St1CAS9 compositions and methods for modulating a genome

Abstract

The disclosure provides, e.g., compositions, systems, and methods for targeting, editing, modifying, or manipulating a host cell's genome at one or more locations in a DNA sequence in a cell, tissue, or subject.

Description

CROSS-REFERENCE TO RELATED APPLICATIONS This application claims priority to U.S. Provisional Patent Application No. 63 / 565,398, filed March 14, 2024, and U.S. Provisional Patent Application No. 63 / 642,617, filed May 3, 2024, the titles of which are “ST1CAS9 COMPOSITIONS AND METHODS FOR MODULATING A GENOME” and the entireties of which are incorporated herein by reference. SEQUENCE LISTING The instant application contains a Sequence Listing which has been submitted electronically in XML file foimat and is hereby incorporated by reference in its entirety. Said XML copy, created on March 14, 2025, is named 2017469_0039_SL.xml and is 16,341,326 bytes in size. BACKGROUND Integration of a nucleic acid of interest into a genome occurs at low frequency and with little site specificity, in the absence of a specialized protein to promote the insertion event. Some existing approaches, like CRISPR / Cas9, are more suited for small edits that rely on host repair pathways, and are less effective at integrating longer sequences. Other existing approaches, like Cre / loxP, require a first step of inserting a loxP site into the genome and then a second step of inserting a sequence of interest into the loxP site. There is a need in the ait for improved compositions (e.g., proteins and nucleic acids) and methods for inserting, altering, or deleting sequences of interest in a genome. SUMMARY OF THE INVENTION This disclosure relates to novel compositions, systems, and methods for altering a genome at one or more locations in a host cell, tissue or subject, in vivo or in vitro. Features of the compositions or methods can include one or more of the following enumerated embodiments. Enumerated Embodiments 1. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain; an Cas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker comprises an amino acid sequence of Table 6, or a sequence having at least 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 2. The gene modifying polypeptide of embodiment 1, wherein the Cas9 nickase domain is a StlCas9 nickase domain. 3. The gene modifying polypeptide of embodiment 2, wherein the StlCas9 nickase domain comprises a sequence according to SEQ ID NO: 10208, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto. 4. The gene modifying polypeptide of any of embodiments 1-3, wherein the retroviral RT domain has an amino acid sequence of Table 1, or an amino acid sequence with at least 90%, 95%, 97%, 98%, or 99% identity thereto. 5. The gene modifying polypeptide of any of embodiments 1-4, wherein the linker comprises an amino acid sequence of WQAAESYEV (SEQ ID NO: 10154). 6. The gene modifying polypeptide of any of embodiments 1-4, wherein the linker comprises an amino acid sequence of AEIKYDGV (SEQ ID NO: 10162). 7.     The gene modifying polypeptide of any of embodiments 1-4, wherein the linker comprises an amino acid sequence of FGMVQGMSTRKGTVVFLDNILEETK (SEQ ID NO: 10166). 8. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain having an amino acid sequence of Table 1, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker comprises an amino acid sequence of Table 5, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 9. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain and the linker are from the same row of Table 10. 10.    The gene modifying polypeptide of embodiment 8 or 9, wherein the retroviral RT domain and the linker arc from the same row of Table 9. 11. The gene modifying polypeptide of any of embodiments 8-10, wherein the retroviral RT domain and the linker are from the same row of Table 8. 12. The gene modifying polypeptide of any of embodiments 8-11, wherein the retroviral RT domain and the linker are from the same row of Table 7. 13.    The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10316, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10301, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 14.    The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10317, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10302, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 15.    The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10318, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10303, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 16.    The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10319, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10304, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 17. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10320, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10305, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 18. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10321, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10306, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1,2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 19. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10322, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10307, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 20. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10323, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10308, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 21. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10324, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10309, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%>, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 22. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10325, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10310, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 23. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10326, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10311, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%>, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 24. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10327, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10312, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 25. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10328, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10313, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 26. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10329, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10314, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1,2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 27. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10330, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10315, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 28. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10316, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10301, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 29. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10317, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10302, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 30. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10318, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10303, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 31. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10319, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10304 or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 32. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10320, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10305, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 33. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10321, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10306, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 34. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10322, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10307, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 35. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10323, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10308, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 36. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10324, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10309, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 37. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10325, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10310, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 38. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10326, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10311, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 39. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10327, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10312, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 40. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10328, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10313, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 41. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10329, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10314, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 42. The gene modifying polypeptide of embodiment 8, wherein: the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10330, or an amino acid sequence with at least 95% identity thereto, and the linker has an amino acid sequence of SEQ ID NO: 10315, or an amino acid sequence with at least 90% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 43. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10316 and the linker has an amino acid sequence of SEQ ID NO: 10301. 44. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10317 and the linker has an amino acid sequence of SEQ ID NO: 10302. 45. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10318 and the linker has an amino acid sequence of SEQ ID NO: 10303. 46. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10319 and the linker has an amino acid sequence of SEQ ID NO: 10304. 47. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10320 and the linker has an amino acid sequence of SEQ ID NO: 10305. 48. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10321 and the linker has an amino acid sequence of SEQ ID NO: 10306. 49. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 100322 and the linker has an amino acid sequence of SEQ ID NO: 10307. 50. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10323 and the linker has an amino acid sequence of SEQ ID NO: 10308. 51. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10324 and the linker has an amino acid sequence of SEQ ID NO: 10309. 52. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10325 and the linker has an amino acid sequence of SEQ ID NO: 10310. 53. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10326 and the linker has an amino acid sequence of SEQ ID NO: 10311. 54. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10327 and the linker has an amino acid sequence of SEQ ID NO: 10312. 55. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10328 and the linker has an amino acid sequence of SEQ ID NO: 10313. 56. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10329 and the linker has an amino acid sequence of SEQ ID NO: 10314. 57. The gene modifying polypeptide of embodiment 8, wherein the retroviral RT domain has an amino acid sequence of SEQ ID NO: 10330 and the linker has an amino acid sequence of SEQ ID NO: 10315. 58. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a PERV RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10301, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 59. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a BAEVM RT domain; an Stl Cas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10302, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 60. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a WMSV RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10303, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 61. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a PERV RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10304, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 62. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a PERV RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10305, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 63. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a MLVMS RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10306, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 64. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a PERV RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10307, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 65. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a BAEVM RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10308, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 66. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a AVIRE RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10309, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 67. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a BAEVM RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10310, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 68. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a XMRV6 RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10311, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 69. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a BAEVM RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10312, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 70. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a AVIRE RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10313, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 71. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a PERV RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10314, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 72. A gene modifying polypeptide comprising: a retroviral reverse transcriptase (RT) domain which is a MLVFF RT domain; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10315, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 73.    A retroviral reverse transcriptase (RT) domain, wherein the RT domain: a) is a HTLV2_P03363 domain; or b) comprises an amino acid sequence of HLPPPPQVDQFPLNLPERLQALNDLVSKALEAGHIEPYSGPGNNPVFPVKKPNGKWRFIH DLRATNAITTTLTSPSPGPPDLTSLPTALPHLQTIDLTDAFFQIPLPKQYQPYFAFTIPQPCN YGPGTRYAWTVLPQGFKNSPTLFEQQLAAVLNPMRKMFPTSTIVQYMDDILLASPTNEE LQQLSQLTLQALTTHGLPISQEKTQQTPGQIRFLGQVISPNHITYESTPTIPIKSQWTLTEL QVILGEIQWVSKGTPILRKHLQSLYSALHGYRDPRACITLTPQQLHALHAIQQALQHNCR GRLNPALPLLGLISLSTSGTTSVIFQPKQNWPLAWLHTPHPPTSLCPWGHLLACTILTLDK YTLQHYGQLCQSFHHNMSKQALCDFLRNSPHPSVGILIHHMGRFHNLGSQPSGPWKTLL HLPTLLQEPRLLRPIFTLSPVVLDTAPCLFSDGSPQKAAYVLWDQTILQQDITPLPSHETH SAQKGELLALICGLRAAKPWPSLNIFLDSKYLIKYLHSLAIGAFLGTSAHQTLQAALPPLL QGKTIYLHHVRSHTNLPDPISTFNEYTDSLILAPLVPL (SEQ ID NO: 10223), or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto. 74. A gene modifying polypeptide comprising: the RT domain of embodiment 100, a Cas9 nickase domain (e.g., as described herein), wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker (e.g., as described herein) disposed between the RT domain and the Cas9 nickase domain, optionally wherein the linker comprises an amino acid sequence of Table 6, or a sequence having at least 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto. 75. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises the amino acid sequence of a linker as listed in Table 7, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 76. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises the amino acid sequence of an RT as listed in Table 7, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 77. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises: (i) the amino acid sequence of a linker as listed in a row of Table 7, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and (ii) the amino acid sequence of an RT as listed in the same row of Table 7, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 78. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises an amino acid sequence as listed in column 6 of Table 7, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 79. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises the amino acid sequence of any one of SEQ ID NOs: 12001 -21744, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 80. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises the amino acid sequence of a linker as listed in Table 8, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 81. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises the amino acid sequence of an RT as listed in Table 8, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 82. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 1 of Table 8, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 2 in the same row of Table 8, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 83. The gene modifying polypeptide of any of embodiments 1-81, wherein the gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 3 of Table 8, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 4 in the same row of Table 8, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 84. The gene modifying polypeptide of any of embodiments 1-81, wherein the gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 5 of Table 8, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 6 in the same row of Table 8, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 85. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises the amino acid sequence of a linker as listed in Table 9, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 86. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises the amino acid sequence of an RT as listed in Table 9, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 87. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 1 of Table 9, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 2 in the same row of Table 9, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 88. The gene modifying polypeptide of any of embodiments 1-86, wherein the gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 3 of Table 9, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 4 in the same row of Table 9, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 89. The gene modifying polypeptide of any of embodiments 1-86, wherein the gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 5 of Table 9, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 6 in the same row of Table 9, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 90. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises the amino acid sequence of a linker as listed in Table 10, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 91. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises the amino acid sequence of an RT as listed in Table 10, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 92. The gene modifying polypeptide of any of the preceding embodiments, wherein the gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 1 of Table 10, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 2 of the same row of Table 10, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 93. The gene modifying polypeptide of any of embodiments 1-91, wherein the gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 4 of Table 10, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 5 of the same row of Table 10, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 94. The gene modifying polypeptide of any of embodiments 1-91, wherein the gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 7 of Table 10, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 8 of the same row of Table 10, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 95. The gene modifying polypeptide of any of embodiments 1-92, wherein the gene modifying polypeptide comprises an amino acid sequence as listed in column 3 of Table 10, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 96. The gene modifying polypeptide of any of embodiments 1 -91, or 93, wherein the gene modifying polypeptide comprises an amino acid sequence as listed in column 6 of Table 10, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 97. The gene modifying polypeptide of any of embodiments 1-91, or 94, wherein the gene modifying polypeptide comprises an amino acid sequence as listed in column 9 of Table 10, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. 98. The gene modifying polypeptide of any of the preceding embodiments, which comprises a nuclear localization signal (NLS). 99. The gene modifying polypeptide of any of the preceding embodiments, which comprises a first NLS which is N-terminal of the Cas9 nickase domain. 100. The gene modifying polypeptide of any of the preceding embodiments, which comprises an NLS which is C-terminal of the RT domain. 101. The gene modifying polypeptide of any of the preceding embodiments, which comprises a first NLS which is N-terminal of the Cas9 nickase domain and a second NLS which is C-terminal of the RT domain. 102. The gene modifying polypeptide of any of the preceding embodiments, which comprises a first NLS which is N-terminal of the Cas9 nickase domain, wherein the first NLS comprises the amino acid sequence of PAAKRVKLD (SEQ ID NO: 11095). 103. The gene modifying polypeptide of embodiment 102, wherein the first NLS comprises the amino acid sequence of PAAKRVKLDGG (SEQ ID NO: 10207). 104. The gene modifying polypeptide of any of the preceding embodiments, which comprises an NLS which is C-terminal of the RT domain and comprises the amino acid sequence of KRTADGSEFE (SEQ ID NO: 4650). 105. The gene modifying polypeptide of any of the preceding embodiments, which comprises an NLS which is C-terminal of the RT domain and comprises the amino acid sequence of KRTADGSEFEKRTADGSEFESPKKKAKVE (SEQ ID NO: 5349). 106. The gene modifying polypeptide of any of the preceding embodiments, which comprises an NLS which is C-terminal of the RT domain and comprises the amino acid sequence of KRTADGSEFESPKKKAKVE (SEQ ID NO: 4651). 107. The gene modifying polypeptide of any of the preceding embodiments, which comprises the amino acid sequence of SEQ ID NO: 10000, which comprises a first NLS and the Cas9 nickase domain. 108. The gene modifying polypeptide of any of the preceding embodiments, which comprises an NLS having the amino acid sequence according to SEQ ID NO: 4649. 109. The gene modifying polypeptide of any of the proceeding embodiments, which comprises a GG amino acid sequence between the Cas9 nickase domain and the linker. 110. The gene modifying polypeptide of embodiment 101, which comprises an AG amino acid sequence between the RT domain and the second NLS. 111. The gene modifying polypeptide of any of the preceding embodiments, which comprises a GG amino acid sequence between the linker and the RT domain. 112. The gene modifying polypeptide of any of the preceding embodiments, which has an amino acid sequence according to any one of SEQ ID NOs: 10001, 10011, 10018-10020, or 17001-21744, or an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto. 113. A nucleic acid molecule encoding a gene modifying polypeptide according to any of the preceding embodiments. 114. The nucleic acid molecule of embodiment 113, which comprises RNA. 115. A cell comprising: i) a gene modifying polypeptide of any of embodiments 1-112, or ii) a nucleic acid encoding the gene modifying polypeptide. 116. A system comprising: i) a gene modifying polypeptide of any of embodiments 1-112, or a nucleic acid molecule encoding the gene modifying polypeptide, and ii) a template RNA that comprises: a) a gRNA spacer that is complementary to a portion of a target nucleic acid sequence; b) a gRNA scaffold (e.g., a StlCas9 gRNA scaffold) that binds the Cas9 nickase domain of the gene modifying polypeptide; c) a heterologous object sequence; and d) a primer binding site (PBS) sequence. 117. The system of embodiment 116, wherein the gene modifying polypeptide comprises: a retroviral reverse transcriptase (RT) domain having an amino acid sequence of Table 1, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto; an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; and a linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker comprises an amino acid sequence of Table 5, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto. 118. The system of embodiment 116 or 117, wherein the gRNA scaffold is a variant StlCas9 scaffold having a deletion of part or all of Stem loop 2. 119. The system of any of embodiments 116-118, wherein the template RNA has a nucleic acid sequence of any of Tables 20, 22, or 24, or a nucleic acid sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto. 120. The system of any of embodiments 116-119, wherein the template RNA comprises one or more chemical modifications. 121. The system of any of embodiments 116-120, wherein the template RNA comprises the chemical modifications set out in any template RNA sequence of Tables 19, 21, or 23. 122. The system of any of embodiments 116-121, wherein the target nucleic acid sequence is a first portion of the human SERPINA1 gene. 123. The system of any of embodiments 116-122, wherein the gRNA spacer has a nucleotide sequence ofAAGGCUGUGCUGACCAUCGA (SEQ ID NO: 21748). 124. The system of any of embodiments 116-123, wherein the heterologous object sequence is to introduce a mutation into (e.g., to correct a mutation in) a second portion of the human SERPINA1 gene. 125. The system of any of embodiments 116-124, wherein the heterologous object sequence has a nucleotide sequence of UUUCUCGUCG (SEQ ID NO: 21749). 126. The system of any of embodiments 116-125, wherein the PBS sequence comprises at least 3, 4, 5, 6, 7, or 8 bases with 100% identity to a third portion of the human SERPINA1 gene. 127. The system of any of embodiments 116-126, wherein the PBS has a nucleotide sequence of AUGGUCAG (SEQ ID NO: 21750). 128. A lipid nanoparticle formulation comprising the system of any of embodiments 116-127. 129. A method for modifying a target nucleic acid molecule in a cell, the method comprising contacting the cell with the system of any of embodiments 116-127, thereby modifying the target nucleic acid molecule. 130. The method of embodiment 129, wherein the cell is a liver cell. 131. A method for modifying a target nucleic acid molecule in a tissue, the method comprising contacting the tissue with the system of any of embodiments 116-127, thereby modifying the target nucleic acid molecule. 132. The method of embodiment 131, wherein the tissue is liver. BRIEF DESCRIPTION OF THE DRAWINGS FIG. 1 is a diagram depicting components of a gene modifying system as described herein. FIG. 1A is a diagram showing a gene modifying polypeptide comprising a Cas nickase domain (e.g., spCas9 N863A) and a reverse transcriptase domain (RT domain) which are linked by a linker. FIG. IB is a diagram showing a template RNA comprising, from 5’ to 3’, a gRNA spacer, a gRNA scaffold, a heterologous object sequence, and a primer binding site sequence (PBS sequence). A heterologous object sequence can comprise a mutation region that comprises one or more sequence differences relative to a target site. A heterologous object sequence can also comprise a pre-edit homology region and a post-edit homology region, which flank a mutation region. Without wishing to be bound by theory, it is thought that a gRNA spacer of a template RNA binds to a second strand of a target site in the genome, and a gRNA scaffold of the template RNA binds to a gene modifying polypeptide, e.g., localizing the gene modifying polypeptide to a target site in the genome. It is thought that a Cas domain of a gene modifying polypeptide nicks a target site (e.g., a first strand of the target site), e.g., allowing a PBS sequence to bind to a sequence adjacent to the target site to be altered on the first strand of the target site. It is thought that an RT domain of a gene modifying polypeptide uses a first strand of a target site that is bound to a complementary sequence comprising a PBS sequence of a template RNA as a primer and a heterologous object sequence of the template RNA as a template to, e.g., polymerize a sequence complementary to the heterologous object sequence. Without wishing to be bound by theory, it is thought that reverse transcription can then proceed through a pre-edit homology region, then through a mutation region, and then through a post-edit homology region, thereby producing a DNA strand comprising a mutation specified by a heterologous object sequence. FIG. 2A is a diagram illustrating the positions of the reference dSL2 StlCas9 scaffold sequence. FIG. 2B is a diagram illustrating the positions of the reference wild-type StlCas9 scaffold sequence. FIG. 3 is a diagram illustrating the hypothesized secondary structure of a wild-type StlCas9 gRNA scaffold and is overlaid with description of valiants described herein. FIG. 4A is a schematic diagram of an exemplary gene modifying polypeptide, a fusion polypeptide comprising, e.g. from N terminus to C terminus, a first nuclear localization signal (NLS) sequence, a Cas nickase domain (e.g., Stl Cas9), a linker selected from Table 5, a reverse transcriptase domain (RT domain) selected from Table 1, and a second NLS sequence. FIG. 4B is a schematic flow diagram of an exemplary polypeptide screen conducted with pooled elements from a library of gene modifying polypeptide candidates. FIG. 4C is a schematic diagram of an exemplary assay for detecting gene editing. A target reporter gene (LP), which comprises a stop codon that prevents the translation of mKate is expressed in a test cell line. If there is perfect mutation (e.g., edit) in the LP stop codon sequence, cells will express green fluorescent protein and red fluorescent protein (GFP-RFP) as compared to only GFP in the event that a mutation in the LP stop codon sequence has not taken place. FIG. 4D is a graph showing mean enrichment scores of exemplary reverse transcriptase (RT) families screened as described herein. Mean enrichment scores are a representative measure of genome editing activity. FIG. 5A is a bar graph showing the rewriting efficiency in the livers of mice administered with exemplary gene modifying systems comprising different template RNAs comprising scaffold chemical modifications. FIG. 5B is a bar graph showing the % indel levels in the livers of mice administered with the exemplary gene modifying systems evaluated in FIG. 5A. FIG. 6A is a bar graph showing the rewriting efficiency in the livers of mice administered with exemplary gene modifying systems comprising different template RNAs comprising scaffold chemical modifications in combination with fluoro modifications at the heterologous object sequence. FIG. 6B is a bar graph showing the % indel levels in the livers of mice administered with the exemplary gene modifying systems evaluated in FIG. 6A. FIG. 7A is a bar graph showing the rewriting efficiency in the livers of mice administered with exemplary gene modifying systems comprising different gene modifying polypeptides and different template RNAs comprising scaffold chemical modifications in combination with fluoro modifications at the heterologous object sequence. FIG. 7B is a bar graph showing the % indel levels in the livers of mice administered with the exemplary gene modifying systems evaluated in FIG. 7A. FIG. 8A is a bar graph showing the % corrected genomic DNA in the