, wherein the candidate test polypeptide is mutated compared to the reference test polypeptide, optionally wherein the RNA modifying domain or fragment thereof is a mutant RNA modifying domain or fragment thereof and / or an engineered RNA modifying domain or fragment thereof.

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