livers of hSERPINAl E342K mice by administered with exemplary gene modifying systems comprising RNAIVT6241 or RNAIVT6898 polypeptides over evaluated dosages. FIG. 8B is a bar graph showing the % corrected genomic DNA in the livers of NSG-PiZ mice by exemplary RNAIVT6898 systems over evaluated dosages at 7 days post-administration. FIG. 8C is a bar graph showing the % corrected genomic DNA in the livers of NSG-PiZ mice by exemplary RNAIVT6898 systems over evaluated dosages at 21 days postadministration. FIG. 9is a bar graph showing the % edited mRNA in the livers of hSERPINAl E342K and NSG-PiZ mice by exemplary RNAIVT6898 systems over evaluated dosages at 21 days postadministration. FIG. 10A is a bar graph showing the % indels introduced into the livers of hSERPINAl E342K by exemplary gene modifying polypeptides RNAVT6241 and RNAIVT6838 over evaluated dosages. FIG. 10B is a bar graph showing the % indels introduced into the livers of NSG-PiZ mice by exemplary RNAIVT6898 systems over evaluated dosages at 7 days post-administration. FIG. 10C is a bar graph showing the % indels introduced into the livers of NSG-PiZ mice by exemplary RNAIVT6898 systems over evaluated dosages at 21 days post-administration. FIG. 11A is a bar- graph showing the serum concentration of human Al AT in hSERPINAl E342K mice administered with exemplary gene modifying systems comprising RNAIVT6241 or RNAIVT6898 polypeptides over evaluated dosages. FIG. 11B is a bar graph showing the serum concentration of human Al AT in NSG-PiZ mice administered with exemplary RNAIVT6898 systems over evaluated dosages at 7 days postadministration. FIG. 11C is a bar graph showing the serum concentration of human Al AT in NSG-PiZ mice administered with exemplary RNAIVT6898 systems over evaluated dosages at 21 days postadministration. FIG. 12A is a bar graph showing the % liver area occupied by globules in NSG-PiZ mice administered with exemplary RNAIVT6898 systems over evaluated dosages at 7 days postadministration. FIG. 12B is a bar graph showing the % liver area occupied by globules in NSG-PiZ mice administered with exemplary RNAIVT6898 systems over evaluated dosages at 21 days postadministration. FIG. 13A is a bar graph showing the % corrected genomic DNA in the livers of NSG-PiZ mice by exemplary gene modifying systems comprising RNAIVT9315 gene modifying polypeptide and RNACS22230 template RNA over evaluated dosages. FIG. 13B is a bar graph showing the % edited mRNA in the livers of NSG-PiZ mice by exemplary gene modifying systems comprising RNAIVT9315 gene modifying polypeptide and RNACS22230 template RNA over evaluated dosages. FIG. 13C is a bar graph showing the % indels introduced into the livers of NSG-PiZ mice by exemplary gene modifying systems comprising RNAIVT9315 gene modifying polypeptide and RNACS22230 template RNA over evaluated dosages. FIG. 14A is a bar graph showing the serum concentration of human Al AT in NSG-PiZ mice administered with exemplary gene modifying systems comprising RNAIVT9315 gene modifying polypeptide and RNACS22230 template RNA over evaluated dosages. FIG. 14B is a line graph showing the scrum concentration of human Al AT as a function of % genomic DNA rewriting in NSG-PiZ mice administered with exemplary gene modifying systems comprising RNAIVT9315 gene modifying polypeptide and RNACS22230 template RNA over evaluated dosages. FIG. 15 is a bar a graph showing the % hAlAT isoform present in liver samples from NSG-PiZ mice treated with saline or an exemplary RNAIVT9315-containing gene modifying system at 0.5 mg / kg (mpk) or 1.5 mg / kg. FIGs. 16A is a bar graph showing the % corrected genomic DNA in the livers of cynomolgus monkeys dosed with an exemplary gene modifying system including an mRNA encoding an exemplary RNAIVT9315 gene modifying polypeptide and an RNACS22390 tgRNA at two different doses (2 mg / kg or 3 mg / kg) and formulated in different LNPs (2 mg / kg in exemplary LNP formulation 1, and 3 mg / kg in exemplary LNP formulation 2) as measured by Amp-Seq. FIG. 16B is a bar graph showing the % indels introduced into the livers of cynomolgus monkeys dosed with an exemplary gene modifying system including an mRNA encoding an exemplary RNAIVT9315 gene modifying polypeptide and an RNACS22390 tgRNA at two different doses (2 mg / kg or 3 mg / kg) and formulated in different LNPs (2 mg / kg in exemplary LNP formulation 1, and 3 mg / kg in exemplary LNP formulation 2) as measured by Amp-Seq. FIG. 17A is a bar graph showing the % corrected genomic DNA in the livers of hSERPINAl E342K mice by exemplary gene modifying systems comprising RNAIVT9315 or RNAIVT9318 gene modifying polypeptides and RNACS22230 template RNA over evaluated dosages. FIG. 17B is a bar graph showing the % indels introduced in the livers of hSERPINAl E342K mice by exemplary gene modifying systems comprising RNAIVT9315 or RNAIVT9318 gene modifying polypeptides and RNACS22230 template RNA over evaluated dosages. FIGs. 18A to 18D show bar- graphs of the rewriting performance in the livers of hSERPINAl E342K mice administered with exemplary StlCas9-based gene modifying systems comprising exemplary RNAIVT9315 gene modifying polypeptide and exemplary template RNAs RNACS24756 or RNACS24757 at 0.012 mg / kg (FIG. 18A), 0.025 mg / kg (FIG. 18B), 0.05 mg / kg (FIG. 18C) and 0.1 mg / kg (FIG. 18D). FIGs. 19A to 19D show bar graphs of the % indel levels in the livers of hSERPINAl E342K mice administered with exemplary StlCas9-based gene modifying systems comprising exemplary RNAIVT9315 gene modifying polypeptide and exemplary template RNAs RNACS24756 or RNACS24757 at 0.012 mg / kg (FIG. 19A), 0.025 mg / kg (FIG. 19B), 0.05 mg / kg (FIG. 19C) and 0.1 mg / kg (FIG. 19D). FIG. 20A is a bar graph showing the % corrected genomic DNA in the livers of hSERPINAl E342K mice by exemplary gene modifying systems comprising RNAIVT9315 gene modifying polypeptide and RNACS27457 template RNA over evaluated dosages (mpk = mg / kg) and formulated in LNP. FIG. 20B is a bar graph showing the % edited mRNA in the livers of hSERPINAl E342K mice by exemplary gene modifying systems comprising RNAIVT9315 gene modifying polypeptide and RNACS27457 template RNA over evaluated dosages (mpk = mg / kg) and formulated in LNP. FIG. 20C is a bar graph showing the % indels introduced in the livers of hSERPINAl E342K mice by exemplary gene modifying systems comprising RNAIVT9315 gene modifying polypeptide and RNACS27457 template RNA over evaluated dosages (mpk = mg / kg) and formulated in LNP. FIG. 21A is a bar graph showing the serum concentration of human Al AT in hSERPINAl E342K mice administered with exemplary gene modifying systems comprising RNAIVT9315 gene modifying polypeptide and RNACS27457 template RNA over evaluated dosages (mpk = mg / kg) and formulated in LNP. FIG. 21B is a line graph showing the serum concentration of human Al AT as a function of % genomic DNA rewriting in hSERPINAl E342K mice administered with exemplary gene modifying systems comprising RNAIVT9315 gene modifying polypeptide and RNACS27457 template RNA over evaluated dosages (mpk = mg / kg) and formulated in LNP. Definitions The term “Cas9 nickase domain,” as used herein, refers to a domain having the amino acid sequence of a Cas9 protein having nickase activity. In some embodiments, a Cas9 sequence has at least 75%, 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% identity to a wild-type St !Cas9 or SpCas9 sequence, A Cas9 sequence may have a point mutation relative to the wild-type sequence. In some embodiments, a Cas9 point mutant has nickase activity. The term “StlCas9 nickase domain” refers to a Cas9 nickase domain having at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, identity to a wild-type Stl Cas9 sequence. An StlCas9 nickase domain does not have 100% identity to a wild-type SpCas9 nickase domain. The term “chemically modified nucleotide,” as used herein, refers to a nucleotide comprising one or more structural differences relative to the canonical ribonucleotides (he., G, U, C, and A). A chemically modified nucleotide may have (relative to a canonical nucleotide) a chemically modified nudcobasc, a chemically modified sugar, a chemically modified phosphodiester linkage, or a combination thereof. In some embodiments, a chemically modified nucleotide is a 2'-O-methyl nucleotide, e.g., 2'-O-methyl-Adenosine, 2'-O-methyl-Cytidine, 2'-O-methyl-Guanosine, or 2'-O-methyl-Uridine. No particular process of making is implied; for instance, a chemically modified nucleotide can be produced directly by chemical synthesis, or by covalently modifying a canonical nucleotide. The term “chemical modification,’" as used herein, refers to a structural difference of a chemical modified nucleotide relative to the canonical ribonucleotides (i.e., G, U, C, and A). A chemical modification may comprise a modification resulting in a chemically modified nucleobase. a chemically modified sugar, a chemically modified phosphodiester linkage, or a combination thereof. In some embodiments, a chemical modification is 2'-O-methylation or 2’-fluoro modification. No particular process of making is implied; for instance, a chemical modification can be produced directly by chemical synthesis, or by covalently modifying a canonical nucleotide. The term “expression cassette,” as used herein, refers to a nucleic acid construct comprising nucleic acid elements sufficient for the expression of the nucleic acid molecule of the instant invention. A “gRNA spacer,” as used herein, refers to a portion of a nucleic acid that has complementarity to a target nucleic acid and can, together with a gRNA scaffold, target a Cas protein to the target nucleic acid. A “gRNA scaffold,” as used herein, refers to a portion of a nucleic acid that can bind a Cas protein and can, together with a gRNA spacer, target the Cas protein to the target nucleic acid. In some embodiments, the gRNA scaffold comprises a crRNA sequence, tetraloop, and tracrRNA sequence. The term “StlCas9 scaffold,” as used herein, refers to a gRNA scaffold that can bind an StlCas9 protein and can, together with a gRNA spacer, target the StlCas9 protein to the target nucleic acid. In some embodiments, an StlCas9 scaffold comprises a crRNA sequence, tetraloop, and tracerRNA sequence. An exemplary position of StlCas9 scaffold within an exemplary template RNA is illustrated in FIG. 1. In some embodiments, an StlCas9 scaffold comprises a full length wild-type sequence. In some embodiments, an StlCas9 scaffold comprises a sequence with at least 80%, 85%. 90%, 95%, 96%, 97%, 98%, or 99% identity to the sequence of GUCUUUGUACUCUGGUACCAGAAGCUACAAAGAUAAGGCUUCAUGCCGAAAUCA ACACCCUGOCAUUUUAUGGCAGGGUGUIJUIJ (SEQ ID NO: 25999). In some embodiments, an StlCas9 scaffold comprises a sequence identical to SEQ ID NO: 25999. In some embodiments, an SdCas9 scaffold comprises a truncation mutant. In some embodiments, an StlCas9 scaffold comprises a sequence with at least 80%, 85%. 90%, 95%, 96%, 97%, 98%, or 99% identity to the sequence of GUCUUUGUACUCUGGUACCAGAAGCUACAAAGAUAAGGCUUCAUGCCGAAAUCA (SEQ ID NO: 26000). In some embodiments, an StlCas9 scaffold comprises a sequence identical to SEQ ID NO: 26000. In some embodiments, an StlCas9 scaffold comprises an insertion, deletion, or substitution to a reference sequence of SEQ ID NO: 25999 or 26000. In some embodiments, an StlCas9 scaffold comprises a chemically modified nucleotide. A “variant gRNA scaffold,” as used herein, refers to gRNA scaffold having a non-naturally occurring sequence. In some embodiments, a variant gRNA scaffold sequence comprises one or more substitutions relative to the closest naturally occurring sequence. In some embodiments, a variant gRNA scaffold sequence comprises one or more insertions relative to the closest naturally occurring sequence. In some embodiments, a variant gRNA scaffold sequence comprises one or more deletions relative to the closest naturally occurring sequence. As used herein, the term “position” with respect to an StlCas9 scaffold refers to a nucleotide of the StlCas9 scaffold that aligns with the corresponding nucleotide of the reference sequence of SEQ ID NO: 25999. The positions of a reference sequence are illustrated in FIG. 2. Alignments of nucleic acid or polypeptide sequences can be performed by using a sequence analysis tool such as Basic Local Alignment Search Tool (BLAST), for instance NIH megablast using default parameters. In some embodiments, a position of an StlCas9 scaffold can be identified by providing an alignment of the StlCas9 scaffold (query sequence) to a reference sequence of SEQ ID NO: 25999 (a full length wild-type sequence, see e.g., FIG 2B) or SEQ ID NO: 26000 (a truncation mutant, see e.g., FIG. 2A), and identifying the position in the query sequence that corresponds to the position in the reference sequence. For example, in an StlCas9 scaffold consisting of the sequence of SEQ ID NO: 25999 except that the 5’ most G is substituted with a single nucleotide other than G, the substituted position is position 1. As another example, in an StlCas9 scaffold consisting of the sequence of SEQ ID NO: 25999 except that a single new nucleotide is inserted just 5’ of the 5’ most G, the G is still position 1. As yet another example, in an StlCas9 scaffold consisting of the sequence of SEQ ID NO: 25999 except that a sequence of n nucleotides is inserted between the G of position 1 and the U of position 2, nucleotides 3’ of the insert maintain their original position number. For example, the U of position 2 is still position 2 rather than position n+2. A nucleotide that is inserted relative to the reference sequence need not be assigned a position number. A range of nucleotides includes all nucleotides in that range regardless of whether they are assigned a number; for example, if a scaffold comprises a chemically modified nucleotide at each of positions 12 through 21, and the scaffold comprises inserted nucleotides anywhere between positions 12 and 21, then the scaffold comprises chemically modified nucleotides at each of the inserted nucleotides situated anywhere between positions 12 and 21 (which inserted nucleotides do not have a position number in this example), as well as chemically modified nucleotides at positions 12, 13, 14, 15, 16, 17, 18, 19, 20, and 21. A “gene modifying polypeptide,” as used herein, refers to a polypeptide comprising a retroviral reverse transcriptase, or a polypeptide comprising an amino acid sequence having at least 75%, 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% amino acid sequence identity to a retroviral reverse transcriptase, which is capable of integrating a nucleic acid sequence (e.g., a sequence provided on a template nucleic acid) into a target DNA molecule (e.g., in a mammalian host cell, such as a genomic DNA molecule in the host cell). In some embodiments, a gene modifying polypeptide is capable of integrating a sequence substantially without relying on host machinery. In some embodiments, a gene modifying polypeptide integrates a sequence into a random position in a genome. In some embodiments, a gene modifying polypeptide integrates a sequence into a specific target site. In some embodiments, a gene modifying polypeptide includes one or more domains that, collectively, facilitate 1) binding a template nucleic acid, 2) binding a target DNA molecule, and 3) integration of at least a portion of the template nucleic acid into the target DNA. Gene modifying polypeptides include both naturally occurring polypeptides as well as engineered variants of the foregoing, e.g., having one or more amino acid substitutions to a naturally occurring sequence. Gene modifying polypeptides also include heterologous constructs, e.g., where one or more of the domains are heterologous to each other, whether through a heterologous fusion (or other conjugate) of otherwise wild-type domains, as well as fusions of modified domains, e.g., by way of replacement or fusion of a heterologous subdomain or other substituted domain. Exemplary gene modifying polypeptides, and systems comprising the same can be used in methods provided herein and described, e.g., in PCT / US2021 / 020948, which is incorporated herein by reference with respect to gene modifying polypeptides that comprise a retroviral reverse transcriptase domain. In some embodiments, a gene modifying polypeptide integrates a sequence into a gene. In some embodiments, a gene modifying polypeptide integrates a sequence into a sequence outside of a gene. A “gene modifying system,” as used herein, refers to a system comprising a gene modifying polypeptide and a template nucleic acid. The term “domain,” as used herein, refers to a structure of a biomolecule that contributes to a specified function of the biomolecule. A domain may comprise a contiguous region (e.g., a contiguous sequence) or distinct, non-contiguous regions (e.g., non-contiguous sequences) of a biomolecule. Examples of protein domains include, but are not limited to, an endonuclease domain, a DNA binding domain, a reverse transcription domain; an example of a domain of a nucleic acid is a regulatory domain, such as a transcription factor binding domain. In some embodiments, a domain (e.g., a Cas domain) can comprise two or more smaller domains (e.g., a DNA binding domain and an endonuclease domain). As used herein, the term “exogenous,” when used with reference to a biomolecule (such as a nucleic acid sequence or polypeptide) means that the biomolecule was introduced into a host genome, cell or organism by the hand of man. For example, a nucleic acid that is as added into an existing genome, cell, tissue or subject using recombinant DNA techniques or other methods is exogenous to the existing nucleic acid sequence, cell, tissue or subject. As used herein, “first strand” and “second strand,” as used to describe the individual DNA strands of target DNA, distinguish the two DNA strands based upon which strand a reverse transcriptase domain initiates polymerization, e.g., based upon where target primed synthesis initiates. A “first strand” refers to the strand of a target DNA upon which a reverse transcriptase domain initiates polymerization, e.g., where target primed synthesis initiates. A “second strand” refers to the other strand of the target DNA. First and second strand designations do not describe a target site DNA strands in other respects; for example, in some embodiments the first and second strands are nicked by a polypeptide described herein, but the designations ‘first’ and ‘second’ strand have no bearing on the order in which such nicks occur. The term “heterologous,” as used herein to describe a first element in reference to a second element means that a first element and second element do not exist in nature disposed as described. For example, a heterologous polypeptide, nucleic acid molecule, construct or sequence refers to (a) a polypeptide, nucleic acid molecule or portion of a polypeptide or nucleic acid molecule sequence that is not native to a cell in which it is expressed, (b) a polypeptide or nucleic acid molecule or portion of a polypeptide or nucleic acid molecule that has been altered or mutated relative to its native state, or (c) a polypeptide or nucleic acid molecule with an altered expression as compared to the native expression levels under similar conditions. For example, a heterologous regulatory sequence (e.g., promoter, enhancer) may be used to regulate expression of a gene or a nucleic acid molecule in a way that is different than the gene or a nucleic acid molecule is normally expressed in nature. In another example, a heterologous domain of a polypeptide or nucleic acid sequence (e.g., a DNA binding domain of a polypeptide or nucleic acid encoding a DNA binding domain of a polypeptide) may be disposed relative to other domains or may be a different sequence or from a different source, relative to other domains or portions of a polypeptide or its encoding nucleic acid. In some embodiments, a heterologous nucleic acid molecule may exist in a native host cell genome but may have an altered expression level or have a different sequence or both. In other embodiments, heterologous nucleic acid molecules may not be endogenous to a host cell or host genome but instead may have been introduced into a host cell by transformation (e.g., transfection, electroporation), wherein the added molecule may integrate into the host genome or can exist as extra-chromosomal genetic material either transiently (e.g., mRNA) or semi-stably for more than one generation (e.g., episomal viral vector, plasmid or other self-replicating vector). As used herein, “insertion” of a sequence into a target site refers to the net addition of DNA sequence at a target site, e.g., where there are new nucleotides in a heterologous object sequence with no cognate positions in the unedited target site. In some embodiments, a nucleotide alignment of a PBS sequence and heterologous object sequence to a target nucleic acid sequence would result in an alignment gap in the target nucleic acid sequence. As used herein, a “deletion” generated by a heterologous object sequence in a target site refers to the net deletion of DNA sequence at the target site, c.g., where there arc nucleotides in the unedited target site with no cognate positions in the heterologous object sequence. In some embodiments, a nucleotide alignment of the PBS sequence and heterologous object sequence to the target nucleic acid sequence would result in an alignment gap in the molecule comprising the PBS sequence and heterologous object sequence. The term “mutation region,” as used herein, refers to a region in a template RNA having one or more sequence difference relative to the corresponding sequence in a target nucleic acid. The one or more sequence difference may comprise, for example, a substitution, insertion, frameshift, or deletion. The term “mutated” when applied to nucleic acid sequences means that nucleotides in a nucleic acid sequence are inserted, deleted, or changed compared to a reference (e.g., native) nucleic acid sequence. A single alteration may be made at a locus (a point mutation), or multiple nucleotides may be inserted, deleted, or changed at a single locus. In addition, one or more alterations may be made at any number of loci within a nucleic acid sequence. A nucleic acid sequence may be mutated by any method known in the art. “Nucleic acid molecule” refers to both RNA and DNA molecules including, without limitation, complementary DNA (“cDNA”), genomic DNA (“gDNA”), and messenger RNA (“mRNA”), and also includes synthetic nucleic acid molecules, such as those that are chemically synthesized or recombinantly produced, such as RNA templates, as described herein. A nucleic acid molecule can be double-stranded or single-stranded, circular, or linear. If single-stranded, a nucleic acid molecule can be a sense strand or an antisense strand. Unless otherwise indicated, and as an example for all sequences described herein under the general format “SEQ ID NO:,” or “nucleic acid comprising SEQ ID NO: 1” refers to a nucleic acid, at least a portion which has either (i) the sequence of SEQ ID NO: 1, or (ii) a sequence complimentary to SEQ ID NO: I. The choice between the two is dictated by the context in which SEQ ID NO: 1 is used. For instance, if a nucleic acid is used as a probe, the choice between the two is dictated by the requirement that the probe be complementary to a desired target. Nucleic acid sequences of the present disclosure may be modified chemically or biochemically or may contain non-natural or derivatized nucleotide bases, as will be readily appreciated by those of skill in the art. Such modifications include, for example, labels, methylation, substitution of one or more naturally occurring nucleotides with an analog, inter-nucleotide modifications such as uncharged linkages (for example, methyl phosphonates, phosphotricstcrs, phosphoramidates, carbamates, etc.), charged linkages (for example, phosphorothioates, phosphorodithioates, etc.), pendant moieties, (for example, polypeptides), intercalators (for example, acridine, psoralen, etc.), chelators, alkylators, and modified linkages (for example, alpha anomeric nucleic acids, etc.). Also included are chemically modified bases (see, for example, Table 13), backbones (see, for example, Table 14), and modified caps (see, for example, Table 15). Also included are synthetic molecules that mimic polynucleotides in their ability to bind to a designated sequence via hydrogen bonding and other chemical interactions. Such molecules are known in the art and include, for example, those in which peptide linkages substitute for phosphate linkages in the backbone of a molecule, e.g., peptide nucleic acids (PNAs). Other modifications can include, for example, analogs in which the ribose ring contains a bridging moiety or other structure such as modifications found in “locked” nucleic acids (LNAs). In some embodiments, nucleic acids are in operative association with additional genetic elements, such as tissue-specific expressioncontrol sequence(s) (e.g., tissue-specific promoters and tissue-specific microRNA recognition sequences), as well as additional elements, such as inverted repeats (e.g., inverted terminal repeats, such as elements from or derived from viruses, e.g., AAV ITRs) and tandem repeats, inverted repeats / direct repeats, homology regions (segments with various degrees of homology to a target DNA), untranslated regions (UTRs) (5', 3", or both 5' and 3' UTRs), and various combinations of the foregoing. Nucleic acid elements of systems disclosed in the present application may be provided in a variety of topologies, including single-stranded, doublestranded, circular, linear, linear with open ends, linear with closed ends, and particular versions of these, such as doggybone DNA (dbDNA), and closed-ended DNA (ceDNA). As used herein, a “gene expression unit” is a nucleic acid sequence comprising at least one regulatory nucleic acid sequence operably linked to at least one effector sequence. A first nucleic acid sequence is operably linked with a second nucleic acid sequence when the first nucleic acid sequence is placed in a functional relationship with the second nucleic acid sequence. For instance, a promoter or enhancer is operably linked to a coding sequence if the promoter or enhancer affects the transcription or expression of the coding sequence. Operably linked DNA sequences may be contiguous or non-contiguous. Where necessary to join two protein-coding regions, operably linked sequences may be in the same reading frame. The terms “host genome” or “host cell,” as used herein, refer to a cell and / or its genome into which protein and / or genetic material has been introduced. It should be understood that such terms are intended to refer not only to the particular subject cell and / or genome, but to the progeny of such a cell and / or the genome of the progeny of such a cell. Because certain modifications may occur in succeeding generations due to either mutation or environmental influences, such progeny may not, in fact, be identical to the parent cell, but are still included within the scope of the term “host cell” as used herein. A host genome or host cell may be an isolated cell or cell line grown in culture, or genomic material isolated from such a cell or cell line, or may be a host cell or host genome which composing living tissue or an organism. In some embodiments, a host cell may be an animal cell or a plant cell, e.g., as described herein. In some embodiments, a host cell may be a mammalian cell, a human cell, avian cell, reptilian cell, bovine cell, horse cell, pig cell, goat cell, sheep cell, chicken cell, or turkey cell. In some embodiments, a host cell may be a corn cell, soy cell, wheat cell, or rice cell. As used herein, “operative association” describes a functional relationship between two nucleic acid sequences, such as a 1) promoter and 2) a heterologous object sequence, and means, in such example, the promoter and heterologous object sequence (e.g., a gene of interest) are oriented such that, under suitable conditions, the promoter drives expression of the heterologous object sequence. For instance, a template nucleic acid carrying a promoter and a heterologous object sequence may be single-stranded, e.g., either the (+) or (-) orientation. An “operative association” between the promoter and the heterologous object sequence in this template means that, regardless of whether the template nucleic acid will be transcribed in a particular state, when it is in the suitable state (e.g., is in the (+) orientation, in the presence of required catalytic factors, and NTPs, etc.), it is accurately transcribed. Operative association applies analogously to other pairs of nucleic acids, including other tissue-specific expression control sequences (such as enhancers, repressors and microRNA recognition sequences), IR / DR, ITRs, UTRs, or homology regions and heterologous object sequences or sequences encoding a retroviral RT domain. The term “primer binding site sequence” or “PBS sequence,” as used herein, refers to a portion of a template RNA capable of binding to a region in a target nucleic acid sequence. In some embodiments, a PBS sequence is a nucleic acid sequence comprising at least 3, 4, 5, 6, 7, or 8 bases with 100% identity to a region in a target nucleic acid sequence. In some embodiments, a primer region comprises at least 5, 6, 7, 8 bases with 100% identity to a region in a target nucleic acid sequence. Without wishing to be bound by theory, in some embodiments, when a template RNA comprises a PBS sequence and a heterologous object sequence, the PBS sequence binds to a region in a target nucleic acid sequence, allowing a reverse transcriptase domain to use that region as a primer for reverse transcription, and to use the heterologous object sequence as a template for reverse transcription. As used herein, a “stem-loop sequence” refers to a nucleic acid sequence (e.g., RNA sequence) with sufficient self-complementarity to form a stem-loop, e.g., having a stem comprising at least two (e.g., 3, 4, 5, 6, 7, 8, 9, or 10) base pairs, and a loop with at least three (e.g., four) base pairs. The stem may comprise mismatches or bulges. As used herein, a “tissue-specific expression-control sequence” means nucleic acid elements that increase or decrease the level of a transcript comprising the heterologous object sequence in a target tissue in a tissue-specific manner, e.g., preferentially in on-target tissue(s), relative to off-target tissue(s). In some embodiments, a tissue-specific expression-control sequence preferentially drives or represses transcription, activity, or the half-life of a transcript comprising the heterologous object sequence in the target tissue in a tissue-specific manner, e.g., preferentially in an on-target tissue(s), relative to an off-target tissue(s). Exemplary tissuespecific expression-control sequences include tissue-specific promoters, repressors, enhancers, or combinations thereof, as well as tissue-specific microRNA recognition sequences. Tissue specificity refers to on-target (tissue(s) where expression or activity of the template nucleic acid is desired or tolerable) and off-target (tissue(s) where expression or activity of the template nucleic acid is not desired or is not tolerable). For example, a tissue-specific promoter drives expression preferentially in on-target tissues, relative to off-target tissues. In contrast, a microRNA that binds the tissue-specific microRNA recognition sequences is preferentially expressed in off-target tissues, relative to on-target tissues, thereby reducing expression of a template nucleic acid in off-target tissues. Accordingly, a promoter and a microRNA recognition sequence that are specific for the same tissue, such as the target tissue, have contrasting functions (promote and repress, respectively, with concordant expression levels, i.e., high levels of the microRNA in off-target tissues and low levels in on-target tissues, while promoters drive high expression in on-target tissues and low expression in off-target tissues) with regard to the transcription, activity, or half-life of an associated sequence in that tissue. As used herein, “indel” refers to a mutation resulting from an insertion, deletion, or a combination thereof. As will be appreciated by those skilled in the ait, an indel in a coding region of a genomic sequence will result in a frameshift mutation, unless the length of the indel is a multiple of three. In some embodiments, a genetic modification is a point mutation. As used herein, "point mutation" refers to a substitution that replaces one of the nucleotides. A system of the present disclosure can be used to induce an indel of any length or a point mutation in a target polynucleotide sequence. As used herein, the term “retroviral reverse transcriptase domain” or “retroviral RT domain” refers to a reverse transcriptase domain having a sequence of a reverse transcriptase domain from a wild-type retrovirus, or a sequence having at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity thereto. DETAILED DESCRIPTION This disclosure provides compositions for targeting, editing, modifying or manipulating a DNA sequence (e.g., inserting a heterologous object sequence into a target site of a mammalian genome) at one or more locations in a DNA sequence in a cell, tissue or subject, e.g., in vivo or in vitro. Gene modifying systems In some embodiments, a gene modifying system described herein comprises: (A) a gene modifying polypeptide or a nucleic acid encoding the gene modifying polypeptide, wherein the gene modifying polypeptide comprises (i) a reverse transcriptase domain, and either (x) an endonuclease domain that contains DNA binding functionality or (y) an endonuclease domain and separate DNA binding domain; and (B) a template RNA. A gene modifying polypeptide, in some embodiments, acts as a substantially autonomous protein machine capable of integrating a template nucleic acid sequence into a target DNA molecule (e.g., in a mammalian host cell, such as a genomic DNA molecule in the host cell), substantially without relying on host machinery. For example, a gene modifying polypeptide may comprise a DNA-binding domain, a reverse transcriptase domain, and an endonuclease domain. In some embodiments, a DNA-binding function may involve an RNA component that directs a gene modifying polypeptide to a DNA sequence, e.g., a gRNA spacer. In other embodiments, a gene modifying polypeptide may comprise a reverse transcriptase domain and an endonuclease domain. An RNA template element of a gene modifying system may be heterologous to a gene modifying polypeptide clement and provides an object sequence to be inserted (reverse transcribed) into a host genome. In some embodiments, a gene modifying polypeptide is capable of target primed reverse transcription. In some embodiments, a gene modifying polypeptide is capable of second-strand synthesis. In some embodiments, a gene modifying system is combined with a second polypeptide. In some embodiments, a second polypeptide may comprise an endonuclease domain. In some embodiments, a second polypeptide may comprise a polymerase domain, e.g., a reverse transcriptase domain. In some embodiments, a second polypeptide may comprise a DNA-dependent DNA polymerase domain. In some embodiments, a second polypeptide aids in completion of a genome edit, e.g., by contributing to second-strand synthesis or DNA repair resolution. A functional gene modifying polypeptide can be made up of unrelated DNA binding, reverse transcription, and endonuclease domains. This modular structure allows combining of functional domains, e.g., dCas9 (DNA binding), MMLV reverse transcriptase (reverse transcription), FokI (endonuclease). In some embodiments, multiple functional domains may arise from a single protein, e.g., Cas9 or Cas9 nickase (DNA binding, endonuclease). In some embodiments, a gene modifying polypeptide includes one or more domains that, collectively, facilitate 1) binding a template nucleic acid, 2) binding a target DNA molecule, and 3) integration of at least a portion of the template nucleic acid into the target DNA. In some embodiments, a gene modifying polypeptide is an engineered polypeptide that comprises one or more amino acid substitutions to a corresponding naturally occurring sequence. In some embodiments, a gene modifying polypeptide comprises two or more domains that are heterologous relative to each other, e.g., through a heterologous fusion (or other conjugate) of otherwise wild-type domains, or well as fusions of modified domains, e.g., by way of replacement or fusion of a heterologous sub-domain or other substituted domain. For instance, in some embodiments, one or more of: an RT domain is heterologous to a DNA-binding domain (DBD); a DBD is heterologous to an endonuclease domain; or an RT domain is heterologous to an endonuclease domain. In some embodiments, a template RNA molecule for use in a system of the present disclosure comprises, from 5' to 3' (1) a gRNA spacer; (2) a gRNA scaffold; (3) a heterologous object sequence; and (4) a primer binding site (PBS) sequence. In some embodiments, a gRNA spacer is aboutl8 to -22 nucleotides in length (c.g., about 20 nucleotides in length). In some embodiments, a gRNA scaffold comprises one or more hairpin loops, e.g., 1, 2, or 3 loops for associating a template RNA with a Cas domain, e.g., a nickase Cas9 domain. In some embodiments, a gRNA scaffold comprises the sequence, from 5' to 3', GTTTTAGAGCTAGAAATAGCAAGTTAAAATAAGGCTAGTCCGTTATCAACTTGAAAA AGTGGGACCGAGTCGGTCC (SEQ ID NO: 5008). In some embodiments, a heterologous object sequence is, e.g., 7-74, e.g., 10-20, 20-30, 30-40, 40-50, 50-60, 60-70, or 70-80 nucleotides or, 80-90 nucleotides in length. In some embodiments, a first (i.e., 5'-most) base of a heterologous object sequence is not C. In some embodiments, a PBS sequence that binds a target priming sequence after nicking occurs is e.g., 3-20 nucleotides, e.g., 7-15 nucleotides, e.g., 12-14 nucleotides in length. In some embodiments, a PBS sequence has 40-60% GC content. In some embodiments, a second gRNA associated with a system of the present disclosure may help drive complete integration. In some embodiments, a second gRNA may target a location that is 0-200 nucleotides away from a first-strand nick, e.g., 0-50, 50-100, 100-200 nucleotides away from the first-strand nick. In some embodiments, a second gRNA can only bind its target sequence after an edit is made, e.g., the gRNA binds a sequence present in a heterologous object sequence, but not in the initial target sequence. In some embodiments, a gene modifying system described herein is used to make an edit in HEK293, K562, U2OS, or HeLa cells. In some embodiment, a gene modifying system is used to make an edit in primary cells, e.g., primary liver cells or primary lung cells. In some embodiments, a gene modifying polypeptide as described herein comprises a reverse transcriptase or RT domain (e.g., as described herein) that comprises a MoMLV RT sequence or variant thereof. In embodiments, a MoMLV RT sequence comprises one or more mutations selected from D200N, L603W, T330P, T306K, W313F, D524G, E562Q, D583N, P51L, S67R, E67K, T197A, H204R, E302K, F309N, L435G, N454K, H594Q, D653N, RI 10S, and K103L. In some embodiments, a MoMLV RT sequence comprises a combination of mutations, such as D200N, L603W, and T33OP, optionally further including T306K and / or W313F. In some embodiments, an endonuclease domain (e.g., as described herein) is Cas9. In some embodiments, an endonuclease domain is nCas9. In some embodiments, an endonuclease domain comprises an N863A mutation (e.g., in spCas9). Tn some embodiments, an endonuclease domain comprises a H840A mutation. In some embodiments, a heterologous object sequence (e.g., of a system as described herein) is about 1-50, 50-100, 100-200, 200-300, 300-400, 400-500, 500-600, 600-700, 700-800, 800-900, 900-1000, or more, nucleotides in length. In some embodiments, RT and endonuclease domains are joined by a flexible linker. In some embodiments, a linker comprises the amino acid sequence SGGSSGGSSGSETPGTSESATPESSGGSSGGSS (SEQ ID NO: 5006). In some embodiments, an endonuclease domain is N-terminal relative to an RT domain. In some embodiments, an endonuclease domain is C-terminal relative to an RT domain. In some embodiments, a system of the present disclosure incorporates a heterologous object sequence into a target site by target primed reverse transcription (TPRT), e.g., as described herein. In some embodiments, a gene modifying polypeptide comprises a DNA binding domain (DBD). In some embodiments, a gene modifying polypeptide comprises an RNA binding domain. In some embodiments, an RNA binding domain comprises an RNA binding domain of B-box protein, MS2 coat protein, dCas, or an element of a sequence of a Table herein. In some embodiments, an RNA binding domain is capable of binding to a template RNA with greater affinity than a reference RNA binding domain. In some embodiments, a gene modifying system is capable of producing an insertion of at least 45, at least 50, at least 55, at least 60, at least 65, at least 70, at least 75, at least 80, at least 85, at least 90, at least 95, or at least 100 nucleotides (and optionally no more than 500, no more than 400, no more than 300, no more than 200, or no more than 100 nucleotides) in a target site. In some embodiments, a gene modifying system is capable of producing an insertion of at least 1, 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 15, at least 20, at least 25, at least 30, at least 35, at least 40, at least 45, at least 50, at least 55, at least 60, at least 65, at least 70, at least 75, at least 80, at least 85, at least 90, at least 95, or at least 100 nucleotides (and optionally no more than 500, no more than 400, no more than 300, no more than 200, or no more than 100 nucleotides) in a target site. In some embodiments, a gene modifying system is capable of producing an insertion of at least 0.2, at least 0.3, at least 0.4, at least 0.5, at least 0.6, at least 0.7, at least 0.8, at least 0.9, at least 1, at least 1.5, at least 2, at least 2.5, at least 3, at least 3.5, at least 4, at least 4.5, at least 5, at least 5.5, at least 6, at least 6.5, at least 7, at least 7.5, at least 8, at least 8.5, at least 9, at least 9.5 or at least 10 kilobascs (and optionally no more than 1, 5, 10, or 20 kilobases) into a target site. In some embodiments, a gene modifying system is capable of producing a deletion of at least 81, at least 85, at least 90, at least 95, at least 100, at least 110, at least 120, at least 130, at least 140, at least 150, at least 160, at least 170, at least 180, at least 190, or at least 200 nucleotides (and optionally no more than 500, no more than 400, no more than 300, or no more than 200 nucleotides). In some embodiments, a gene modifying system is capable of producing a deletion of at least 81, at least 85, at least 90, at least 95, at least 100, at least 110, at least 120, at least 130, at least 140, at least 150, at least 160, at least 170, at least 180, at least 190, or at least 200 nucleotides (and optionally no more than 500, 400, 300, or 200 nucleotides). In some embodiments, a gene modifying system is capable of producing a deletion of at least 1, 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 15, at least 20, at least 25, at least 30, at least 35, at least 40, at least 45, at least 50, at least 55, at least 60, at least 65, at least 70, at least 75, at least 80, at least 85, at least 90, at least 95, or at least 100 nucleotides (and optionally no more than 500, no more than 400, no more than 300, no more than 200, or no more than 100 nucleotides). In some embodiments, a gene modifying system is capable of producing a deletion of at least 0.2, at least 0.3, at least 0.4, at least 0.5, at least 0.6, at least 0.7, at least 0.8, at least 0.9, at least 1, at least 1.5, at least 2, at least 2.5, at least 3, at least 3.5, at least 4, at least 4.5, at least 5, at least 5.5, at least 6, at least 6.5, at least 7, at least 7.5, at least 8, at least 8.5, at least 9, at least 9.5 or at least 10 kilobases (and optionally no more than 1, 5, 10, or 20 kilobases). In some embodiments, a gene modifying system is capable of producing a substitution of at least 1, 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 15, at least 20, at least 25, at least 30, at least 35, at least 40, at least 45, at least 50, at least 55, at least 60, at least 65, at least 70, at least 75, at least 80, at least 85, at least 90, at least 95, or at least 100, or more nucleotides in a target site. In some embodiments, a gene modifying system is capable of producing a substitution of 1-2, 2-3, 3-4, 4-5, 5-10, 10-15, 15-20, 20-30, 30-40, 4050, 50-60, 60-70, 70-80, 80-90, or 90-100 nucleotides in a target site. In some embodiments, a substitution is a transition mutation. In some embodiments, a substitution is a transversion mutation. In some embodiments, a substitution converts an adenine to a thymine, an adenine to a guanine, an adenine to a cytosine, a guanine to a thymine, a guanine to a cytosine, a guanine to an adenine, a thymine to a cytosine, a thymine to an adenine, a thymine to a guanine, a cytosine to an adenine, a cytosine to a guanine, or a cytosine to a thymine. In some embodiments, an insertion, deletion, substitution, or combination thereof, increases or decreases expression (e.g., transcription or translation) of a gene. In some embodiments, an insertion, deletion, substitution, or combination thereof, increases or decreases expression (e.g., transcription or translation) of a gene by altering, adding, or deleting sequences in a promoter or enhancer, e.g., sequences that bind transcription factors. In some embodiments, an insertion, deletion, substitution, or combination thereof alters translation of a gene (e.g., alters an amino acid sequence), inserts or deletes a start or stop codon, or alters or fixes the translation frame of a gene. In some embodiments, an insertion, deletion, substitution, or combination thereof alters splicing of a gene, e.g., by inserting, deleting, or altering a splice acceptor or donor site. In some embodiments, an insertion, deletion, substitution, or combination thereof alters transcript or protein half-life. In some embodiments, an insertion, deletion, substitution, or combination thereof alters protein localization in the cell (e.g., from the cytoplasm to a mitochondria, from the cytoplasm into the extracellular' space (e.g., adds a secretion tag)). In some embodiments, an insertion, deletion, substitution, or combination thereof alters (e.g., improves) protein folding (e.g., to prevent accumulation of misfolded proteins). In some embodiments, an insertion, deletion, substitution, or combination thereof, alters, increases, decreases the activity of a gene, e.g., a protein encoded by the gene. Exemplary gene modifying polypeptides, systems comprising the same, and methods of using the same are described, e.g., in PCT / US2021 / 020948, which is incorporated herein by reference with respect to retroviral RT domains, including the amino acid and nucleic acid sequences therein. Exemplary gene modifying polypeptides and retroviral RT domain sequences are also described, e.g., in International Application No. PCT / US21 / 20948, filed March 4, 2021, e.g., at Table 30, Table 31, and Table 44 therein; the entire application is incorporated by reference herein with respect to retroviral RTs, e.g., in said sequences and Tables. Accordingly, a gene modifying polypeptide described herein may comprise an amino acid sequence according to any of the Tables mentioned in this paragraph, or a domain thereof (e.g., a retroviral RT domain), or a functional fragment or variant of any of the foregoing, or an amino acid sequence having at least 70%, 80%, 85%, 90%, 95%, or 99% identity thereto. Polypeptide components of gene modifying systems In some embodiments, a gene modifying polypeptide possesses the functions of DNA target site binding, template nucleic acid (e.g., template RNA) binding, DNA target site cleavage, and template nucleic acid (e.g., template RNA) writing (e.g., reverse transcription). In some embodiments, each function is contained within a distinct domain. In some embodiments, a function may be attributed to two or more domains (e.g., two or more domains, together, exhibit the functionality). In some embodiments, two or more domains may have the same or similar function (e.g., two or more domains each independently have DNA-binding functionality, e.g., for two different DNA sequences). In some embodiments, one or more domains may be capable of enabling one or more functions, e.g., a Cas9 domain enabling both DNA binding and target site cleavage. In some embodiments, domains are all located within a single polypeptide. In some embodiments, a gene modifying polypeptide comprises, in N-terminal to C-terminal order, one or more (e.g., 1, 2, 3, 4, 5, or all 6) of an N-terminal methionine residue, a first nuclear localization signal (NLS), a DNA binding domain, a linker, an RT domain, and / or a second NLS. In some embodiments, a gene modifying polypeptide further comprises an N-terminal methionine residue. In some embodiments, a nucleic acid encoding a gene modifying polypeptide (e.g., as described herein) encodes a T2A sequence, e.g., wherein the T2A sequence is situated between a region encoding the gene modifying polypeptide and a second region, wherein the second region optionally encodes a selectable marker, e.g., puromycin. In some embodiments, a gene modifying polypeptide further comprises a spacer sequence between a first NLS and a DNA binding domain. In some embodiments, a spacer sequence between a first NLS and a DNA binding domain comprises 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acids. In some embodiments, a spacer sequence between a first NLS and the DNA binding domain comprises the amino acid sequence GG. In some embodiments, a gene modifying polypeptide further comprises a spacer sequence between a DNA binding domain and a linker. In some embodiments, a spacer sequence between a DNA binding domain and a linker comprises 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acids. In some embodiments, a spacer sequence between a DNA binding domain and a linker comprises the amino acid sequence GG. In some embodiments, a gene modifying polypeptide further comprises a spacer sequence between a linker and an RT domain. In some embodiments, a spacer sequence between a linker and an RT domain comprises 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acids. In some embodiments, a spacer sequence between a linker and an RT domain comprises the amino acid sequence GG. In some embodiments, a gene modifying polypeptide further comprises a spacer sequence between an RT domain and a second NLS. In some embodiments, a spacer sequence between an RT domain and a second NLS comprises 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acids. In some embodiments, a spacer sequence between an RT domain and a second NLS comprises the amino acid sequence AG. In some embodiments, a gene modifying polypeptide further comprises a spacer sequence between a second NLS and a T2A sequence and / or puromycin sequence. In some embodiments, a spacer sequence between a second NLS and a T2A sequence and / or puromycin sequence comprises 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acids. In some embodiments, a spacer sequence between a second NLS and a T2A sequence and / or puromycin sequence comprises the amino acid sequence GSG. RT Domains In some embodiments of the present invention, a writing domain of a gene modifying system possesses reverse transcriptase activity and is also referred to as a reverse transcriptase domain (an RT domain). In some embodiments, an RT domain comprises an RT catalytic portion and RNA-binding region (e.g., a region that binds a template RNA). In some embodiments, a nucleic acid encoding a reverse transcriptase is altered from its natural sequence to have altered codon usage, e.g., improved for human cells. In some embodiments, a reverse transcriptase domain is a heterologous reverse transcriptase from a retrovirus. In some embodiments, an RT domain has been mutated from its original amino acid sequence, e.g., has at least about 1, at least about 2, at least about 3, at least about 4, at least about 5, at least about 6, at least about 7, at least about 8, at least about 9, at least about 10, at least about 20, at least about 30, at least about 40, at least about 50, at least about 60, at least about 70, at least about 80, at least about 90, or at least about 100 substitutions. In some embodiments, an RT domain is derived from an RT of a retrovirus, e.g., HIV-1 RT, Moloney Murine Leukemia Virus (MMLV) RT, avian myeloblastosis virus (AMV) RT, or Rous Sarcoma Virus (RSV) RT. In some embodiments, an RT domain has a length of about 400-500, about 500-600, about 600-700, about 700-800, about 800-900, or about 900-1000 amino acids. In some embodiments, a retroviral reverse transcriptase (RT) domain exhibits enhanced stringency of target-primed reverse transcription (TPRT) initiation, e.g., relative to an endogenous RT domain. In some embodiments, an RT domain initiates TPRT when the 3 nucleotides in a target site immediately upstream of a first strand nick, e.g., genomic DNA priming of an RNA template, have at least 66% or 100% complementarity to 3 nucleotides of homology in the RNA template. In some embodiments, an RT domain initiates TPRT when there are less than 5 nucleotides mismatched (e.g., less than 1, less than 2, less than 3, less than 4, or less than 5 nt mismatched) between an RNA template and a target DNA priming reverse transcription. In some embodiments, an RT domain is modified such that the stringency for mismatches in priming a TPRT reaction is increased, e.g., wherein the RT domain does not tolerate any mismatches or tolerates fewer mismatches in a priming region relative to a wild-type (e.g., unmodified) RT domain. In some embodiments, an RT domain comprises a HIV-1 RT domain. In embodiments, an HIV-1 RT domain initiates lower levels of synthesis even with three nucleotide mismatches relative to an alternative RT domain (e.g., as described by Jamburuthugoda and Eickbush J Mol Biol 407(5):661-672 (2011); incorporated herein by reference in its entirety). In some embodiments, an RT domain forms a dimer (e.g., a heterodimer or homodimer). In some embodiments, an RT domain is monomeric. In some embodiments, an RT domain naturally functions as a monomer or as a dimer (e.g., heterodimer or homodimer). In some embodiments, an RT domain naturally functions as a monomer, e.g., is derived from a virus wherein it functions as a monomer. In embodiments, an RT domain is selected from an RT domain from murine leukemia virus (MLV; sometimes referred to as MoMLV) (e.g., P03355), porcine endogenous retrovirus (PERV) (e.g., UniProt Q4VFZ2), mouse mammary tumor virus (MMTV) (e.g., UniProt P03365), Avian reticuloendotheliosis virus (AVIRE) (e.g., UniProtKB accession: P03360); Feline leukemia virus (FLV or FeLV) (e.g., e.g., UniProtKB accession: P10273); Mason-Pfizer monkey virus (MPMV) (e.g., UniProt P07572), bovine leukemia virus (BLV) (e.g., UniProt P03361), human T-cell leukemia virus-1 (HTLV-1) (e.g., UniProt P03362), human foamy virus (HFV) (e.g., UniProt P14350), simian foamy virus (SFV) (e.g., SFV3L) (e.g., UniProt P23074 or P27401), or bovine foamy / syncytial virus (BFV / BSV) (e.g., UniProt 041894), or a functional fragment or variant thereof (e.g., an amino acid sequence having at least 70%, at least 80%, at least 90%, at least 95%, or at least 99% identity thereto). In some embodiments, an RT domain is dimeric in its natural functioning. In some embodiments, an RT domain is derived from a virus wherein it functions as a dimer. In embodiments, an RT domain is selected from an RT domain from avian sarcoma / lcukcmia virus (ASLV) (e.g., UniProt A0A142BKH1), Rous sarcoma virus (RSV) (e.g., UniProt P03354), avian myeloblastosis virus (AMV) (e.g., UniProt Q83133), human immunodeficiency virus type I (HIV-1) (e.g., UniProt P03369), human immunodeficiency virus type II (HIV-2) (e.g., UniProt P15833), simian immunodeficiency virus (SIV) (e.g., UniProt P05896), bovine immunodeficiency virus (BIV) (e.g., UniProt P19560), equine infectious anemia virus (EIAV) (e.g., UniProt P03371), or feline immunodeficiency virus (FIV) (e.g., UniProt P16088) (Herschhom and Hizi Cell Mol Life Sci 67(16):2717-2747 (2010)), or a functional fragment or variant thereof (e.g., an amino acid sequence having at least 70%, at least 80%, at least 90%, at least 95%, or at least 99% identity thereto). Naturally heterodimeric RT domains may, in some embodiments, also be functional as homodimers. In some embodiments, dimeric RT domains are expressed as fusion proteins, e.g., as homodimeric fusion proteins or heterodimeric fusion proteins. In some embodiments, an RT function of a system of the present disclosure is fulfilled by multiple RT domains (e.g., as described herein). In further embodiments, multiple RT domains are fused or separate, e.g., may be on the same polypeptide or on different polypeptides. In some embodiments, a gene modifying system described herein comprises an integrase domain, e.g., wherein the integrase domain may be part of an RT domain. In some embodiments, an RT domain (e.g., as described herein) comprises an integrase domain. In some embodiments, an RT domain (e.g., as described herein) lacks an integrase domain, or comprises an integrase domain that has been inactivated by mutation or deleted. In some embodiment, a gene modifying system described herein comprises an RNase H domain, e.g., wherein the RNase H domain may be part of an RT domain. In some embodiments, an RNase H domain is not part of an RT domain and is covalently linked via a flexible linker. In some embodiments, an RT domain (e.g., as described herein) comprises an RNase H domain, e.g., an endogenous RNAse H domain or a heterologous RNase H domain. In some embodiments, an RT domain (e.g., as described herein) lacks an RNase H domain. In some embodiments, an RT domain (e.g., as described herein) comprises an RNase H domain that has been added, deleted, mutated, or swapped for a heterologous RNase H domain. In some embodiments, a gene modifying polypeptide comprises an inactivated endogenous RNase H domain. In some embodiments, an endogenous RNase H domain of a polypeptide is genetically removed such that it is not included in the polypeptide, e.g., the endogenous RNase H domain is partially or completely truncated from the polypeptide. In some embodiments, one or more mutations of an RNase H domain yields a polypeptide exhibiting lower RNase activity, e.g., as determined by the methods described in Kotewicz et al. Nucleic Acids Res 16(1):265-277 (1988) (incorporated herein by reference in its entirety), e.g., lower by at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, or at least 90% compared to an otherwise similar domain without the one or more mutations, hi some embodiments, RNase H activity of a gene modifying polypeptide is abolished. In some embodiments, an RT domain is mutated to increase fidelity compared to an otherwise similar domain without the mutation. In some embodiments, a YADD or YMDD motif in an RT domain (e.g., in a reverse transcriptase) is replaced with YVDD. In some embodiments, replacement of a YADD, YMDD, or YVDD motif results in higher fidelity in retroviral reverse transcriptase activity (e.g., as described in Jamburuthugoda and Eickbush J Mol Biol 2011; incorporated herein by reference in its entirety). In some embodiments, a gene modifying polypeptide described herein comprises an RT domain having an amino acid sequence according to any RT domain described in Table 1, or a sequence having at least 70%, at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, at least 98%, or at least 99% identity thereto. In some embodiments, a nucleic acid described herein encodes an RT domain having an amino acid sequence according to any RT domain described in Table 1, or a sequence having at least 70%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity thereto. Table 1: Exemplary reverse transcriptase domains from retroviruses RT name RT amino acid sequence SEQID NOs AVIRE_PO 3360_3mu tA TAPLEEEYRLFLEAPIQNVTLLEQWKREIPKVWAEINPPGLASTQAPIHVQLL STALPVRVRQYPITLEAKRSLRETIRKFRAAGILRPVHSPWNTPLLPVRKSGT SEYRMVQDLREVNKRVETIHPTVPNPYTLLSLLPPDRIWYSVLDLKDAFFCIP LAPESQLIFAFEWADAEEGESGQLTWTRLPQGFKNSPTLFNEALNRDLQGF RLDHPSVSLLQYVDDLLIAADTQAACLSATRDLLMTLAELGYRVSGKKAQLC QEEVTYLGFKIHKGSRSLSNSRTQAILQIPVPKTKRQVREFLGKIGYCRLFIP GFAELAQPLYAATRPGNDPLVWGEKEEEAFQSLKLALTQPPALALPSLDKPF QLFVEETSGAAKGVLTQALGPWKRPVAYLSKRLDPVAAGWPRCLRAIAAAA LLTREASKLTFGQDIEITSSHNLESLLRSPPDKWLTNARITQYQVLLLDPPRV RFKQTAALNPATLLPETDDTLPIHHCLDTLDSLTSTRPDLTDQPLAQAEATLF TDGSSYIRDGKRYAGAAWTLDSVIWAEPLPIGTSAQKAELIALTKALEWSKD 10213 RT name RT amino acid sequence SEQID NOs KSVNIYTDSRYAFATLHVHGMIYRERGWLTAGGKAIKNAPEILALLTAVWLPK RVAVMHCKGHQKDDAPTSTGNRRADEVAREVAIRPLSTQATIS BAEVM.P 10272_3m utA TVSLQDEHRLFDIPVTTSLPDVWLQDFPQAWAETGGLGRAKCQAPIIIDLKPT AVPVSIKQYPMSLEAHMGIRQHIIKFLELGVLRPCRSPWNTPLLPVKKPGTQ DYRPVQDLREINKRTVDIHPTVPNPYNLLSTLKPDYSWYTVLDLKDAFFCLPL APQSQELFAFEWKDPERGISGQLTWTRLPQGFKNSPTLFNEALHRDLTDFR TQHPEVTLLQYVDDLLLAAPTKKACTQGTRHLLQELGEKGYRASAKKAQICQ TKVTYLGYILSEGKRWLTPGRIETVARIPPPRNPREVREFLGKAGFCRLFIPG FAELAAPLYALTKPSTPFTWQTEHQLAFEALKKALLSAPALGLPDTSKPFTLF LDERQGIAKGVLTQKLGPWKRPVAYLSKKLDPVAAGWPPCLRIMAATAMLV KDSAKLTLGQPLTVITPHTLEAIVRQPPDRWITNARLTHYQALLLDTDRVQFG PPVTLNPATLLPVPENQPSPHDCRQVLAETHGTREDLKDQELPDADHTWYT DGSSYLDSGTRRAGAAVVDGHNTIWAQSLPPGTSAQKAELIALTKALELSKG KKANIYTDSRYAFATAHTHGSIYERRGWLTSEGKEIKNKAEIIALLKALFLPQE VAIIHCPGHQKGQDPVAVGNRQADRVARQAAMAEVLTLATEPDNTSHIT 10214 FFV_O93 209 MDLLKPLTVERKGVKIKGYWNSQADITCVPKDLLQGEEPVRQQNVTTIHGT QEGDVYYVNLKIDGRRINTEVIGTTLDYAIITPGDVPWILKKPLELTIKLDLEEQ QGTLLNNSILSKKGKEELKQLFEKYSALWQSWENQVGHRRIRPHKIATGTVK PTPQKQYHINPKAKPDIQIVINDLLKQGVLIQKESTMNTPVYPVPKPNGRWR MVLDYRAVNKVTPLIAVQNQHSYGILGSLFKGRYKTTIDLSNGFWAHPIVPE DYWITAFTWQGKQYCWTVLPQGFLNSPGLFTGDWDLLQGIPNVEVYVDDV YISHDSEKEHLEYLDILFNRLKEAGYIISLKKSNIANSIVDFLGFQITNEGRGLT DTFKEKLENITAPTTLKQLQSILGLLNFARNFIPDFTELIAPLYALIPKSTKNYVP WQIEHSTTLETLITKLNGAEYLQGRKGDKTLIMKVNASYTTGYIRYYNEGEKK PISYVSIVFSKTELKFTELEKLLTTVHKGLLKALDLSMGQNIHVYSPIVSMQNI QKTPQTAKKALASRWLSWLSYLEDPRIRFFYDPQMPALKDLPAVDTGKDNK KHPSNFQHIFYTDGSAITSPTKEGHLNAGMGIVYFINKDGNLQKQQEWSISL GNHTAQFAEIAAFEFALKKCLPLGGNILWTDSNYVAKAYNEELDVWASNGF VNNRKKPLKHISKWKSVADLKRLRPDVWTHEPGHQKLDSSPHAYGNNLAD QLATQASFKVH 10215 FFVJ393 209-Pro VPWILKKPLELTIKLDLEEQQGTLLNNSILSKKGKEELKQLFEKYSALWQSWE NQVGHRRIRPHKIATGTVKPTPQKQYHINPKAKPDIQIVINDLLKQGVLIQKES TMNTPVYPVPKPNGRWRMVLDYRAVNKVTPLIAVQNQHSYGILGSLFKGRY KTTIDLSNGFWAHPIVPEDYWITAFTWQGKQYCWTVLPQGFLNSPGLFTGD VVDLLQGIPNVEVYVDDVYISHDSEKEHLEYLDILFNRLKEAGYIISLKKSNIAN SIVDFLGFQITNEGRGLTDTFKEKLENITAPTTLKQLQSILGLLNFARNFIPDFT ELIAPLYALIPKSTKNYVPWQIEHSTTLETLITKLNGAEYLQGRKGDKTLIMKV NASYTTGYIRYYNEGEKKPISYVSIVFSKTELKFTELEKLLTTVHKGLLKALDL SMGQNIHVYSPIVSMQNIQKTPQTAKKALASRWLSWLSYLEDPRIRFFYDPQ MPALKDLPAVDTGKDNKKHPSNFQHIFYTDGSAITSPTKEGHLNAGMGIVYF INKDGNLQKQQEWSISLGNHTAQFAEIAAFEFALKKCLPLGGNILWTDSNYV AKAYNEELDVWASNGFVNNRKKPLKHISKWKSVADLKRLRPDVWTHEPGH QKLDSSPHAYGNNLADQLATQASFKVH 10216 RT name RT amino acid sequence SEQID NOs FLV_P102 73_3mutA TLQLEEEYRLFEPESTQKQEMDIWLKNFPQAWAETGGMGTAHCQAPVLIQL KATATPISIRQYPMPHEAYQGIKPHIRRMLDQGILKPCQSPWNTPLLPVKKP GTEDYRPVQDLREVNKRVEDIHPTVPNPYNLLSTLPPSHPWYTVLDLKDAFF CLRLHSESQLLFAFEWRDPEIGLSGQLTWTRLPQGFKNSPTLFNEALHSDLA DFRVRYPALVLLQYVDDLLLAAATRTECLEGTKALLETLGNKGYRASAKKAQ ICLQEVTYLGYSLKDGQRWLTKARKEAILSIPVPKNSRQVREFLGKAGYCRL FIPGFAELAAPLYPLTRPGTLFQWGTEQQLAFEDIKKALLSSPALGLPDITKPF ELFIDENSGFAKGVLVQKLGPWKRPVAYLSKKLDTVASGWPPCLRMVAAIAI LVKDAGKLTLGQPLTILTSHPVEALVRQPPNKWLSNARMTHYQAMLLDAER VHFGPTVSLNPATLLPLPSGGNHHDCLQILAETHGTRPDLTDQPLPDADLTW YTDGSSFIRNGEREAGAAVTTESEVIWAAPLPPGTSAQRAELIALTQALKMA EGKKLTVYTDSRYAFATTHVHGEIYRRRGWLTSEGKEIKNKNEILALLEALFL PKRLSIIHCPGHQKGDSPQAKGNRLADDTAKKAATETHSSLTVLP 10217 FOAMV_P 14350_2m ut MNPLQLLQPLPAEIKGTKLLAHWNSGATITCIPESFLEDEQPIKKTLIKTIHGEK QQNVYYVTFKVKGRKVEAEVIASPYEYILLSPTDVPWLTQQPLQLTILVPLQE YQEKILSKTALPEDQKQQLKTLFVKYDNLWQHWENQVGHRKIRPHNIATGD YPPRPQKQYPINPKAKPSIQIVIDDLLKQGVLTPQNSTMNTPVYPVPKPDGR WRMVLDYREVNKTIPLTAAQNQHSAGILATIVRQKYKTTLDLANGFWAHPIT PESYWLTAFTWQGKQYCWTRLPQGFLNSPALFNADWDLLKEIPNVQVYVD DIYLSHDDPKEHVQQLEKVFQILLQAGYVVSLKKSEIGQKTVEFLGFNITKEG RGLTDTFKTKLLNITPPKDLKQLQSILGLLNFARNFIPNFAELVQPLYNLIAPAK GKYIEWSEENTKQLNMVIEALNTASNLEERLPEQRLVIKVNTSPSAGYVRYY NETGKKPIMYLNYVFSKAELKFSMLEKLLTTMHKALIKAMDLAMGQEILVYSP IVSMTKIQKTPLPERKALPIRWITWMTYLEDPRIQFHYDKTLPELKHIPDVYTS SQSPVKHPSQYEGVFYTDGSAIKSPDPTKSNNAGMGIVHATYKPEYQVLNQ WSIPLGNHTAQMAEIAAVEFACKKALKIPGPVLVITDSFYVAESANKELPYWK SNGFVNNKKKPLKHISKWKSIAECLSMKPDITIQHEKGISLQIPVFILKGNALA DKLATQGSYWN 10218 FOAMV.P 14350_2m utA MNPLQLLQPLPAEIKGTKLLAHWNSGATITCIPESFLEDEQPIKKTLIKTIHGEK QQNVYYVTFKVKGRKVEAEVIASPYEYILLSPTDVPWLTQQPLQLTILVPLQE YQEKILSKTALPEDQKQQLKTLFVKYDNLWQHWENQVGHRKIRPHNIATGD YPPRPQKQYPINPKAKPSIQIVIDDLLKQGVLTPQNSTMNTPVYPVPKPDGR WRMVLDYREVNKTIPLTAAQNQHSAGILATIVRQKYKTTLDLANGFWAHPIT PESYWLTAFTWQGKQYCWTRLPQGFLNSPALFNADWDLLKEIPNVQVYVD DIYLSHDDPKEHVQQLEKVFQILLQAGYVVSLKKSEIGQKTVEFLGFNITKEG RGLTDTFKTKLLNITPPKDLKQLQSILGKLNFARNFIPNFAELVQPLYNLIAPA KGKYIEWSEENTKQLNMVIEALNTASNLEERLPEQRLVIKVNTSPSAGYVRY YNETGKKPIMYLNYVFSKAELKFSMLEKLLTTMHKALIKAMDLAMGQEILVYS PIVSMTKIQKTPLPERKALPIRWITWMTYLEDPRIQFHYDKTLPELKHIPDVYT SSQSPVKHPSQYEGVFYTDGSAIKSPDPTKSNNAGMGIVHATYKPEYQVLN QWSIPLGNHTAQMAEIAAVEFACKKALKIPGPVLVITDSFYVAESANKELPYW KSNGFVNNKKKPLKHISKWKSIAECLSMKPDITIQHEKGISLQIPVFILKGNAL ADKLATQGSYWN 10219 RT name RT amino acid sequence SEQID NOs FOAMV.P 14350-Pro_2mut VPWLTQQPLQLTILVPLQEYQEKILSKTALPEDQKQQLKTLFVKYDNLWQHW ENQVGHRKIRPHNIATGDYPPRPQKQYPINPKAKPSIQIVIDDLLKQGVLTPQ NSTMNTPVYPVPKPDGRWRMVLDYREVNKTIPLTAAQNQHSAGILATIVRQ KYKTTLDLANGFWAHPITPESYWLTAFTWQGKQYCWTRLPQGFLNSPALFN ADWDLLKEIPNVQVYVDDIYLSHDDPKEHVQQLEKVFQILLQAGYWSLKKS EIGQKTVEFLGFNITKEGRGLTDTFKTKLLNITPPKDLKQLQSILGLLNFARNFI PNFAELVQPLYNLIAPAKGKYIEWSEENTKQLNMVIEALNTASNLEERLPEQR LVIKVNTSPSAGYVRYYNETGKKPIMYLNYVFSKAELKFSMLEKLLTTMHKAL IKAMDLAMGQEILVYSPIVSMTKIQKTPLPERKALPIRWITWMTYLEDPRIQFH YDKTLPELKHIPDVYTSSQSPVKHPSQYEGVFYTDGSAIKSPDPTKSNNAGM GIVHATYKPEYQVLNQWSIPLGNHTAQMAEIAAVEFACKKALKIPGPVLVITD SFYVAESANKELPYWKSNGFVNNKKKPLKHISKWKSIAECLSMKPDITIQHE KGISLQIPVFILKGNALADKLATQGSYVVN 10220 FOAMV-P 14350-Pro_2mut A VPWLTQQPLQLTILVPLQEYQEKILSKTALPEDQKQQLKTLFVKYDNLWQHW ENQVGHRKIRPHNIATGDYPPRPQKQYPINPKAKPSIQIVIDDLLKQGVLTPQ NSTMNTPVYPVPKPDGRWRMVLDYREVNKTIPLTAAQNQHSAGILATIVRQ KYKTTLDLANGFWAHPITPESYWLTAFTWQGKQYCWTRLPQGFLNSPALFN ADWDLLKEIPNVQVYVDDIYLSHDDPKEHVQQLEKVFQILLQAGYWSLKKS EIGQKTVEFLGFNITKEGRGLTDTFKTKLLNITPPKDLKQLQSILGKLNFARNFI PNFAELVQPLYNLIAPAKGKYIEWSEENTKQLNMVIEALNTASNLEERLPEQR LVIKVNTSPSAGYVRYYNETGKKPIMYLNYVFSKAELKFSMLEKLLTTMHKAL IKAMDLAMGQEILVYSPIVSMTKIQKTPLPERKALPIRWITWMTYLEDPRIQFH YDKTLPELKHIPDVYTSSQSPVKHPSQYEGVFYTDGSAIKSPDPTKSNNAGM GIVHATYKPEYQVLNQWSIPLGNHTAQMAEIAAVEFACKKALKIPGPVLVITD SFYVAESANKELPYWKSNGFVNNKKKPLKHISKWKSIAECLSMKPDITIQHE KGISLQIPVFILKGNALADKLATQGSYVVN 10221 GALV.P2 1414_3mu tA VLNLEEEYRLHEKPVPSSIDPSWLQLFPTVWAERAGMGLANQVPPWVELR SGASPVAVRQYPMSKEAREGIRPHIQKFLDLGVLVPCRSPWNTPLLPVKKP GTNDYRPVQDLREINKRVQDIHPTVPNPYNLLSSLPPSYTWYSVLDLKDAFF CLRLHPNSQPLFAFEWKDPEKGNTGQLTWTRLPQGFKNSPTLFNEALHRDL APFRALNPQVVLLQYVDDLLVAAPTYEDCKKGTQKLLQELSKLGYRVSAKKA QLCQREVTYLGYLLKEGKRWLTPARKATVMKIPVPTTPRQVREFLGKAGFC RLFIPGFASLAAPLYPLTKPSIPFIWTEEHQQAFDHIKKALLSAPALALPDLTK PFTLYIDERAGVARGVLTQTLGPWRRPVAYLSKKLDPVASGWPTCLKAVAA VALLLKDADKLTLGQNVTVIASHSLESIVRQPPDRWMTNARMTHYQSLLLNE RVSFAPPAVLNPATLLPVESEATPVHRCSEILAEETGTRRDLEDQPLPGVPT WYTDGSSFITEGKRRAGAPIVDGKRTVWASSLPEGTSAQKAELVALTQALR LAEGKNINIYTDSRYAFATAHIHGAIYKQRGWLTSAGKDIKNKEEILALLEAIHL PRRVAIIHCPGHQRGSNPVATGNRRADEAAKQAALSTRVLAGTTKP 10222 HTLV2_P 03363 HLPPPPQVDQFPLNLPERLQALNDLVSKALEAGHIEPYSGPGNNPVFPVKKP NGKWRFIHDLRATNAITTTLTSPSPGPPDLTSLPTALPHLQTIDLTDAFFQIPL PKQYQPYFAFTIPQPCNYGPGTRYAWTVLPQGFKNSPTLFEQQLAAVLNPM RKMFPTSTIVQYMDDILLASPTNEELQQLSQLTLQALTTHGLPISQEKTQQTP GQIRFLGQVISPNHITYESTPTIPIKSQWTLTELQVILGEIQWVSKGTPILRKHL 10223 RT name RT amino acid sequence SEQID NOs QSLYSALHGYRDPRACITLTPQQLHALHAIQQALQHNCRGRLNPALPLLGLIS LSTSGTTSVIFQPKQNWPLAWLHTPHPPTSLCPWGHLLACTILTLDKYTLQH YGQLCQSFHHNMSKQALCDFLRNSPHPSVGILIHHMGRFHNLGSQPSGPW KTLLHLPTLLQEPRLLRPIFTLSPWLDTAPCLFSDGSPQKAAYVLWDQTILQ QDITPLPSHETHSAQKGELLALICGLRAAKPWPSLNIFLDSKYLIKYLHSLAIG AFLGTSAHQTLQAALPPLLQGKTIYLHHVRSHTNLPDPISTFNEYTDSLILAPL VPL HTLV2.P 03363_2m ut HLPPPPQVDQFPLNLPERLQALNDLVSKALEAGHIEPYSGPGNNPVFPVKKP NGKWRFIHDLRATNAITTTLTSPSPGPPDLTSLPTALPHLQTIDLTDAFFQIPL PKQYQPYFAFTIPQPCNYGPGTRYAWTVLPQGFKNSPTLFQQQLAAVLNPM RKMFPTSTIVQYMDDILLASPTNEELQQLSQLTLQALTTHGLPISQEKTQQTP GQIRFLGQVISPNHITYESTPTIPIKSQWTLTELQVILGEIQWVSKGTPILRKHL QSLYSALHPYRDPRACITLTPQQLHALHAIQQALQHNCRGRLNPALPLLGLIS LSTSGTTSVIFQPKQNWPLAWLHTPHPPTSLCPWGHLLACTILTLDKYTLQH YGQLCQSFHHNMSKQALCDFLRNSPHPSVGILIHHMGRFHNLGSQPSGPW KTLLHLPTLLQEPRLLRPIFTLSPWLDTAPCLFSDGSPQKAAYVLWDQTILQ QDITPLPSHETHSAQKGELLALICGLRAAKPWPSLNIFLDSKYLIKYLHSLAIG AFLGTSAHQTLQAALPPLLQGKTIYLHHVRSHTNLPDPISTFNEYTDSLILAPL VPL 10224 K0RV_Q9 TTC1_3m ut TLGDQGSRGSDPLPEPRVTLTVEGIPTEFLVNTGAEHSVLTKPMGKMGSKR TWAGATGSKVYPWTTKRLLKIGQKQVTHSFLVIPECPAPLLGRDLLTKLKA QIQFSTEGPQVTWEDRPAMCLVLNLEEEYRLHEKPVPPSIDPSWLQLFPMV WAEKAGMGLANQVPPWVELKSDASPVAVRQYPMSKEAREGIRPHIQRFLD LGILVPCQSPWNTPLLPVKKPGTNDYRPVQDLREVNKRVQDIHPTVPNPYN LLSSLPPSHTWYSVLDLKDAFFCLKLHPNSQPLFAFEWRDPEKGNTGQLTW TRLPQGFKNSPTLFNEALHRDLASFRALNPQWMLQYVDDLLVAAPTYRDC KEGTRRLLQELSKLGYRVSAKKAQLCREEVTYLGYLLKGGKRWLTPARKAT VMKIPTPTTPRQVREFLGTAGFCRLWIPGFASLAAPLYPLTRPKVPFTWTEA HQEAFGRIKEALLSAPALALPDLTKPFALYVDEKEGVARGVLTQTLGPWRRP VAYLSKKLDPVASGWPTCLKAIAAVALLLKDADKLTLGQNVLVIAPHNLESIV RQPPDRWMTNARMTHYQSLLLNERVSFAPPAILNPATLLPVESDDTPIHICS EILAEETGTRPDLRDQPLPGVPAWYTDGSSFIMDGRRQAGAAIVDNKRTVW ASNLPEGTSAQKAELIALTQALRLAEGKSINIYTDSRYAFATAHVHGAIYKQR GWLTSAGKDIKNKEEILALLEAIHLPKRVAIIHCPGHQRGTDPVATGNRKADE AAKQAAQSTRILTETTKN 10225 K0RV_Q9 TTC1_3m utA TLGDQGSRGSDPLPEPRVTLTVEGIPTEFLVNTGAEHSVLTKPMGKMGSKR TWAGATGSKVYPWTTKRLLKIGQKQVTHSFLVIPECPAPLLGRDLLTKLKA QIQFSTEGPQVTWEDRPAMCLVLNLEEEYRLHEKPVPPSIDPSWLQLFPMV WAEKAGMGLANQVPPVWELKSDASPVAVRQYPMSKEAREGIRPHIQRFLD LGILVPCQSPWNTPLLPVKKPGTNDYRPVQDLREVNKRVQDIHPTVPNPYN LLSSLPPSHTWYSVLDLKDAFFCLKLHPNSQPLFAFEWRDPEKGNTGQLTW TRLPQGFKNSPTLFNEALHRDLASFRALNPQWMLQYVDDLLVAAPTYRDC KEGTRRLLQELSKLGYRVSAKKAQLCREEVTYLGYLLKGGKRWLTPARKAT VMKIPTPTTPRQVREFLGKAGFCRLFIPGFASLAAPLYPLTRPKVPFTWTEA 10226 RT name RT amino acid sequence SEQID NOs HQEAFGRIKEALLSAPALALPDLTKPFALYVDEKEGVARGVLTQTLGPWRRP VAYLSKKLDPVASGWPTCLKAIAAVALLLKDADKLTLGQNVLVIAPHNLESIV RQPPDRWMTNARMTHYQSLLLNERVSFAPPAILNPATLLPVESDDTPIHICS EILAEETGTRPDLRDQPLPGVPAWYTDGSSFIMDGRRQAGAAIVDNKRTVW ASNLPEGTSAQKAELIALTQALRLAEGKSINIYTDSRYAFATAHVHGAIYKQR GWLTSAGKDIKNKEEILALLEAIHLPKRVAIIHCPGHQRGTDPVATGNRKADE AAKQAAQSTRILTETTKN K0RV_Q9 TTC1- Pro_3mut LLGRDLLTKLKAQIQFSTEGPQVTWEDRPAMCLVLNLEEEYRLHEKPVPPSI DPSWLQLFPMVWAEKAGMGLANQVPPVWELKSDASPVAVRQYPMSKEA REGIRPHIQRFLDLGILVPCQSPWNTPLLPVKKPGTNDYRPVQDLREVNKRV QDIHPTVPNPYNLLSSLPPSHTWYSVLDLKDAFFCLKLHPNSQPLFAFEWRD PEKGNTGQLTWTRLPQGFKNSPTLFNEALHRDLASFRALNPQVVMLQYVD DLLVAAPTYRDCKEGTRRLLQELSKLGYRVSAKKAQLCREEVTYLGYLLKG GKRWLTPARKATVMKIPTPTTPRQVREFLGTAGFCRLWIPGFASLAAPLYPL TRPKVPFTWTEAHQEAFGRIKEALLSAPALALPDLTKPFALYVDEKEGVARG VLTQTLGPWRRPVAYLSKKLDPVASGWPTCLKAIAAVALLLKDADKLTLGQN VLVIAPHNLESIVRQPPDRWMTNARMTHYQSLLLNERVSFAPPAILNPATLLP VESDDTPIHICSEILAEETGTRPDLRDQPLPGVPAWYTDGSSFIMDGRRQAG AAIVDNKRTVWASNLPEGTSAQKAELIALTQALRLAEGKSINIYTDSRYAFAT AHVHGAIYKQRGWLTSAGKDIKNKEEILALLEAIHLPKRVAIIHCPGHQRGTD PVATGNRKADEAAKQAAQSTRILTETTKN 10227 K0RV_Q9 TTC1-Pro_3mut A LLGRDLLTKLKAQIQFSTEGPQVTWEDRPAMCLVLNLEEEYRLHEKPVPPSI DPSWLQLFPMVWAEKAGMGLANQVPPVWELKSDASPVAVRQYPMSKEA REGIRPHIQRFLDLGILVPCQSPWNTPLLPVKKPGTNDYRPVQDLREVNKRV QDIHPTVPNPYNLLSSLPPSHTWYSVLDLKDAFFCLKLHPNSQPLFAFEWRD PEKGNTGQLTWTRLPQGFKNSPTLFNEALHRDLASFRALNPQVVMLQYVD DLLVAAPTYRDCKEGTRRLLQELSKLGYRVSAKKAQLCREEVTYLGYLLKG GKRWLTPARKATVMKIPTPTTPRQVREFLGKAGFCRLFIPGFASLAAPLYPL TRPKVPFTWTEAHQEAFGRIKEALLSAPALALPDLTKPFALYVDEKEGVARG VLTQTLGPWRRPVAYLSKKLDPVASGWPTCLKAIAAVALLLKDADKLTLGQN VLVIAPHNLESIVRQPPDRWMTNARMTHYQSLLLNERVSFAPPAILNPATLLP VESDDTPIHICSEILAEETGTRPDLRDQPLPGVPAWYTDGSSFIMDGRRQAG AAIVDNKRTVWASNLPEGTSAQKAELIALTQALRLAEGKSINIYTDSRYAFAT AHVHGAIYKQRGWLTSAGKDIKNKEEILALLEAIHLPKRVAIIHCPGHQRGTD PVATGNRKADEAAKQAAQSTRILTETTKN 10228 MLVAV.P 03356_3m utA TLNLEDEYRLYETSAEPEVSPGSTWLSDFPQAWAETGGMGLAVRQAPLIIPL KATSTPVSIKQYPMSQEAKLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPG TNDYRPVQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHRWYTVLDLKDAFF CLRLHPTSQPLFAFEWRDPGMGISGQLTWTRLPQGFKNSPTLFNEALHRDL ADFRIQHPDLILLQYVDDILLAATSELDCQQGTRALLLTLGNLGYRASAKKAQ LCQKQVKYLGYLLKEGQRWLTEARKETVMGQPTPKTPRQLREFLGKAGFC RLFIPGFAEMAAPLYPLTKPGTLFNWGPDQQKAYQEIKQALLTAPALGLPDL TKPFELFVDEKQGYAKGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLRM VAAIAVLRKDAGKLTMGQPLVILAPHAVEALVKQPPDRWLSNARMTHYQAM 10229 RT name RT amino acid sequence SEQID NOs LLDTDRVQFGPWALNPATLLPLPEEGAPHDCLEILAETHGTRPDLTDQPIPD ADHTWYTDGSSFLQEGQRKAGAAVTTETEVIWARALPAGTSAQRAELIALT QALKMAEGKRLNVYTDSRYAFATAHIHGEIYRRRGWLTSEGREIKNKSEILA LLKALFLPKRLSIIHCLGHQKGDSAEARGNRLADQAAREAAIKTPPDTSTLL MLVBM_ Q7SVK7_ 3mutA_W S LGIEDEYRLHETSTEPDVSLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPLK ATSTPVSIQQYPMSHEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPG TNDYRPVQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAFF CLRLHPTSQPLFAFEWRDPGMGISGQLTWTRLPQGFKNSPTLFNEALHRDL ADFRIQHPDLILLQYVDDILLAATSELDCQQGTRALLQTLGDLGYRASAKKAQ ICQKQVKYLGYLLREGQRWLTEARKETVMGQPVPKTPRQLREFLGKAGFC RLFIPGFAEMAAPLYPLTKPGTLFSWGPDQQKAYQEIKQALLTAPALGLPDL TKPFELFVDEKQGYAKGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLRM VAAIAVLTKDAGKLTMGQPLVILAPHAVEALVKQPPDRWLSNARMTHYQAM LLDTDRVQFGPWALNPATLLPLPEEGAPHDCLEILAETHGTRPDLTDQPIPD ADHTWYTDGSSFLQEGQRKAGAAVTTETEVIWAGALPAGTSAQRAELIALT QALKMAEGKRLNVYTDSRYAFATAHIHGEIYRRRGWLTSEGREIKNKSEILA LLKALFLPKRLSIIHCLGHQKGDSAEARGNRLADQAAREAAIKTPPDTSTLLI 10230 MLVCB_P 08361 _3m utA TLNIEDEYRLHETSKEPDVSLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPL KATSTPVSIKQYPMSQEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKP GTNDYRPVQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAF FCLRLHPTSQPLFAFEWRDPEMGISGQLTWTRLPQGFKNSPTLFNEALHRD LAGFRIQHPDLILLQYVDDLLLAATSELDCQQGTRALLQTLGDLGYRASAKKA QICQKQVKYLGYLLKEGQRWLTEARKETVMGQPIPKTPRQLREFLGKAGFC RLFIPGFAEMAAPLYPLTKPGTLFNWGPDQQKAFQEIKQALLTAPALGLPDL TKPFELFVDEKQGYAKGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLRM VAAIAVLTKDAGKLTMGQPLVILAPHAVEALVKQPPDRWLSNARMTHYQALL LDTDRVQFGPVVALNPATLLPLPEEGLQHDCLDILAEAHGTRSDLMDQPLPD ADHTWYTDGSSFLQEGQRKAGAAVTTETEVIWARALPAGTSAQRAELIALT QALKMAEGKKLNVYTDSRYAFATAHIHGEIYRRRGWLTSEGKEIKNKDEILAL LKALFLPKRLSIIHCPGHQKGNSAEARGNRMADQAAREVATRETPETSTLL 10231 MLVFF.P 26809_3m utA TLNIEDEYRLHETSKGPDVPLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPL KATSTPVSIKQYPMSQEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKP GTNDYRPVQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAF FCLRLHPTSQSLFAFEWRDPEMGISGQLTWTRLPQGFKNSPTLFNEALHRD LADFRIQHPDLILLQYVDDLLLAATSELDCQQGTRALLQTLGDLGYRASAKKA QICQKQVKYLGYLLKEGQRWLTEARKETVMGQPTPKTPRQLREFLGKAGF CRLFIPGFAEMAAPLYPLTKPGTLFEWGPDQQKAYQEIKQALLTAPALGLPD LTKPFELFVDEKQGYAKGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLR MVAAIAVLTKDAGKLTMGQPLVILAPHAVEALVKQPPDRWLSNARMTHYQA LLLDTDRVQFGPIVALNPATLLPLPEEGLQHDCLDILAEAHGTRPDLTDQPLP DADHTWYTDGSSFLQEGQRKAGAAVTTETEWWAKALPAGTSAQRAELIAL TQALKMAEGKKLNVYTDSRYAFATAHIHGEIYRRRGWLTSEGKEIKNKDEIL ALLKALFLPKRLSIIHCPGHQKGNRAEARGNRMADQAAREVATRETPETSTL L 10232 RT name RT amino acid sequence SEQID NOs MLVMS.P 03355_3m utA.WS TLNIEDEHRLHETSKEPDVSLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPL KATSTPVSIKQYPMSQEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKP GTNDYRPVQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAF FCLRLHPTSQPLFAFEWRDPEMGISGQLTWTRLPQGFKNSPTLFNEALHRD LADFRIQHPDLILLQYVDDLLLAATSELDCQQGTRALLQTLGNLGYRASAKKA QICQKQVKYLGYLLKEGQRWLTEARKETVMGQPTPKTPRQLREFLGKAGF CRLFIPGFAEMAAPLYPLTKPGTLFNWGPDQQKAYQEIKQALLTAPALGLPD LTKPFELFVDEKQGYAKGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLR MVAAIAVLTKDAGKLTMGQPLVILAPHAVEALVKQPPDRWLSNARMTHYQA LLLDTDRVQFGPWALNPATLLPLPEEGLQHNCLDILAEAHGTRPDLTDQPL PDADHTWYTDGSSLLQEGQRKAGAAVTTETEVIWAKALPAGTSAQRAELIA LTQALKMAEGKKLNVYTDSRYAFATAHIHGEIYRRRGWLTSEGKEIKNKDEIL ALLKALFLPKRLSIIHCPGHQKGHSAEARGNRMADQAARKAAITETPDTSTLL 10233 PERV.Q4 VFZ2_3m ut TLQLDDEYRLYSPLVKPDQNIQFWLEQFPQAWAETAGMGLAKQVPPQVIQL KASATPVSVRQYPLSKEAQEGIRPHVQRLIQQGILVPVQSPWNTPLLPVRKP GTNDYRPVQDLREVNKRVQDIHPTVPNPYNLLCALPPQRSWYTVLDLKDAF FCLRLHPTSQPLFAFEWRDPGTGRTGQLTWTRLPQGFKNSPTIFNEALHRD LANFRIQHPQVTLLQYVDDLLLAGATKQDCLEGTKALLLELSDLGYRASAKK AQICRREVTYLGYSLRDGQRWLTEARKKTVVQIPAPTTAKQVREFLGTAGF CRLWIPGFATLAAPLYPLTKPKGEFSWAPEHQKAFDAIKKALLSAPALALPDV TKPFTLYVDERKGVARGVLTQTLGPWRRPVAYLSKKLDPVASGWPVCLKAI AAVAILVKDADKLTLGQNITVIAPHALENIVRQPPDRWMTNARMTHYQSLLLT ERVTFAPPAALNPATLLPEETDEPVTHDCHQLLIEETGVRKDLTDIPLTGEVL TWFTDGSSYVVEGKRMAGAAWDGTRTIWASSLPEGTSAQKAELMALTQA LRLAEGKSINIYTDSRYAFATAHVHGAIYKQRGWLTSAGREIKNKEEILSLLEA LHLPKRLAIIHCPGHQKAKDPISRGNQMADRVAKQAAQGVNLL 10234 PERV.Q4 VFZ2_3m utA.WS LDDEYRLYSPLVKPDQNIQFWLEQFPQAWAETAGMGLAKQVPPQVIQLKAS ATPVSVRQYPLSKEAQEGIRPHVQRLIQQGILVPVQSPWNTPLLPVRKPGTN DYRPVQDLREVNKRVQDIHPTVPNPYNLLCALPPQRSWYTVLDLKDAFFCL RLHPTSQPLFAFEWRDPGTGRTGQLTWTRLPQGFKNSPTIFNEALHRDLAN FRIQHPQVTLLQYVDDLLLAGATKQDCLEGTKALLLELSDLGYRASAKKAQIC RREVTYLGYSLRDGQRWLTEARKKTWQIPAPTTAKQVREFLGKAGFCRLFI PGFATLAAPLYPLTKPKGEFSWAPEHQKAFDAIKKALLSAPALALPDVTKPFT LYVDERKGVARGVLTQTLGPWRRPVAYLSKKLDPVASGWPVCLKAIAAVAIL VKDADKLTLGQNITVIAPHALENIVRQPPDRWMTNARMTHYQSLLLTERVTF APPAALNPATLLPEETDEPVTHDCHQLLIEETGVRKDLTDIPLTGEVLTWFTD GSSYWEGKRMAGAAWDGTRTIWASSLPEGTSAQKAELMALTQALRLAEG KSINIYTDSRYAFATAHVHGAIYKQRGWLTSAGREIKNKEEILSLLEALHLPKR LAIIHCPGHQKAKDPISRGNQMADRVAKQAAQGVNLLP 10235 SFV1.P2 3074 MDPLQLLQPLEAEIKGTKLKAHWNSGATITCVPEAFLEDERPIQTMUKTIHG EKQQDVYYLTFKVQGRKVEAEVLASPYDYILLNPSDVPWLMKKPLQLTVLVP LHEYQERLLQQTALPKEQKELLQKLFLKYDALWQHWENQVGHRRIKPHNIA TGTLAPRPQKQYPINPKAKPSIQIVIDDLLKQGVLIQQNSTMNTPVYPVPKPD GKWRMVLDYREVNKTIPLIAAQNQHSAGILSSIYRGKYKTTLDLTNGFWAHPI 10236 RT name RT amino acid sequence SEQID NOs TPESYWLTAFTWQGKQYCWTRLPQGFLNSPALFTADVVDLLKEIPNVQAYV DDIYISHDDPQEHLEQLEKIFSILLNAGYWSLKKSEIAQREVEFLGFNITKEG RGLTDTFKQKLLNITPPKDLKQLQSILGLLNFARNFIPNYSELVKPLYTIVANA NGKFISWTEDNSNQLQHIISVLNQADNLEERNPETRLIIKVNSSPSAGYIRYY NEGSKRPIMYVNYIFSKAEAKFTQTEKLLTTMHKGLIKAMDLAMGQEILVYSP IVSMTKIQRTPLPERKALPVRWITWMTYLEDPRIQFHYDKSLPELQQIPNVTE DVIAKTKHPSEFAMVFYTDGSAIKHPDVNKSHSAGMGIAQVQFIPEYKIVHQ WSIPLGDHTAQLAEIAAVEFACKKALKISGPVLIVTDSFYVAESANKELPYWK SNGFLNNKKKPLRHVSKWKSIAECLQLKPDIIIMHEKGHQQPMTTLHTEGNN LADKLATQGSYWH SFV1_P2 3074-Pro VPWLMKKPLQLTVLVPLHEYQERLLQQTALPKEQKELLQKLFLKYDALWQH WENQVGHRRIKPHNIATGTLAPRPQKQYPINPKAKPSIQIVIDDLLKQGVLIQ QNSTMNTPVYPVPKPDGKWRMVLDYREVNKTIPLIAAQNQHSAGILSSIYRG KYKTTLDLTNGFWAHPITPESYWLTAFTWQGKQYCWTRLPQGFLNSPALFT ADWDLLKEIPNVQAYVDDIYISHDDPQEHLEQLEKIFSILLNAGYWSLKKSEI AQREVEFLGFNITKEGRGLTDTFKQKLLNITPPKDLKQLQSILGLLNFARNFIP NYSELVKPLYTIVANANGKFISWTEDNSNQLQHIISVLNQADNLEERNPETRL IIKVNSSPSAGYIRYYNEGSKRPIMYVNYIFSKAEAKFTQTEKLLTTMHKGLIK AMDLAMGQEILVYSPIVSMTKIQRTPLPERKALPVRWITWMTYLEDPRIQFH YDKSLPELQQIPNVTEDVIAKTKHPSEFAMVFYTDGSAIKHPDVNKSHSAGM GIAQVQFIPEYKIVHQWSIPLGDHTAQLAEIAAVEFACKKALKISGPVLIVTDSF YVAESANKELPYWKSNGFLNNKKKPLRHVSKWKSIAECLQLKPDIIIMHEKG HQQPMTTLHTEGNNLADKLATQGSYWH 10237 SFV3L_P 27401 _2m ut MDPLQLLQPLEAEIKGTKLKAHWNSGATITCVPQAFLEEEVPIKNIWIKTIHGE KEQPVYYLTFKIQGRKVEAEVISSPYDYILVSPSDIPWLMKKPLQLTTLVPLQ EYEERLLKQTMLTGSYKEKLQSLFLKYDALWQHWENQVGHRRIKPHHIATG TVNPRPQKQYPINPKAKASIQTVINDLLKQGVLIQQNSIMNTPVYPVPKPDGK WRMVLDYREVNKTIPLIAAQNQHSAGILSSIFRGKYKTTLDLSNGFWAHSITP ESYWLTAFTWLGQQYCWTRLPQGFLNSPALFNADWDLLKEVPNVQVYVD DIYISHDDPREHLEQLEKVFSLLLNAGYWSLKKSEIAQHEVEFLGFNITKEGR GLTETFKQKLLNITPPRDLKQLQSILGLLNFARNFIPNFSELVKPLYNIIATAPG KYITWTTDNSQQLQNIISMLNSAENLEERNPEVRLIMKVNTSPSAGYIRFYNE FAKRPIMYLNYVYTKAEVKFTNTEKLLTTIHKGLIKALDLGMGQEILVYSPIVS MTKIQKTPLPERKALPIRWITWMSYLEDPRIQFHYDKTLPELQQVPTVTDDIIA KIKHPSEFSMVFYTDGSAIKHPNVNKSHNAGMGIAQVQFKPEFTVINTWSIPL GDHTAQLAEVAAVEFACKKALKIDGPVLIVTDSFYVAESVNKELPYWQSNGF FNNKKKPLKHVSKWKSIADCIQLKPDIIIIHEKGHQPTASTFHTEGNNLADKLA TQGSYWN 10238 SFV3L_P 27401-Pro_2mut A IPWLMKKPLQLTTLVPLQEYEERLLKQTMLTGSYKEKLQSLFLKYDALWQH WENQVGHRRIKPHHIATGTVNPRPQKQYPINPKAKASIQTVINDLLKQGVLIQ QNSIMNTPVYPVPKPDGKWRMVLDYREVNKTIPLIAAQNQHSAGILSSIFRG KYKTTLDLSNGFWAHSITPESYWLTAFTWLGQQYCWTRLPQGFLNSPALFN ADWDLLKEVPNVQVYVDDIYISHDDPREHLEQLEKVFSLLLNAGYWSLKKS EIAQHEVEFLGFNITKEGRGLTETFKQKLLNITPPRDLKQLQSILGKLNFARNF 10239 RT name RT amino acid sequence SEQID NOs IPNFSELVKPLYNIIATAPGKYITWTTDNSQQLQNIISMLNSAENLEERNPEVR LIMKVNTSPSAGYIRFYNEFAKRPIMYLNYVYTKAEVKFTNTEKLLTTIHKGLI KALDLGMGQEILVYSPIVSMTKIQKTPLPERKALPIRWITWMSYLEDPRIQFH YDKTLPELQQVPTVTDDIIAKIKHPSEFSMVFYTDGSAIKHPNVNKSHNAGM GIAQVQFKPEFTVINTWSIPLGDHTAQLAEVAAVEFACKKALKIDGPVLIVTDS FYVAESVNKELPYWQSNGFFNNKKKPLKHVSKWKSIADCIQLKPDIIIIHEKG HQPTASTFHTEGNNLADKLATQGSYWN WDSV_O 92815 SCQTKNTLNIDEYLLQFPDQLWASLPTDIGRMLVPPITIKIKDNASLPSIRQYP LPKDKTEGLRPLISSLENQGIUKCHSPCNTPIFPIKKAGRDEYRMIHDLRAINN IVAPLTAWASPTTVLSNLAPSLHWFTVIDLSNAFFSVPIHKDSQYLFAFTFEG HQYTWTVLPQGFIHSPTLFSQALYQSLHKIKFKISSEICIYMDDVLIASKDRDT NLKDTAVMLQHLASEGHKVSKKKLQLCQQEWYLGQLLTPEGRKILPDRKV TVSQFQQPTTIRQIRAFLGLVGYCRHWIPEFSIHSKFLEKQLKKDTAEPFQLD DQQVEAFNKLKHAITTAPVLWPDPAKPFQLYTSHSEHASIAVLTQKHAGRT RPIAFLSSKFDAIESGLPPCLKACASIHRSLTQADSFILGAPLIIYTTHAICTLLQ RDRSQLVTASRFSKWEADLLRPELTFVACSAVSPAHLYMQSCENNIPPHDC VLLTHTISRPRPDLSDLPIPDPDMTLFSDGSYTTGRGGAAWMHRPVTDDFIII HQQPGGASAQTAELLALAAACHLATDKTVNIYTDSRYAYGWHDFGHLWM HRGFVTSAGTPIKNHKEIEYLLKQIMKPKQVSVIKIEAHTKGVSMEVRGNAAA DEAAKNAVFLVQR 10240 WDSV_O 92815_2m ut SCQTKNTLNIDEYLLQFPDQLWASLPTDIGRMLVPPITIKIKDNASLPSIRQYP LPKDKTEGLRPLISSLENQGIUKCHSPCNTPIFPIKKAGRDEYRMIHDLRAINN IVAPLTAWASPTTVLSNLAPSLHWFTVIDLSNAFFSVPIHKDSQYLFAFTFEG HQYTWTVLPQGFIHSPTLFNQALYQSLHKIKFKISSEICIYMDDVLIASKDRDT NLKDTAVMLQHLASEGHKVSKKKLQLCQQEWYLGQLLTPEGRKILPDRKV TVSQFQQPTTIRQIRAFLGLVGYCRHWIPEFSIHSKFLEKQLKPDTAEPFQLD DQQVEAFNKLKHAITTAPVLWPDPAKPFQLYTSHSEHASIAVLTQKHAGRT RPIAFLSSKFDAIESGLPPCLKACASIHRSLTQADSFILGAPLIIYTTHAICTLLQ RDRSQLVTASRFSKWEADLLRPELTFVACSAVSPAHLYMQSCENNIPPHDC VLLTHTISRPRPDLSDLPIPDPDMTLFSDGSYTTGRGGAAWMHRPVTDDFIII HQQPGGASAQTAELLALAAACHLATDKTVNIYTDSRYAYGWHDFGHLWM HRGFVTSAGTPIKNHKEIEYLLKQIMKPKQVSVIKIEAHTKGVSMEVRGNAAA DEAAKNAVFLVQR 10241 WDSV_O 92815_2m utA SCQTKNTLNIDEYLLQFPDQLWASLPTDIGRMLVPPITIKIKDNASLPSIRQYP LPKDKTEGLRPLISSLENQGIUKCHSPCNTPIFPIKKAGRDEYRMIHDLRAINN IVAPLTAWASPTTVLSNLAPSLHWFTVIDLSNAFFSVPIHKDSQYLFAFTFEG HQYTWTVLPQGFIHSPTLFNQALYQSLHKIKFKISSEICIYMDDVLIASKDRDT NLKDTAVMLQHLASEGHKVSKKKLQLCQQEWYLGQLLTPEGRKILPDRKV TVSQFQQPTTIRQIRAFLGKVGYCRHFIPEFSIHSKFLEKQLKPDTAEPFQLD DQQVEAFNKLKHAITTAPVLWPDPAKPFQLYTSHSEHASIAVLTQKHAGRT RPIAFLSSKFDAIESGLPPCLKACASIHRSLTQADSFILGAPLIIYTTHAICTLLQ RDRSQLVTASRFSKWEADLLRPELTFVACSAVSPAHLYMQSCENNIPPHDC VLLTHTISRPRPDLSDLPIPDPDMTLFSDGSYTTGRGGAAWMHRPVTDDFIII HQQPGGASAQTAELLALAAACHLATDKTVNIYTDSRYAYGWHDFGHLWM 10242 RT name RT amino acid sequence SEQID NOs HRGFVTSAGTPIKNHKEIEYLLKQIMKPKQVSVIKIEAHTKGVSMEVRGNAAA DEAAKNAVFLVQR WMSV.P 03359_3m utA VLNLEEEYRLHEKPVPSSIDPSWLQLFPTVWAERAGMGLANQVPPWVELR SGASPVAVRQYPMSKEAREGIRPHIQRFLDLGVLVPCQSPWNTPLLPVKKP GTNDYRPVQDLREINKRVQDIHPTVPNPYNLLSSLPPSHTWYSVLDLKDAFF CLKLHPNSQPLFAFEWRDPEKGNTGQLTWTRLPQGFKNSPTLFNEALHRDL APFRALNPQVVLLQYVDDLLVAAPTYRDCKEGTQKLLQELSKLGYRVSAKK AQLCQKEVTYLGYLLKEGKRWLTPARKATVMKIPPPTTPRQVREFLGKAGF CRLFIPGFASLAAPLYPLTKPSIPFIWTEEHQKAFDRIKEALLSAPALALPDLTK PFTLYVDERAGVARGVLTQTLGPWRRPVAYLSKKLDPVASGWPTCLKAVAA VALLLKDADKLTLGQNVTVIASHSLESIVRQPPDRWMTNARMTHYQSLLLNE RVSFAPPAVLNPATLLPVESEATPVHRCSEILAEETGTRRDLKDQPLPGVPA WYTDGSSFIAEGKRRAGAAIVDGKRTVWASSLPEGTSAQKAELVALTQALR LAEGKDINIYTDSRYAFATAHIHGAIYKQRGWLTSAGKDIKNKEEILALLEAIHL PKRVAIIHCPGHQKGNDPVATGNRRADEAAKQAALSTRVLAETTKP 10243 XMRV6.A 1Z651_3m utA TLNIEDEYRLHETSKEPDVPLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPL KATSTPVSIKQYPMSQEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKP GTNDYRPVQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAF FCLRLHPTSQPLFAFEWRDPEMGISGQLTWTRLPQGFKNSPTLFNEALHRD LADFRIQHPDLILLQYVDDLLLAATSEQDCQRGTRALLQTLGNLGYRASAKK AQICQKQVKYLGYLLKEGQRWLTEARKETVMGQPTPKTPRQLREFLGKAGF CRLFIPGFAEMAAPLYPLTKPGTLFNWGPDQQKAYQEIKQALLTAPALGLPD LTKPFELFVDEKQGYAKGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLR MVAAIAVLTKDAGKLTMGQPLVILAPHAVEALVKQPPDRWLSNARMTHYQA MLLDTDRVQFGPWALNPATLLPLPEKEAPHDCLEILAETHGTRPDLTDQPIP DADYTWYTDGSSFLQEGQRRAGAAVTTETEVIWARALPAGTSAQRAELIAL TQALKMAEGKKLNVYTDSRYAFATAHVHGEIYRRRGWLTSEGREIKNKNEIL ALLKALFLPKRLSIIHCPGHQKGNSAEARGNRMADQAAREAAMKAVLETSTL L 10244 In some embodiments, an RT domain described herein is modified, for example, by site specific mutation. In some embodiments, an RT domain is engineered to have improved properties, e.g., SuperScript IV (SSIV) RT derived from the MMLV RT. In some embodiments, an RT domain may be engineered to have lower error rates as compared to a reference RT 5 domain, e.g., as described in WO2001068895, incorporated herein by reference. In some embodiments, an RT domain may be engineered to be more thermostable as compared to a reference RT domain. In some embodiments, an RT domain may be engineered to be more processive as compared to a reference RT domain. In some embodiments, an RT domain may be engineered to have improved tolerance to inhibitors as compared to a reference RT domain. In 10 some embodiments, an RT domain may be engineered to be faster as compared to a reference RT domain. In some embodiments, an RT domain may be engineered to better tolerate modified nucleotides in an RNA template as compared to a reference RT domain. In some embodiments, an RT domain may be engineered to be capable of inserting modified DNA nucleotides. In some embodiments, an RT domain is engineered to bind a template RNA. In some embodiments, one or more mutations are chosen from D200N, L603W, T33OP, D524G, E562Q, D583N, P51L, S67R, E67K, T197A, H204R, E302K, F309N, W313F, L435G, N454K, H594Q, L671P, E69K, H8Y, T306K, or D653N in an RT domain of murine leukemia virus reverse transcriptase or a corresponding mutation at a corresponding position of another RT domain. In some embodiments, a gene modifying polypeptide comprises an RT domain from a retroviral reverse transcriptase, e.g., a wild-type M-MLV RT, e.g., comprising the following sequence: M-MLV (WT): TLNIEDEYRLHETSKEPDVSLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPLKA TSTPVSIKQYPMSQEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPGTNDY RPVQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAFFCLRLHPT SQPLFAFEWRDPEMGISGQLTWTRLPQGFKNSPTLFDEALHRDLADFRIQHPDLI LLQYVDDLLLAATSELDCQQGTRALLQTLGNLGYRASAKKAQICQKQVKYLG YLLKEGQRWLTEARKETVMGQPTPKTPRQLREFLGTAGFCRLWIPGFAEMAAP LYPLTKTGTLFNWGPDQQKAYQEIKQALLTAPALGLPDLTKPFELFVDEKQGYA KGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLRMVAAIAVLTKDAGKLTMG QPLVILAPHAVEALVKQPPDRWLSNARMTHYQALLLDTDRVQFGPVVALNPAT LLPLPEEGLQHNCLDILAEAHGTRPDLTDQPLPDADHTWYTDGSSLLQEGQRKA GAAVTTETEVIWAKALPAGTSAQRAELIALTQALKMAEGKKLNVYTDSRYAFA TAHIHGEIYRRRGLLTSEGKEIKNKDEILALLKALFLPKRLSIIHCPGHQKGHSAE ARGNRMADQAARKAAITETPDTSTLLI (SEQ ID NO: 5002) In some embodiments, a gene modifying polypeptide comprises an RT domain from a retroviral reverse transcriptase, e.g., an M-MLV RT, e.g., comprising the following sequence: TLNIEDEHRLHETSKEPDVSLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPLKA TSTPVSIKQYPMSQEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPGTNDY RPVQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAFFCLRLHPT SQPLFAFEWRDPEMGISGQLTWTRLPQGFKNSPTLFDEALHRDLADFRIQHPDLI LLQYVDDLLLAATSELDCQQGTRALLQTLGNLGYRASAKKAQICQKQVKYLG YLLKEGQRWLTEARKETVMGQPTPKTPRQLREFLGTAGFCRLWIPGFAEMAAP LYPLTKTGTLFNWGPDQQKAYQEIKQALLTAPALGLPDLTKPFELFVDEKQGYA KGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLRMVAAIAVLTKDAGKLTMG QPLVILAPHAVEALVKQPPDRWLSNARMTHYQALLLDTDRVQFGPVVALNPAT LLPLPEEGLQHNCLDILAEAHGTRPDLTDQPLPDADHTWYTDGSSLLQEGQRKA GAAVTTETEVIWAKALPAGTSAQRAELIALTQALKMAEGKKLNVYTDSRYAFA TAHIHGEIYRRRGLLTSEGKEIKNKDEILALLKALFLPKRLSIIHCPGHQKGHSAE ARGNRMADQAARKAAITETPDTSTLL (SEQ ID NO: 5003) In some embodiments, a gene modifying polypeptide comprises an RT domain from a retroviral reverse transcriptase comprising the sequence of amino acids 659-1329 of NP_057933. In some embodiments, a gene modifying polypeptide further comprises one additional amino acid at the N-terminus of the sequence of amino acids 659-1329 of NP_057933, e.g., as shown below: TLNIEDEHRLHETSKEPDVSLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPLKATS TPVSIKQYPMSQEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPGTNDYRPV QDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAFFCLRLHPTS QPLFAFEWRDPEMGISGQLTWTRLPQGFKNSPTLFDEALHRDLADFRIQHPD LILLQYVDDLLLAATSELDCQQGTRALLQTLGNLGYRASAKKAQICQKQVK YLGYLLKEGQRWLTEARKETVMGQPTPKTPRQLREFLGTAGFCRLWIPGFAEMA APLYPLTKTGTLFNWGPDQQKAYQEIKQALLTAPALGLPDLTKPFELFVDEKQGY AKGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLRMVAAIAVLTKDAGKLTMG QPLVILAPHAVEALVKQPPDRWLSNARMTHYQALLLDTDRVQFGPVVALNPATL LPLPEEGLQHNCLDILAEAHGTRPDLTDQPLPDADH7WETDG55LLeEGeR / C4GA4 VTTETEVIWAKALPAGTSAQRAELIALTQALKMAEGKKLNVYTDSRYAFATAHIHGEIYR RRGEETSEGKEIKNKDEIEAEEKAEEEPKRESI1HCPGHQKGHSAEARGNRMADQAARK AA (SEQ ID NO: 5004) Core RT (bold), annotated per above RNAseH (italics), annotated per above In some embodiments, a gene modifying polypeptide further comprises one additional amino acid at the C-terminus of the sequence of amino acids 659-1329 of NP_057933. In embodiments, a gene modifying polypeptide comprises an RNaseHl domain (e.g., amino acids 1178-1318 of NP_057933). In some embodiments, a retroviral reverse transcriptase domain, e.g., M-MLV RT, may comprise one or more mutations from a wild-type sequence that may improve features of the RT, e.g., thermostability, processivity, and / or template binding. In some embodiments, an M-MLV RT domain comprises, relative to the M-MLV (WT) sequence above, one or more mutations, e.g., selected from D200N, L603W, T330P, T306K, W313F, D524G, E562Q, D583N, P51L, S67R, E67K, T197A, H204R, E302K, F309N, L435G, N454K, H594Q, D653N, RI 10S, K103L, or a combination thereof. In some embodiments, an M-MLV RT domain comprises, relative to the M-MLV (WT) sequence above, a combination of mutations including D200N, L603W, and T330P, and optionally further including T306K and W313F. In some embodiments, an M-MLV RT used herein comprises D200N, L603W, T33OP, T306K and W313F mutations. In some embodiments, a mutant M-MLV RT comprises the following amino acid sequence: M-MLV (PE2): TLNIEDEYRLHETSKEPDVSLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPLKAT STPVS1KQYPMSQEARLG1KPH1QRLLDQG1LVPCQSPWNTPLLPVKKPGTNDYRP VQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAFFCLRLHPTSQP LFAFEWRDPEMGISGQLTWTRLPQGFKNSPTLFNEALHRDLADFRIQHPDLILLQ YVDDLLLAATSELDCQQGTRALLQTLGNLGYRASAKKAQICQKQVKYLGYLLK EGQRWLTEARKETVMGQPTPKTPRQLREFLGKAGFCRLFIPGFAEMAAPLYPLT KPGTLFNWGPDQQKAYQEIKQALLTAPALGLPDLTKPFELFVDEKQGYAKGVLT QKLGPWRRPVAYLSKKLDPVAAGWPPCLRMVAAIAVLTKDAGKLTMGQPLVIL APHAVEALVKQPPDRWLSNARMTHYQALLLDTDRVQFGPVVALNPATLLPLPE EGLQHNCLDILAEAHGTRPDLTDQPLPDADHTWYTDGSSLLQEGQRKAGAAVT TETEVIWAKALPAGTSAQRAELIALTQALKMAEGKKLNVYTDSRYAFATAHIHG EIYRRRGWLTSEGKEIKNKDEILALLKALFLPKRLSIIHCPGHQKGHSAEARGNR MADQAARKAAITETPDTSTLLI (SEQ ID NO: 5005) RT Families and Mutants In some embodiments, a gene modifying polypeptide comprises the amino acid sequence of an RT domain sequence from a family selected from: AVIRE, BAEVM, FFV, FLV, FOAMV, GALV, KORV, MLVAV, MLVBM, MLVCB, MLVFF, ML VMS, PERV, SFV1, SFV3L, WMSV, XMRV6, BLVAU, BLVJ, HTL1A, HTL1C, HTL1L, HTL32, HTL3P, HTLV2, JSRV, MLVF5, MLVRD, MMTVB, MPMV, SFVCP, SMRVH, SRV1, SRV2, and WDSV. In some embodiments, a gene modifying polypeptide comprises the amino acid sequence of an RT domain sequence from a family selected from: AVIRE, BAEVM, FFV, FLV, FOAMV, GALV, KORV, MLVAV, MLVBM, MLVCB, MLVFF, MLVMS, PERV, SFV1, SFV3L, WMSV, and XMRV6. In some embodiments, a gene modifying polypeptide comprises the amino acid sequence of an RT domain sequence from an MLVMS RT domain. In some embodiments, the amino acid sequence of an RT domain sequence comprises one or more point mutations as listed in column 1 of Table 2, or a point mutation corresponding thereto. In some embodiments, the amino acid sequence of an RT domain sequence comprises one or more point mutations as listed in column 3 of Table 2 (Genl MLVMS), or a point mutation corresponding thereto. In some embodiments, the amino acid sequence of an RT domain sequence comprises one or more point mutations at an amino acid position of the RT domain as listed in columns 1 and 2 of Table 3, or an amino acid position corresponding thereto. In some embodiments, a gene modifying polypeptide comprises the amino acid sequence of an RT domain sequence from an AVIRE RT domain. In some embodiments, the amino acid sequence of an RT domain sequence comprises one or more point mutations as listed in column 2 of Table 2, or a point mutation corresponding thereto. In some embodiments, the amino acid 5 sequence of an RT domain sequence comprises one or more point mutations as listed in column 4 of Table 2 (Gen2 AVIRE), or a point mutation corresponding thereto. In some embodiments, the amino acid sequence of an RT domain sequence comprises one or more point mutations at an amino acid position of the RT domain as listed in columns 3 and 4 of Table 3, or an amino acid position corresponding thereto. In some embodiments, an RT domain comprises an IENSSP 10   (e.g., at the C-terminus). Table 2. Exemplary point mutations in ML VMS and AVIRE RT domains RT-linker filing (MLVMS) Corresponding AVIRE Genl MLVMS (PLV4921) Gen2 AVIRE (PLV10990) H8Y P51L Q51L S67R T67R E67K E67K E69K E69K T197A T197A D200N D200N D200N D200N H204R N204R E302K E302K T306K T306K F309N Y309N W313F W313F W313F W313F T330P G330P T330P G330P L435G T436G N454K N455K D524G D526G E562Q E564Q D583N D585N H594Q H596Q L603W L605W L603W L605W D653N D655N L671P L673P IENSSP atC-term Table 3. Positions that can be mutated in exemplary ML VMS and AVIRE RT domains WT residue & position MLVMS aa MLVMS position # * AVIRE aa AVIRE position # * H 8 Y 8 P 51 Q 51 S 67 T 67 E 69 E 69 T 197 T 197 D 200 D 200 H 204 N 204 E 302 E 302 T 306 T 306 F 309 Y 309 W 313 W 313 T 330 G 330 L 435 T 436 N 454 N 455 D 524 D 526 E 562 E 564 D 583 D 585 H 594 H 596 L 603 L 605 D 653 D 655 L 671 S 673 In some embodiments, a gene modifying polypeptide comprises a gamma retrovirus derived RT domain. In some embodiments, a gamma retrovirus-derived RT domain of a gene modifying polypeptide comprises the amino acid sequence of an RT domain sequence from a 5 family selected from: AVIRE, BAEVM, FFV, FLV, FOAMV, GALV, KORV, MLVAV, MLVBM, MLVCB, MLVFF, ML VMS, PERV, SFV1, SFV3L, WMSV, and XMRV6. In some embodiments, a gamma retrovirus-derived RT domain of a gene modifying polypeptide is not derived from PERV. In some embodiments, an RT domain includes one, two, three, four, five, six or more mutations shown in Table 4 and corresponding to mutations D200N, L603W, 10   T330P, D524G, E562Q, D583N, P51L, S67R, E67K, T197A, H204R, E302K, F309N, W313F, L435G, N454K, H594Q, L671P, E69K, or D653N in the RT domain of murine leukemia virus reverse transcriptase. In some embodiments, a gene modifying polypeptide further comprises a linker having at least 99% or 100% identity to SEQ ID NO: 5217. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of an AVIRE RT (e.g., an AVIRE_P03360 sequence, e.g., SEQ ID NO: 8001), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of an AVIRE RT further comprising one, two, three, four, or five mutations selected from the group consisting of D200N, G33OP, L605W, T306K, and W313F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an AVIRE RT further comprising one, two, or three mutations selected from the group consisting of D200N, G33OP, and L605W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of a BAEVM RT (e.g., an BAEVM_P10272 sequence, e.g., SEQ ID NO: 8004), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a BAEVM RT further comprising one, two, three, four, or five mutations selected from the group consisting of D198N, E328P, L602W, T304K, and W311F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a BAEVM RT further comprising one, two, or three mutations selected from the group consisting of D198N, E328P, and L602W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of an FFV RT (e.g., an FFV_O93209 sequence, e.g., SEQ ID NO: 8012), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of an FFV RT further comprising one, two, three, or four mutations selected from the group consisting of D21N, T293N, T419P, and L393K, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an FFV RT further comprising one, two, or three mutations selected from the group consisting of D21N, T293N, and T419P, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an FFV RT further comprising the mutation D21N. In some embodiments, an RT domain comprises the amino acid sequence of an FFV RT further comprising one, two, or three mutations selected from the group consisting of T207N, T333P, and L307K, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an FFV RT further comprising one or two mutations selected from the group consisting of T207N and T333P, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of an FLV RT (e.g., an FLV_P10273 sequence, e.g., SEQ ID NO: 8019), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of an FLV RT further comprising one, two, three, or four mutations selected from the group consisting of D199N, L602W, T305K, and W312F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an FLV RT further comprising one or two mutations selected from the group consisting of D199N and L602W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of a FOAMV RT (e.g., a FOAMV_P14350 sequence, e.g., SEQ ID NO: 8021), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a FOAMV RT further comprising one, two, three, or four mutations selected from the group consisting of D24N, T296N, S420P, and L396K, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a FOAMV RT further comprising one, two, or three mutations selected from the group consisting of D24N, T296N, and S420P, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a FOAMV RT further comprising the mutation D24N, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a FOAMV RT further comprising one, two, or three mutations selected from the group consisting of T207N, S331P, and L307K, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a FOAMV RT further comprising one or two mutations selected from the group consisting of T207N and S331P, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of a GALV RT (e.g., an GALV_P21414 sequence, e.g., SEQ ID NO: 8027), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a GALV RT further comprising one, two, three, four, or five mutations selected from the group consisting of D198N, E328P, L600W, T304K, and W31 IF, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a GALV RT further comprising one, two, or three mutations selected from the group consisting of D198N, E328P, and L600W, or a corresponding position in a homologous RT domain. In embodiments, an RT domain comprises the amino acid sequence of an RT domain of a KORV RT (e.g., an KORV_Q9TTC1 sequence, e.g., SEQ ID NO: 8047), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a GALV RT further comprising one, two, three, four, five, or six mutations selected from the group consisting of D32N, D322N, E452P, L274W, T428K, and W435F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a GALV RT further comprising one, two, three, or four mutations selected from the group consisting of D32N, D322N, E452P, and L274W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a GALV RT further comprising the mutation D32N. In some embodiments, an RT domain comprises the amino acid sequence of a KORV RT further comprising one, two, three, four, or five mutations selected from the group consisting of D23IN, E361P, L633W, T337K, and W344F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a KORV RT further comprising one, two, or three mutations selected from the group consisting of D231N, E361P, and L633W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of a MLVAV RT (e.g., an MLVAV_P03356 sequence, e.g., SEQ ID NO: 8053), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a MLVAV RT further comprising one, two, three, four, or five mutations selected from the group consisting of D200N, T33OP, L603W, T306K, and W313F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a MLVAV RT further comprising one, two, or three mutations selected from the group consisting of D200N, T33OP, and L603W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of a MLVBM RT (e.g., an MLVBM_Q7SVK7 sequence, e.g., SEQ ID NO: 8056), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a MLVBM RT further comprising one, two, three, four, or five mutations selected from the group consisting of D199N, T329P, L602W, T305K, and W312F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a MLVBM RT further comprising one, two, and three mutations selected from the group consisting of D200N, T33OP, and L603W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of a MLVCB RT (e.g., an MLVCB_P08361 sequence, e.g., SEQ ID NO: 8062), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a MLVCB RT further comprising one, two, three, four, or five mutations selected from the group consisting of D200N, T33OP, L603W, T306K, and W313F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a MLVCB RT further comprising one, two, and three mutations selected from the group consisting of D200N, T33OP, and L603W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of a MLVFF RT, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a MLVFF RT further comprising one, two, three, four, or five mutations selected from the group consisting of D200N, T330P, L603W, T306K, and W313F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a MLVFF RT further comprising one, two, and three mutations selected from the group consisting of D200N, T330P, and L603W, or a corresponding position in a homologous RT domain. In embodiments, an RT domain comprises the amino acid sequence of an RT domain of a MLVMS RT (e.g., an MLVMS_reference sequence, e.g., SEQ ID NO: 8137; or an MLVMS_P03355 sequence, e.g., SEQ ID NO: 8070), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a MLVMS RT further comprising one, two, three, four, five, or six mutations selected from the group consisting of D200N, T330P, L603W, T306K, W313F, and H8Y, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a MLVMS RT further comprising one, two, three, four, or five mutations selected from the group consisting of D200N, T330P, L603W, T306K, and W313F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a MLVMS RT further comprising one, two, or three mutations selected from the group consisting of D200N, T330P, and L603W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of a PERV RT (e.g., an PERV_Q4VFZ2 sequence, e.g., SEQ ID NO: 8099), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a PERV RT further comprising one, two, three, four, or five mutations selected from the group consisting of D196N, E326P, L599W, T302K, and W309F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a PERV RT further comprising one, two, or three mutations selected from the group consisting of D196N, E326P, and L599W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of a SFV1 RT (c.g., an SFV1_P23O74 sequence, c.g., SEQ ID NO: 8105), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a SFV1 RT further comprising one, two, three, or four mutations selected from the group consisting of D24N, T296N, N420P, and L396K, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a SFV 1 RT further comprising one, two, or three mutations selected from the group consisting of D24N, T296N, and N420P, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a SFV1 RT further comprising the D24N, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of a SFV3L RT (e.g., an SFV3L_P27401 sequence, e.g., SEQ ID NO: 8111), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a SFV3L RT further comprising one, two, three, or four mutations selected from the group consisting of D24N, T296N, N422P, and L396K, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a SFV3L RT further comprising one, two, or three mutations selected from the group consisting of D24N, T296N, and N422P, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a SFV3L RT further comprising the mutation D24N, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a SFV3L RT further comprising one, two, or three mutations selected from the group consisting of T307N, N333P, and L307K, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a SFV3L RT further comprising one or two mutations selected from the group consisting of T307N and N333P, or a corresponding position in a homologous RT domain. In embodiments, an RT domain comprises the amino acid sequence of an RT domain of a WMSV RT (e.g., an WMSV_P03359 sequence, e.g., SEQ ID NO: 8131), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a WMSV RT further comprising one, two, three, four, or five mutations selected from the group consisting of D198N, E328P, L600W, T304K, and W31 IF, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a WMSV RT further comprising one, two, or three mutations selected from the group consisting of D198N, E328P, and L600W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of an RT domain of a XMRV6 RT (e.g., an XMRV6_A1Z651 sequence, e.g., SEQ ID NO: 8134), or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, an RT domain comprises the amino acid sequence of a XMRV6 RT further comprising one, two, three, four, or five mutations selected from the group consisting of D200N, T33OP, L603W, T306K, and W313F, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain comprises the amino acid sequence of a XMRV6 RT further comprising one, two, or three mutations selected from the group consisting of D200N, T33OP, and L603W, or a corresponding position in a homologous RT domain. In some embodiments, an RT domain of a gene modifying polypeptide comprises the amino acid sequence of an RT domain of an AVIRE RT, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide further comprises a linker having at least 99% or 100% identity to SEQ ID NO: 5217. In some embodiments, the RT domain of a gene modifying polypeptide comprises the amino acid sequence of an RT domain of an MLVMS RT, or an amino acid sequence having at least 70%, 75%, 80%, 85%, 90%, 95%, or 99% identity thereto. In some embodiments, the gene modifying polypeptide further comprises a linker having at least 99% or 100% identity to SEQ ID NO: 5217. In some embodiments, an RT domain (e.g., as listed in Table 1) comprises one or more mutations as listed in Table 4 below. In some embodiments, an RT domain as listed in Table 1 comprises one, two, three, four, five, or six of the mutations listed in the corresponding row of Table 4 below. Table 4. Exemplary RT domain mutations (relative to corresponding wild-type sequences) RT Domain Name Mutation [s) AVIRE_P03360 AVIRE_P03360_3mut D200N G330P L605W AVIRE_P03360_3mutA D200N G330P L605W T306K W313F BAEVM_P10272 BAEVM_P10272_3mut D198N E328P L602W BAEVM_P10272_3mutA D198N E328P L602W T304K W311F BLVAU_P25059 BLVAU_P25059_2mut E159Q G286P BLVJ_P03361 BLVJ_P03361_2mut E159Q L524W BLVJ_P03361_2mutB E159Q L524W I97P FFV_O93209 D21N FFV_O93209_2mut D21N T293N T419P FFV_O93209_2mutA D21N T293N T419P L393K FFV_O93209-Pro FFV_O93209-Pro_2mut T207N T333P FFV_O93209-Pro_2mutA T207N T333P L307K FLVP10273 FLV_P10273_3mut D199N L602W FLV_P10273_3mutA D199N L602W T305K W312F FOAMV_P 14350 D24N FOAMV_P14350_2mut D24N T296N S420P FOAMV_P14350_2mutA D24N T296N S420P L396K FOAMV_P14350-Pro FOAMV_P14350-Pro_2mut T207N S331P FOAMV_P14350-Pro_2mutA T207N S331P L307K GALV_P21414 GALV_P21414_3mut D198N E328P L600W GALV_P21414_3mutA D198N E328P L600W T304K W311F HTL1A_P03362 HTL1A_P03362_2mut E152Q R279P HTL1A_P03362_2mutB E152Q R279P L90P HTL1C_P14078 HTL1C_P14078_2mut E152Q R279P HTL1L_P0C211 HTL1L_P0C211_2mut E149Q L527W HTL1L_P0C211_2mutB E149Q L527W L87P RT Domain Name Mutation [s) HTL32_Q0R5R2 HTL32_Q0R5R2_2mut E149Q L526W HTL32_Q0R5R2_2mutB E149Q L526W L87P HTL3P_Q4U0X6 HTL3P_Q4U0X6_2mut E149Q L526W HTL3P_Q4U0X6_2mutB E149Q L526W L87P HTLV2_P03363_2mut E147Q G274P JSRV_P31623 JSRV_P31623_2mutB A100P K0RV_Q9TTC1 D32N KORV_Q9TTC1_3mut D32N D322N E452P L724W KORV_Q9TTC1_3mutA D32N D322N E452P L724W T428K W435F KORV_Q9TTC1-Pro KORV_Q9TTC1-Pro_3mut D231N E361P L633W KORV_Q9TTC1-Pro_3mutA D231N E361P L633W T337K W344F MLVAV_P03356 MLVAV_P03356_3mut D200N T330P L603W MLVAV_P03356_3mutA D200N T330P L603W T306K W313F MLVBM_Q7SVK7 MLVBM_Q7SVK7 MLVBM_Q7SVK7_3mut D200N T330P L603W MLVBM_Q7SVK7_3mut D200N T330P L603W MLVBM_Q7SVK7_3mutA_WS D199N T329P L602W T305K W312F MLVBM_Q7SVK7_3mutA_WS D199N T329P L602W T305K W312F MLVCB_P08361 MLVCB_P08361_3mut D200N T330P L603W MLVCB_P08361_3mutA D200N T330P L603W T306K W313F MLVF5_P26810 MLVF5_P26810_3mut D200N T330P L603W MLVF5_P26810_3mutA D200N T330P L603W T306K W313F MLVFF_P26809_3mut D200N T330P L603W MLVFF_P26809_3mutA D200N T330P L603W T306K W313F MLVMS_P03355 MLVMS_P03355 MLVMS_P03355_3mut D200N T330P L603W MLVMS_P03355_3mut D200N T330P L603W MLVMS_P03355_3mutA_WS D200N T330P L603W T306K W313F MLVMS_P03355_3mutA_WS D200N T330P L603W T306K W313F RT Domain Name Mutation [s) MLVMS_P03355_PLV919 D200N T330P L603W T306K W313F H8Y MLVMS_P03355_PLV919 D200N T330P L603W T306K W313F H8Y MLVRD_P11227 MLVRD_P11227_3mut D200N T330P L603W MMTVB_P03365 D26N MMTVB_P03365 D26N MMTVB_P03365_2mut D26N G401P MMTVB_P03365_2mut_WS G400P MMTVB_P03365_2mut_WS G400P MMTVB_P03365_2mutB D26N G401P V215P MMTVB_P03365_2mutB D26N G401P V215P MMTVB_P03365_2mutB_WS G400P V212P MMTVB_P03365_2mutB_WS G400P V212P MMTVB_P03365_WS MMTVB_P03365_WS MMTVB_P03365-Pro MMTVB_P03365-Pro MMTVB_P03365-Pro_2mut G309P MMTVB_P03365-Pro_2mut G309P MMTVB_P03365-Pro_2mutB G309P V123P MMTVB_P03365-Pro_2mutB G309P V123P MPMV_P07572 MPMV_P07572_2mutB G289P I103P PERV.Q4VFZ2 PERV.Q4VFZ2 PERV_Q4VFZ2_3mut D199N E329P L602W PERV_Q4VFZ2_3mut D199N E329P L602W PERV_Q4VFZ2_3mutA_WS D196N E326P L599W T302K W309F PERV_Q4VFZ2_3mutA_WS D196N E326P L599W T302K W309F SFV1_P23074 D24N SFV1_P23074_2mut D24N T296N N420P SFV1_P23074_2mutA D24N T296N N420P L396K SFV1_P23074-Pro SFV1_P23074-Pro_2mut T207N N331P SFV1_P23074-Pro_2mutA T207N N331P L307K SFV3L_P27401 D24N SFV3L_P27401_2mut D24N T296N N422P SFV3L_P27401_2mutA D24N T296N N422P L396K RT Domain Name Mutation [s) SFV3L_P27401-Pro SFV3L_P27401-Pro_2mut T307N N333P SFV3L_P27401-Pro_2mutA T307N N333P L307K SFVCP_Q87040 D24N SFVCP_Q87040_2mut D24N T296N K422P SFVCP_Q87040_2mutA D24N T296N K422P L396K SFVCP_Q87040-Pro SFVCP_Q87040-Pro_2mut T207N K333P SFVCP_Q87040-Pro_2mutA T207N K333P L307K SMRVH_P03364 SMRVH_P03364_2mut G288P SMRVH_P03364_2mutB G288P I102P SRV2_P51517 SRV2_P51517_2mutB I103P WDSV_O92815 WDSV_O92815_2mut S183N K312P WDSV_O92815_2mutA S183N K312P L288K W295F WMSV_P03359 WMSV_P03359_3mut D198N E328P L600W WMSV_P03359_3mutA D198N E328P L600W T304K W311F XMRV6_A1Z651 XMRV6_A1Z651_3mut D200N T330P L603W XMRV6_A1Z651_3mutA D200N T330P L603W T306K W313F Cas domains In some embodiments, a gene modifying polypeptide described herein comprises a Cas domain. In some embodiments, a Cas domain can direct a gene modifying polypeptide to a 5 target site specified by a gRNA spacer, thereby modifying a target nucleic acid sequence in “cis”. In some embodiments, a Cas domain comprises two or more smaller domains, e.g., a DNA binding domain and an endonuclease domain. In some embodiments, a Cas domain possesses DNA target site cleavage functionality via an endonuclease domain. In some 10 embodiments, a Cas domain has DNA binding activity. It is understood that when a Cas domain is said to bind to a target nucleic acid sequence, in some embodiments, the binding is mediated by a gRNA spacer. In some embodiments, a Cas domain has RNA binding activity, e.g., a Cas domain may bind a gRNA scaffold region of a template RNA. CRISPR endonucleases identified from various prokaryotic species have unique PAM sequence requirements; An example of a PAM sequences is 5'-NGG (Streptococcus pyogenes). Some endonucleases, e.g., Cas9 endonucleases, are associated with G-rich PAM sites, e. g., 5'- NGG, and perform blunt-end cleaving of the target DNA at a location 3 nucleotides upstream from (5" from) the PAM site. In some embodiments, a gene modifying polypeptide comprises a GG amino acid sequence between the Cas domain and the linker, an AG amino acid sequence between the RT domain and the second NLS, and / or a GG amino acid sequence between the linker and the RT domain. In some embodiments, a gene modifying polypeptide may comprise an StlCas9 domain. In some embodiments, a gene modifying polypeptide comprises the amino acid sequence of SEQ ID NO: 10208, or an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99% sequence identity thereto. StlCas9 Domain: SDLVLGLDIGIGSVGVGILNKVTGEIIHKNSRIFPAAQAENNLVRRTNRQGRRLAR RKKHRRVRLNRLFEESGLITDFTKISINLNPYQLRVKGLTDELSNEELFIALKNMV KHRGISYLDDASDDGNSSVGDYAQIVKENSKQLETKTPGQIQLERYQTYGQLRG DFTVEKDGKKHRLINVFPTSAYRSEALRILQTQQEFNPQITDEFINRYLEILTGKRK YYHGPGNEKSRTDYGRYRTSGETLDNIFGILIGKCTFYPDEFRAAKASYTAQEFN LLNDLNNLTVPTETKKLSKEQKNQIINYVKNEKAMGPAKLFKYIAKLLSCDVADI KGYRIDKSGKAEIHTFEAYRKMKTLETLDIEQMDRETLDKLAYVLTLNTEREGIQ EALEHEFADGSFSQKQVDELVQFRKANSSIFGKGWHNFSVKLMMELIPELYETSE EQMTILTRLGKQKTTSSSNKTKYIDEKLLTEEIYNPVVAKSVRQAIKIVNAAIKEY GDFDNIVIEMARETNEDDEKKAIQKIQKANKDEKDAAMLKAANQYNGKAELPH SVFHGHKQLATKIRLWHQQGERCLYTGKTISIHDLINNSNQFEVDHILPLSITFDD SLANKVLVYATAAQEKGQRTPYQALDSMDDAWSFRELKAFVRESKTLSNKKKE YLLTEEDISKFDVRKKFIERNLVDTRYASRVVLNALQEHFRAHKIDTKVSVVRGQ FTSQLRRHWGIEKTRDTYHHHAVDALIIAASSQLNLWKKQKNTLVSYSEDQLLDI ETGELISDDEYKESVFKAPYQHFVDTLKSKEFEDSILFSYQVDSKFNRKISDATIY ATRQAKVGKDKADETYVLGKIKDIYTQDGYDAFMKIYKKDKSKFLMYRHDPQT FEKVIEPILENYPNKQINEKGKEVPCNPFLKYKEEHGYIRKYSKKGNGPEIKSLKY YDSKLGNHIDITPKDSNNKVVLQSVSPWRADVYFNKTTGKYEILGLKYADLQFE KGTGTYKISQEKYNDIKKKEGVDSDSEFKFTLYKNDLLLVKDTETKEQQLFRFLS RTMPKQKHYVELKPYDKQKFEGGEALIKVLGNVANSGQCKKGLGKSNISIYKVR TDVLGNQHIIKNEGDKPKLDF (SEQ ID NO: 10208) In some embodiments, a gene modifying polypeptide may comprise the amino acid sequence of SEQ ID NO: 4001 below, or a sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity thereto. In some embodiments, the amino acid sequence of SEQ ID NO: 4001 below, or a sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity thereto, is positioned at the C-terminal end of a gene modifying polypeptide. In embodiments, the amino acid sequence of SEQ ID NO: 4001 below, or the sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity thereto, is positioned within 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, or 30 amino acids of the C-terminal end of a gene modifying polypeptide. Exemplary C-terminal sequence comprising an NLS: AGKRTADGSEFEKRTADGSEFESPKKKAKVE (SEQ ID NO: 4001) In some embodiments, a Cas protein is catalytically active and cuts one or both strands of a target DNA site. In some embodiments, cutting a target DNA site is followed by formation of an alteration, e.g., an insertion or deletion, e.g., by cellular repair machinery. In some embodiments, a Cas protein is modified to deactivate or partially deactivate the nuclease, e.g., nuclease-deficient Cas9. Whereas wild-type Cas9 generates double-strand breaks (DSBs) at specific DNA sequences targeted by a gRNA, a number of CRISPR endonucleases having modified functionalities are available, for example: a “nickase” version of Cas9 that has been partially deactivated generates only a single-strand break; a catalytically inactive Cas9 (“dCas9”) does not cut target DNA. In some embodiments, an endonuclease domain has nickase activity and cleaves one strand of a target DNA. In some embodiments, nickase activity reduces the formation of double-stranded breaks at a target site. In some embodiments, an endonuclease domain has nickase activity and does not form double-stranded breaks. In some embodiments, an endonuclease domain forms single-stranded breaks at a higher frequency than doublestranded breaks, e.g., at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% of the breaks are single-stranded breaks, or less than 10%, less than 5%, less than 4%, less than 3%, less than 2%, or less than 1% of the breaks are double-stranded breaks. In some embodiments, an endonuclease forms substantially no double-stranded breaks. In some embodiments, an endonuclease does not form detectable levels of double-stranded breaks. In some embodiments, a catalytically inactive or partially inactive CRISPR / Cas domain comprises a Cas protein comprising one or more mutations. Linkers In some embodiments, a gene modifying polypeptide may comprise a linker, e.g., a peptide linker, e.g., a linker as described in Table 5 or Table 6. In some embodiments, a gene modifying polypeptide comprises a linker (e.g., as described herein) and an RT domain (e.g., as described herein). In some embodiments, a gene modifying polypeptide comprises, in N-terminal to C-terminal order, a linker (e.g., as described herein, e.g., in Table 5 or Table 6, or a sequence having at least 70%, at least 80%, at least 85%, at least 90%, at least 95, or at least 99% identity thereto) and an RT domain (e.g., as described herein). In some embodiments, a gene modifying polypeptide comprises, in an N-terminal to C-terminal direction, a Cas domain (e.g., a Cas domain as described herein, e.g., an StlCas9 domain), a linker of Table 5 or Table 6 (or a sequence having at least 70%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto), and an RT domain (e.g., an RT domain of Table 1). In some embodiments, a gene modifying polypeptide comprises a flexible linker between the endonuclease and the RT domain, e.g., a linker comprising the amino acid sequence SGGSSGGSSGSETPGTSESATPESSGGSSGGSS (SEQ ID NO: 11002). In some embodiments, an RT domain of a gene modifying polypeptide may be located C-terminal to a Cas domain. In some embodiments, an RT domain of a gene modifying polypeptide may be located N-terminal to a Cas domain. In some embodiments, a linker of a gene modifying polypeptide comprises a motif chosen from: (SGGS)n(SEQ ID NO: 5025), (GGGS)n(SEQ ID NO: 5026), (GGGGS)n(SEQ ID NO: 5027), (G)n, (EAAAK)n (SEQ ID NO: 5028), (GGS)n, or (XP)n. In some embodiments, a gene modifying polypeptide may comprise a linker, e.g., a peptide linker, e.g., a linker as described in Table 5. In some embodiments, a gene modifying polypeptide comprises a linker (e.g., as described in Table 5) and an RT domain (e.g., as described herein, e.g., in Table 1). In some embodiments, a gene modifying polypeptide comprises, in N-terminal to C-terminal order, a linker (e.g., as described herein, e.g., in Table 5) and an RT domain (e.g., as described herein, e.g., in Table 1). In some embodiments, a gene modifying polypeptide comprises, in an N-terminal to C-terminal direction, a Cas domain (e.g., a Cas domain as described herein, e.g., an StlCas9 domain, e.g., comprising the amino acid sequence of SEQ ID NO: 10208, or a sequence having at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity thereto), a linker of Table 5 (or a sequence having at least 70%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto), and an RT domain (e.g., an RT 5 domain of Table 1). Table 5. Exemplary linker amino acid sequences Linker ID Linker Amino Acid Sequence SEQ ID NO LIB1_1_1 GGS 10030 LIB1_1_10 GGGGSGGGGSGGGGSGGGGS 10031 LIB1_1_100 GGGPAPGSS 10032 LIB1_1_101 GSSGGGPAP 10033 LIB1_1_102 GSSPAPGGG 10034 LIB1_1_103 PAPGGGGSS 10035 LIB1_1_104 PAPGSSGGG 10036 LIB1_1_105 GGGEAAAKPAP 10037 LIB1_1_106 GGGPAPEAAAK 10038 LIB1_1_107 EAAAKGGGPAP 10039 LIB1_1_108 EAAAKPAPGGG 10040 LIB1_1_109 PAPGGGEAAAK 10041 LIB1_1_11 GGGGSGGGGSGGGGSGGGGSGGGGS 10042 LIB1_1_110 PAPEAAAKGGG 10043 LIB1_1_111 GSSEAAAKPAP 10044 LIB1_1_112 GSSPAPEAAAK 10045 LIB1_1_113 EAAAKGSSPAP 10046 LIB1_1_114 EAAAKPAPGSS 10047 LIB1_1_115 PAPGSSEAAAK 10048 LIB1_1_116 PAPEAAAKGSS 10049 LIB1_1_117 AEAAAKEAAAKEAAAKEAAAKALEAEAAAKEAAAKEAAAKEAAAKA 10050 LIB1_1_118 GGGGSEAAAKGGGGS 10051 LIB1_1_119 EAAAKGGGGSEAAAK 10052 LIB1_1_12 GGGGSGGGGSGGGGSGGGGSGGGGSGGGGS 10053 LIB1_1_120 SGSETPGTSESATPES 10054 LIB1_1_121 GSAGSAAGSGEF 10055 LIB1_1_122 SGGSSGGSSGSETPGTSESATPESSGGSSGGSS 10056 LIB1_1_13 GGG 10057 LIB1_1_14 GGGG 10058 LIB1_1_15 GGGGG 10059 Linker ID Linker Amino Acid Sequence SEQID NO LIB1_1_16 GGGGGG 10060 LIB1_1_17 GGGGGGG 10061 LIB1_1_18 GGGGGGGG 10062 LIB1_1_19 GSS 10063 LIB1_1_2 GGSGGS 10064 LIB1_1_20 GSSGSS 10065 LIB1_1_21 GSSGSSGSS 10066 LIB1_1_22 GSSGSSGSSGSS 10067 LIB1_1_23 GSSGSSGSSGSSGSS 10068 LIB1_1_24 GSSGSSGSSGSSGSSGSS 10069 LIB1_1_25 EAAAK 10070 LIB1_1_26 EAAAKEAAAK 10071 LIB1_1_27 EAAAKEAAAKEAAAK 10072 LIB1_1_28 EAAAKEAAAKEAAAKEAAAK 10073 LIB1_1_29 EAAAKEAAAKEAAAKEAAAKEAAAK 10074 LIB1_1_3 GGSGGSGGS 10075 LIB1_1_30 EAAAKEAAAKEAAAKEAAAKEAAAKEAAAK 10076 LIB1_1_31 PAP 10077 LIB1_1_32 PAPAP 10078 LIB1_1_33 PAPAPAP 10079 LIB1_1_34 PAPAPAPAP 10080 LIB1_1_35 PAPAPAPAPAP 10081 LIB1_1_37 GGSGGG 10082 LIB1_1_38 GGGGGS 10083 LIB1_1_39 GGSGSS 10084 LIB1_1_4 GGSGGSGGSGGS 10085 LIB1_1_40 GSSGGS 10086 LIB1_1_41 GGSEAAAK 10087 LIB1_1_42 EAAAKGGS 10088 LIB1_1_43 GGSPAP 10089 LIB1_1_44 PAPGGS 10090 LIB1_1_45 GGGGSS 10091 LIB1_1_46 GSSGGG 10092 LIB1_1_47 GGGEAAAK 10093 LIB1_1_48 EAAAKGGG 10094 LIB1_1_49 GGGPAP 10095 LIB1_1_50 PAPGGG 10096 Linker ID Linker Amino Acid Sequence SEQID NO LIB1_1_51 GSSEAAAK 10097 LIB1_1_52 EAAAKGSS 10098 LIB1_1_53 GSSPAP 10099 LIB1_1_54 PAPGSS 10100 LIB1_1_55 EAAAKPAP 10101 LIB1_1_56 PAPEAAAK 10102 LIB1_1_57 GGSGGGGSS 10103 LIB1_1_58 GGSGSSGGG 10104 LIB1_1_59 GGGGGSGSS 10105 LIB1_1_6 GGSGGSGGSGGSGGSGGS 10106 LIB1_1_60 GGGGSSGGS 10107 LIB1_1_61 GSSGGSGGG 10108 LIB1_1_62 GSSGGGGGS 10109 LIB1_1_63 GGSGGGEAAAK 10110 LIB1_1_64 GGSEAAAKGGG 10111 LIB1_1_65 GGGGGSEAAAK 10112 LIB1_1_66 GGGEAAAKGGS 10113 LIB1_1_67 EAAAKGGSGGG 10114 LIB1_1_68 EAAAKGGGGGS 10115 LIB1_1_69 GGSGGGPAP 10116 LIB1_1_7 GGGGS 10117 LIB1_1_70 GGSPAPGGG 10118 LIB1_1_71 GGGGGSPAP 10119 LIB1_1_72 GGGPAPGGS 10120 LIB1_1_73 PAPGGSGGG 10121 LIB1_1_74 PAPGGGGGS 10122 LIB1_1_75 GGSGSSEAAAK 10123 LIB1_1_76 GGSEAAAKGSS 10124 LIB1_1_77 GSSGGSEAAAK 10125 LIB1_1_78 GSSEAAAKGGS 10126 LIB1_1_79 EAAAKGGSGSS 10127 LIB1_1_8 GGGGSGGGGS 10128 LIB1_1_80 EAAAKGSSGGS 10129 LIB1_1_81 GGSGSSPAP 10130 LIB1_1_82 GGSPAPGSS 10131 LIB1_1_83 GSSGGSPAP 10132 LIB1_1_84 GSSPAPGGS 10133 Linker ID Linker Amino Acid Sequence SEQID NO LIB1_1_85 PAPGGSGSS 10134 LIB1_1_86 PAPGSSGGS 10135 LIB1_1_87 GGSEAAAKPAP 10136 LIB1_1_88 GGSPAPEAAAK 10137 LIB1_1_89 EAAAKGGSPAP 10138 LIB1_1_9 GGGGSGGGGSGGGGS 10139 LIB1_1_90 EAAAKPAPGGS 10140 LIB1_1_91 PAPGGSEAAAK 10141 LIB1_1_92 PAPEAAAKGGS 10142 LIB1_1_93 GGGGSSEAAAK 10143 LIB1_1_94 GGGEAAAKGSS 10144 LIB1_1_95 GSSGGGEAAAK 10145 LIB1_1_96 GSSEAAAKGGG 10146 LIB1_1_97 EAAAKGGGGSS 10147 LIB1_1_98 EAAAKGSSGGG 10148 LIB1_1_99 GGGGSSPAP 10149 LIB2_EA_1 LEGSGQGPGSGQGSGSPGSGQG 10150 LIB2_EA_10 VRHKLKRV 10151 LIB2_EA_11 LWSP 10152 LIB2_EA_12 ARNVEERLCL 10153 LIB2_EA_13 WQAAESYEV 10154 LIB2_EA_14 MKPENEA 10155 LIB2_EA_15 FVNLYSDYIL 10156 LIB2_EA_16 ICGSRNL 10157 LIB2_EA_17 LKTSDSPTQRI 10158 LIB2_EA_18 AIDG 10159 LIB2_EA_19 VNPERRRC 10160 LIB2_EA_2 GGGGSLVPRGSGGGGS 10161 LIB2_EA_20 AEIKYDGV 10162 LIB2_EA_21 FNPQFLA 10163 LIB2_EA_22 GDWGKQFG 10164 LIB2_EA_23 FREFSIEKYIDTY 10165 LIB2_EA_24 FGMVQGMSTRKGTVVFLDNILEETK 10166 LIB2_EA_25 YVEFEGEQGVDEGGVSKEFF 10167 LIB2_EA_26 SHPVLYQSLKDL 10168 LIB2_EA_27 KDLSEAQ 10169 Linker ID Linker Amino Acid Sequence SEQ ID NO LIB2_EA_28 CYGKKYGPKGKGKGMGAGTLSTDKGESLGIKYEEGQSHRPTNPNAS RMAQKVGGSDGCGG 10170 LIB2_EA_3 GSGSGS 10171 LIB2_EA_4 YDKYGRKTLPW 10172 LIB2_EA_5 LPGVGRSTAG 10173 LIB2_EA_6 LWSLSEQV 10174 LIB2_EA_7 APILYENDHF 10175 LIB2_EA_8 PAAAFARECRGF 10176 LIB2_EA_9 PLETT 10177 In some embodiments, a gene modifying polypeptide may comprise a linker, e.g., a peptide linker, e.g., a linker as described in Table 6. In some embodiments, a gene modifying polypeptide comprises a linker (e.g., as described in Table 6) and an RT domain (e.g., as described herein, e.g., in Table 1). In some embodiments, a gene modifying polypeptide 5 comprises, in N-terminal to C-terminal order, a linker (e.g., as described herein, e.g., in Table 6) and an RT domain (e.g., as described herein, e.g., in Table 1). In some embodiments, a gene modifying polypeptide comprises, in an N-terminal to C-terminal direction, a Cas domain (e.g., a Cas domain as described herein, e.g., an StlCas9 domain, e.g., comprising the amino acid sequence of SEQ ID NO: 10208, or a sequence having at least 75%, at least 80%, at least 85%, at 10 least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity thereto), a linker of Table 6 (or a sequence having at least 70%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto), and an RT domain (e.g., an RT domain of Table 1). Table 6. Exemplary linker amino acid sequences SEQUENCE SEQ ID NO LEGSGQGPGSGQGSGSPGSGQG 10178 VRHKLKRV 10179 LWSP 10180 ARNVEERLCL 10181 WQAAESYEV 10182 MKPENEA 10183 FVNLYSDYIL 10184 ICGSRNL 10185 LKTSDSPTQRI 10186 AIDG 10187 SEQUENCE SEQ ID NO VNPERRRC 10188 GGGGSLVPRGSGGGGS 10189 AEIKYDGV 10190 FNPQFLA 10191 GDWGKQFG 10192 FREFSIEKYIDTY 10193 FGMVQGMSTRKGTVVFLDNILEETK 10194 YVEFEGEQGVDEGGVSKEFF 10195 SHPVLYQSLKDL 10196 KDLSEAQ 10197 CYGKKYGPKGKGKGMGAGTLSTDKGESLGIKYEEGQSHRPTNPNASRMAQKVG GSDGCGG 10198 GSGSGS 10199 YDKYGRKTLPW 10200 LPGVGRSTAG 10201 LWSLSEQV 10202 APILYENDHF 10203 PAAAFARECRGF 10204 PLETT 10205 Exemplary Gene Modifying Polypeptides In some embodiments, a gene modifying polypeptide (e.g., a gene modifying polypeptide that is pail of a system described herein) comprises an amino acid sequence of any one of SEQ 5 ID NOs: 12,001-21,744, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises an amino acid sequence as listed in Table 7, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a 10 gene modifying polypeptide comprises a linker comprising a linker sequence as listed in Table 7, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises an RT domain comprising an RT domain sequence as listed in Table 7, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, 15 at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of Table 7, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in the same row of Table 7, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% 5 identity thereto. In some embodiments, a gene modifying polypeptide comprises an amino acid sequence as listed in column 6 of Table 7, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. Table 7. Exemplary RT-linker combinations Linker ID Linker amino acid SEQ ID NOs RT name SEQ ID NOs Full length SEQ ID NOs LIB1_1_11 5 PAPGSSEAAAK 10301 PERV_Q4VFZ 2_3mutA_WS 10316 10331 LIB1_1_29 EAAAKEAAAKEA AAKEAAAKEAA AK 10302 BAEVM_P102 72_3mutA 10317 10332 LIB1_1_55 EAAAKPAP 10303 WMSV_P0335 9_3mutA 10318 10333 LIBl_l_80 EAAAKGSSGGS 10304 PERV_Q4VFZ 2_3mutA_WS 10319 10334 LIB1_1_92 PAPEAAAKGGS 10305 PERV_Q4VFZ 2_3mutA_WS 10320 10335 LIB1_1_11 0 PAPEAAAKGGG 10306 MLVMS_P033 55_3mutA_W S 10321 10336 LIB1_1_29 EAAAKEAAAKEA AAKEAAAKEAA AK 10307 PERV_Q4VFZ 2_3mutA_WS 10322 10337 LIB1_1_29 EAAAKEAAAKEA AAKEAAAKEAA AK 10308 BAEVM_P102 72_3mutA 10323 10338 LIB1_1_35 PAPAPAPAPAP 10309 AVIRE_P0336 0_3mutA 10324 10339 LIB1_1_36 PAPAPAPAPAPAP 10310 BAEVM_P102 72_3mutA 10325 10340 LIB1_1_42 EAAAKGGS 10311 XMRV6_A1Z 65 l_3mutA 10326 10341 LIB1_1_75 GGSGSSEAAAK 10312 BAEVM_P102 72_3mutA 10327 10342 LIB2_EA_ 13 WQAAESYEV 10313 AVIRE_P0336 0_3mutA 10328 10343 Linker ID Linker amino acid SEQ ID NOs RT name SEQ ID NOs Full length SEQ ID NOs LIB2_EA_ 20 AEIKYDGV 10314 PERV_Q4VFZ 2_3mutA_WS 10329 10344 LIB2_EA_ 24 FGMVQGMSTRK GTVVFLDNILEET K 10315 MLVFF_P268 09_3mutA 10330 10345 In some embodiments, a gene modifying polypeptide comprises an amino acid sequence as listed in Table 8, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises a linker comprising a linker sequence as listed in Table 8, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises an RT domain comprising an RT domain sequence as listed in Table 8, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 1 of Table 8, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 2 in the same row of Table 8, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 3 of Table 8, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 4 in the same row of Table 8, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 5 of Table 8, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 6 in the same row of Table 8, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. Table 8. Exemplary linker-RT combinations Linker id RT name Linker id RT name Linker id RT name LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ MLVCB P08361 3m LIB1J_ GALV P21414 3mut 115 tA_WS 122 utA 55 A LIB1J_ BAEVM P10272 3m LIB1J_ SFV3L P27401 2mu LIB1J_ KORV_Q9TTC1- 29 utA 14 t 55 Pro_3mut LIB1J_ WMSV P03359 3mu LIB1J_ MLVAV P03356 3m LIB1J_ PERV_Q4VFZ2_3mu 55 tA 19 utA 58 t LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ WMSV P03359 3mu LIB1J_ MLVBM_Q7SVK7_3 80 tA_WS 2 tA 59 mutA_WS LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ MLVMS P03355 3m LIB1J_ XMRV6 A1Z651 3m 92 tA_WS 2 utA.WS 62 utA LIB1J_ MLVMS P03355 3m LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ FOAMV P14350 2m 110 utA_WS 22 tA_WS 66 utA LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ BAEVM P10272 3m 29 tA_WS 24 tA_WS 66 utA LIB1J_ BAEVM P10272 3m LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ SFV3L_P27401- 29 utA 24 t 67 Pro_2mutA LIB1J_ AVIRE P03360 3mu LIB1J_ GALV P21414 3mut LIB1J_ WMSV P03359 3mu 35 tA 24 A 67 tA LIB1J_ BAEVM P10272 3m LIB1J_ WMSV P03359 3mu LIB1J_ AVIRE P03360 3mu 36 utA 25 tA 67 tA LIB1J_ XMRV6 A1Z651 3m LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ AVIRE P03360 3mu 42 utA 26 t 67 tA LIB1J_ BAEVM P10272 3m LIB1J_ WMSV P03359 3mu LIB1J_ MLVCB P08361 3m 75 utA 27 tA 67 utA LIB2_EA AVIRE P03360 3mu LIB1J_ WMSV P03359 3mu LIB1J_ MLVFF P26809 3m _13 tA 27 tA 67 utA LIB2_EA PERV_Q4VFZ2_3mu LIB1J_ GALV P21414 3mut LIB1J_ PERV_Q4VFZ2_3mu _20 tA_WS 27 A 69 tA_WS LIB2_EA MLVFF P26809 3m LIB1J_ MLVFF P26809 3m LIB1J_ MLVFF P26809 3m _24 utA 28 utA 70 utA LIB1J_ XMRV6 A1Z651 3m LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ SFV3L_P27401- 1 utA 29 t 74 Pro_2mutA LIB1J_ SFV3L_P27401- LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ MLVFF P26809 3m 10 Pro_2mutA 29 t 74 utA LIB1J_ SFV3L P27401 2mu LIB1J_ SFV3L_P27401- LIB1J_ BAEVM P10272 3m 10 t 29 Pro_2mutA 75 utA LIB1J_ KORV_Q9TTC1- LIB1J_ SFV3L_P27401- LIB1_L SFV3L_P27401- 10 Pro_3mut 29 Pro_2mutA 77 Pro_2mutA Linker id RT name Linker id RT name Linker id RT name LIB1J_ MLVFF P26809 3m LIB1J_ SFV3L P27401 2mu LIB1J_ KORV_Q9TTC1_3m 101 utA 29 t 79 utA LIB1J_ FOAMV_P 14350- LIB1J_ SFV3L P27401 2mu LIB1J_ AVIRE P03360 3mu 103 Pro_2mut 29 t 8 tA LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ WMSV P03359 3mu LIB1J_ AVIRE P03360 3mu 105 t 29 tA 8 tA LIB1J_ WDSV 092815 2mu LIB1J_ AVIRE P03360 3mu LIB1J_ MLVAV P03356 3m 105 tA 29 tA 8 utA LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ AVIRE P03360 3mu LIB1J_ PERV_Q4VFZ2_3mu 106 t 29 tA 80 tA_WS LIB1J_ SFV3L_P27401- LIB1J_ K0RV_Q9TTC1- LIB1J_ FOAMV P14350 2m 106 Pro_2mutA 29 Pro_3mut 82 utA LIB1J_ MLVCB P08361 3m LIB1J_ K0RV_Q9TTC1- LIB1J_ KORV_Q9TTC1_3m 106 utA 29 Pro_3mut 82 utA LIB1J_ AVIRE P03360 3mu LIB1J_ MLVBM_Q7SVK7_3 LIB1J_ MLVFF P26809 3m 108 tA 29 mutA_WS 83 utA LIB1J_ MLVAV P03356 3m LIB1J_ AVIRE P03360 3mu LIB1J_ KORV_Q9TTC1- 108 utA 3 tA 84 Pro_3mut LIB1J_ FOAMV_P 14350- LIB1J_ AVIRE P03360 3mu LIB1_L KORV_Q9TTC1- 109 Pro_2mutA 3 tA 84 Pro_3mut LIB1J_ K0RV_Q9TTC1- LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ XMRV6 A1Z651 3m 110 Pro_3mut 30 t 85 utA LIB1J_ MLVFF P26809 3m LIB1J_ FOAMV_P 14350- LIB1J_ KORV_Q9TTC1- 110 utA 30 Pro_2mut 85 Pro_3mutA LIB1J_ AVIRE P03360 3mu LIB1J_ FOAMV P14350 2m LIB1J_ AVIRE P03360 3mu 112 tA 30 ut 86 tA LIB1J_ AVIRE P03360 3mu LIB1 1 MLVBM_Q7SVK7_3 LIB1J_ AVIRE P03360 3mu 112 tA 30 mutA_WS 86 tA LIB1J_ K0RV_Q9TTC1- LIB1J_ WMSV P03359 3mu LIB1J_ BAEVM P10272 3m 112 Pro_3mutA 31 tA 86 utA LIB1J_ WMSV P03359 3mu LIB1J_ GALV P21414 3mut LIB1J_ WMSV P03359 3mu 113 tA 32 A 88 tA LIB1J_ K0RV_Q9TTC1- LIB1J_ MLVAV P03356 3m LIB1J_ WMSV P03359 3mu 113 Pro_3mutA 32 utA 88 tA LIB1J_ XMRV6 A1Z651 3m LIB1J_ MLVCB P08361 3m LIB1J_ MLVFF P26809 3m 114 utA 32 utA 88 utA LIB1J_ PERV_Q4VFZ2_3mu LIB1 1 PERV_Q4VFZ2_3mu LIB1J_ PERV_Q4VFZ2_3mu 115 tA_WS 33 tA_WS 90 t LIB1J_ WMSV P03359 3mu LIB1J_ FOAMV_P 14350- LIB1J_ BAEVM P10272 3m 115 tA 33 Pro_2mutA 91 utA LIB1J_ MLVBM_Q7SVK7_3 LIB1J_ XMRV6 A1Z651 3m LIB1J_ PERV_Q4VFZ2_3mu 116 mutA_WS 35 utA 92 tA_WS LIB1J_ MLVFF P26809 3m LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ PERV_Q4VFZ2_3mu 116 utA 36 tA_WS 93 t Linker id RT name Linker id RT name Linker id RT name LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ MLVCB P08361 3m 117 tA_WS 36 tA_WS 93 utA LIB1J_ SFV3L_P27401- LIB1J_ PERV_Q4VFZ2_3mu LIB1J_ K0RV.Q9TTC1- 117 Pro_2mutA 36 t 94 Pro_3mutA LIB1J_ SFV3L_P27401- LIB1J_ SFV3L_P27401- LIB1J_ WMSV P03359 3mu 117 Pro_2mutA 36 Pro_2mutA 97 tA LIB1J_ SFV3L P27401 2mu LIB1J_ SFV3L P27401 2mu LIB1J_ WMSV P03359 3mu 117 t 36 t 97 tA LIB1J_ WDSV 092815 2mu LIB1J_ AVIRE P03360 3mu LIB2.EA MLVMS P03355 3m 117 tA 36 tA _1 utA.WS LIB1J_ WMSV P03359 3mu LIB1J_ MLVAV P03356 3m LIB2.EA WMSV P03359 3mu 117 tA 37 utA _12 tA LIB1J_ WMSV P03359 3mu LIB1J_ PERV_Q4VFZ2_3mu LIB2.EA FOAMV.P14350- 117 tA 38 tA_WS _13 Pro_2mutA LIB1J_ XMRV6 A1Z651 3m LIB1J_ WMSV P03359 3mu LIB2.EA K0RV.Q9TTC1- 117 utA 38 tA _13 Pro_3mutA LIB1J_ AVIRE P03360 3mu LIB1J_ MLVCB P08361 3m LIB2.EA MLVFF P26809 3m 117 tA 38 utA _13 utA LIB1J_ AVIRE P03360 3mu LIB1J_ PERV_Q4VFZ2_3mu LIB2.EA KORV_Q9TTC1_3m 117 tA 39 tA_WS _17 utA LIB1J_ BAEVM P10272 3m LIB1J_ WMSV P03359 3mu LIB2.EA MLVAV P03356 3m 117 utA 39 tA _18 utA LIB1J_ BAEVM P10272 3m LIB1J_ AVIRE P03360 3mu LIB2.EA SFV3L P27401 2mu 117 utA 41 tA _20 t LIB1J_ MLVBM_Q7SVK7_3 LIB1J_ PERV_Q4VFZ2_3mu LIB2.EA FOAMV.P14350- 117 mutA_WS 42 t _20 Pro_2mutA LIB1J_ SFV3L_P27401- LIB1 1 MLVAV P03356 3m LIB2.EA FOAMV P14350 2m 118 Pro_2mutA 42 utA _20 utA LIB1J_ FOAMV_P 14350- LIB1J_ MLVBM_Q7SVK7_3 LIB2.EA MLVAV P03356 3m 118 Pro_2mutA 43 mutA_WS _23 utA LIB1J_ MLVBM_Q7SVK7_3 LIB1J_ SFV3L_P27401- LIB2.EA MLVMS P03355 3m 118 mutA_WS 45 Pro_2mutA _23 utA.WS LIB1J_ MLVFF P26809 3m LIB1J_ WMSV P03359 3mu LIB2.EA FLV P10273 3mutA 119 utA 45 tA _25 LIB1J_ XMRV6 A1Z651 3m LIB1J_ XMRV6 A1Z651 3m LIB2.EA MLVBM.Q7SVK7.3 12 utA 45 utA _25 mutA_WS LIB1J_ AVIRE P03360 3mu LIB1 1 FOAMV_P 14350- LIB2.EA MLVCB P08361 3m 12 tA 45 Pro_2mutA _25 utA LIB1J_ AVIRE P03360 3mu LIB1J_ WMSV P03359 3mu LIB2.EA MLVMS P03355 3m 12 tA 46 tA .25 utA.WS LIB1J_ XMRV6 A1Z651 3m LIB1J_ SFV3L_P27401- LIB2.EA KORV.Q9TTC1- 120 utA 47 Pro_2mutA _6 Pro_3mut LIB1J_ AVIRE P03360 3mu LIB1J_ MLVMS P03355 3m LIB2.EA KORV_Q9TTC1_3m 120 tA 47 utA.WS J ut Linker id RT name Linker id RT name Linker id RT name LIB1J_ AVIRE P03360 3mu LIB1J_ MLVFF P26809 3m LIB2_EA WDSV 092815 2mu 120 tA 49 utA _8 tA LIB1J_ SFV3L_P27401- LIB1J_ PERV_Q4VFZ2_3mu LIB2_EA K0RV_Q9TTC1- 122 Pro_2mutA 50 tA_WS _8 Pro_3mutA LIB1J_ K0RV_Q9TTC1- LIB1J_ KORV_Q9TTC1_3m LIB2_EA MLVMS P03355 3m 122 Pro_3mutA 54 utA _9 utA.WS LIB1_1_ 122 MLVAV_P03356_3m utA LIB1_1_ 55 WMSV_P03359_3mu tA In some embodiments, a gene modifying polypeptide comprises an amino acid sequence as listed in Table 9, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises a linker comprising a linker sequence as listed in Table 9, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises an RT domain comprising an RT domain sequence as listed in Table 9, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 1 of Table 9, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 2 in the same row of Table 9, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 3 of Table 9, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 4 in the same row of Table 9, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 5 of Table 9, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 6 in the same row of Table 9, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. Table 9. Gene modifying polypeptides with Z score > 1 Linker id RT name Linke rid RT name Linker id RT name LIB1_1 _1 FLV_P10273_3mut A LIB1_ l_30 KORV_Q9TTC1- Pro_3mut LIB1_1 _75 XMRV6_A1Z651_ 3mutA LIB1_1 _1 FOAMV_P14350- Pro_2mutA LIB1_ 1_31 MLVCB_P08361_ 3mutA LIB1_1 _75 KORV_Q9TTC1_3 mutA LIB1_1 _1 GALV_P21414_3 mutA LIB1_ 1_31 MLVFF_P26809_3 mutA LIB1_1 _75 PERV_Q4VFZ2_3 mutA_WS LIB1_1 KORV_Q9TTC1- Pro_3mutA LIB1_ 1_31 SFV3L_P27401_2 mut LIB1_1 _76 BAEVM_P10272_ 3mutA LIB1_1 _1 KORV_Q9TTC1_3 mut LIB1_ 1_31 WMSV_P03359_3 mutA LIB1_1 _76 FFV_O93209-Pro LIB1_1 _1 MLVAV_P03356_ 3mutA LIB1_ 1_31 XMRV6_A1Z651_ 3mutA LIB1_1 _76 MLVCB_P08361_ 3mutA LIB1_1 _1 MLVBM_Q7SVK7 _3mutA_WS LIB1_ 1_31 WDSV_O92815 LIB1_1 _76 WMSV_P03359_3 mutA LIB1_1 MLVCB_P08361_ 3mutA LIB1_ 1_31 WDSV_O92815_2 mutA LIB1_1 _76 XMRV6_A1Z651_ 3mutA LIB1_1 _1 MLVMS_P03355_ 3mutA_WS LIB1_ 1_32 BAEVM_P10272_ 3mutA LIB1_1 _77 KORV_Q9TTC1- Pro_3mutA LIB1_1 _1 PERV_Q4VFZ2_3 mut LIB1_ 1_32 FFV_O93209 LIB1_1 _77 MLVCB_P08361_ 3mutA LIB1_1 _1 XMRV6_A1Z651_ 3mutA LIB1_ 1_32 GALV_P21414_3 mutA LIB1_1 _77 MLVMS_P03355_ 3mutA_WS LIB1_1 _1 KORV_Q9TTC1- Pro_3mut LIB1_ 1_32 KORV_Q9TTC1- Pro_3mutA LIB1_1 _78 BAEVM_P10272_ 3mutA LIB1_1 PERV_Q4VFZ2_3 mutA_WS LIB1_ 1_32 MLVAV_P03356_ 3mutA LIB1_1 _78 KORV_Q9TTC1- Pro_3mutA LIB1_1 _io FLV_P10273_3mut A LIB1_ 1_32 MLVBM_Q7SVK7 _3mutA_WS LIB1_1 _78 MLVAV_P03356_ 3mutA LIB1_1 _io MLVCB_P08361_ 3mutA LIB1_ 1_32 MLVCB_P08361_ 3mutA LIB1_1 _78 MLVCB_P08361_ 3mutA LIB 1_1 _io MLVMS_P03355_ 3mutA_WS LIB1_ 1_32 MLVFF_P26809_3 mutA LIB1_1 _78 MLVMS_P03355_ 3mutA_WS LIB1_1 _io PERV_Q4VFZ2_3 mut LIB1_ 1_32 PERV_Q4VFZ2_3 mut LIB1_1 _78 WMSV_P03359_3 mutA LIB1_1 _io SFV1_P23O74 LIB1_ 1_32 WMSV_P03359_3 mutA LIB1_1 _79 AVIRE_P03360_3 mutA LIB1_1 _io SFV3L_P27401- Pro_2mutA LIB1_ 1_32 FOAMV_P14350- Pro_2mut LIB1_1 _79 BAEVM_P10272_ 3mutA Linker id RT name Linke r id RT name Linker id RT name LIB1_1 SFV3L_P27401_2 LIB1_ KORV_Q9TTC1- LIB1_1 FOAMV_P14350- _io mut 1_32 Pro_3mut _79 Pro_2mutA LIB1_1 KORV_Q9TTC1- LIB1_ KORV_Q9TTC1_3 LIB1_1 MLVFF_P26809_3 _io Pro_3mut 1_32 mutA _79 mutA LIB1_1 WDSV_O92815 LIB1_ PERV_Q4VFZ2_3 LIB1_1 SFV3L_P27401- _io 1_32 mutA_WS _79 Pro_2mutA LIB1_1 WDSV_O92815_2 LIB1_ WDSV_O92815_2 LIB1_1 WMSV_P03359_3 _io mut 1_32 mutA _79 mutA LIB1_1 GALV P21414 3 LIB1_ BAEVM P10272 LIB1_1 XMRV6 A1Z651 -100 mutA 1_33 3mutA _79 3mutA LIB1_1 MLVCB_P08361_ LIB1_ MLVMS_P03355_ LIB1_1 KORV_Q9TTC1- _100 3mutA 1_33 3mutA_WS _79 Pro_3mut LIB1_1 MLVFF_P26809_3 LIB1_ WMSV_P03359_3 LIB1_1 KORV_Q9TTC1_3 -100 mutA 1_33 mutA _79 mutA LIB1_1 KORV_Q9TTC1_3 LIB1_ XMRV6_A1Z651_ LIB1_1 WDSV_O92815 -100 mutA 1_33 3mutA _79 LIB1_1 BAEVM_P10272_ LIB1_ PERV_Q4VFZ2_3 LIB1_1 MLVAV_P03356_ -101 3mutA 1_33 mutA_WS _8 3mutA LIB1_1 MLVAV_P03356_ LIB1_ AVIRE_P03360_3 LIB1_1 MLVBM_Q7SVK7 -101 3mutA 1_34 mutA _8 _3mutA_WS LIB1_1 MLVBM_Q7SVK7 LIB1_ MLVCB_P08361_ LIB1_1 MLVCB_P08361_ -101 _3mutA_WS 1_34 3mutA _8 3mutA LIB1_1 MLVFF P26809 3 LIB1_ WMSV P03359 3 LIB1_1 MLVFF P26809 3 -101 mutA 1_34 mutA _8 mutA LIB1_1 SFV3L_P27401- LIB1_ XMRV6_A1Z651_ LIB1_1 KORV_Q9TTC1_3 -101 Pro_2mutA 1_34 3mutA _8 mutA LIB1_1 FOAMV_P14350_ LIB1_ KORV_Q9TTC1- LIB1_1 WDSV_O92815_2 -101 2mutA 1_35 Pro_3mutA _8 mutA LIB1_1 GALV P21414 3 LIB1_ MLVCB P08361 LIB1_1 BAEVM Pl0272 _102 mutA 1_35 3mutA _80 3mutA LIB1_1 SFV3L P27401 2 LIB1_ MLVFF P26809 3 LIB1_1 FFV_O93209 _102 mut 1_35 mutA _80 LIB1_1 WMSV_P03359_3 LIB1_ PERV_Q4VFZ2_3 LIB1_1 FOAMV_P14350- _102 mutA 1_35 mut _80 Pro_2mutA LIB1_1 XMRV6_A1Z651_ LIB1_ SFV3L_P27401- LIB1_1 GALV_P21414_3 _102 3mutA 1_35 Pro_2mutA _80 mutA LIB1_1 BAEVM_P10272_ LIB1_ XMRV6_A1Z651_ LIB1_1 KORV_Q9TTCL _103 3mutA 1_35 3mutA _80 Pro_3mutA LIB1_1 GALV_P21414_3 LIB1_ KORV_Q9TTC1_3 LIB1_1 MLVAV_P03356_ _103 mutA 1_35 mutA _80 3mutA LIB1_1 MLVAV_P03356_ LIB1_ BAEVM_P10272_ LIB1_1 MLVBM_Q7SVK7 _103 3mutA 1_37 3mutA _80 _3mutA_WS LIB1_1 SFV3L_P27401- LIB1_ FLV P10273 3mut LIB1_1 MLVCB P08361 _103 Pro_2mutA 1_37 A _80 3mutA Linker id RT name Linke r id RT name Linker id RT name LIB1_1 XMRV6 A1Z651 LIB1_ FOAMV_P14350- LIB1_1 XMRV6 A1Z651 _103 3mutA 1_37 Pro_2mutA _80 3mutA LIB1_1 FOAMV_P 14350- LIB1_ MLVAV P03356 LIB1_1 MLVCB P08361 _103 Pro_2mut 1_37 3mutA _81 3mutA LIB1_1 KORV_Q9TTC1- LIB1_ MLVBM_Q7SVK7 LIB1_1 XMRV6_A1Z651_ _103 Pro_3mut 1_37 _3mutA_WS _81 3mutA LIB1_1 KORV_Q9TTC1_3 LIB1_ MLVCB_P08361_ LIB1_1 KORV_Q9TTC1- _103 mutA 1_37 3mutA _81 Pro_3mut LIB1_1 FFV_O93209-Pro LIB1_ KORV_Q9TTC1- LIB1_1 KORV_Q9TTC1_3 _104 1_37 Pro_3mut _81 mutA LIB1_1 KORV_Q9TTC1- LIB1_ PERV_Q4VFZ2_3 LIB1_1 BAEVM_P10272_ _104 Pro_3mutA 1_37 mutA_WS _82 3mutA LIB1_1 MLVFF P26809 3 LIB1_ BAEVM Pl0272 LIB1_1 FLV P10273 3mut _104 mutA 1_38 3mutA _82 A LIB1_1 MLVMS_P03355_ LIB1_ FOAMV_P14350- LIB1_1 KORV_Q9TTC1- _104 3mutA_WS 1_38 Pro_2mutA _82 Pro_3mutA LIB1_1 SFV3L_P27401- LIB1_ MLVCB P08361 LIB1_1 MLVAV P03356 _104 Pro_2mutA 1_38 3mutA _82 3mutA LIB1_1 WMSV_P03359_3 LIB1_ PERV_Q4VFZ2_3 LIB1_1 MLVBM_Q7SVK7 _104 mutA 1_38 mut _82 _3mutA_WS LIB1_1 XMRV6 A1Z651 LIB1_ WMSV P03359 3 LIB1_1 MLVCB P08361 _104 3mutA 1_38 mutA _82 3mutA LIB1_1 KORV_Q9TTC1- LIB1_ KORV_Q9TTC1- LIB1_1 MLVFF_P26809_3 _104 Pro_3mut 1_38 Pro_3mut _82 mutA LIB1_1 KORV_Q9TTC1_3 LIB1_ PERV_Q4VFZ2_3 LIB1_1 MLVMS_P03355_ _104 mutA 1_38 mutA_WS _82 3mutA_WS LIB1_1 AVIRE P03360 3 LIB1_ BAEVM P10272 LIB1_1 SFV3L P27401 2 _105 mutA 1_39 3mutA _82 mut LIB1_1 FOAMV_P 14350- LIB1_ FOAMV_P14350- LIB1_1 FOAMV P14350 _105 Pro_2mutA 1_39 Pro_2mutA _82 2mutA LIB1_1 GALV_P21414_3 LIB1_ KORV_Q9TTC1- LIB1_1 KORV_Q9TTC1_3 _105 mutA 1_39 Pro_3mutA _82 mutA LIB1_1 MLVAV P03356 LIB1_ MLVCB P08361 LIB1_1 BAEVM Pl0272 _105 3mutA 1_39 3mutA _83 3mutA LIB1_1 MLVBM_Q7SVK7 LIB1_ PERV_Q4VFZ2_3 LIB1_1 FOAMV_P14350_ _105 _3mutA_WS 1_39 mut _83 2mut LIB1_1 MLVFF_P26809_3 LIB1_ WMSV_P03359_3 LIB1_1 KORV_Q9TTCL _105 mutA 1_39 mutA _83 Pro_3mutA LIB1_1 SFV3L_P27401- LIB1_ XMRV6 A1Z651 LIB1_1 MLVCB P08361 -105 Pro_2mutA 1_39 3mutA _83 3mutA LIB1_1 WMSV_P03359_3 LIB1_ KORV_Q9TTC1- LIB1_1 MLVFF_P26809_3 _105 mutA 1_39 Pro_3mut _83 mutA LIB1_1 XMRV6_A1Z651_ LIB1_ KORV_Q9TTC1_3 LIB1_1 KORV_Q9TTC1_3 _105 3mutA 1_39 mutA _83 mutA Linker id RT name Linke r id RT name Linker id RT name LIB1_1 WDSV_O92815_2 LIB1_ PERV_Q4VFZ2_3 LIB1_1 PERV_Q4VFZ2_3 _105 mut 1_39 mutA_WS _83 mutA_WS LIB1_1 KORV_Q9TTC1- LIB1_ WDSV_O92815_2 LIB1_1 WDSV_O92815_2 _106 Pro_3mutA 1_39 mut _83 mut LIB1_1 MLVBM_Q7SVK7 LIB1_ AVIRE_P03360_3 LIB1_1 BAEVM_P10272_ _106 _3mutA_WS 1_4 mutA _84 3mutA LIB1_1 MLVCB_P08361_ LIB1_ BAEVM_P10272_ LIB1_1 FFV_O93209-Pro _106 3mutA 1_4 3mutA _84 LIB1_1 MLVMS P03355 LIB1_ FFV_O93209-Pro LIB1_1 MLVCB P08361 _106 3mutA_WS 1_4 _84 3mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ GALV_P21414_3 LIB1_1 MLVFF_P26809_3 _106 mut 1_4 mutA _84 mutA LIB1_1 SFV3L_P27401_2 LIB1_ KORV_Q9TTC1_3 LIB1_1 MLVMS_P03355_ _106 mut 1_4 mut _84 3mutA_WS LIB1_1 XMRV6 A1Z651 LIB1_ MLVAV P03356 LIB1_1 XMRV6 A1Z651 _106 3mutA 1_4 3mutA _84 3mutA LIB1_1 KORV_Q9TTC1- LIB1_ MLVBM_Q7SVK7 LIB1_1 GALV_P21414_3 _106 Pro_3mut 1_4 _3mutA_WS _85 mutA LIB1_1 BAEVM_P10272_ LIB1_ MLVCB_P08361_ LIB1_1 KORV_Q9TTC1- _107 3mutA 1_4 3mutA _85 Pro_3mutA LIB1_1 KORV_Q9TTC1- LIB1_ MLVMS_P03355_ LIB1_1 MLVFF_P26809_3 _107 Pro_3mutA 1_4 3mutA_WS _85 mutA LIB1_1 MLVAV P03356 LIB1_ WMSV P03359 3 LIB1_1 MLVMS P03355 _107 3mutA 1_4 mutA _85 3mutA_WS LIB1_1 MLVBM_Q7SVK7 LIB1_ FOAMV_P14350_ LIB1_1 PERV_Q4VFZ2_3 _107 _3mutA_WS 1_4 2mutA _85 mut LIB1_1 PERV_Q4VFZ2_3 LIB1_ KORV_Q9TTC1- LIB1_1 WMSV_P03359_3 _107 mut 1_4 Pro_3mut _85 mutA LIB1_1 WMSV_P03359_3 LIB1_ PERV_Q4VFZ2_3 LIB1_1 XMRV6_A1Z651_ _107 mutA 1_4 mutA_WS _85 3mutA LIB1_1 XMRV6_A1Z651_ LIB1_ MLVAV_P03356_ LIB1_1 KORV_Q9TTC1_3 _107 3mutA l_40 3mutA _85 mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ MLVBM_Q7SVK7 LIB1_1 BAEVM_P10272_ _107 mutA_WS l_40 _3mutA_WS _86 3mutA LIB1_1 WDSV_O92815 LIB1_ MLVCB_P08361_ LIB1_1 FLV_P10273_3mut _107 l_40 3mutA _86 A LIB1_1 BAEVM P10272 LIB1_ MLVFF P26809 3 LIB1_1 MLVFF P26809 3 _108 3mutA l_40 mutA _86 mutA LIB1_1 MLVAV_P03356_ LIB1_ PERV_Q4VFZ2_3 LIB1_1 MLVMS_P03355_ _108 3mutA l_40 mut _86 3mutA_WS LIB1_1 MLVBM_Q7SVK7 LIB1_ WMSV P03359 3 LIB1_1 SFV3L_P27401- _108 _3mutA_WS l_40 mutA _86 Pro_2mutA LIB1_1 MLVFF P26809 3 LIB1_ XMRV6 A1Z651 LIB1_1 SFV3L P27401 2 _108 mutA l_40 3mutA _86 mut Linker id RT name Linke r id RT name Linker id RT name LIB1_1 MLVMS P03355 LIB1_ FOAMV P14350 LIB1_1 WMSV P03359 3 _108 3mutA_WS l_40 2mutA _86 mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ KORV_Q9TTC1- LIB1_1 XMRV6_A1Z651_ _108 mut l_40 Pro_3mut _86 3mutA LIB1_1 WMSV_P03359_3 LIB1_ KORV_Q9TTC1_3 LIB1_1 PERV_Q4VFZ2_3 _108 mutA l_40 mutA _86 mutA_WS LIB1_1 XMRV6_A1Z651_ LIB1_ PERV_Q4VFZ2_3 LIB1_1 WDSV_O92815_2 _108 3mutA l_40 mutA_WS _86 mut LIB1_1 KORV_Q9TTC1- LIB1_ AVIRE_P03360_3 LIB1_1 BAEVM_P10272_ _108 Pro_3mut 1_41 mutA _87 3mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ GALV_P21414_3 LIB1_1 KORV_Q9TTC1- _108 mutA_WS 1_41 mutA _87 Pro_3mutA LIB1_1 BAEVM_P10272_ LIB1_ KORV_Q9TTC1- LIB1_1 MLVCB_P08361_ _109 3mutA 1_41 Pro_3mutA _87 3mutA LIB1_1 FLV_P10273_3mut LIB1_ KORV_Q9TTC1_3 LIB1_1 MLVMS_P03355_ _109 A 1_41 mut _87 3mutA_WS LIB1_1 FOAMV_P14350- LIB1_ MLVAV P03356 LIB1_1 SFV3L P27401 2 _109 Pro_2mutA 1_41 3mutA _87 mut LIB1_1 GALV P21414 3 LIB1_ MLVCB P08361 LIB1_1 FOAMV P14350 _109 mutA 1_41 3mutA _87 2mutA LIB1_1 MLVAV P03356 LIB1_ MLVFF P26809 3 LIB1_1 MLVAV P03356 _109 3mutA 1_41 mutA _88 3mutA LIB1_1 MLVBM_Q7SVK7 LIB1_ MLVMS P03355 LIB1_1 MLVBM_Q7SVK7 _109 _3mutA_WS 1_41 3mutA_WS _88 _3mutA_WS LIB1_1 MLVFF_P26809_3 LIB1_ KORV_Q9TTC1- LIB1_1 MLVCB_P08361_ _109 mutA 1_41 Pro_3mut _88 3mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ KORV_Q9TTC1_3 LIB1_1 MLVFF_P26809_3 _109 mut 1_41 mutA _88 mutA LIB1_1 SFV1_P23074-Pro LIB1_ PERV_Q4VFZ2_3 LIB1_1 MLVMS_P03355_ _109 1_41 mutA_WS _88 3mutA_WS LIB1_1 SFV3L_P27401- LIB1_ WDSV_O92815 LIB1_1 BAEVM Pl0272 _109 Pro_2mutA 1_41 _89 3mutA LIB1_1 WMSV P03359 3 LIB1_ BAEVM Pl0272 LIB1_1 FFV_O93209 _109 mutA 1_42 3mutA _89 LIB1_1 XMRV6_A1Z651_ LIB1_ FLV_P10273_3mut LIB1_1 MLVAV_P03356_ _109 3mutA 1_42 A _89 3mutA LIB1_1 KORV_Q9TTC1- LIB1_ FOAMV_P14350- LIB1_1 MLVBM_Q7SVK7 _109 Pro_3mut 1_42 Pro_2mutA _89 _3mutA_WS LIB1_1 KORV_Q9TTC1_3 LIB1_ KORV_Q9TTC1_3 LIB1_1 MLVFF_P26809_3 _109 mutA 1_42 mut _89 mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ MLVAV_P03356_ LIB1_1 MLVMS_P03355_ _109 mutA_WS 1_42 3mutA _89 3mutA_WS LIB1_1 WDSV_O92815 LIB1_ MLVBM_Q7SVK7 LIB1_1 WMSV P03359 3 _109 1_42 _3mutA_WS _89 mutA Linker id RT name Linke r id RT name Linker id RT name LIB1_1 WDSV_O92815_2 LIB1_ MLVCB_P08361_ LIB1_1 KORV_Q9TTC1_3 _109 mutA 1_42 3mutA _89 mutA LIB1_1 MLVCB P08361 LIB1_ MLVMS P03355 LIB1_1 BAEVM Pl0272 _11 3mutA 1_42 3mutA_WS _9 3mutA LIB1_1 XMRV6_A1Z651_ LIB1_ PERV_Q4VFZ2_3 LIB1_1 GALV_P21414_3 _11 3mutA 1_42 mut _9 mutA LIB1_1 HTLV2_P03363_2 LIB1_ WMSV_P03359_3 LIB1_1 KORV_Q9TTC1- _11 mut 1_42 mutA _9 Pro_3mutA LIB1_1 FOAMV P14350 LIB1_ XMRV6 A1Z651 LIB1_1 MLVAV P03356 .no 2mut 1_42 3mutA _9 3mutA LIB1_1 MLVAV_P03356_ LIB1_ KORV_Q9TTC1_3 LIB1_1 MLVBM_Q7SVK7 _iio 3mutA 1_42 mutA _9 _3mutA_WS LIB1_1 MLVCB_P08361_ LIB1_ PERV_Q4VFZ2_3 LIB1_1 MLVCB_P08361_ .no 3mutA 1_42 mutA_WS _9 3mutA LIB1_1 MLVFF P26809 3 LIB1_ AVIRE P03360 3 LIB1_1 MLVFF P26809 3 .no mutA 1_43 mutA _9 mutA LIB1_1 MLVMS_P03355_ LIB1_ BAEVM_P10272_ LIB1_1 PERV_Q4VFZ2_3 _no 3mutA_WS 1_43 3mutA _9 mut LIB1_1 WMSV P03359 3 LIB1_ GALV P21414 3 LIB1_1 WMSV P03359 3 .no mutA 1_43 mutA _9 mutA LIB1_1 XMRV6 A1Z651 LIB1_ MLVBM_Q7SVK7 LIB1_1 PERV_Q4VFZ2_3 .no 3mutA 1_43 _3mutA_WS _9 mutA_WS LIB1_1 KORV_Q9TTC1- LIB1_ MLVCB_P08361_ LIB1_1 KORV_Q9TTC1- .no Pro_3mut 1_43 3mutA _90 Pro_3mutA LIB1_1 KORV_Q9TTC1_3 LIB1_ WMSV_P03359_3 LIB1_1 MLVAV_P03356_ .no mutA 1_43 mutA _90 3mutA LIB1_1 FFV_O93209 LIB1_ XMRV6 A1Z651 LIB1_1 MLVMS P03355 _m 1_43 3mutA _90 3mutA_WS LIB1_1 KORV_Q9TTC1- LIB1_ FOAMV_P14350_ LIB1_1 XMRV6_A1Z651_ _H1 Pro_3mutA 1_43 2mutA _90 3mutA LIB1_1 MLVBM_Q7SVK7 LIB1_ KORV_Q9TTC1- LIB1_1 KORV_Q9TTC1_3 -111 _3mutA_WS 1_43 Pro_3mut _90 mutA LIB1_1 MLVCB_P08361_ LIB1_ KORV_Q9TTC1_3 LIB1_1 FOAMV_P14350- .111 3mutA 1_43 mutA _91 Pro_2mutA LIB1_1 MLVFF_P26809_3 LIB1_ PERV_Q4VFZ2_3 LIB1_1 FOAMV_P14350_ .111 mutA 1_43 mutA_WS _91 2mut LIB1_1 MLVMS P03355 LIB1_ WDSV 092815 2 LIB1_1 MLVFF P26809 3 .111 3mutA_WS 1_43 mut _91 mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ BAEVM_P10272_ LIB1_1 MLVMS_P03355_ .Hl mut 1_44 3mutA _91 3mutA_WS LIB1_1 XMRV6 A1Z651 LIB1_ FLV P10273 3mut LIB1_1 FOAMV_P14350- .111 3mutA 1_44 A _92 Pro_2mutA LIB1_1 WDSV_O92815 LIB1_ GALV P21414 3 LIB1_1 GALV P21414 3 .111 1_44 mutA _92 mutA Linker id RT name Linke r id RT name Linker id RT name LIB1_1 BAEVM_P10272_ LIB1_ KORV_Q9TTC1_3 LIB1_1 KORV_Q9TTC1_3 _112 3mutA 1_44 mut _92 mut LIB1_1 FLV P10273 3mut LIB1_ MLVAV P03356 LIB1_1 MLVMS P03355 _112 A 1_44 3mutA _92 3mutA_WS LIB1_1 KORV_Q9TTC1- LIB1_ MLVBM_Q7SVK7 LIB1_1 PERV_Q4VFZ2_3 _112 Pro_3mutA 1_44 _3mutA_WS _92 mut LIB1_1 MLVFF_P26809_3 LIB1_ WMSV_P03359_3 LIB1_1 PERV_Q4VFZ2_3 _112 mutA 1_44 mutA _92 mutA_WS LIB1_1 MLVMS_P03355_ LIB1_ FOAMV_P14350- LIB1_1 MLVBM_Q7SVK7 _112 3mutA_WS 1_44 Pro_2mut _93 _3mutA_WS LIB1_1 WMSV P03359 3 LIB1_ BAEVM Pl0272 LIB1_1 MLVCB P08361 _112 mutA 1_45 3mutA _93 3mutA LIB1_1 BAEVM P10272 LIB1_ FOAMV P14350 LIB1_1 MLVMS P03355 _113 3mutA 1_45 2mut _93 3mutA_WS LIB1_1 FLV_P10273_3mut LIB1_ KORV_Q9TTC1- LIB1_1 SFV3L_P27401- _113 A 1_45 Pro_3mutA _93 Pro_2mutA LIB1_1 FOAMV_P14350- LIB1_ MLVAV P03356 LIB1_1 WMSV P03359 3 _113 Pro_2mutA 1_45 3mutA _93 mutA LIB1_1 GALV_P21414_3 LIB1_ PERV_Q4VFZ2_3 LIB1_1 KORV_Q9TTC1- _113 mutA 1_45 mut _94 Pro_3mutA LIB1_1 KORV_Q9TTC1- LIB1_ SFV3L_P27401- LIB1_1 KORV_Q9TTC1_3 J 13 Pro_3mutA 1_45 Pro_2mutA _94 mut LIB1_1 MLVBM_Q7SVK7 LIB1_ WMSV P03359 3 LIB1_1 MLVBM_Q7SVK7 _113 _3mutA_WS 1_45 mutA _94 _3mutA_WS LIB1_1 MLVCB P08361 LIB1_ XMRV6 A1Z651 LIB1_1 MLVCB P08361 _113 3mutA 1_45 3mutA _94 3mutA LIB1_1 MLVFF P26809 3 LIB1_ FOAMV P14350 LIB1_1 MLVFF P26809 3 _113 mutA 1_45 2mutA _94 mutA LIB1_1 MLVMS_P03355_ LIB1_ KORV_Q9TTC1_3 LIB1_1 MLVMS_P03355_ _113 3mutA_WS 1_45 mutA _94 3mutA_WS LIB1_1 PERV_Q4VFZ2_3 LIB1_ WDSV_O92815 LIB1_1 SFV1_P23O74 _113 mut 1_45 _94 LIB1_1 SFV3L P27401 2 LIB1_ MLVAV P03356 LIB1_1 MLVCB P08361 _113 mut 1_46 3mutA _95 3mutA LIB1_1 WMSV_P03359_3 LIB1_ MLVBM_Q7SVK7 LIB1_1 MLVFF_P26809_3 _113 mutA 1_46 _3mutA_WS _95 mutA LIB1_1 XMRV6 A1Z651 LIB1_ SFV1_P23O74 LIB1_1 MLVMS P03355 _113 3mutA 1_46 _95 3mutA_WS LIB1_1 FOAMV P14350 LIB1_ SFV1_P23074-Pro LIB1_1 FLV P10273 3mut _113 2mutA 1_46 _96 A LIB1_1 KORV_Q9TTC1- LIB1_ SFV3L_P27401- LIB1_1 KORV_Q9TTC1- _113 Pro_3mut 1_46 Pro_2mutA _96 Pro_3mutA LIB1_1 KORV_Q9TTC1_3 LIB1_ WMSV_P03359_3 LIB1_1 KORV_Q9TTC1_3 _113 mutA 1_46 mutA _96 mut Linker id RT name Linke r id RT name Linker id RT name LIB1_1 WDSV 092815 2 LIB1_ FOAMV_P14350- LIB1_1 MLVAV P03356 _113 mut 1_46 Pro_2mut _96 3mutA LIB1_1 AVIRE_P03360_3 LIB1_ KORV_Q9TTC1- LIB1_1 MLVBM_Q7SVK7 _114 mutA 1_46 Pro_3mut _96 _3mutA_WS LIB1_1 BAEVM_P10272_ LIB1_ PERV_Q4VFZ2_3 LIB1_1 MLVMS_P03355_ _114 3mutA 1_46 mutA_WS _96 3mutA_WS LIB1_1 GALV_P21414_3 LIB1_ AVIRE_P03360_3 LIB1_1 PERV_Q4VFZ2_3 _114 mutA 1_47 mutA _96 mut LIB1_1 KORV_Q9TTC1- LIB1_ BAEVM_P10272_ LIB1_1 WMSV_P03359_3 _114 Pro_3mutA 1_47 3mutA _96 mutA LIB1_1 MLVBM_Q7SVK7 LIB1_ FOAMV_P14350_ LIB1_1 XMRV6_A1Z651_ _114 _3mutA_WS 1_47 2mut _96 3mutA LIB1_1 MLVCB_P08361_ LIB1_ MLVAV_P03356_ LIB1_1 KORV_Q9TTC1- _114 3mutA 1_47 3mutA _96 Pro_3mut LIB1_1 WMSV_P03359_3 LIB1_ MLVBM_Q7SVK7 LIB1_1 PERV_Q4VFZ2_3 _114 mutA 1_47 _3mutA_WS _96 mutA_WS LIB1_1 XMRV6 A1Z651 LIB1_ MLVFF P26809 3 LIB1_1 BAEVM P10272 _114 3mutA 1_47 mutA _97 3mutA LIB1_1 FOAMV_P14350- LIB1_ MLVMS_P03355_ LIB1_1 KORV_Q9TTC1- _114 Pro_2mut 1_47 3mutA_WS _97 Pro_3mutA LIB1_1 WDSV_O92815 LIB1_ XMRV6 A1Z651 LIB1_1 MLVCB P08361 J 14 1_47 3mutA _97 3mutA LIB1_1 FLV_P10273_3mut LIB1_ KORV_Q9TTC1_3 LIB1_1 MLVFF_P26809_3 _115 A 1_47 mutA _97 mutA LIB1_1 KORV_Q9TTC1_3 LIB1_ BAEVM_P10272_ LIB1_1 MLVMS_P03355_ _115 mut 1_48 3mutA _97 3mutA_WS LIB1_1 MLVBM_Q7SVK7 LIB1_ FLV_P10273_3mut LIB1_1 WMSV_P03359_3 _115 _3mutA_WS 1_48 A _97 mutA LIB1_1 MLVCB P08361 LIB1_ MLVAV P03356 LIB1_1 XMRV6 A1Z651 _115 3mutA 1_48 3mutA _97 3mutA LIB1_1 MLVFF_P26809_3 LIB1_ MLVBM_Q7SVK7 LIB1_1 BAEVM_P10272_ _115 mutA 1_48 _3mutA_WS _98 3mutA LIB1_1 SFV1_P23074-Pro LIB1_ MLVCB P08361 LIB1_1 MLVBM_Q7SVK7 _115 1_48 3mutA _98 _3mutA_WS LIB1_1 WMSV_P03359_3 LIB1_ MLVFF_P26809_3 LIB1_1 MLVCB_P08361_ _115 mutA 1_48 mutA _98 3mutA LIB1_1 XMRV6 A1Z651 LIB1_ MLVMS P03355 LIB1_1 MLVFF P26809 3 _115 3mutA 1_48 3mutA_WS _98 mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ SFV3L_P27401- LIB1_1 MLVMS_P03355_ _115 mutA_WS 1_48 Pro_2mutA _98 3mutA_WS LIB1_1 FOAMV_P 14350- LIB1_ XMRV6 A1Z651 LIB1_1 SFV3L_P27401- _116 Pro_2mutA 1_48 3mutA _98 Pro_2mutA LIB1_1 GALV_P21414_3 LIB1_ KORV_Q9TTC1- LIB1_1 WMSV_P03359_3 _116 mutA 1_48 Pro_3mut _98 mutA Linker id RT name Linke r id RT name Linker id RT name LIB1_1 KORV_Q9TTC1- LIB1_ PERV_Q4VFZ2_3 LIB1_1 FLV_P10273_3mut _116 Pro_3mutA 1_48 mutA_WS _99 A LIB1_1 MLVAV P03356 LIB1_ BAEVM Pl0272 LIB1_1 FOAMV_P14350- _116 3mutA 1_49 3mutA _99 Pro_2mutA LIB1_1 MLVBM_Q7SVK7 LIB1_ KORV_Q9TTC1- LIB1_1 KORV_Q9TTC1- _116 _3mutA_WS 1_49 Pro_3mutA _99 Pro_3mutA LIB1_1 MLVCB_P08361_ LIB1_ MLVBM_Q7SVK7 LIB1_1 MLVAV_P03356_ _116 3mutA 1_49 _3mutA_WS _99 3mutA LIB1_1 MLVFF P26809 3 LIB1_ MLVCB P08361 LIB1_1 MLVCB P08361 _116 mutA 1_49 3mutA _99 3mutA LIB1_1 MLVMS P03355 LIB1_ MLVFF P26809 3 LIB2_E BAEVM Pl0272 _116 3mutA_WS 1_49 mutA A_1 3mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ SFV1_P23074-Pro LIB2_E FLV_P10273_3mut _116 mutA_WS 1_49 A_1 A LIB1_1 AVIRE P03360 3 LIB1_ WMSV P03359 3 LIB2_E FOAMV_P14350- _117 mutA 1_49 mutA A_1 Pro_2mutA LIB1_1 BAEVM_P10272_ LIB1_ XMRV6_A1Z651_ LIB2_E KORV_Q9TTC1_3 _117 3mutA 1_49 3mutA A_1 mut LIB1_1 MLVBM_Q7SVK7 LIB1_ PERV_Q4VFZ2_3 LIB2_E MLVBM_Q7SVK7 _117 _3mutA_WS 1_49 mutA_WS A_1 _3mutA_WS LIB1_1 MLVCB P08361 LIB1_ BAEVM Pl0272 LIB2_E MLVCB P08361 J 17 3mutA l_50 3mutA A_1 3mutA LIB1_1 XMRV6 A1Z651 LIB1_ FOAMV P14350 LIB2_E MLVMS P03355 _117 3mutA l_50 2mut A_1 3mutA_WS LIB1_1 HTLV2_P03363 LIB1_ GALV P21414 3 LIB2_E SFV1_P23074-Pro _117 l_50 mutA A_1 LIB1_1 WDSV_O92815_2 LIB1_ KORV_Q9TTC1- LIB2_E XMRV6_A1Z651_ _117 mut l_50 Pro_3mutA A_1 3mutA LIB1_1 WDSV 092815 2 LIB1_ MLVBM_Q7SVK7 LIB2_E FOAMV_P14350- _117 mutA l_50 _3mutA_WS A_1 Pro_2mut LIB1_1 FOAMV_P 14350- LIB1_ MLVMS P03355 LIB2_E HTLV2 P03363 2 _118 Pro_2mutA l_50 3mutA_WS A_1 mut LIB1_1 MLVBM_Q7SVK7 LIB1_ WMSV_P03359_3 LIB2_E WDSV_O92815_2 _118 _3mutA_WS l_50 mutA A_1 mut LIB1_1 MLVCB_P08361_ LIB1_ XMRV6_A1Z651_ LIB2_E BAEVM_P10272_ _118 3mutA l_50 3mutA A_10 3mutA LIB1_1 MLVFF_P26809_3 LIB1_ PERV_Q4VFZ2_3 LIB2_E KORV_Q9TTCL _118 mutA l_50 mutA_WS A_10 Pro_3mutA LIB1_1 MLVMS P03355 LIB1_ WDSV_O92815 LIB2_E MLVCB P08361 _118 3mutA_WS l_50 A_10 3mutA LIB1_1 SFV3L_P27401- LIB1_ BAEVM_P10272_ LIB2_E KORV_Q9TTC1_3 _118 Pro_2mutA 1_51 3mutA A_10 mutA LIB1_1 WMSV_P03359_3 LIB1_ KORV_Q9TTC1- LIB2_E FLV_P10273_3mut _118 mutA 1_51 Pro_3mutA A_H A Linker id RT name Linke r id RT name Linker id RT name LIB1_1 _118 KORV_Q9TTC1- Pro_3mut LIB1_ 1_51 MLVMS_P03355_ 3mutA_WS LIB2_E A_H GALV_P21414_3 mutA LIB1_1 _119 FOAMV_P14350_ 2mut LIB1_ 1_51 WMSV_P03359_3 mutA LIB2_E A_ll KORV_Q9TTC1- Pro_3mutA LIB1_1 _119 MLVBM_Q7SVK7 _3mutA_WS LIB1_ 1_51 XMRV6_A1Z651_ 3mutA LIB2_E A_ll MLVAV_P03356_ 3mutA LIB1_1 _119 MLVFF_P26809_3 mutA LIB1_ 1_52 FFV_O93209 LIB2_E A_H MLVBM_Q7SVK7 _3mutA_WS LIB1_1 _119 MLVMS_P03355_ 3mutA_WS LIB1_ 1_52 FLV_P10273_3mut A LIB2_E A_ll MLVCB_P08361_ 3mutA LIB1_1 _119 SFV1_P23O74 LIB1_ 1_52 MLVCB_P08361_ 3mutA LIB2_E A_ll WMSV_P03359_3 mutA LIB1_1 _119 WMSV_P03359_3 mutA LIB1_ 1_52 MLVMS_P03355_ 3mutA_WS LIB2_E A_ll KORV_Q9TTC1_3 mutA LIB1_1 _119 KORV_Q9TTC1- Pro_3mut LIB1_ 1_52 PERV_Q4VFZ2_3 mut LIB2_E A_H PERV_Q4VFZ2_3 mutA_WS LIB1_1 _119 KORV_Q9TTC1_3 mutA LIB1_ 1_52 SFV3L_P27401- Pro_2mutA LIB2_E A_12 GALV_P21414_3 mutA LIB1_1 _12 KORV_Q9TTC1- Pro_3mutA LIB1_ 1_53 AVIRE_P03360_3 mutA LIB2_E A_12 MLVBM_Q7SVK7 _3mutA_WS LIB1_1 _12 MLVBM_Q7SVK7 _3mutA_WS LIB1_ 1_53 BAEVM_P10272_ 3mutA LIB2_E A_12 MLVCB_P08361_ 3mutA LIB1_1 _12 MLVMS_P03355_ 3mutA_WS LIB1_ 1_53 GALV_P21414_3 mutA LIB2_E A_12 MLVFF_P26809_3 mutA LIB1_1 _12 PERV_Q4VFZ2_3 mut LIB1_ 1_53 KORV_Q9TTC1- Pro_3mutA LIB2_E A_12 PERV_Q4VFZ2_3 mut LIB1_1 _12 SFV3L_P27401- Pro_2mutA LIB1_ 1_53 MLVBM_Q7SVK7 _3mutA_WS LIB2_E A_12 WMSV_P03359_3 mutA LIB1_1 _12 XMRV6_A1Z651_ 3mutA LIB1_ 1_53 MLVCB_P08361_ 3mutA LIB2_E A_12 KORV_Q9TTC1_3 mutA LIB1_1 _12 KORV_Q9TTC1_3 mutA LIB1_ 1_53 SFV3L_P27401_2 mut LIB2_E A_12 HTLV2_P03363_2 mut LIB1_1 _120 BAEVM_P10272_ 3mutA LIB1_ 1_53 WMSV_P03359_3 mutA LIB2_E A_13 AVIRE_P03360_3 mutA LIB1_1 _120 FLV_P10273_3mut A LIB1_ 1_53 KORV_Q9TTC1_3 mutA LIB2_E A_13 BAEVM_P10272_ 3mutA LIB1_1 _120 GALV_P21414_3 mutA LIB1_ 1_54 FOAMV_P14350_ 2mut LIB2_E A_13 FLV_P10273_3mut A LIB1_1 _120 KORV_Q9TTC1- Pro_3mutA LIB1_ 1_54 KORV_Q9TTC1_3 mut LIB2_E A_13 KORV_Q9TTC1- Pro_3mutA LIB1_1 _120 MLVBM_Q7SVK7 _3mutA_WS LIB1_ 1_54 MLVCB_P08361_ 3mutA LIB2_E A_13 MLVAV_P03356_ 3mutA LIB1_1 _120 MLVFF_P26809_3 mutA LIB1_ 1_54 MLVFF_P26809_3 mutA LIB2_E A_13 MLVCB_P08361_ 3mutA Linker id RT name Linke r id RT name Linker id RT name LIB1_1 _120 WMSV_P03359_3 mutA LIB1_ 1_54 PERV_Q4VFZ2_3 mut LIB2_E A_13 MLVFF_P26809_3 mutA LIB1_1 _120 XMRV6_A1Z651_ 3mutA LIB1_ 1_54 KORV_Q9TTC1_3 mutA LIB2_E A_13 SFV3L_P27401- Pro_2mutA LIB1_1 _120 KORV_Q9TTC1_3 mutA LIB1_ 1_54 WDSV_O92815_2 mutA LIB2_E A_13 WMSV_P03359_3 mutA LIB1_1 _121 BAEVM_P10272_ 3mutA LIB1_ 1_55 FFV_O93209 LIB2_E A_13 XMRV6_A1Z651_ 3mutA LIB1_1 _121 FOAMV_P14350- Pro_2mutA LIB1_ 1_55 FLV_P10273_3mut A LIB2_E A_13 KORV_Q9TTC1- Pro_3mut LIB1_1 _121 FOAMV_P14350_ 2mut LIB1_ 1_55 FOAMV_P14350- Pro_2mutA LIB2_E A_13 KORV_Q9TTC1_3 mutA LIB1_1 _121 GALV_P21414_3 mutA LIB1_ 1_55 GALV_P21414_3 mutA LIB2_E A_13 WDSV_O92815_2 mutA LIB1_1 _121 MLVCB_P08361_ 3mutA LIB1_ 1_55 KORV_Q9TTC1- Pro_3mutA LIB2_E A_14 BAEVM_P10272_ 3mutA LIB1_1 _121 MLVMS_P03355_ 3mutA_WS LIB1_ 1_55 MLVCB_P08361_ 3mutA LIB2_E A_14 FOAMV_P14350- Pro_2mutA LIB1_1 _121 FOAMV_P14350_ 2mutA LIB1_ 1_55 MLVFF_P26809_3 mutA LIB2_E A_14 MLVAV_P03356_ 3mutA LIB1_1 _122 BAEVM_P10272_ 3mutA LIB1_ 1_55 MLVMS_P03355_ 3mutA_WS LIB2_E A_14 MLVCB_P08361_ 3mutA LIB1_1 _122 FLV_P10273_3mut A LIB1_ 1_55 WMSV_P03359_3 mutA LIB2_E A_14 MLVFF_P26809_3 mutA LIB1_1 _122 KORV_Q9TTC1- Pro_3mutA LIB1_ 1_55 XMRV6_A1Z651_ 3mutA LIB2_E A_14 MLVMS_P03355_ 3mutA_WS LIB1_1 _122 MLVAV_P03356_ 3mutA LIB1_ 1_55 KORV_Q9TTC1- Pro_3mut LIB2_E A_14 KORV_Q9TTC1_3 mutA LIB1_1 _122 MLVBM_Q7SVK7 _3mutA_WS LIB1_ 1_55 KORV_Q9TTC1_3 mutA LIB2_E A_15 KORV_Q9TTC1- Pro_3mutA LIB1_1 _122 MLVCB_P08361_ 3mutA LIB1_ 1_55 PERV_Q4VFZ2_3 mutA_WS LIB2_E A_15 MLVAV_P03356_ 3mutA LIB1_1 _122 MLVFF_P26809_3 mutA LIB1_ 1_56 KORV_Q9TTC1- Pro_3mutA LIB2_E A_15 MLVCB_P08361_ 3mutA LIB1_1 _122 MLVMS_P03355_ 3mutA_WS LIB1_ 1_56 MLVAV_P03356_ 3mutA LIB2_E A_15 MLVFF_P26809_3 mutA LIB1_1 _122 PERV_Q4VFZ2_3 mut LIB1_ 1_56 MLVCB_P08361_ 3mutA LIB2_E A_15 WMSV_P03359_3 mutA LIB1_1 _122 SFV3L_P27401- Pro_2mutA LIB1_ 1_56 MLVFF_P26809_3 mutA LIB2_E A_15 PERV_Q4VFZ2_3 mutA_WS LIB1_1 _122 SFV3L_P27401_2 mut LIB1_ 1_56 MLVMS_P03355_ 3mutA_WS LIB2_E A_16 MLVAV_P03356_ 3mutA LIB1_1 _122 WMSV_P03359_3 mutA LIB1_ 1_56 PERV_Q4VFZ2_3 mut LIB2_E A_16 MLVFF_P26809_3 mutA Linker id RT name Linke r id RT name Linker id RT name LIB1_1 _122 PERV_Q4VFZ2_3 mutA_WS LIB1_ 1_56 XMRV6_A1Z651_ 3mutA LIB2_E A_16 SFV3L_P27401- Pro_2mutA LIB1_1 _122 WDSV_O92815_2 mutA LIB1_ 1_56 KORV_Q9TTC1_3 mutA LIB2_E A_16 XMRV6_A1Z651_ 3mutA LIB1_1 _13 BAEVM_P10272_ 3mutA LIB1_ 1_56 PERV_Q4VFZ2_3 mutA_WS LIB2_E A_17 AVIRE_P03360_3 mutA LIB1_1 _13 GALV_P21414_3 mutA LIB1_ 1_57 FLV_P10273_3mut A LIB2_E A_17 BAEVM_P10272_ 3mutA LIB1_1 _13 KORV_Q9TTC1- Pro_3mutA LIB1_ 1_57 MLVAV_P03356_ 3mutA LIB2_E A_17 KORV_Q9TTC1- Pro_3mutA LIB1_1 _13 KORV_Q9TTC1_3 mut LIB1_ 1_57 MLVBM_Q7SVK7 _3mutA_WS LIB2_E A_17 KORV_Q9TTC1_3 mut LIB1_1 _13 MLVAV_P03356_ 3mutA LIB1_ 1_57 MLVFF_P26809_3 mutA LIB2_E A_17 MLVAV_P03356_ 3mutA LIB1_1 _13 MLVFF_P26809_3 mutA LIB1_ 1_57 MLVMS_P03355_ 3mutA_WS LIB2_E A_17 MLVCB_P08361_ 3mutA LIB1_1 _13 MLVMS_P03355_ 3mutA_WS LIB1_ 1_57 PERV_Q4VFZ2_3 mut LIB2_E A_17 MLVFF_P26809_3 mutA LIB1_1 _13 WMSV_P03359_3 mutA LIB1_ 1_57 SFV3L_P27401- Pro_2mutA LIB2_E A_17 MLVMS_P03355_ 3mutA_WS LIB1_1 J 3 FOAMV_P 14350- Pro_2mut LIB1_ 1_57 WMSV_P03359_3 mutA LIB2_E A_17 PERV_Q4VFZ2_3 mut LIB1_1 _13 KORV_Q9TTC1- Pro_3mut LIB1_ 1_57 KORV_Q9TTC1- Pro_3mut LIB2_E A_17 SFV3L_P27401- Pro_2mutA LIB1_1 _13 KORV_Q9TTC1_3 mutA LIB1_ 1_58 BAEVM_P10272_ 3mutA LIB2_E A_17 KORV_Q9TTC1_3 mutA LIB1_1 _13 PERV_Q4VFZ2_3 mutA_WS LIB1_ 1_58 KORV_Q9TTC1- Pro_3mutA LIB2_E A_17 PERV_Q4VFZ2_3 mutA_WS LIB1_1 _14 BAEVM_P10272_ 3mutA LIB1_ 1_58 MLVBM_Q7SVK7 _3mutA_WS LIB2_E A_17 HTLV2_P03363 LIB1_1 _14 FOAMV_P 14350- Pro_2mutA LIB1_ 1_58 MLVCB_P08361_ 3mutA LIB2_E A_18 BAEVM_P10272_ 3mutA LIB1_1 _14 GALV_P21414_3 mutA LIB1_ 1_58 MLVFF_P26809_3 mutA LIB2_E A_18 FLV_P10273_3mut A LIB1_1 _14 MLVAV_P03356_ 3mutA LIB1_ 1_58 MLVMS_P03355_ 3mutA_WS LIB2_E A_18 GALV_P21414_3 mutA LIB1_1 _14 MLVCB_P08361_ 3mutA LIB1_ 1_58 PERV_Q4VFZ2_3 mut LIB2_E A_18 KORV_Q9TTC1- Pro_3mutA LIB1_1 _14 XMRV6_A1Z651_ 3mutA LIB1_ 1_58 WMSV_P03359_3 mutA LIB2_E A_18 MLVAV_P03356_ 3mutA LIB1_1 _14 KORV_Q9TTC1- Pro_3mut LIB1_ 1_58 KORV_Q9TTC1_3 mutA LIB2_E A_18 MLVCB_P08361_ 3mutA LIB1_1 _14 WDSV_O92815_2 mut LIB1_ 1_58 WDSV_O92815 LIB2_E A_18 MLVFF_P26809_3 mutA Linker id RT name Linke r id RT name Linker id RT name LIB1_1 BAEVM P10272 LIB1_ GALV P21414 3 LIB2_E SFV3L_P27401- _15 3mutA 1_59 mutA A_18 Pro_2mutA LIB1_1 MLVAV P03356 LIB1_ MLVAV P03356 LIB2_E SFV3L P27401 2 _15 3mutA 1_59 3mutA A_18 mut LIB1_1 MLVCB_P08361_ LIB1_ MLVBM_Q7SVK7 LIB2_E WMSV_P03359_3 _15 3mutA 1_59 _3mutA_WS A_18 mutA LIB1_1 KORV_Q9TTC1- LIB1_ MLVMS_P03355_ LIB2_E KORV_Q9TTC1- _15 Pro_3mut 1_59 3mutA_WS A_19 Pro_3mutA LIB1_1 KORV_Q9TTC1_3 LIB1_ WMSV_P03359_3 LIB2_E KORV_Q9TTC1_3 _15 mutA 1_59 mutA A_19 mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ KORV_Q9TTC1- LIB2_E AVIRE_P03360_3 _15 mutA_WS 1_59 Pro_3mut A_2 mutA LIB1_1 WDSV_O92815_2 LIB1_ PERV_Q4VFZ2_3 LIB2_E FLV_P10273_3mut _15 mutA 1_59 mutA_WS A_2 A LIB1_1 BAEVM P10272 LIB1_ BAEVM Pl0272 LIB2_E GALV P21414 3 _16 3mutA 1_6 3mutA A_2 mutA LIB1_1 GALV P21414 3 LIB1_ FLV P10273 3mut LIB2_E MLVCB P08361 _16 mutA 1_6 A A_2 3mutA LIB1_1 KORV_Q9TTC1- LIB1_ FOAMV_P14350- LIB2_E WMSV_P03359_3 _16 Pro_3mutA 1_6 Pro_2mutA A_2 mutA LIB1_1 MLVBM_Q7SVK7 LIB1_ GALV_P21414_3 LIB2_E XMRV6_A1Z651_ _16 _3mutA_WS 1_6 mutA A_2 3mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ KORV_Q9TTC1- LIB2_E KORV_Q9TTC1- _16 mut 1_6 Pro_3mutA A_20 Pro_3mutA LIB1_1 XMRV6 A1Z651 LIB1_ MLVFF P26809 3 LIB2_E MLVAV P03356 _16 3mutA 1_6 mutA A_20 3mutA LIB1_1 KORV_Q9TTC1- LIB1_ KORV_Q9TTC1_3 LIB2_E MLVBM_Q7SVK7 _16 Pro_3mut 1_6 mutA A_20 _3mutA_WS LIB1_1 PERV_Q4VFZ2_3 LIB1_ WDSV_O92815 LIB2_E MLVCB_P08361_ _16 mutA_WS 1_6 A_20 3mutA LIB1_1 WDSV 092815 2 LIB1_ BAEVM Pl0272 LIB2_E MLVFF P26809 3 _16 mut l_60 3mutA A_20 mutA LIB1_1 WDSV 092815 2 LIB1_ MLVAV P03356 LIB2_E MLVMS P03355 _16 mutA 1_61 3mutA A_20 3mutA_WS LIB1_1 AVIRE_P03360_3 LIB1_ MLVCB_P08361_ LIB2_E WMSV_P03359_3 _17 mutA 1_61 3mutA A_20 mutA LIB1_1 MLVFF P26809 3 LIB1_ MLVFF P26809 3 LIB2_E XMRV6 A1Z651 _17 mutA 1_61 mutA A_20 3mutA LIB1_1 MLVMS_P03355_ LIB1_ MLVMS_P03355_ LIB2_E KORV_Q9TTC1_3 _17 3mutA_WS 1_61 3mutA_WS A_20 mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ PERV_Q4VFZ2_3 LIB2_E PERV_Q4VFZ2_3 _17 mut 1_61 mut A_20 mutA_WS LIB1_1 SFV3L_P27401- LIB1_ WMSV P03359 3 LIB2_E FLV P10273 3mut _17 Pro_2mutA 1_61 mutA A_21 A Linker id RT name Linke r id RT name Linker id RT name LIB1_1 _17 XMRV6_A1Z651_ 3mutA LIB1_ 1_61 KORV_Q9TTC1- Pro_3mut LIB2_E A_21 GALV_P21414_3 mutA LIB1_1 _17 FOAMV_P14350_ 2mutA LIB1_ 1_62 FOAMV_P14350_ 2mut LIB2_E A_21 MLVAV_P03356_ 3mutA LIB1_1 _18 FFV_O93209 LIB1_ 1_62 MLVAV_P03356_ 3mutA LIB2_E A_21 MLVBM_Q7SVK7 _3mutA_WS LIB1_1 _18 FLV_P10273_3mut A LIB1_ 1_62 MLVFF_P26809_3 mutA LIB2_E A_21 WMSV_P03359_3 mutA LIB1_1 _18 GALV_P21414_3 mutA LIB1_ 1_62 MLVMS_P03355_ 3mutA_WS LIB2_E A_22 BAEVM_P10272_ 3mutA LIB1_1 _18 KORV_Q9TTC1- Pro_3mutA LIB1_ 1_62 SFV3L_P27401_2 mut LIB2_E A_22 FLV_P10273_3mut A LIB1_1 _18 MLVBM_Q7SVK7 _3mutA_WS LIB1_ 1_62 XMRV6_A1Z651_ 3mutA LIB2_E A_22 MLVAV_P03356_ 3mutA LIB1_1 _18 MLVMS_P03355_ 3mutA_WS LIB1_ 1_63 FOAMV_P14350- Pro_2mutA LIB2_E A_22 MLVCB_P08361_ 3mutA LIB1_1 _18 XMRV6_A1Z651_ 3mutA LIB1_ 1_63 MLVAV_P03356_ 3mutA LIB2_E A_22 MLVFF_P26809_3 mutA LIB1_1 _19 AVIRE_P03360_3 mutA LIB1_ 1_63 MLVBM_Q7SVK7 _3mutA_WS LIB2_E A_22 MLVMS_P03355_ 3mutA_WS LIB1_1 _19 BAEVM_P10272_ 3mutA LIB1_ 1_63 MLVMS_P03355_ 3mutA_WS LIB2_E A_22 PERV_Q4VFZ2_3 mut LIB1_1 _19 KORV_Q9TTC1- Pro_3mutA LIB1_ 1_63 XMRV6_A1Z651_ 3mutA LIB2_E A_22 XMRV6_A1Z651_ 3mutA LIB1_1 _19 MLVAV_P03356_ 3mutA LIB1_ 1_63 KORV_Q9TTC1_3 mutA LIB2_E A_22 KORV_Q9TTC1_3 mutA LIB1_1 _19 MLVBM_Q7SVK7 _3mutA_WS LIB1_ 1_64 BAEVM_P10272_ 3mutA LIB2_E A_23 BAEVM_P10272_ 3mutA LIB1_1 _19 XMRV6_A1Z651_ 3mutA LIB1_ 1_64 KORV_Q9TTC1- Pro_3mutA LIB2_E A_23 FOAMV_P14350- Pro_2mutA LIB1_1 _19 KORV_Q9TTC1_3 mutA LIB1_ 1_64 KORV_Q9TTC1_3 mut LIB2_E A_23 KORV_Q9TTC1_3 mut LIB1_1 _2 BAEVM_P10272_ 3mutA LIB1_ 1_64 MLVBM_Q7SVK7 _3mutA_WS LIB2_E A_23 MLVAV_P03356_ 3mutA LIB1_1 _2 KORV_Q9TTC1- Pro_3mutA LIB1_ 1_64 MLVFF_P26809_3 mutA LIB2_E A_23 MLVCB_P08361_ 3mutA LIB1_1 _2 MLVBM_Q7SVK7 _3mutA_WS LIB1_ 1_64 PERV_Q4VFZ2_3 mut LIB2_E A_23 MLVMS_P03355_ 3mutA_WS LIB1_1 _2 MLVFF_P26809_3 mutA LIB1_ 1_64 SFV3L_P27401- Pro_2mutA LIB2_E A_23 PERV_Q4VFZ2_3 mut LIB1_1 _2 MLVMS_P03355_ 3mutA_WS LIB1_ 1_64 SFV3L_P27401_2 mut LIB2_E A_23 WMSV_P03359_3 mutA LIB1_1 _2 WMSV_P03359_3 mutA LIB1_ 1_64 XMRV6_A1Z651_ 3mutA LIB2_E A_23 PERV_Q4VFZ2_3 mutA_WS Linker id RT name Linke r id RT name Linker id RT name LIB1_1 _2 XMRV6_A1Z651_ 3mutA LIB1_ 1_65 MLVFF_P26809_3 mutA LIB2_E A_24 AVIRE_P03360_3 mutA LIB1_1 _20 BAEVM_P10272_ 3mutA LIB1_ 1_65 MLVMS_P03355_ 3mutA_WS LIB2_E A_24 BAEVM_P10272_ 3mutA LIB1_1 _20 GALV_P21414_3 mutA LIB1_ 1_65 KORV_Q9TTC1- Pro_3mut LIB2_E A_24 FOAMV_P14350- Pro_2mutA LIB1_1 _20 KORV_Q9TTC1_3 mut LIB1_ 1_65 PERV_Q4VFZ2_3 mutA_WS LIB2_E A_24 GALV_P21414_3 mutA LIB1_1 _20 MLVAV_P03356_ 3mutA LIB1_ 1_66 AVIRE_P03360_3 mutA LIB2_E A_24 MLVAV_P03356_ 3mutA LIB1_1 _20 MLVCB_P08361_ 3mutA LIB1_ 1_66 KORV_Q9TTC1- Pro_3mutA LIB2_E A_24 MLVFF_P26809_3 mutA LIB1_1 _20 MLVMS_P03355_ 3mutA_WS LIB1_ 1_66 MLVAV_P03356_ 3mutA LIB2_E A_24 MLVMS_P03355_ 3mutA_WS LIB1_1 _20 WMSV_P03359_3 mutA LIB1_ 1_66 MLVBM_Q7SVK7 _3mutA_WS LIB2_E A_24 PERV_Q4VFZ2_3 mut LIB1_1 _20 KORV_Q9TTC1- Pro_3mut LIB1_ 1_66 MLVCB_P08361_ 3mutA LIB2_E A_24 WMSV_P03359_3 mutA LIB1_1 _21 FLV_P10273_3mut A LIB1_ 1_66 MLVMS_P03355_ 3mutA_WS LIB2_E A_24 XMRV6_A1Z651_ 3mutA LIB1_1 _21 FOAMV_P 14350- Pro_2mutA LIB1_ 1_66 KORV_Q9TTC1_3 mutA LIB2_E A_24 PERV_Q4VFZ2_3 mutA_WS LIB1_1 _21 MLVAV_P03356_ 3mutA LIB1_ 1_67 BAEVM_P10272_ 3mutA LIB2_E A_25 BAEVM_P10272_ 3mutA LIB1_1 _21 MLVCB_P08361_ 3mutA LIB1_ 1_67 FFV_O93209 LIB2_E A_25 FOAMV_P14350_ 2mut LIB1_1 _21 MLVFF_P26809_3 mutA LIB1_ 1_67 GALV_P21414_3 mutA LIB2_E A_25 GALV_P21414_3 mutA LIB1_1 _21 MLVMS_P03355_ 3mutA_WS LIB1_ 1_67 KORV_Q9TTC1- Pro_3mutA LIB2_E A_25 MLVBM_Q7SVK7 _3mutA_WS LIB1_1 _21 PERV_Q4VFZ2_3 mutA_WS LIB1_ 1_67 MLVAV_P03356_ 3mutA LIB2_E A_25 MLVCB_P08361_ 3mutA LIB1_1 _21 WDSV_O92815_2 mutA LIB1_ 1_67 MLVBM_Q7SVK7 _3mutA_WS LIB2_E A_25 MLVMS_P03355_ 3mutA_WS LIB1_1 _22 AVIRE_P03360_3 mutA LIB1_ 1_67 MLVCB_P08361_ 3mutA LIB2_E A_25 XMRV6_A1Z651_ 3mutA LIB1_1 _22 BAEVM_P10272_ 3mutA LIB1_ 1_67 MLVFF_P26809_3 mutA LIB2_E A_25 FOAMV_P14350_ 2mutA LIB1_1 _22 GALV_P21414_3 mutA LIB1_ 1_67 MLVMS_P03355_ 3mutA_WS LIB2_E A_25 KORV_Q9TTC1_3 mutA LIB1_1 _22 MLVAV_P03356_ 3mutA LIB1_ 1_67 SFV3L_P27401- Pro_2mutA LIB2_E A_25 PERV_Q4VFZ2_3 mutA_WS LIB1_1 _22 MLVFF_P26809_3 mutA LIB1_ 1_67 WMSV_P03359_3 mutA LIB2_E A_26 FFV_O93209-Pro Linker id RT name Linke r id RT name Linker id RT name LIB1_1 SFV3L P27401 2 LIB1_ XMRV6 A1Z651 LIB2_E FOAMV_P14350- _22 mut 1_67 3mutA A_26 Pro_2mutA LIB1_1 WMSV_P03359_3 LIB1_ KORV_Q9TTC1_3 LIB2_E GALV_P21414_3 _22 mutA 1_67 mutA A_26 mutA LIB1_1 KORV_Q9TTC1_3 LIB1_ BAEVM_P10272_ LIB2_E KORV_Q9TTC1- _22 mutA 1_68 3mutA A_26 Pro_3mutA LIB1_1 BAEVM_P10272_ LIB1_ MLVAV_P03356_ LIB2_E MLVAV_P03356_ _23 3mutA 1_68 3mutA A_26 3mutA LIB1_1 FFV_O93209-Pro LIB1_ MLVCB P08361 LIB2_E MLVFF P26809 3 _23 1_68 3mutA A_26 mutA LIB1_1 MLVCB P08361 LIB1_ MLVMS P03355 LIB2_E WMSV P03359 3 _23 3mutA 1_68 3mutA_WS A_26 mutA LIB1_1 KORV_Q9TTC1- LIB1_ WMSV_P03359_3 LIB2_E KORV_Q9TTC1- _23 Pro_3mut 1_68 mutA A_27 Pro_3mutA LIB1_1 BAEVM_P10272_ LIB1_ XMRV6_A1Z651_ LIB2_E MLVBM_Q7SVK7 _24 3mutA 1_68 3mutA A_27 _3mutA_WS LIB1_1 FOAMV P14350 LIB1_ GALV P21414 3 LIB2_E MLVCB P08361 _24 2mut 1_69 mutA A_27 3mutA LIB1_1 GALV_P21414_3 LIB1_ KORV_Q9TTC1- LIB2_E MLVFF_P26809_3 _24 mutA 1_69 Pro_3mutA A_27 mutA LIB1_1 KORV_Q9TTC1- LIB1_ MLVAV_P03356_ LIB2_E PERV_Q4VFZ2_3 _24 Pro_3mutA 1_69 3mutA A_27 mut LIB1_1 MLVBM_Q7SVK7 LIB1_ MLVBM_Q7SVK7 LIB2_E AVIRE P03360 3 _24 _3mutA_WS 1_69 _3mutA_WS A_28 mutA LIB1_1 MLVCB_P08361_ LIB1_ MLVCB_P08361_ LIB2_E KORV_Q9TTC1- _24 3mutA 1_69 3mutA A_28 Pro_3mutA LIB1_1 MLVFF_P26809_3 LIB1_ MLVFF_P26809_3 LIB2_E PERV_Q4VFZ2_3 _24 mutA 1_69 mutA A_28 mut LIB1_1 FOAMV P14350 LIB1_ MLVMS P03355 LIB2_E SFV3L P27401 2 _24 2mutA 1_69 3mutA_WS A_28 mut LIB1_1 PERV_Q4VFZ2_3 LIB1_ XMRV6_A1Z651_ LIB2_E WMSV_P03359_3 _24 mutA_WS 1_69 3mutA A_28 mutA LIB1_1 MLVAV_P03356_ LIB1_ KORV_Q9TTC1- LIB2_E WDSV_O92815_2 _25 3mutA 1_69 Pro_3mut A_28 mut LIB1_1 MLVBM_Q7SVK7 LIB1_ KORV_Q9TTC1_3 LIB2_E MLVBM_Q7SVK7 _25 _3mutA_WS 1_69 mutA A_3 _3mutA_WS LIB1_1 MLVFF_P26809_3 LIB1_ PERV_Q4VFZ2_3 LIB2_E MLVCB_P08361_ _25 mutA 1_69 mutA_WS A_3 3mutA LIB1_1 MLVMS P03355 LIB1_ BAEVM Pl0272 LIB2_E XMRV6 A1Z651 _25 3mutA_WS 1_7 3mutA A_3 3mutA LIB1_1 WMSV P03359 3 LIB1_ MLVAV P03356 LIB2_E BAEVM Pl0272 _25 mutA 1_7 3mutA A_4 3mutA LIB1_1 AVIRE_P03360_3 LIB1_ MLVBM_Q7SVK7 LIB2_E FLV_P10273_3mut _26 mutA 1_7 _3mutA_WS A_4 A Linker id RT name Linke r id RT name Linker id RT name LIB1_1 FFV_O93209 LIB1_ MLVCB_P08361_ LIB2_E KORV_Q9TTC1- _26 1_7 3mutA A_4 Pro_3mutA LIB1_1 MLVAV P03356 LIB1_ MLVFF P26809 3 LIB2_E MLVAV P03356 _26 3mutA 1_7 mutA A_4 3mutA LIB1_1 MLVBM_Q7SVK7 LIB1_ XMRV6_A1Z651_ LIB2_E MLVBM_Q7SVK7 _26 _3mutA_WS 1_7 3mutA A_4 _3mutA_WS LIB1_1 MLVCB_P08361_ LIB1_ KORV_Q9TTC1_3 LIB2_E MLVCB_P08361_ _26 3mutA 1_7 mutA A_4 3mutA LIB1_1 MLVFF P26809 3 LIB1_ WDSV 092815 2 LIB2_E MLVMS P03355 _26 mutA 1_7 mutA A_4 3mutA_WS LIB1_1 PERV_Q4VFZ2_3 LIB1_ FOAMV_P14350_ LIB2_E PERV_Q4VFZ2_3 _26 mut l_70 2mut A_4 mut LIB1_1 WMSV_P03359_3 LIB1_ KORV_Q9TTC1- LIB2_E KORV_Q9TTC1_3 _26 mutA l_70 Pro_3mutA A_4 mutA LIB1_1 PERV_Q4VFZ2_3 LIB1_ MLVCB_P08361_ LIB2_E WMSV_P03359_3 _26 mutA_WS l_70 3mutA A_5 mutA LIB1_1 MLVBM_Q7SVK7 LIB1_ MLVFF_P26809_3 LIB2_E WDSV_O92815_2 _27 _3mutA_WS l_70 mutA A_5 mut LIB1_1 MLVFF P26809 3 LIB1_ WMSV P03359 3 LIB2_E BAEVM Pl0272 _27 mutA l_70 mutA A_6 3mutA LIB1_1 XMRV6 A1Z651 LIB1_ KORV_Q9TTC1- LIB2_E KORV_Q9TTC1_3 _27 3mutA l_70 Pro_3mut A_6 mut LIB1_1 WDSV_O92815 LIB1_ KORV_Q9TTC1_3 LIB2_E MLVAV_P03356_ _27 l_70 mutA A_6 3mutA LIB1_1 GALV P21414 3 LIB1_ BAEVM Pl0272 LIB2_E MLVCB P08361 _28 mutA 1_71 3mutA A_6 3mutA LIB1_1 MLVBM_Q7SVK7 LIB1_ FFV_O93209 LIB2_E MLVFF P26809 3 _28 _3mutA_WS 1_71 A_6 mutA LIB1_1 MLVFF_P26809_3 LIB1_ KORV_Q9TTC1_3 LIB2_E SFV3L_P27401- _28 mutA 1_71 mut A_6 Pro_2mutA LIB1_1 WMSV P03359 3 LIB1_ MLVFF P26809 3 LIB2_E XMRV6 A1Z651 _28 mutA 1_71 mutA A_6 3mutA LIB1_1 KORV_Q9TTC1- LIB1_ PERV_Q4VFZ2_3 LIB2_E KORV_Q9TTC1- _28 Pro_3mut 1_71 mut A_6 Pro_3mut LIB1_1 KORV_Q9TTC1_3 LIB1_ XMRV6_A1Z651_ LIB2_E PERV_Q4VFZ2_3 _28 mutA 1_71 3mutA A_6 mutA_WS LIB1_1 WDSV_O92815_2 LIB1_ PERV_Q4VFZ2_3 LIB2_E WDSV_O92815_2 _28 mut 1_71 mutA_WS A_6 mutA LIB1_1 BAEVM P10272 LIB1_ BAEVM Pl0272 LIB2_E FLV P10273 3mut _29 3mutA 1_72 3mutA A_7 A LIB1_1 MLVAV_P03356_ LIB1_ KORV_Q9TTC1- LIB2_E FOAMV_P14350- _29 3mutA 1_72 Pro_3mutA A_7 Pro_2mutA LIB1_1 MLVBM_Q7SVK7 LIB1_ MLVCB_P08361_ LIB2_E KORV_Q9TTC1- _29 _3mutA_WS 1_72 3mutA A_7 Pro_3mutA Linker id RT name Linke r id RT name Linker id RT name LIB1_1 _29 MLVCB_P08361_ 3mutA LIB1_ 1_72 MLVMS_P03355_ 3mutA_WS LIB2_E A_7 KORV_Q9TTC1_3 mut LIB1_1 _29 MLVFF_P26809_3 mutA LIB1_ 1_72 WMSV_P03359_3 mutA LIB2_E A_7 WMSV_P03359_3 mutA LIB1_1 _29 MLVMS_P03355_ 3mutA_WS LIB1_ 1_72 XMRV6_A1Z651_ 3mutA LIB2_E A_8 BAEVM_P10272_ 3mutA LIB1_1 _29 SFV3L_P27401- Pro_2mutA LIB1_ 1_73 AVIRE_P03360_3 mutA LIB2_E A_8 FOAMV_P14350- Pro_2mutA LIB1_1 _29 XMRV6_A1Z651_ 3mutA LIB1_ 1_73 MLVCB_P08361_ 3mutA LIB2_E A_8 FOAMV_P14350_ 2mut LIB1_1 _29 PERV_Q4VFZ2_3 mutA_WS LIB1_ 1_73 MLVFF_P26809_3 mutA LIB2_E A_8 KORV_Q9TTC1- Pro_3mutA LIB1_1 _3 BAEVM_P10272_ 3mutA LIB1_ 1_73 SFV3L_P27401_2 mut LIB2_E A_8 MLVAV_P03356_ 3mutA LIB1_1 _3 FFV_O93209 LIB1_ 1_73 KORV_Q9TTC1- Pro_3mut LIB2_E A_8 MLVBM_Q7SVK7 _3mutA_WS LIB1_1 _3 FOAMV_P14350- Pro_2mutA LIB1_ 1_73 WDSV_O92815_2 mutA LIB2_E A_8 MLVCB_P08361_ 3mutA LIB1_1 _3 MLVCB_P08361_ 3mutA LIB1_ 1_74 AVIRE_P03360_3 mutA LIB2_E A_8 WMSV_P03359_3 mutA LIB1_1 _3 MLVFF_P26809_3 mutA LIB1_ 1_74 BAEVM_P10272_ 3mutA LIB2_E A_8 KORV_Q9TTC1- Pro_3mut LIB1_1 _3 PERV_Q4VFZ2_3 mut LIB1_ 1_74 GALV_P21414_3 mutA LIB2_E A_8 KORV_Q9TTC1_3 mutA LIB1_1 _3 XMRV6_A1Z651_ 3mutA LIB1_ 1_74 MLVFF_P26809_3 mutA LIB2_E A_8 WDSV_O92815_2 mutA LIB1_1 _3 KORV_Q9TTC1- Pro_3mut LIB1_ 1_74 MLVMS_P03355_ 3mutA_WS LIB2_E A_9 MLVCB_P08361_ 3mutA LIB1_1 _30 AVIRE_P03360_3 mutA LIB1_ 1_74 WMSV_P03359_3 mutA LIB2_E A_9 MLVMS_P03355_ 3mutA_WS LIB1_1 _30 BAEVM_P10272_ 3mutA LIB1_ 1_74 FOAMV_P14350- Pro_2mut LIB2_E A_9 WMSV_P03359_3 mutA LIB1_1 _30 FLV_P10273_3mut A LIB1_ 1_74 KORV_Q9TTC1- Pro_3mut LIB2_E A_9 PERV_Q4VFZ2_3 mutA_WS LIB1_1 _30 KORV_Q9TTC1- Pro_3mutA LIB1_ 1_74 PERV_Q4VFZ2_3 mutA_WS LIB1_1 _30 WMSV_P03359_3 mutA LIB1_1 _30 MLVAV_P03356_ 3mutA LIB1_ 1_74 WDSV_O92815_2 mutA LIB1_1 _30 XMRV6_A1Z651_ 3mutA LIB1_1 _30 MLVBM_Q7SVK7 _3mutA_WS LIB1_ 1_75 BAEVM_P10272_ 3mutA LIB1_1 _30 FOAMV_P14350_ 2mutA LIB1_1 _30 MLVCB_P08361_ 3mutA LIB1_ 1_75 FLV_P10273_3mut A LIB1_1 _75 MLVBM_Q7SVK7 _3mutA_WS LIB1_1 _30 MLVFF_P26809_3 mutA LIB1_ 1_75 GALV_P21414_3 mutA LIB1_1 _75 MLVCB_P08361_ 3mutA Linker id RT name Linke r id RT name Linker id RT name LIB1_1 MLVMS_P03355_ LIB1_ KORV_Q9TTC1- LIB1_1 MLVFF_P26809_3 _30 3mutA_WS 1_75 Pro_3mutA _75 mutA LIB1_1 _30 PERV_Q4VFZ2_3 mut LIB1_ 1_75 MLVAV_P03356_ 3mutA In some embodiments, a gene modifying polypeptide comprises an amino acid sequence as listed in Table 10, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises a linker comprising a linker sequence as listed in Table 10, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises an RT domain comprising an RT domain sequence as listed in Table 10, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 1 of Table 10, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 2 of the same row of Table 10, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises an amino acid sequence as listed in column 3 of Table 10, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 4 of Table 10, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 5 of the same row of Table 10, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises an amino acid sequence as listed in column 6 of Table 10, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises: (i) a linker comprising a linker sequence as listed in a row of column 7 of Table 10, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto; and (ii) an RT domain comprising an RT domain sequence as listed in column 8 of the same row of Table 10, or an amino acid sequence having at least 70%, 5 at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. In some embodiments, a gene modifying polypeptide comprises an amino acid sequence as listed in column 9 of Table 10, or an amino acid sequence having at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or at least 99% identity thereto. Table 10. Linker-RT combination of screened gene modifying polypeptides Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_1 AVIRE_P03360 _3mutA 17001 LIB1_ 1_80 HTLV2_P03363 18582 LIB1_ 1_35 PERV_Q4VFZ 2_3mut 20163 LIB1_ 1_10 AVIRE_P03360 _3mutA 17002 LIB1_ 1_81 HTLV2_P03363 18583 LIB1_ 1_37 PERV_Q4VFZ 2_3mut 20164 LIB1_ 1_100 AVIRE_P03360 _3mutA 17003 LIB1_ 1_82 HTLV2_P03363 18584 LIB1_ 1_38 PERV_Q4VFZ 2_3mut 20165 LIB1_ 1_101 AVIRE_P03360 _3mutA 17004 LIB1_ 1_83 HTLV2_P03363 18585 LIB1_ 1_39 PERV_Q4VFZ 2_3mut 20166 LIB1_ 1_102 AVIRE_P03360 _3mutA 17005 LIB1_ 1_84 HTLV2_P03363 18586 LIB1_ 1_4 PERV_Q4VFZ 2_3mut 20167 LIB1_ 1_103 AVIRE_P03360 _3mutA 17006 LIB1_ 1_85 HTLV2_P03363 18587 LIB1_ 1_40 PERV_Q4VFZ 2_3mut 20168 LIB1_ 1_104 AVIRE.P03360 _3mutA 17007 LIB1_ 1_86 HTLV2.P03363 18588 LIB1_ 1_41 PERV.Q4VFZ 2_3mut 20169 LIB1_ 1_105 AVIRE_P03360 _3mutA 17008 LIB1_ 1_87 HTLV2_P03363 18589 LIB1_ 1_42 PERV_Q4VFZ 2_3mut 20170 LIB1_ 1_106 AVIRE_P03360 _3mutA 17009 LIB1_ 1_88 HTLV2_P03363 18590 LIB1_ 1_43 PERV_Q4VFZ 2_3mut 20171 LIB1_ 1_107 AVIRE_P03360 _3mutA 17010 LIB1_ 1_89 HTLV2_P03363 18591 LIB1_ 1_44 PERV_Q4VFZ 2_3mut 20172 LIB1_ 1_108 AVIRE_P03360 _3mutA 17011 LIB1_ 1_9 HTLV2_P03363 18592 LIB1_ 1_45 PERV_Q4VFZ 2_3mut 20173 LIB1_ 1_109 AVIRE.P03360 _3mutA 17012 LIB1_ 1_90 HTLV2.P03363 18593 LIB1_ 1_46 PERV.Q4VFZ 2_3mut 20174 LIBI-UI AVIRE_P03360 _3mutA 17013 LIB1_ 1_91 HTLV2_P03363 18594 LIB1_ 1_47 PERV_Q4VFZ 2_3mut 20175 LIB1_ 1.110 AVIRE_P03360 _3mutA 17014 LIB1_ 1.92 HTLV2_P03363 18595 LIB1_ 1.48 PERV_Q4VFZ 2_3mut 20176 LIB1_ 1.111 AVIRE_P03360 _3mutA 17015 LIB1_ 1_93 HTLV2_P03363 18596 LIB1_ 1_49 PERV_Q4VFZ 2_3mut 20177 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_112 AVIRE_P03360 _3mutA 17016 LIB1_ 1_94 HTLV2_P03363 18597 LIB1_ 1_50 PERV_Q4VFZ 2_3mut 20178 LIB1_ 1_113 AVIRE_P03360 _3mutA 17017 LIB1_ 1_95 HTLV2_P03363 18598 LIB1_ 1_51 PERV_Q4VFZ 2_3mut 20179 LIB1_ 1_114 AVIRE_P03360 _3mutA 17018 LIB1_ 1_96 HTLV2_P03363 18599 LIB1_ 1_52 PERV_Q4VFZ 2_3mut 20180 LIB1_ 1_115 AVIRE_P03360 _3mutA 17019 LIB1_ 1_97 HTLV2_P03363 18600 LIB1_ 1_53 PERV_Q4VFZ 2_3mut 20181 LIB1_ 1_116 AVIRE_P03360 _3mutA 17020 LIB1_ 1_98 HTLV2_P03363 18601 LIB1_ 1_54 PERV_Q4VFZ 2_3mut 20182 LIB1_ 1_117 AVIRE_P03360 _3mutA 17021 LIB1_ 1_99 HTLV2_P03363 18602 LIB1_ 1_55 PERV.Q4VFZ 2_3mut 20183 LIB1_ 1_118 AVIRE_P03360 _3mutA 17022 LIB2_ EA_1 HTLV2_P03363 18603 LIB1_ 1_56 PERV.Q4VFZ 2_3mut 20184 LIB1_ 1_119 AVIRE_P03360 _3mutA 17023 LIB2_ EA_1 0 HTLV2_P03363 18604 LIB1_ 1_57 PERV.Q4VFZ 2_3mut 20185 LIB1_ 1_12 AVIRE_P03360 _3mutA 17024 LIB2_ EA_1 1 HTLV2_P03363 18605 LIB1_ 1_58 PERV.Q4VFZ 2_3mut 20186 LIB1_ 1_120 AVIRE_P03360 _3mutA 17025 LIB2_ EA_1 2 HTLV2.P03363 18606 LIB1_ 1_59 PERV.Q4VFZ 2_3mut 20187 LIB1_ 1_121 AVIRE_P03360 _3mutA 17026 LIB2_ EA_1 3 HTLV2.P03363 18607 LIB1_ 1_6 PERV.Q4VFZ 2_3mut 20188 LIB1_ 1_122 AVIRE_P03360 _3mutA 17027 LIB2_ EA_1 4 HTLV2_P03363 18608 LIB1_ 1_60 PERV_Q4VFZ 2_3mut 20189 LIB1_ 1_13 AVIRE_P03360 _3mutA 17028 LIB2_ EA_1 5 HTLV2.P03363 18609 LIB1_ 1_61 PERV.Q4VFZ 2_3mut 20190 LIB1_ 1_14 AVIRE_P03360 _3mutA 17029 LIB2_ EA_1 6 HTLV2.P03363 18610 LIB1_ 1_62 PERV.Q4VFZ 2_3mut 20191 LIB1_ 1_15 AVIRE_P03360 _3mutA 17030 LIB2_ EA_1 7 HTLV2.P03363 18611 LIB1_ 1_63 PERV.Q4VFZ 2_3mut 20192 LIB1_ 1_16 AVIRE_P03360 _3mutA 17031 LIB2_ EA_1 8 HTLV2.P03363 18612 LIB1_ 1_64 PERV.Q4VFZ 2_3mut 20193 LIB1_ 1_17 AVIRE_P03360 _3mutA 17032 LIB2_ EA_1 9 HTLV2_P03363 18613 LIB1_ 1_65 PERV.Q4VFZ 2_3mut 20194 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_18 AVIRE_P03360 _3mutA 17033 LIB2_ EA_2 HTLV2_P03363 18614 LIB1_ 1_66 PERV.Q4VFZ 2_3mut 20195 LIB1_ 1_19 AVIRE_P03360 _3mutA 17034 LIB2_ EA_2 0 HTLV2_P03363 18615 LIB1_ 1_67 PERV.Q4VFZ 2_3mut 20196 LIB1_ 1_2 AVIRE_P03360 _3mutA 17035 LIB2_ EA_2 1 HTLV2_P03363 18616 LIB1_ 1_68 PERV.Q4VFZ 2_3mut 20197 LIB1_ 1_20 AVIRE_P03360 _3mutA 17036 LIB2_ EA_2 2 HTLV2_P03363 18617 LIB1_ 1_69 PERV.Q4VFZ 2_3mut 20198 LIB1_ 1_21 AVIRE_P03360 _3mutA 17037 LIB2_ EA_2 3 HTLV2_P03363 18618 LIB1_ 1_7 PERV.Q4VFZ 2_3mut 20199 LIB1_ 1_22 AVIRE_P03360 _3mutA 17038 LIB2_ EA_2 4 HTLV2_P03363 18619 LIB1_ 1_70 PERV.Q4VFZ 2_3mut 20200 LIB1_ 1_23 AVIRE_P03360 _3mutA 17039 LIB2_ EA_2 5 HTLV2_P03363 18620 LIB1_ 1_71 PERV.Q4VFZ 2_3mut 20201 LIB1_ 1_24 AVIRE_P03360 _3mutA 17040 LIB2_ EA_2 6 HTLV2_P03363 18621 LIB1_ 1_72 PERV.Q4VFZ 2_3mut 20202 LIB1_ 1_25 AVIRE_P03360 _3mutA 17041 LIB2_ EA_2 7 HTLV2_P03363 18622 LIB1_ 1_73 PERV.Q4VFZ 2_3mut 20203 LIB1_ 1_26 AVIRE_P03360 _3mutA 17042 LIB2_ EA_2 8 HTLV2_P03363 18623 LIB1_ 1_74 PERV.Q4VFZ 2_3mut 20204 LIB1_ 1_27 AVIRE_P03360 _3mutA 17043 LIB2_ EA_3 HTLV2_P03363 18624 LIB1_ 1_75 PERV.Q4VFZ 2_3mut 20205 LIB1_ 1_28 AVIRE_P03360 _3mutA 17044 LIB2_ EA_4 HTLV2_P03363 18625 LIB1_ 1_76 PERV.Q4VFZ 2_3mut 20206 LIB1_ 1_29 AVIRE_P03360 _3mutA 17045 LIB2_ EA_5 HTLV2_P03363 18626 LIB1_ 1_77 PERV.Q4VFZ 2_3mut 20207 LIB1_ 1_3 AVIRE_P03360 _3mutA 17046 LIB2_ EA_6 HTLV2_P03363 18627 LIB1_ 1_78 PERV.Q4VFZ 2_3mut 20208 LIB1_ 1_30 AVIRE_P03360 _3mutA 17047 LIB2_ EA_7 HTLV2.P03363 18628 LIB1_ 1_79 PERV.Q4VFZ 2_3mut 20209 LIB1_ 1_31 AVIRE_P03360 _3mutA 17048 LIB2_ EA_8 HTLV2_P03363 18629 LIB1_ 1_8 PERV.Q4VFZ 2_3mut 20210 LIB1_ 1_32 AVIRE_P03360 _3mutA 17049 LIB2_ EA_9 HTLV2_P03363 18630 LIB1_ 1_80 PERV.Q4VFZ 2_3mut 20211 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_33 AVIRE_P03360 _3mutA 17050 LIB1_ 1_1 HTLV2_P03363 _2mut 18631 LIB1_ 1_81 PERV.Q4VFZ 2_3mut 20212 LIB1_ 1_34 AVIRE_P03360 _3mutA 17051 LIB1_ 1_10 HTLV2_P03363 _2mut 18632 LIB1_ 1_82 PERV.Q4VFZ 2_3mut 20213 LIB1_ 1_35 AVIRE_P03360 _3mutA 17052 LIB1_ 1_100 HTLV2_P03363 _2mut 18633 LIB1_ 1_83 PERV.Q4VFZ 2_3mut 20214 LIB1_ 1_37 AVIRE_P03360 _3mutA 17053 LIB1_ 1_101 HTLV2_P03363 _2mut 18634 LIB1_ 1_84 PERV.Q4VFZ 2_3mut 20215 LIB1_ 1_38 AVIRE_P03360 _3mutA 17054 LIB1_ 1_102 HTLV2.P03363 _2mut 18635 LIB1_ 1_85 PERV.Q4VFZ 2_3mut 20216 LIB1_ 1_39 AVIRE_P03360 _3mutA 17055 LIB1_ 1_103 HTLV2_P03363 _2mut 18636 LIB1_ 1_86 PERV.Q4VFZ 2_3mut 20217 LIB1_ 1_4 AVIRE_P03360 _3mutA 17056 LIB1_ 1_104 HTLV2_P03363 _2mut 18637 LIB1_ 1_87 PERV.Q4VFZ 2_3mut 20218 LIB1_ 1_40 AVIRE_P03360 _3mutA 17057 LIB1_ 1_105 HTLV2_P03363 _2mut 18638 LIB1_ 1_88 PERV.Q4VFZ 2_3mut 20219 LIB1_ 1_41 AVIRE_P03360 _3mutA 17058 LIB1_ 1_106 HTLV2_P03363 _2mut 18639 LIB1_ 1_89 PERV.Q4VFZ 2_3mut 20220 LIB1_ 1_42 AVIRE_P03360 _3mutA 17059 LIB1_ 1_107 HTLV2.P03363 _2mut 18640 LIB1_ 1_9 PERV.Q4VFZ 2_3mut 20221 LIB1_ 1_43 AVIRE_P03360 _3mutA 17060 LIB1_ 1_108 HTLV2_P03363 _2mut 18641 LIB1_ 1_90 PERV.Q4VFZ 2_3mut 20222 LIB1_ 1_44 AVIRE_P03360 _3mutA 17061 LIB1_ 1_109 HTLV2_P03363 _2mut 18642 LIB1_ 1_91 PERV.Q4VFZ 2_3mut 20223 LIB1_ 1_45 AVIRE_P03360 _3mutA 17062 LIB1_ 1_11 HTLV2_P03363 _2mut 18643 LIB1_ 1_92 PERV.Q4VFZ 2_3mut 20224 LIB1_ 1_46 AVIRE_P03360 _3mutA 17063 LIB1_ 1_110 HTLV2_P03363 _2mut 18644 LIB1_ 1_93 PERV.Q4VFZ 2_3mut 20225 LIB1_ 1_47 AVIRE_P03360 _3mutA 17064 LIB1_ 1_111 HTLV2.P03363 _2mut 18645 LIB1_ 1_94 PERV.Q4VFZ 2_3mut 20226 LIB1_ 1_48 AVIRE_P03360 _3mutA 17065 LIB1_ 1_112 HTLV2_P03363 _2mut 18646 LIB1_ 1_95 PERV.Q4VFZ 2_3mut 20227 LIB1_ 1_49 AVIRE_P03360 _3mutA 17066 LIB1_ 1_113 HTLV2_P03363 _2mut 18647 LIB1_ 1_96 PERV.Q4VFZ 2_3mut 20228 LIB1_ 1_50 AVIRE_P03360 _3mutA 17067 LIB1_ 1_114 HTLV2_P03363 _2mut 18648 LIB1_ 1_97 PERV.Q4VFZ 2_3mut 20229 LIB1_ 1_51 AVIRE_P03360 _3mutA 17068 LIB1_ 1_115 HTLV2.P03363 _2mut 18649 LIB1_ 1_98 PERV.Q4VFZ 2_3mut 20230 LIB1_ 1_52 AVIRE_P03360 _3mutA 17069 LIB1_ 1_116 HTLV2.P03363 _2mut 18650 LIB1_ 1_99 PERV.Q4VFZ 2_3mut 20231 LIB1_ 1_53 AVIRE_P03360 _3mutA 17070 LIB1_ 1_117 HTLV2_P03363 _2mut 18651 LIB2_ EA_1 PERV.Q4VFZ 2_3mut 20232 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_54 AVIRE_P03360 _3mutA 17071 LIB1_ 1_118 HTLV2_P03363 _2mut 18652 LIB2_ EA_1 0 PERV_Q4VFZ 2_3mut 20233 LIB1_ 1_55 AVIRE_P03360 _3mutA 17072 LIB1_ 1_119 HTLV2_P03363 _2mut 18653 LIB2_ EA_1 1 PERV_Q4VFZ 2_3mut 20234 LIB1_ 1_56 AVIRE_P03360 _3mutA 17073 LIB1_ 1_12 HTLV2_P03363 _2mut 18654 LIB2_ EA_1 2 PERV_Q4VFZ 2_3mut 20235 LIB1_ 1_57 AVIRE_P03360 _3mutA 17074 LIB1_ 1_120 HTLV2_P03363 _2mut 18655 LIB2_ EA_1 3 PERV_Q4VFZ 2_3mut 20236 LIB1_ 1_58 AVIRE_P03360 _3mutA 17075 LIB1_ 1_121 HTLV2_P03363 _2mut 18656 LIB2_ EA_1 4 PERV_Q4VFZ 2_3mut 20237 LIB1_ 1_59 AVIRE_P03360 _3mutA 17076 LIB1_ 1_122 HTLV2_P03363 _2mut 18657 LIB2_ EA_1 5 PERV_Q4VFZ 2_3mut 20238 LIB1_ 1_6 AVIRE_P03360 _3mutA 17077 LIB1_ 1_13 HTLV2_P03363 _2mut 18658 LIB2_ EA_1 6 PERV_Q4VFZ 2_3mut 20239 LIB1_ 1_60 AVIRE_P03360 _3mutA 17078 LIB1_ 1_14 HTLV2_P03363 _2mut 18659 LIB2_ EA_1 7 PERV_Q4VFZ 2_3mut 20240 LIB1_ 1_61 AVIRE_P03360 _3mutA 17079 LIB1_ 1_15 HTLV2_P03363 _2mut 18660 LIB2_ EA_1 8 PERV_Q4VFZ 2_3mut 20241 LIB1_ 1_62 AVIRE_P03360 _3mutA 17080 LIB1_ 1_16 HTLV2_P03363 _2mut 18661 LIB2_ EA_1 9 PERV_Q4VFZ 2_3mut 20242 LIB1_ 1_63 AVIRE_P03360 _3mutA 17081 LIB1_ 1_17 HTLV2_P03363 _2mut 18662 LIB2_ EA_2 PERV_Q4VFZ 2_3mut 20243 LIB1_ 1_64 AVIRE_P03360 _3mutA 17082 LIB1_ 1_18 HTLV2_P03363 _2mut 18663 LIB2_ EA_2 0 PERV_Q4VFZ 2_3mut 20244 LIB1_ 1_65 AVIRE_P03360 _3mutA 17083 LIB1_ 1_19 HTLV2_P03363 _2mut 18664 LIB2_ EA_2 1 PERV_Q4VFZ 2_3mut 20245 LIB1_ 1_66 AVIRE_P03360 _3mutA 17084 LIB1_ 1_2 HTLV2_P03363 _2mut 18665 LIB2_ EA_2 2 PERV_Q4VFZ 2_3mut 20246 LIB1_ 1_67 AVIRE_P03360 _3mutA 17085 LIB1_ 1_20 HTLV2_P03363 _2mut 18666 LIB2_ EA_2 3 PERV_Q4VFZ 2_3mut 20247 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_68 AVIRE_P03360 _3mutA 17086 LIB1_ 1_21 HTLV2_P03363 _2mut 18667 LIB2_ EA_2 4 PERV_Q4VFZ 2_3mut 20248 LIB1_ 1_69 AVIRE_P03360 _3mutA 17087 LIB1_ 1_22 HTLV2_P03363 _2mut 18668 LIB2_ EA_2 5 PERV_Q4VFZ 2_3mut 20249 LIB1_ 1_7 AVIRE.P03360 _3mutA 17088 LIB1_ 1_23 HTLV2.P03363 _2mut 18669 LIB2_ EA_2 6 PERV.Q4VFZ 2_3mut 20250 LIB1_ 1_70 AVIRE_P03360 _3mutA 17089 LIB1_ 1_24 HTLV2_P03363 _2mut 18670 LIB2_ EA_2 7 PERV_Q4VFZ 2_3mut 20251 LIB1_ 1_71 AVIRE_P03360 _3mutA 17090 LIB1_ 1_25 HTLV2_P03363 _2mut 18671 LIB2_ EA_2 8 PERV_Q4VFZ 2_3mut 20252 LIB1_ 1_72 AVIRE_P03360 _3mutA 17091 LIB1_ 1_26 HTLV2_P03363 _2mut 18672 LIB2_ EA_3 PERV_Q4VFZ 2_3mut 20253 LIB1_ 1_73 AVIRE_P03360 _3mutA 17092 LIB1_ 1_27 HTLV2_P03363 _2mut 18673 LIB2_ EA_4 PERV_Q4VFZ 2_3mut 20254 LIB1_ 1_74 AVIRE_P03360 _3mutA 17093 LIB1_ 1_28 HTLV2_P03363 _2mut 18674 LIB2_ EA_5 PERV_Q4VFZ 2_3mut 20255 LIB1_ 1_75 AVIRE.P03360 _3mutA 17094 LIB1_ 1_29 HTLV2.P03363 _2mut 18675 LIB2_ EA_6 PERV.Q4VFZ 2_3mut 20256 LIB1_ 1_76 AVIRE_P03360 _3mutA 17095 LIB1_ 1_3 HTLV2_P03363 _2mut 18676 LIB2_ EA_7 PERV_Q4VFZ 2_3mut 20257 LIB1_ 1_77 AVIRE_P03360 _3mutA 17096 LIB1_ 1_30 HTLV2_P03363 _2mut 18677 LIB2_ EA_8 PERV_Q4VFZ 2_3mut 20258 LIB1_ 1_78 AVIRE_P03360 _3mutA 17097 LIB1_ 1_31 HTLV2_P03363 _2mut 18678 LIB2_ EA_9 PERV_Q4VFZ 2_3mut 20259 LIB1_ 1_79 AVIRE_P03360 _3mutA 17098 LIB1_ 1_32 HTLV2_P03363 _2mut 18679 LIB1_ 1_36 PERV_Q4VFZ 2_3mut 20260 LIB1_ 1_8 AVIRE.P03360 _3mutA 17099 LIB1_ 1_33 HTLV2_P03363 _2mut 18680 LIB1_ 1_1 PERV.Q4VFZ 2_3mutA_WS 20261 LIB1_ 1_80 AVIRE_P03360 _3mutA 17100 LIB1_ 1_34 HTLV2_P03363 _2mut 18681 LIB1_ 1_10 PERV_Q4VFZ 2_3mutA_WS 20262 LIB1_ 1_81 AVIRE_P03360 _3mutA 17101 LIB1_ 1_35 HTLV2_P03363 _2mut 18682 LIB1_ 1.100 PERV_Q4VFZ 2_3mutA_WS 20263 LIB1_ 1_82 AVIRE_P03360 _3mutA 17102 LIB1_ 1_37 HTLV2_P03363 _2mut 18683 LIB1_ 1.101 PERV_Q4VFZ 2_3mutA_WS 20264 LIB1_ 1_83 AVIRE_P03360 _3mutA 17103 LIB1_ 1_38 HTLV2_P03363 _2mut 18684 LIB1_ 1_102 PERV_Q4VFZ 2_3mutA_WS 20265 LIB1_ 1_84 AVIRE.P03360 _3mutA 17104 LIB1_ 1_39 HTLV2_P03363 _2mut 18685 LIB1_ 1_103 PERV.Q4VFZ 2_3mutA_WS 20266 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_85 AVIRE_P03360 _3mutA 17105 LIB1_ 1_4 HTLV2_P03363 _2mut 18686 LIB1_ 1_104 PERV.Q4VFZ 2_3mutA_WS 20267 LIB1_ 1_86 AVIRE_P03360 _3mutA 17106 LIB1_ 1_40 HTLV2_P03363 _2mut 18687 LIB1_ 1_105 PERV.Q4VFZ 2_3mutA_WS 20268 LIB1_ 1_87 AVIRE_P03360 _3mutA 17107 LIB1_ 1_41 HTLV2_P03363 _2mut 18688 LIB1_ 1_106 PERV.Q4VFZ 2_3mutA_WS 20269 LIB1_ 1_88 AVIRE_P03360 _3mutA 17108 LIB1_ 1_42 HTLV2_P03363 _2mut 18689 LIB1_ 1_107 PERV.Q4VFZ 2_3mutA_WS 20270 LIB1_ 1_89 AVIRE_P03360 _3mutA 17109 LIB1_ 1_43 HTLV2_P03363 _2mut 18690 LIB1_ 1_108 PERV.Q4VFZ 2_3mutA_WS 20271 LIB1_ 1_9 AVIRE_P03360 _3mutA 17110 LIB1_ 1_44 HTLV2_P03363 _2mut 18691 LIB1_ 1_109 PERV.Q4VFZ 2_3mutA_WS 20272 LIB1_ 1_90 AVIRE_P03360 _3mutA 17111 LIB1_ 1_45 HTLV2_P03363 _2mut 18692 LIB1_ 1_11 PERV.Q4VFZ 2_3mutA_WS 20273 LIB1_ 1_91 AVIRE_P03360 _3mutA 17112 LIB1_ 1_46 HTLV2_P03363 _2mut 18693 LIB1_ 1_110 PERV.Q4VFZ 2_3mutA_WS 20274 LIB1_ 1_92 AVIRE_P03360 _3mutA 17113 LIB1_ 1_47 HTLV2_P03363 _2mut 18694 LIB1_ 1_111 PERV.Q4VFZ 2_3mutA_WS 20275 LIB1_ 1_93 AVIRE_P03360 _3mutA 17114 LIB1_ 1_48 HTLV2_P03363 _2mut 18695 LIB1_ 1_112 PERV.Q4VFZ 2_3mutA_WS 20276 LIB1_ 1_94 AVIRE_P03360 _3mutA 17115 LIB1_ 1_49 HTLV2_P03363 _2mut 18696 LIB1_ 1_113 PERV.Q4VFZ 2_3mutA_WS 20277 LIB1_ 1_95 AVIRE_P03360 _3mutA 17116 LIB1_ 1_50 HTLV2_P03363 _2mut 18697 LIB1_ 1_114 PERV.Q4VFZ 2_3mutA_WS 20278 LIB1_ 1_96 AVIRE_P03360 _3mutA 17117 LIB1_ 1_51 HTLV2_P03363 _2mut 18698 LIB1_ 1_115 PERV.Q4VFZ 2_3mutA_WS 20279 LIB1_ 1_97 AVIRE_P03360 _3mutA 17118 LIB1_ 1_52 HTLV2_P03363 _2mut 18699 LIB1_ 1_116 PERV.Q4VFZ 2_3mutA_WS 20280 LIB1_ 1_98 AVIRE_P03360 _3mutA 17119 LIB1_ 1_53 HTLV2_P03363 _2mut 18700 LIB1_ 1_117 PERV.Q4VFZ 2_3mutA_WS 20281 LIB1_ 1_99 AVIRE_P03360 _3mutA 17120 LIB1_ 1_54 HTLV2_P03363 _2mut 18701 LIB1_ 1_118 PERV.Q4VFZ 2_3mutA_WS 20282 LIB2_ EA_1 AVIRE_P03360 _3mutA 17121 LIB1_ 1_55 HTLV2_P03363 _2mut 18702 LIB1_ 1_119 PERV.Q4VFZ 2_3mutA_WS 20283 LIB2_ EA_1 0 AVIRE_P03360 _3mutA 17122 LIB1_ 1_56 HTLV2_P03363 _2mut 18703 LIB1_ 1_12 PERV.Q4VFZ 2_3mutA_WS 20284 LIB2_ EA_1 1 AVIRE_P03360 _3mutA 17123 LIB1_ 1_57 HTLV2_P03363 _2mut 18704 LIB1_ 1_120 PERV.Q4VFZ 2_3mutA_WS 20285 LIB2_ EA_1 2 AVIRE_P03360 _3mutA 17124 LIB1_ 1_58 HTLV2_P03363 _2mut 18705 LIB1_ 1_121 PERV.Q4VFZ 2_3mutA_WS 20286 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB2_ EA_1 3 AVIRE_P03360 _3mutA 17125 LIB1_ 1_59 HTLV2_P03363 _2mut 18706 LIB1_ 1_122 PERV_Q4VFZ 2_3mutA_WS 20287 LIB2_ EA_1 4 AVIRE_P03360 _3mutA 17126 LIB1_ 1_6 HTLV2_P03363 _2mut 18707 LIB1_ 1_13 PERV_Q4VFZ 2_3mutA_WS 20288 LIB2_ EA_1 5 AVIRE_P03360 _3mutA 17127 LIB1_ 1_60 HTLV2_P03363 _2mut 18708 LIB1_ 1_14 PERV_Q4VFZ 2_3mutA_WS 20289 LIB2_ EA_1 6 AVIRE_P03360 _3mutA 17128 LIB1_ 1_61 HTLV2_P03363 _2mut 18709 LIB1_ 1_15 PERV_Q4VFZ 2_3mutA_WS 20290 LIB2_ EA_1 7 AVIRE_P03360 _3mutA 17129 LIB1_ 1_62 HTLV2_P03363 _2mut 18710 LIB1_ 1_16 PERV_Q4VFZ 2_3mutA_WS 20291 LIB2_ EA_1 8 AVIRE_P03360 _3mutA 17130 LIB1_ 1_63 HTLV2_P03363 _2mut 18711 LIB1_ 1_17 PERV_Q4VFZ 2_3mutA_WS 20292 LIB2_ EA_1 9 AVIRE_P03360 _3mutA 17131 LIB1_ 1_64 HTLV2_P03363 _2mut 18712 LIB1_ 1_18 PERV_Q4VFZ 2_3mutA_WS 20293 LIB2_ EA_2 AVIRE_P03360 _3mutA 17132 LIB1_ 1_65 HTLV2_P03363 _2mut 18713 LIB1_ 1_19 PERV_Q4VFZ 2_3mutA_WS 20294 LIB2_ EA_2 0 AVIRE_P03360 _3mutA 17133 LIB1_ 1_66 HTLV2_P03363 _2mut 18714 LIB1_ 1_2 PERV_Q4VFZ 2_3mutA_WS 20295 LIB2_ EA_2 1 AVIRE_P03360 _3mutA 17134 LIB1_ 1_67 HTLV2_P03363 _2mut 18715 LIB1_ 1_20 PERV_Q4VFZ 2_3mutA_WS 20296 LIB2_ EA_2 2 AVIRE_P03360 _3mutA 17135 LIB1_ 1_68 HTLV2_P03363 _2mut 18716 LIB1_ 1_21 PERV_Q4VFZ 2_3mutA_WS 20297 LIB2_ EA_2 3 AVIRE_P03360 _3mutA 17136 LIB1_ 1_69 HTLV2_P03363 _2mut 18717 LIB1_ 1_22 PERV_Q4VFZ 2_3mutA_WS 20298 LIB2_ EA_2 4 AVIRE_P03360 _3mutA 17137 LIB1_ 1_7 HTLV2_P03363 _2mut 18718 LIB1_ 1_23 PERV_Q4VFZ 2_3mutA_WS 20299 LIB2_ EA_2 5 AVIRE_P03360 _3mutA 17138 LIB1_ 1_70 HTLV2_P03363 _2mut 18719 LIB1_ 1_24 PERV_Q4VFZ 2_3mutA_WS 20300 LIB2_ EA_2 6 AVIRE_P03360 _3mutA 17139 LIB1_ 1_71 HTLV2_P03363 _2mut 18720 LIB1_ 1_25 PERV_Q4VFZ 2_3mutA_WS 20301 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB2_ EA_2 7 AVIRE_P03360 _3mutA 17140 LIB1_ 1_72 HTLV2_P03363 _2mut 18721 LIB1_ 1_26 PERV_Q4VFZ 2_3mutA_WS 20302 LIB2_ EA_2 8 AVIRE_P03360 _3mutA 17141 LIB1_ 1_73 HTLV2_P03363 _2mut 18722 LIB1_ 1_27 PERV_Q4VFZ 2_3mutA_WS 20303 LIB2_ EA_3 AVIRE_P03360 _3mutA 17142 LIB1_ 1_74 HTLV2_P03363 _2mut 18723 LIB1_ 1_28 PERV_Q4VFZ 2_3mutA_WS 20304 LIB2_ EA_4 AVIRE_P03360 _3mutA 17143 LIB1_ 1_75 HTLV2_P03363 _2mut 18724 LIB1_ 1_29 PERV_Q4VFZ 2_3mutA_WS 20305 LIB2_ EA_5 AVIRE_P03360 _3mutA 17144 LIB1_ 1_76 HTLV2_P03363 _2mut 18725 LIB1_ 1_3 PERV_Q4VFZ 2_3mutA_WS 20306 LIB2_ EA_6 AVIRE_P03360 _3mutA 17145 LIB1_ 1_77 HTLV2_P03363 _2mut 18726 LIB1_ 1_30 PERV_Q4VFZ 2_3mutA_WS 20307 LIB2_ EA_7 AVIRE_P03360 _3mutA 17146 LIB1_ 1_78 HTLV2_P03363 _2mut 18727 LIB1_ 1_31 PERV_Q4VFZ 2_3mutA_WS 20308 LIB2_ EA_8 AVIRE_P03360 _3mutA 17147 LIB1_ 1_79 HTLV2_P03363 _2mut 18728 LIB1_ 1_32 PERV_Q4VFZ 2_3mutA_WS 20309 LIB2_ EA_9 AVIRE_P03360 _3mutA 17148 LIB1_ 1_8 HTLV2_P03363 _2mut 18729 LIB1_ 1_33 PERV_Q4VFZ 2_3mutA_WS 20310 LIB1_ 1_36 AVIRE_P03360 _3mutA 17149 LIB1_ 1_80 HTLV2_P03363 _2mut 18730 LIB1_ 1_34 PERV_Q4VFZ 2_3mutA_WS 20311 LIB1_ 1_1 BAEVM_P1027 2_3mutA 17150 LIB1_ 1_81 HTLV2_P03363 _2mut 18731 LIB1_ 1_35 PERV_Q4VFZ 2_3mutA_WS 20312 LIB1_ 1_10 BAEVM_P1027 2_3mutA 17151 LIB1_ 1_82 HTLV2_P03363 _2mut 18732 LIB1_ 1_37 PERV_Q4VFZ 2_3mutA_WS 20313 LIB1_ 1_100 BAEVM_P1027 2_3mutA 17152 LIB1_ 1_83 HTLV2_P03363 _2mut 18733 LIB1_ 1_38 PERV_Q4VFZ 2_3mutA_WS 20314 LIB1_ 1_101 BAEVM_P1027 2_3mutA 17153 LIB1_ 1_84 HTLV2_P03363 _2mut 18734 LIB1_ 1_39 PERV_Q4VFZ 2_3mutA_WS 20315 LIB1_ 1_102 BAEVM_P1027 2_3mutA 17154 LIB1_ 1_85 HTLV2_P03363 _2mut 18735 LIB1_ 1_4 PERV_Q4VFZ 2_3mutA_WS 20316 LIB1_ 1_103 BAEVM_P1027 2_3mutA 17155 LIB1_ 1_86 HTLV2_P03363 _2mut 18736 LIB1_ 1_40 PERV_Q4VFZ 2_3mutA_WS 20317 LIB1_ 1_104 BAEVM_P1027 2_3mutA 17156 LIB1_ 1_87 HTLV2_P03363 _2mut 18737 LIB1_ 1_41 PERV_Q4VFZ 2_3mutA_WS 20318 LIB1_ 1_105 BAEVM_P1027 2_3mutA 17157 LIB1_ 1_88 HTLV2_P03363 _2mut 18738 LIB1_ 1_42 PERV_Q4VFZ 2_3mutA_WS 20319 LIB1_ 1_106 BAEVM_P1027 2_3mutA 17158 LIB1_ 1_89 HTLV2_P03363 _2mut 18739 LIB1_ 1_43 PERV_Q4VFZ 2_3mutA_WS 20320 LIB1_ 1_107 BAEVM_P1027 2_3mutA 17159 LIB1_ 1_9 HTLV2_P03363 _2mut 18740 LIB1_ 1_44 PERV_Q4VFZ 2_3mutA_WS 20321 LIB1_ 1_108 BAEVM_P1027 2_3mutA 17160 LIB1_ 1_90 HTLV2_P03363 _2mut 18741 LIB1_ 1_45 PERV_Q4VFZ 2_3mutA_WS 20322 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_109 BAEVM_P1027 2_3mutA 17161 LIB1_ 1_91 HTLV2_P03363 _2mut 18742 LIB1_ 1_46 PERV.Q4VFZ 2_3mutA_WS 20323 LIB1_ 1_11 BAEVM_P1027 2_3mutA 17162 LIB1_ 1_92 HTLV2_P03363 _2mut 18743 LIB1_ 1_47 PERV.Q4VFZ 2_3mutA_WS 20324 LIB1_ 1_110 BAEVM_P1027 2_3mutA 17163 LIB1_ 1_93 HTLV2_P03363 _2mut 18744 LIB1_ 1_48 PERV.Q4VFZ 2_3mutA_WS 20325 LIB1_ 1_111 BAEVM_P1027 2_3mutA 17164 LIB1_ 1_94 HTLV2_P03363 _2mut 18745 LIB1_ 1_49 PERV.Q4VFZ 2_3mutA_WS 20326 LIB1_ 1_112 BAEVM_P1027 2_3mutA 17165 LIB1_ 1_95 HTLV2_P03363 _2mut 18746 LIB1_ 1_50 PERV.Q4VFZ 2_3mutA_WS 20327 LIB1_ 1_113 BAEVM_P1027 2_3mutA 17166 LIB1_ 1_96 HTLV2_P03363 _2mut 18747 LIB1_ 1_51 PERV.Q4VFZ 2_3mutA_WS 20328 LIB1_ 1_114 BAEVM_P1027 2_3mutA 17167 LIB1_ 1_97 HTLV2_P03363 _2mut 18748 LIB1_ 1_52 PERV.Q4VFZ 2_3mutA_WS 20329 LIB1_ 1_115 BAEVM_P1027 2_3mutA 17168 LIB1_ 1_98 HTLV2_P03363 _2mut 18749 LIB1_ 1_53 PERV.Q4VFZ 2_3mutA_WS 20330 LIB1_ 1_116 BAEVM_P1027 2_3mutA 17169 LIB1_ 1_99 HTLV2_P03363 _2mut 18750 LIB1_ 1_54 PERV.Q4VFZ 2_3mutA_WS 20331 LIB1_ 1_117 BAEVM_P1027 2_3mutA 17170 LIB2_ EA_1 HTLV2_P03363 _2mut 18751 LIB1_ 1_55 PERV.Q4VFZ 2_3mutA_WS 20332 LIB1_ 1_118 BAEVM_P1027 2_3mutA 17171 LIB2_ EA_1 0 HTLV2_P03363 _2mut 18752 LIB1_ 1_56 PERV.Q4VFZ 2_3mutA_WS 20333 LIB1_ 1_119 BAEVM_P1027 2_3mutA 17172 LIB2_ EA_1 1 HTLV2_P03363 _2mut 18753 LIB1_ 1_57 PERV.Q4VFZ 2_3mutA_WS 20334 LIB1_ 1_12 BAEVM_P1027 2_3mutA 17173 LIB2_ EA_1 2 HTLV2_P03363 _2mut 18754 LIB1_ 1_58 PERV.Q4VFZ 2_3mutA_WS 20335 LIB1_ 1_120 BAEVM_P1027 2_3mutA 17174 LIB2_ EA_1 3 HTLV2.P03363 _2mut 18755 LIB1_ 1_59 PERV.Q4VFZ 2_3mutA_WS 20336 LIB1_ 1_121 BAEVM_P1027 2_3mutA 17175 LIB2_ EA_1 4 HTLV2.P03363 _2mut 18756 LIB1_ 1_6 PERV.Q4VFZ 2_3mutA_WS 20337 LIB1_ 1_122 BAEVM_P1027 2_3mutA 17176 LIB2_ EA_1 5 HTLV2.P03363 _2mut 18757 LIB1_ 1_60 PERV.Q4VFZ 2_3mutA_WS 20338 LIB1_ 1_13 BAEVM_P1027 2_3mutA 17177 LIB2_ EA_1 6 HTLV2.P03363 _2mut 18758 LIB1_ 1_61 PERV.Q4VFZ 2_3mutA_WS 20339 LIB1_ 1_14 BAEVM_P1027 2_3mutA 17178 LIB2_ EA_1 7 HTLV2_P03363 _2mut 18759 LIB1_ 1_62 PERV_Q4VFZ 2_3mutA_WS 20340 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_15 BAEVM_P1027 2_3mutA 17179 LIB2_ EA_1 8 HTLV2_P03363 _2mut 18760 LIB1_ 1_63 PERV.Q4VFZ 2_3mutA_WS 20341 LIB1_ 1_16 BAEVM_P1027 2_3mutA 17180 LIB2_ EA_1 9 HTLV2_P03363 _2mut 18761 LIB1_ 1_64 PERV.Q4VFZ 2_3mutA_WS 20342 LIB1_ 1_17 BAEVM_P1027 2_3mutA 17181 LIB2_ EA_2 HTLV2_P03363 _2mut 18762 LIB1_ 1_65 PERV_Q4VFZ 2_3mutA_WS 20343 LIB1_ 1_18 BAEVM_P1027 2_3mutA 17182 LIB2_ EA_2 0 HTLV2_P03363 _2mut 18763 LIB1_ 1_66 PERV.Q4VFZ 2_3mutA_WS 20344 LIB1_ 1_19 BAEVM_P1027 2_3mutA 17183 LIB2_ EA_2 1 HTLV2_P03363 _2mut 18764 LIB1_ 1_67 PERV.Q4VFZ 2_3mutA_WS 20345 LIB1_ 1_2 BAEVM_P1027 2_3mutA 17184 LIB2_ EA_2 2 HTLV2_P03363 _2mut 18765 LIB1_ 1_68 PERV.Q4VFZ 2_3mutA_WS 20346 LIB1_ 1_20 BAEVM_P1027 2_3mutA 17185 LIB2_ EA_2 3 HTLV2_P03363 _2mut 18766 LIB1_ 1_69 PERV.Q4VFZ 2_3mutA_WS 20347 LIB1_ 1_21 BAEVM_P1027 2_3mutA 17186 LIB2_ EA_2 4 HTLV2_P03363 _2mut 18767 LIB1_ 1_7 PERV.Q4VFZ 2_3mutA_WS 20348 LIB1_ 1_22 BAEVM_P1027 2_3mutA 17187 LIB2_ EA_2 5 HTLV2_P03363 _2mut 18768 LIB1_ 1_70 PERV.Q4VFZ 2_3mutA_WS 20349 LIB1_ 1_23 BAEVM_P1027 2_3mutA 17188 LIB2_ EA_2 6 HTLV2_P03363 _2mut 18769 LIB1_ 1_71 PERV.Q4VFZ 2_3mutA_WS 20350 LIB1_ 1_24 BAEVM_P1027 2_3mutA 17189 LIB2_ EA_2 7 HTLV2_P03363 _2mut 18770 LIB1_ 1_72 PERV.Q4VFZ 2_3mutA_WS 20351 LIB1_ 1_25 BAEVM_P1027 2_3mutA 17190 LIB2_ EA_2 8 HTLV2_P03363 _2mut 18771 LIB1_ 1_73 PERV.Q4VFZ 2_3mutA_WS 20352 LIB1_ 1_26 BAEVM_P1027 2_3mutA 17191 LIB2_ EA_3 HTLV2_P03363 _2mut 18772 LIB1_ 1_74 PERV.Q4VFZ 2_3mutA_WS 20353 LIB1_ 1_27 BAEVM_P1027 2_3mutA 17192 LIB2_ EA_4 HTLV2_P03363 _2mut 18773 LIB1_ 1_75 PERV.Q4VFZ 2_3mutA_WS 20354 LIB1_ 1_28 BAEVM_P1027 2_3mutA 17193 LIB2_ EA_5 HTLV2_P03363 _2mut 18774 LIB1_ 1_76 PERV.Q4VFZ 2_3mutA_WS 20355 LIB1_ 1_29 BAEVM_P1027 2_3mutA 17194 LIB2_ EA_6 HTLV2.P03363 _2mut 18775 LIB1_ 1_77 PERV.Q4VFZ 2_3mutA_WS 20356 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_3 BAEVM_P1027 2_3mutA 17195 LIB2_ EA.7 HTLV2_P03363 _2mut 18776 LIB1_ 1.78 PERV.Q4VFZ 2_3mutA_WS 20357 LIB1_ 1_30 BAEVM_P1027 2_3mutA 17196 LIB2_ EA_8 HTLV2_P03363 _2mut 18777 LIB1_ 1_79 PERV.Q4VFZ 2_3mutA_WS 20358 LIB1_ 1_31 BAEVM_P1027 2_3mutA 17197 LIB2_ EA_9 HTLV2_P03363 _2mut 18778 LIB1_ 1_8 PERV.Q4VFZ 2_3mutA_WS 20359 LIB1_ 1_32 BAEVM_P1027 2_3mutA 17198 LIB1_ 1_1 KORV_Q9TTC1 _3mut 18779 LIB1_ 1_80 PERV.Q4VFZ 2_3mutA_WS 20360 LIB1_ 1_33 BAEVM_P1027 2_3mutA 17199 LIB1_ 1_10 KORV_Q9TTC1 _3mut 18780 LIB1_ 1_81 PERV.Q4VFZ 2_3mutA_WS 20361 LIB1_ 1_34 BAEVM_P1027 2_3mutA 17200 LIB1_ 1.100 KORV_Q9TTC1 _3mut 18781 LIB1_ 1.82 PERV.Q4VFZ 2_3mutA_WS 20362 LIB1_ 1_35 BAEVM_P1027 2_3mutA 17201 LIB1_ 1.101 KORV_Q9TTC1 _3mut 18782 LIB1_ 1_83 PERV.Q4VFZ 2_3mutA_WS 20363 LIB1_ 1_37 BAEVM_P1027 2_3mutA 17202 LIB1_ 1_102 KORV_Q9TTC1 _3mut 18783 LIB1_ 1_84 PERV.Q4VFZ 2_3mutA_WS 20364 LIB1_ 1_38 BAEVM_P1027 2_3mutA 17203 LIB1_ 1_103 KORV_Q9TTC1 _3mut 18784 LIB1_ 1_85 PERV.Q4VFZ 2_3mutA_WS 20365 LIB1_ 1_39 BAEVM_P1027 2_3mutA 17204 LIB1_ 1_104 KORV_Q9TTC1 _3mut 18785 LIB1_ 1_86 PERV.Q4VFZ 2_3mutA_WS 20366 LIB1_ 1_4 BAEVM_P1027 2_3mutA 17205 LIB1_ 1_105 KORV_Q9TTC1 _3mut 18786 LIB1_ 1_87 PERV.Q4VFZ 2_3mutA_WS 20367 LIB1_ 1_40 BAEVM_P1027 2_3mutA 17206 LIB1_ 1_106 KORV_Q9TTC1 _3mut 18787 LIB1_ 1_88 PERV.Q4VFZ 2_3mutA_WS 20368 LIB1_ 1_41 BAEVM_P1027 2_3mutA 17207 LIB1_ 1_107 KORV_Q9TTC1 _3mut 18788 LIB1_ 1_89 PERV.Q4VFZ 2_3mutA_WS 20369 LIB1_ 1_42 BAEVM_P1027 2_3mutA 17208 LIB1_ 1_108 KORV_Q9TTC1 _3mut 18789 LIB1_ 1_9 PERV.Q4VFZ 2_3mutA_WS 20370 LIB1_ 1_43 BAEVM_P1027 2_3mutA 17209 LIB1_ 1_109 KORV_Q9TTC1 _3mut 18790 LIB1_ 1_90 PERV.Q4VFZ 2_3mutA_WS 20371 LIB1_ 1_44 BAEVM_P1027 2_3mutA 17210 LIB1_ 1_11 KORV_Q9TTC1 _3mut 18791 LIB1_ 1_91 PERV.Q4VFZ 2_3mutA_WS 20372 LIB1_ 1_45 BAEVM_P1027 2_3mutA 17211 LIB1_ 1_110 KORV_Q9TTC1 _3mut 18792 LIB1_ 1_92 PERV.Q4VFZ 2_3mutA_WS 20373 LIB1_ 1_46 BAEVM_P1027 2_3mutA 17212 LIB1_ 1_111 KORV_Q9TTC1 _3mut 18793 LIB1_ 1_93 PERV.Q4VFZ 2_3mutA_WS 20374 LIB1_ 1_47 BAEVM_P1027 2_3mutA 17213 LIB1_ 1_112 KORV_Q9TTC1 _3mut 18794 LIB1_ 1_94 PERV.Q4VFZ 2_3mutA_WS 20375 LIB1_ 1_48 BAEVM_P1027 2_3mutA 17214 LIB1_ 1_113 KORV_Q9TTC1 _3mut 18795 LIB1_ 1_95 PERV.Q4VFZ 2_3mutA_WS 20376 LIB1_ 1_49 BAEVM_P1027 2_3mutA 17215 LIB1_ 1_114 KORV_Q9TTC1 _3mut 18796 LIB1_ 1_96 PERV.Q4VFZ 2_3mutA_WS 20377 LIB1_ 1_50 BAEVM_P1027 2_3mutA 17216 LIB1_ 1_115 KORV_Q9TTC1 _3mut 18797 LIB1_ 1_97 PERV.Q4VFZ 2_3mutA_WS 20378 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_51 BAEVM_P1027 2_3mutA 17217 LIB1_ 1_116 K0RV_Q9TTC1 _3mut 18798 LIB1_ 1_98 PERV.Q4VFZ 2_3mutA_WS 20379 LIB1_ 1_52 BAEVM_P1027 2_3mutA 17218 LIB1_ 1_117 K0RV_Q9TTC1 _3mut 18799 LIB1_ 1_99 PERV.Q4VFZ 2_3mutA_WS 20380 LIB1_ 1_53 BAEVM_P1027 2_3mutA 17219 LIB1_ 1_118 K0RV_Q9TTC1 _3mut 18800 LIB2_ EA_1 PERV.Q4VFZ 2_3mutA_WS 20381 LIB1_ 1_54 BAEVM_P1027 2_3mutA 17220 LIB1_ 1_119 K0RV_Q9TTC1 _3mut 18801 LIB2_ EA_1 0 PERV.Q4VFZ 2_3mutA_WS 20382 LIB1_ 1_55 BAEVM_P1027 2_3mutA 17221 LIB1_ 1_12 K0RV_Q9TTC1 _3mut 18802 LIB2_ EA_1 1 PERV.Q4VFZ 2_3mutA_WS 20383 LIB1_ 1_56 BAEVM_P1027 2_3mutA 17222 LIB1_ 1_120 K0RV_Q9TTC1 _3mut 18803 LIB2_ EA_1 2 PERV.Q4VFZ 2_3mutA_WS 20384 LIB1_ 1_57 BAEVM_P1027 2_3mutA 17223 LIB1_ 1_121 K0RV_Q9TTC1 _3mut 18804 LIB2_ EA_1 3 PERV.Q4VFZ 2_3mutA_WS 20385 LIB1_ 1_58 BAEVM_P1027 2_3mutA 17224 LIB1_ 1_122 K0RV_Q9TTC1 _3mut 18805 LIB2_ EA_1 4 PERV.Q4VFZ 2_3mutA_WS 20386 LIB1_ 1_59 BAEVM_P1027 2_3mutA 17225 LIB1_ 1_13 K0RV_Q9TTC1 _3mut 18806 LIB2_ EA_1 5 PERV_Q4VFZ 2_3mutA_WS 20387 LIB1_ 1_6 BAEVM_P1027 2_3mutA 17226 LIB1_ 1_14 K0RV_Q9TTC1 _3mut 18807 LIB2_ EA_1 6 PERV.Q4VFZ 2_3mutA_WS 20388 LIB1_ 1_60 BAEVM_P1027 2_3mutA 17227 LIB1_ 1_15 K0RV_Q9TTC1 _3mut 18808 LIB2_ EA_1 7 PERV.Q4VFZ 2_3mutA_WS 20389 LIB1_ 1_61 BAEVM_P1027 2_3mutA 17228 LIB1_ 1_16 K0RV_Q9TTC1 _3mut 18809 LIB2_ EA_1 8 PERV.Q4VFZ 2_3mutA_WS 20390 LIB1_ 1_62 BAEVM_P1027 2_3mutA 17229 LIB1_ 1_17 K0RV_Q9TTC1 _3mut 18810 LIB2_ EA_1 9 PERV.Q4VFZ 2_3mutA_WS 20391 LIB1_ 1_63 BAEVM_P1027 2_3mutA 17230 LIB1_ 1_18 K0RV_Q9TTC1 _3mut 18811 LIB2_ EA_2 PERV.Q4VFZ 2_3mutA_WS 20392 LIB1_ 1_64 BAEVM_P1027 2_3mutA 17231 LIB1_ 1_19 K0RV_Q9TTC1 _3mut 18812 LIB2_ EA_2 0 PERV.Q4VFZ 2_3mutA_WS 20393 LIB1_ 1_65 BAEVM_P1027 2_3mutA 17232 LIB1_ 1_2 K0RV_Q9TTC1 _3mut 18813 LIB2_ EA_2 1 PERV.Q4VFZ 2_3mutA_WS 20394 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_66 BAEVM_P1027 2_3mutA 17233 LIB1_ 1_20 K0RV_Q9TTC1 _3mut 18814 LIB2_ EA_2 2 PERV.Q4VFZ 2_3mutA_WS 20395 LIB1_ 1_67 BAEVM_P1027 2_3mutA 17234 LIB1_ 1_21 K0RV_Q9TTC1 _3mut 18815 LIB2_ EA_2 3 PERV.Q4VFZ 2_3mutA_WS 20396 LIB1_ 1_68 BAEVM_P1027 2_3mutA 17235 LIB1_ 1_22 K0RV_Q9TTC1 _3mut 18816 LIB2_ EA_2 4 PERV_Q4VFZ 2_3mutA_WS 20397 LIB1_ 1_69 BAEVM_P1027 2_3mutA 17236 LIB1_ 1_23 K0RV_Q9TTC1 _3mut 18817 LIB2_ EA_2 5 PERV.Q4VFZ 2_3mutA_WS 20398 LIB1_ 1_7 BAEVM_P1027 2_3mutA 17237 LIB1_ 1_24 K0RV_Q9TTC1 _3mut 18818 LIB2_ EA_2 6 PERV.Q4VFZ 2_3mutA_WS 20399 LIB1_ 1_70 BAEVM_P1027 2_3mutA 17238 LIB1_ 1_25 K0RV_Q9TTC1 _3mut 18819 LIB2_ EA_2 7 PERV.Q4VFZ 2_3mutA_WS 20400 LIB1_ 1_71 BAEVM_P1027 2_3mutA 17239 LIB1_ 1_26 K0RV_Q9TTC1 _3mut 18820 LIB2_ EA_2 8 PERV.Q4VFZ 2_3mutA_WS 20401 LIB1_ 1_72 BAEVM_P1027 2_3mutA 17240 LIB1_ 1_27 K0RV_Q9TTC1 _3mut 18821 LIB2_ EA_3 PERV.Q4VFZ 2_3mutA_WS 20402 LIB1_ 1_73 BAEVM_P1027 2_3mutA 17241 LIB1_ 1_28 K0RV_Q9TTC1 _3mut 18822 LIB2_ EA_4 PERV.Q4VFZ 2_3mutA_WS 20403 LIB1_ 1_74 BAEVM_P1027 2_3mutA 17242 LIB1_ 1_29 K0RV_Q9TTC1 _3mut 18823 LIB2_ EA_5 PERV.Q4VFZ 2_3mutA_WS 20404 LIB1_ 1_75 BAEVM_P1027 2_3mutA 17243 LIB1_ 1_3 K0RV_Q9TTC1 _3mut 18824 LIB2_ EA_6 PERV.Q4VFZ 2_3mutA_WS 20405 LIB1_ 1_76 BAEVM_P1027 2_3mutA 17244 LIB1_ 1_30 K0RV_Q9TTC1 _3mut 18825 LIB2_ EA_7 PERV.Q4VFZ 2_3mutA_WS 20406 LIB1_ 1_77 BAEVM_P1027 2_3mutA 17245 LIB1_ 1_31 K0RV_Q9TTC1 _3mut 18826 LIB2_ EA_8 PERV.Q4VFZ 2_3mutA_WS 20407 LIB1_ 1_78 BAEVM_P1027 2_3mutA 17246 LIB1_ 1_32 K0RV_Q9TTC1 _3mut 18827 LIB2_ EA_9 PERV.Q4VFZ 2_3mutA_WS 20408 LIB1_ 1_79 BAEVM_P1027 2_3mutA 17247 LIB1_ 1_33 K0RV_Q9TTC1 _3mut 18828 LIB1_ 1_36 PERV.Q4VFZ 2_3mutA_WS 20409 LIB1_ 1_8 BAEVM_P1027 2_3mutA 17248 LIB1_ 1_34 K0RV_Q9TTC1 _3mut 18829 LIB1_ 1_1 SFV1_P23074 20410 LIB1_ 1_80 BAEVM_P1027 2_3mutA 17249 LIB1_ 1_35 K0RV_Q9TTC1 _3mut 18830 LIB1_ 1_10 SFV1_P23074 20411 LIB1_ 1_81 BAEVM_P1027 2_3mutA 17250 LIB1_ 1_37 K0RV_Q9TTC1 _3mut 18831 LIB1_ 1_100 SFV1P23074 20412 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_82 BAEVM_P1027 2_3mutA 17251 LIB1_ 1_38 K0RV_Q9TTC1 _3mut 18832 LIB1_ 1.101 SFV1.P23074 20413 LIB1_ 1_83 BAEVM_P1027 2_3mutA 17252 LIB1_ 1_39 K0RV_Q9TTC1 _3mut 18833 LIB1_ 1.102 SFV1.P23074 20414 LIB1_ 1_84 BAEVM_P1027 2_3mutA 17253 LIB1_ 1_4 K0RV_Q9TTC1 _3mut 18834 LIB1_ 1_103 SFV1.P23074 20415 LIB1_ 1_85 BAEVM_P1027 2_3mutA 17254 LIB1_ 1_40 K0RV_Q9TTC1 _3mut 18835 LIB1_ 1_104 SFV1.P23074 20416 LIB1_ 1_86 BAEVM_P1027 2_3mutA 17255 LIB1_ 1_41 K0RV_Q9TTC1 _3mut 18836 LIB1_ 1_105 SFV1-P23074 20417 LIB1_ 1_87 BAEVM_P1027 2_3mutA 17256 LIB1_ 1_42 K0RV_Q9TTC1 _3mut 18837 LIB1_ 1.106 SFV1_P23074 20418 LIB1_ 1_88 BAEVM_P1027 2_3mutA 17257 LIB1_ 1_43 K0RV_Q9TTC1 _3mut 18838 LIB1_ 1_107 SFV1_P23074 20419 LIB1_ 1_89 BAEVM_P1027 2_3mutA 17258 LIB1_ 1_44 K0RV_Q9TTC1 _3mut 18839 LIB1_ 1_108 SFV1.P23074 20420 LIB1_ 1_9 BAEVM_P1027 2_3mutA 17259 LIB1_ 1_45 K0RV_Q9TTC1 _3mut 18840 LIB1_ 1_109 SFV1.P23074 20421 LIB1_ 1_90 BAEVM_P1027 2_3mutA 17260 LIB1_ 1_46 K0RV_Q9TTC1 _3mut 18841 LIB1_ 1_11 SFV1.P23074 20422 LIB1_ 1_91 BAEVM_P1027 2_3mutA 17261 LIB1_ 1_47 K0RV_Q9TTC1 _3mut 18842 LIB1_ 1_110 SFV1-P23074 20423 LIB1_ 1_92 BAEVM_P1027 2_3mutA 17262 LIB1_ 1_48 K0RV_Q9TTC1 _3mut 18843 LIB1_ 1_111 SFV1_P23074 20424 LIB1_ 1_93 BAEVM_P1027 2_3mutA 17263 LIB1_ 1_49 K0RV_Q9TTC1 _3mut 18844 LIB1_ 1_112 SFV1.P23074 20425 LIB1_ 1_94 BAEVM_P1027 2_3mutA 17264 LIB1_ 1_50 K0RV_Q9TTC1 _3mut 18845 LIB1_ 1_113 SFV1_P23074 20426 LIB1_ 1_95 BAEVM_P1027 2_3mutA 17265 LIB1_ 1_51 K0RV_Q9TTC1 _3mut 18846 LIB1_ 1_114 SFV1.P23074 20427 LIB1_ 1_96 BAEVM_P1027 2_3mutA 17266 LIB1_ 1_52 K0RV_Q9TTC1 _3mut 18847 LIB1_ 1_115 SFV1-P23074 20428 LIB1_ 1_97 BAEVM_P1027 2_3mutA 17267 LIB1_ 1_53 K0RV_Q9TTC1 _3mut 18848 LIB1_ 1_116 SFV1_P23074 20429 LIB1_ 1_98 BAEVM_P1027 2_3mutA 17268 LIB1_ 1_54 K0RV_Q9TTC1 _3mut 18849 LIB1_ 1_117 SFV1.P23074 20430 LIB1_ 1_99 BAEVM_P1027 2_3mutA 17269 LIB1_ 1_55 K0RV_Q9TTC1 _3mut 18850 LIB1_ 1_118 SFV1_P23074 20431 LIB2_ EA_1 BAEVM_P1027 2_3mutA 17270 LIB1_ 1_56 K0RV_Q9TTC1 _3mut 18851 LIB1_ 1_119 SFV1.P23074 20432 LIB2_ EA_1 0 BAEVM_P1027 2_3mutA 17271 LIB1_ 1_57 K0RV_Q9TTC1 _3mut 18852 LIB1_ 1_12 SFV1_P23074 20433 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB2_ EA_1 1 BAEVM_P1027 2_3mutA 17272 LIB1_ 1_58 K0RV_Q9TTC1 _3mut 18853 LIB1_ 1_120 SFV1_P23074 20434 LIB2_ EA_1 2 BAEVM_P1027 2_3mutA 17273 LIB1_ 1_59 K0RV_Q9TTC1 _3mut 18854 LIB1_ 1_121 SFV1_P23074 20435 LIB2_ EA_1 3 BAEVM_P1027 2_3mutA 17274 LIB1_ 1_6 K0RV_Q9TTC1 _3mut 18855 LIB1_ 1_122 SFV1P23074 20436 LIB2_ EA_1 4 BAEVM_P1027 2_3mutA 17275 LIB1_ 1_60 K0RV_Q9TTC1 _3mut 18856 LIB1_ 1_13 SFV1_P23074 20437 LIB2_ EA_1 5 BAEVM_P1027 2_3mutA 17276 LIB1_ 1_61 K0RV_Q9TTC1 _3mut 18857 LIB1_ 1_14 SFV1_P23074 20438 LIB2_ EA_1 6 BAEVM_P1027 2_3mutA 17277 LIB1_ 1_62 K0RV_Q9TTC1 _3mut 18858 LIB1_ 1_15 SFV1_P23074 20439 LIB2_ EA_1 7 BAEVM_P1027 2_3mutA 17278 LIB1_ 1_63 K0RV_Q9TTC1 _3mut 18859 LIB1_ 1_16 SFV1_P23074 20440 LIB2_ EA_1 8 BAEVM_P1027 2_3mutA 17279 LIB1_ 1_64 K0RV_Q9TTC1 _3mut 18860 LIB1_ 1_17 SFV1_P23074 20441 LIB2_ EA_1 9 BAEVM_P1027 2_3mutA 17280 LIB1_ 1_65 K0RV_Q9TTC1 _3mut 18861 LIB1_ 1_18 SFV1_P23074 20442 LIB2_ EA_2 BAEVM_P1027 2_3mutA 17281 LIB1_ 1_66 K0RV_Q9TTC1 _3mut 18862 LIB1_ 1_19 SFV1_P23074 20443 LIB2_ EA_2 0 BAEVM_P1027 2_3mutA 17282 LIB1_ 1_67 K0RV_Q9TTC1 _3mut 18863 LIB1_ 1_2 SFV1_P23074 20444 LIB2_ EA_2 1 BAEVM_P1027 2_3mutA 17283 LIB1_ 1_68 K0RV_Q9TTC1 _3mut 18864 LIB1_ 1_20 SFV1_P23074 20445 LIB2_ EA_2 2 BAEVM_P1027 2_3mutA 17284 LIB1_ 1_69 K0RV_Q9TTC1 _3mut 18865 LIB1_ 1_21 SFV1_P23074 20446 LIB2_ EA_2 3 BAEVM_P1027 2_3mutA 17285 LIB1_ 1_7 K0RV_Q9TTC1 _3mut 18866 LIB1_ 1_22 SFV1P23074 20447 LIB2_ EA_2 4 BAEVM_P1027 2_3mutA 17286 LIB1_ 1_70 K0RV_Q9TTC1 _3mut 18867 LIB1_ 1_23 SFV1_P23074 20448 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB2_ EA_2 5 BAEVM_P1027 2_3mutA 17287 LIB1_ 1_71 KORV_Q9TTC1 _3mut 18868 LIB1_ 1_24 SFV1_P23074 20449 LIB2_ EA_2 6 BAEVM_P1027 2_3mutA 17288 LIB1_ 1_72 KORV_Q9TTC1 _3mut 18869 LIB1_ 1_25 SFV1_P23074 20450 LIB2_ EA_2 7 BAEVM_P1027 2_3mutA 17289 LIB1_ 1_73 KORV_Q9TTC1 _3mut 18870 LIB1_ 1_26 SFV1P23074 20451 LIB2_ EA_2 8 BAEVM_P1027 2_3mutA 17290 LIB1_ 1_74 KORV_Q9TTC1 _3mut 18871 LIB1_ 1_27 SFV1_P23074 20452 LIB2_ EA_3 BAEVM_P1027 2_3mutA 17291 LIB1_ 1_75 KORV_Q9TTC1 _3mut 18872 LIB1_ 1_28 SFV1_P23074 20453 LIB2_ EA_4 BAEVM_P1027 2_3mutA 17292 LIB1_ 1_76 KORV_Q9TTC1 _3mut 18873 LIB1_ 1_29 SFV1_P23074 20454 LIB2_ EA_5 BAEVM_P1027 2_3mutA 17293 LIB1_ 1_77 KORV_Q9TTC1 _3mut 18874 LIB1_ 1_3 SFV1P23074 20455 LIB2_ EA_6 BAEVM_P1027 2_3mutA 17294 LIB1_ 1_78 KORV_Q9TTC1 _3mut 18875 LIB1_ 1_30 SFV1_P23074 20456 LIB2_ EA_7 BAEVM_P1027 2_3mutA 17295 LIB1_ 1_79 KORV_Q9TTC1 _3mut 18876 LIB1_ 1_31 SFV1_P23074 20457 LIB2_ EA_8 BAEVM_P1027 2_3mutA 17296 LIB1_ 1_8 KORV_Q9TTC1 _3mut 18877 LIB1_ 1_32 SFV1_P23074 20458 LIB2_ EA_9 BAEVM_P1027 2_3mutA 17297 LIB1_ 1_80 KORV_Q9TTC1 _3mut 18878 LIB1_ 1_33 SFV1_P23074 20459 LIB1_ 1_36 BAEVM_P1027 2_3mutA 17298 LIB1_ 1_81 KORV_Q9TTC1 _3mut 18879 LIB1_ 1_34 SFV1P23074 20460 LIB1_ 1_1 FFV_O93209 17299 LIB1_ 1_82 KORV_Q9TTC1 _3mut 18880 LIB1_ 1_35 SFV1_P23074 20461 LIB1_ 1_10 FFVJ393209 17300 LIB1_ 1_83 KORV_Q9TTC1 _3mut 18881 LIB1_ 1_37 SFV1_P23074 20462 LIB1_ 1_100 FFVJ393209 17301 LIB1_ 1_84 KORV_Q9TTC1 _3mut 18882 LIB1_ 1_38 SFV1_P23074 20463 LIB1_ 1_101 FFVJ393209 17302 LIB1_ 1_85 KORV_Q9TTC1 _3mut 18883 LIB1_ 1_39 SFV1_P23074 20464 LIB1_ 1_102 FFV_O93209 17303 LIB1_ 1_86 KORV_Q9TTC1 _3mut 18884 LIB1_ 1_4 SFV1_P23074 20465 LIB1_ 1_103 FFV_O93209 17304 LIB1_ 1_87 KORV_Q9TTC1 _3mut 18885 LIB1_ 1_40 SFV1_P23074 20466 LIB1_ 1_104 FFVJ393209 17305 LIB1_ 1_88 KORV_Q9TTC1 _3mut 18886 LIB1_ 1_41 SFV1_P23074 20467 LIB1_ 1_105 FFVJ393209 17306 LIB1_ 1_89 KORV_Q9TTC1 _3mut 18887 LIB1_ 1_42 SFV1_P23074 20468 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_106 FFV-O93209 17307 LIB1_ 1_9 KORV_Q9TTC1 _3mut 18888 LIB1_ 1_43 SFV1_P23074 20469 LIB1_ 1_107 FFV_O93209 17308 LIB1_ 1_90 KORV_Q9TTC1 _3mut 18889 LIB1_ 1_44 SFV1_P23074 20470 LIB1_ 1_108 FFV.O93209 17309 LIB1_ 1_91 KORV_Q9TTC1 _3mut 18890 LIB1_ 1_45 SFV1.P23074 20471 LIB1_ 1_109 FFV.O93209 17310 LIB1_ 1_92 KORV_Q9TTC1 _3mut 18891 LIB1_ 1_46 SFV1.P23074 20472 LIB1_ 1_11 FFV.O93209 17311 LIB1_ 1_93 KORV_Q9TTC1 _3mut 18892 LIB1_ 1_47 SFV1-P23074 20473 LIB1_ 1_110 FFV_O93209 17312 LIB1_ 1_94 KORV_Q9TTC1 _3mut 18893 LIB1_ 1_48 SFV1_P23074 20474 LIB1_ 1_111 FFV_O93209 17313 LIB1_ 1_95 KORV_Q9TTC1 _3mut 18894 LIB1_ 1_49 SFV1_P23074 20475 LIB1_ 1_112 FFV.O93209 17314 LIB1_ 1_96 KORV_Q9TTC1 _3mut 18895 LIB1_ 1_50 SFV1.P23074 20476 LIB1_ 1_113 FFV.O93209 17315 LIB1_ 1_97 KORV_Q9TTC1 _3mut 18896 LIB1_ 1_51 SFV1.P23074 20477 LIB1_ 1_114 FFV.O93209 17316 LIB1_ 1_98 KORV_Q9TTC1 _3mut 18897 LIB1_ 1_52 SFV1.P23074 20478 LIB1_ 1_115 FFV_O93209 17317 LIB1_ 1_99 KORV_Q9TTC1 _3mut 18898 LIB1_ 1_53 SFV1_P23074 20479 LIB1_ 1_116 FFV_O93209 17318 LIB2_ EA_1 KORV_Q9TTC1 _3mut 18899 LIB1_ 1_54 SFV1_P23074 20480 LIB1_ 1_117 FFV.O93209 17319 LIB2_ EA_1 0 KORV_Q9TTC1 _3mut 18900 LIB1_ 1_55 SFV1.P23074 20481 LIB1_ 1_118 FFV_O93209 17320 LIB2_ EA_1 1 KORV_Q9TTC1 _3mut 18901 LIB1_ 1_56 SFV1_P23074 20482 LIB1_ 1_119 FFV_O93209 17321 LIB2_ EA_1 2 KORV_Q9TTC1 _3mut 18902 LIB1_ 1_57 SFV1_P23074 20483 LIB1_ 1_12 FFV.O93209 17322 LIB2_ EA_1 3 KORV_Q9TTC1 _3mut 18903 LIB1_ 1_58 SFV1.P23074 20484 LIB1_ 1_120 FFV.O93209 17323 LIB2_ EA_1 4 KORV_Q9TTC1 _3mut 18904 LIB1_ 1_59 SFV1.P23074 20485 LIB1_ 1_121 FFV.O93209 17324 LIB2_ EA_1 5 KORV_Q9TTC1 _3mut 18905 LIB1_ 1_6 SFV1_P23074 20486 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_122 FFVJ393209 17325 LIB2_ EA_1 6 K0RV_Q9TTC1 _3mut 18906 LIB1_ 1_60 SFV1_P23074 20487 LIB1_ 1_13 FFV_O93209 17326 LIB2_ EA_1 7 K0RV_Q9TTC1 _3mut 18907 LIB1_ 1_61 SFV1_P23074 20488 LIB1_ 1_14 FFV_O93209 17327 LIB2_ EA_1 8 K0RV_Q9TTC1 _3mut 18908 LIB1_ 1_62 SFV1P23074 20489 LIB1_ 1_15 FFV_O93209 17328 LIB2_ EA_1 9 K0RV_Q9TTC1 _3mut 18909 LIB1_ 1_63 SFV1_P23074 20490 LIB1_ 1_16 FFVJ393209 17329 LIB2_ EA_2 K0RV_Q9TTC1 _3mut 18910 LIB1_ 1_64 SFV1_P23074 20491 LIB1_ 1_17 FFV_O93209 17330 LIB2_ EA_2 0 K0RV_Q9TTC1 _3mut 18911 LIB1_ 1_65 SFV1_P23074 20492 LIB1_ 1_18 FFVJ393209 17331 LIB2_ EA_2 1 K0RV_Q9TTC1 _3mut 18912 LIB1_ 1_66 SFV1_P23074 20493 LIB1_ 1_19 FFV_O93209 17332 LIB2_ EA_2 2 K0RV_Q9TTC1 _3mut 18913 LIB1_ 1_67 SFV1_P23074 20494 LIB1_ 1_2 FFV_O93209 17333 LIB2_ EA_2 3 K0RV_Q9TTC1 _3mut 18914 LIB1_ 1_68 SFV1_P23074 20495 LIB1_ 1_20 FFV_O93209 17334 LIB2_ EA_2 4 K0RV_Q9TTC1 _3mut 18915 LIB1_ 1_69 SFV1_P23074 20496 LIB1_ 1_21 FFVJ393209 17335 LIB2_ EA_2 5 K0RV_Q9TTC1 _3mut 18916 LIB1_ 1_7 SFV1_P23074 20497 LIB1_ 1_22 FFVJ393209 17336 LIB2_ EA_2 6 K0RV_Q9TTC1 _3mut 18917 LIB1_ 1_70 SFV1_P23074 20498 LIB1_ 1_23 FFV_O93209 17337 LIB2_ EA_2 7 K0RV_Q9TTC1 _3mut 18918 LIB1_ 1_71 SFV1_P23074 20499 LIB1_ 1_24 FFVJ393209 17338 LIB2_ EA_2 8 K0RV_Q9TTC1 _3mut 18919 LIB1_ 1_72 SFV1P23074 20500 LIB1_ 1_25 FFV_O93209 17339 LIB2_ EA_3 K0RV_Q9TTC1 _3mut 18920 LIB1_ 1_73 SFV1_P23074 20501 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_26 FFV_O93209 17340 LIB2_ EA_4 KORV_Q9TTC1 _3mut 18921 LIB1_ 1_74 SFV1_P23074 20502 LIB1_ 1_27 FFV_O93209 17341 LIB2_ EA_5 KORV_Q9TTC1 _3mut 18922 LIB1_ 1_75 SFV1_P23074 20503 LIB1_ 1_28 FFV_O93209 17342 LIB2_ EA_6 KORV_Q9TTC1 _3mut 18923 LIB1_ 1_76 SFV1_P23074 20504 LIB1_ 1_29 FFV_O93209 17343 LIB2_ EA_7 KORV_Q9TTC1 _3mut 18924 LIB1_ 1_77 SFV1_P23074 20505 LIB1_ 1_3 FFV_O93209 17344 LIB2_ EA_8 KORV_Q9TTC1 _3mut 18925 LIB1_ 1_78 SFV1_P23074 20506 LIB1_ 1_30 FFV_O93209 17345 LIB2_ EA_9 KORV_Q9TTC1 _3mut 18926 LIB1_ 1_79 SFV1_P23074 20507 LIB1_ 1_31 FFV_O93209 17346 LIB1_ 1_1 KORV_Q9TTC1 _3mutA 18927 LIB1_ 1_8 SFV1_P23074 20508 LIB1_ 1_32 FFV_O93209 17347 LIB1_ 1_10 KORV_Q9TTC1 _3mutA 18928 LIB1_ 1_80 SFV1_P23074 20509 LIB1_ 1_33 FFV_O93209 17348 LIB1_ 1_100 KORV_Q9TTC1 _3mutA 18929 LIB1_ 1_81 SFV1_P23074 20510 LIB1_ 1_34 FFV_O93209 17349 LIB1_ 1_101 KORV_Q9TTC1 _3mutA 18930 LIB1_ 1_82 SFV1_P23074 20511 LIB1_ 1_35 FFV_O93209 17350 LIB1_ 1_102 KORV_Q9TTC1 _3mutA 18931 LIB1_ 1_83 SFV1_P23074 20512 LIB1_ 1_37 FFV_O93209 17351 LIB1_ 1_103 KORV_Q9TTC1 _3mutA 18932 LIB1_ 1_84 SFV1_P23074 20513 LIB1_ 1_38 FFV_O93209 17352 LIB1_ 1_104 KORV_Q9TTC1 _3mutA 18933 LIB1_ 1_85 SFV1_P23074 20514 LIB1_ 1_39 FFV_O93209 17353 LIB1_ 1_105 KORV_Q9TTC1 _3mutA 18934 LIB1_ 1_86 SFV1_P23074 20515 LIB1_ 1_4 FFV_O93209 17354 LIB1_ 1_106 KORV_Q9TTC1 _3mutA 18935 LIB1_ 1_87 SFV1_P23074 20516 LIB1_ 1_40 FFV_O93209 17355 LIB1_ 1_107 KORV_Q9TTC1 _3mutA 18936 LIB1_ 1_88 SFV1_P23074 20517 LIB1_ 1_41 FFV_O93209 17356 LIB1_ 1_108 KORV_Q9TTC1 _3mutA 18937 LIB1_ 1_89 SFV1_P23074 20518 LIB1_ 1_42 FFV_O93209 17357 LIB1_ 1_109 KORV_Q9TTC1 _3mutA 18938 LIB1_ 1_9 SFV1_P23074 20519 LIB1_ 1_43 FFV_O93209 17358 LIB1_ 1_11 K0RV_Q9TTC1 _3mutA 18939 LIB1_ 1_90 SFV1_P23074 20520 LIB1_ 1_44 FFV_O93209 17359 LIB1_ 1_110 KORV_Q9TTC1 _3mutA 18940 LIB1_ 1_91 SFV1_P23074 20521 LIB1_ 1_45 FFV_O93209 17360 LIB1_ 1_111 KORV_Q9TTC1 _3mutA 18941 LIB1_ 1_92 SFV1_P23074 20522 LIB1_ 1_46 FFV_O93209 17361 LIB1_ 1_112 KORV_Q9TTC1 _3mutA 18942 LIB1_ 1_93 SFV1_P23074 20523 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_47 FFV_O93209 17362 LIB1_ 1_113 K0RV_Q9TTC1 _3mutA 18943 LIB1_ 1_94 SFV1_P23074 20524 LIB1_ 1_48 FFV_O93209 17363 LIB1_ 1_114 K0RV_Q9TTC1 _3mutA 18944 LIB1_ 1_95 SFV1_P23074 20525 LIB1_ 1_49 FFV_O93209 17364 LIB1_ 1_115 K0RV_Q9TTC1 _3mutA 18945 LIB1_ 1_96 SFV1_P23074 20526 LIB1_ 1_50 FFV_O93209 17365 LIB1_ 1_116 K0RV_Q9TTC1 _3mutA 18946 LIB1_ 1_97 SFV1_P23074 20527 LIB1_ 1_51 FFV_O93209 17366 LIB1_ 1_117 K0RV_Q9TTC1 _3mutA 18947 LIB1_ 1_98 SFV1_P23074 20528 LIB1_ 1_52 FFV_O93209 17367 LIB1_ 1_118 K0RV_Q9TTC1 _3mutA 18948 LIB1_ 1_99 SFV1_P23074 20529 LIB1_ 1_53 FFV_O93209 17368 LIB1_ 1_119 K0RV_Q9TTC1 _3mutA 18949 LIB2_ EA_1 SFV1_P23074 20530 LIB1_ 1_54 FFV_O93209 17369 LIB1_ 1_12 K0RV_Q9TTC1 _3mutA 18950 LIB2_ EA_1 0 SFV1_P23074 20531 LIB1_ 1_55 FFV_O93209 17370 LIB1_ 1_120 K0RV_Q9TTC1 _3mutA 18951 LIB2_ EA_1 1 SFV1_P23074 20532 LIB1_ 1_56 FFV_O93209 17371 LIB1_ 1_121 K0RV_Q9TTC1 _3mutA 18952 LIB2_ EA_1 2 SFV1_P23074 20533 LIB1_ 1_57 FFV_O93209 17372 LIB1_ 1_122 K0RV_Q9TTC1 _3mutA 18953 LIB2_ EA_1 3 SFV1_P23074 20534 LIB1_ 1_58 FFV_O93209 17373 LIB1_ 1_13 K0RV_Q9TTC1 _3mutA 18954 LIB2_ EA_1 4 SFV1_P23074 20535 LIB1_ 1_59 FFV_O93209 17374 LIB1_ 1_14 K0RV_Q9TTC1 _3mutA 18955 LIB2_ EA_1 5 SFV1_P23074 20536 LIB1_ 1_6 FFV_O93209 17375 LIB1_ 1_15 K0RV_Q9TTC1 _3mutA 18956 LIB2_ EA_1 6 SFV1_P23074 20537 LIB1_ 1_60 FFV_O93209 17376 LIB1_ 1_16 K0RV_Q9TTC1 _3mutA 18957 LIB2_ EA_1 7 SFV1_P23074 20538 LIB1_ 1_61 FFV_O93209 17377 LIB1_ 1_17 K0RV_Q9TTC1 _3mutA 18958 LIB2_ EA_1 8 SFV1_P23074 20539 LIB1_ 1_62 FFV_O93209 17378 LIB1_ 1_18 K0RV_Q9TTC1 _3mutA 18959 LIB2_ EA_1 9 SFV1_P23074 20540 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_63 FFVJ393209 17379 LIB1_ 1_19 K0RV_Q9TTC1 _3mutA 18960 LIB2_ EA_2 SFV1_P23074 20541 LIB1_ 1_64 FFVJ393209 17380 LIB1_ 1_2 K0RV_Q9TTC1 _3mutA 18961 LIB2_ EA_2 0 SFV1_P23074 20542 LIB1_ 1_65 FFV_O93209 17381 LIB1_ 1_20 K0RV_Q9TTC1 _3mutA 18962 LIB2_ EA_2 1 SFV1_P23074 20543 LIB1_ 1_66 FFV_O93209 17382 LIB1_ 1_21 K0RV_Q9TTC1 _3mutA 18963 LIB2_ EA_2 2 SFV1_P23074 20544 LIB1_ 1_67 FFV_O93209 17383 LIB1_ 1_22 K0RV_Q9TTC1 _3mutA 18964 LIB2_ EA_2 3 SFV1_P23074 20545 LIB1_ 1_68 FFVJ393209 17384 LIB1_ 1_23 K0RV_Q9TTC1 _3mutA 18965 LIB2_ EA_2 4 SFV1_P23074 20546 LIB1_ 1_69 FFVJ393209 17385 LIB1_ 1_24 K0RV_Q9TTC1 _3mutA 18966 LIB2_ EA_2 5 SFV1_P23074 20547 LIB1_ 1_7 FFV_O93209 17386 LIB1_ 1_25 K0RV_Q9TTC1 _3mutA 18967 LIB2_ EA_2 6 SFV1_P23074 20548 LIB1_ 1_70 FFV_O93209 17387 LIB1_ 1_26 K0RV_Q9TTC1 _3mutA 18968 LIB2_ EA_2 7 SFV1_P23074 20549 LIB1_ 1_71 FFVJ393209 17388 LIB1_ 1_27 K0RV_Q9TTC1 _3mutA 18969 LIB2_ EA_2 8 SFV1_P23074 20550 LIB1_ 1_72 FFVJ393209 17389 LIB1_ 1_28 K0RV_Q9TTC1 _3mutA 18970 LIB2_ EA_3 SFV1_P23074 20551 LIB1_ 1_73 FFVJ393209 17390 LIB1_ 1_29 K0RV_Q9TTC1 _3mutA 18971 LIB2_ EA_4 SFV1_P23074 20552 LIB1_ 1_74 FFV_O93209 17391 LIB1_ 1_3 K0RV_Q9TTC1 _3mutA 18972 LIB2_ EA_5 SFV1_P23074 20553 LIB1_ 1_75 FFV_O93209 17392 LIB1_ 1_30 K0RV_Q9TTC1 _3mutA 18973 LIB2_ EA_6 SFV1_P23074 20554 LIB1_ 1_76 FFVJ393209 17393 LIB1_ 1_31 K0RV_Q9TTC1 _3mutA 18974 LIB2_ EA_7 SFV1_P23074 20555 LIB1_ 1_77 FFVJ393209 17394 LIB1_ 1_32 K0RV_Q9TTC1 _3mutA 18975 LIB2_ EA_8 SFV1_P23074 20556 LIB1_ 1_78 FFVJ393209 17395 LIB1_ 1_33 K0RV_Q9TTC1 _3mutA 18976 LIB2_ EA_9 SFV1_P23074 20557 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_79 FFV_O93209 17396 LIB1_ 1_34 KORV_Q9TTC1 _3mutA 18977 LIB1_ 1_1 SFV1 -Pro _P23074 20558 LIB1_ 1_8 FFV_O93209 17397 LIB1_ 1_35 KORV_Q9TTC1 _3mutA 18978 LIB1_ 1_10 SFV1 -Pro _P23074 20559 LIB1_ 1_80 FFV_O93209 17398 LIB1_ 1_37 KORV_Q9TTC1 _3mutA 18979 LIB1_ 1_100 SFV1 -Pro _P23074 20560 LIB1_ 1_81 FFV_O93209 17399 LIB1_ 1_38 KORV_Q9TTC1 _3mutA 18980 LIB1_ 1_101 SFV1 -Pro _P23074 20561 LIB1_ 1_82 FFVJ393209 17400 LIB1_ 1_39 KORV_Q9TTC1 _3mutA 18981 LIB1_ 1_102 SFV1 -Pro _P23074 20562 LIB1_ 1_83 FFV_O93209 17401 LIB1_ 1_4 KORV_Q9TTC1 _3mutA 18982 LIB1_ 1_103 SFV1 -Pro _P23074 20563 LIB1_ 1_84 FFV_O93209 17402 LIB1_ 1_40 KORV_Q9TTC1 _3mutA 18983 LIB1_ 1_104 SFV1 -Pro _P23074 20564 LIB1_ 1_85 FFV_O93209 17403 LIB1_ 1_41 KORV_Q9TTC1 _3mutA 18984 LIB1_ 1_105 SFV1 -Pro _P23074 20565 LIB1_ 1_86 FFV_O93209 17404 LIB1_ 1_42 KORV_Q9TTC1 _3mutA 18985 LIB1_ 1_106 SFV1 -Pro _P23074 20566 LIB1_ 1_87 FFV_O93209 17405 LIB1_ 1_43 KORV_Q9TTC1 _3mutA 18986 LIB1_ 1_107 SFV1 -Pro _P23074 20567 LIB1_ 1_88 FFV_O93209 17406 LIB1_ 1_44 KORV_Q9TTC1 _3mutA 18987 LIB1_ 1_108 SFV1 -Pro _P23074 20568 LIB1_ 1_89 FFV_O93209 17407 LIB1_ 1_45 KORV_Q9TTC1 _3mutA 18988 LIB1_ 1_109 SFV1 -Pro _P23074 20569 LIB1_ 1_9 FFV_O93209 17408 LIB1_ 1_46 KORV_Q9TTC1 _3mutA 18989 LIB1_ 1_11 SFV1 -Pro _P23074 20570 LIB1_ 1_90 FFV_O93209 17409 LIB1_ 1_47 KORV_Q9TTC1 _3mutA 18990 LIB1_ 1_110 SFV1 -Pro _P23074 20571 LIB1_ 1_91 FFV_O93209 17410 LIB1_ 1_48 KORV_Q9TTC1 _3mutA 18991 LIB1_ 1_111 SFV1 -Pro _P23074 20572 LIB1_ 1_92 FFV_O93209 17411 LIB1_ 1_49 KORV_Q9TTC1 _3mutA 18992 LIB1_ 1_112 SFV1 -Pro _P23074 20573 LIB1_ 1_93 FFV_O93209 17412 LIB1_ 1_50 KORV_Q9TTC1 _3mutA 18993 LIB1_ 1_113 SFV1 -Pro _P23074 20574 LIB1_ 1_94 FFV_O93209 17413 LIB1_ 1_51 KORV_Q9TTC1 _3mutA 18994 LIB1_ 1_114 SFV1 -Pro _P23074 20575 LIB1_ 1_95 FFV_O93209 17414 LIB1_ 1_52 KORV_Q9TTC1 _3mutA 18995 LIB1_ 1_115 SFV1 -Pro _P23074 20576 LIB1_ 1_96 FFV_O93209 17415 LIB1_ 1_53 KORV_Q9TTC1 _3mutA 18996 LIB1_ 1_116 SFV1 -Pro _P23074 20577 LIB1_ 1_97 FFV_O93209 17416 LIB1_ 1_54 KORV_Q9TTC1 _3mutA 18997 LIB1_ 1_117 SFV1 -Pro _P23074 20578 LIB1_ 1_98 FFV_O93209 17417 LIB1_ 1_55 KORV_Q9TTC1 _3mutA 18998 LIB1_ 1_118 SFV1 -Pro _P23074 20579 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_99 FFV_O93209 17418 LIB1_ 1_56 K0RV_Q9TTC1 _3mutA 18999 LIB1_ 1_119 SFV1_P23074 -Pro 20580 LIB2_ EA_1 FFV_O93209 17419 LIB1_ 1_57 K0RV_Q9TTC1 _3mutA 19000 LIB1_ 1_12 SFV1_P23074 -Pro 20581 LIB2_ EA_1 0 FFV_O93209 17420 LIB1_ 1_58 K0RV_Q9TTC1 _3mutA 19001 LIB1_ 1_120 SFV1_P23074 -Pro 20582 LIB2_ EA_1 1 FFV_O93209 17421 LIB1_ 1_59 K0RV_Q9TTC1 _3mutA 19002 LIB1_ 1_121 SFV1_P23074 -Pro 20583 LIB2_ EA_1 2 FFV_O93209 17422 LIB1_ 1_6 K0RV_Q9TTC1 _3mutA 19003 LIB1_ 1_122 SFV1_P23074 -Pro 20584 LIB2_ EA_1 3 FFV_O93209 17423 LIB1_ 1_60 K0RV_Q9TTC1 _3mutA 19004 LIB1_ 1_13 SFV1_P23074 -Pro 20585 LIB2_ EA_1 4 FFV_O93209 17424 LIB1_ 1_61 K0RV_Q9TTC1 _3mutA 19005 LIB1_ 1_14 SFV1_P23074 -Pro 20586 LIB2_ EA_1 5 FFV_O93209 17425 LIB1_ 1_62 K0RV_Q9TTC1 _3mutA 19006 LIB1_ 1_15 SFV1_P23074 -Pro 20587 LIB2_ EA_1 6 FFV_O93209 17426 LIB1_ 1_63 K0RV_Q9TTC1 _3mutA 19007 LIB1_ 1_16 SFV1_P23074 -Pro 20588 LIB2_ EA_1 7 FFV_O93209 17427 LIB1_ 1_64 K0RV_Q9TTC1 _3mutA 19008 LIB1_ 1_17 SFV1_P23074 -Pro 20589 LIB2_ EA_1 8 FFV_O93209 17428 LIB1_ 1_65 K0RV_Q9TTC1 _3mutA 19009 LIB1_ 1_18 SFV1_P23074 -Pro 20590 LIB2_ EA_1 9 FFV_O93209 17429 LIB1_ 1_66 K0RV_Q9TTC1 _3mutA 19010 LIB1_ 1_19 SFV1_P23074 -Pro 20591 LIB2_ EA_2 FFV_O93209 17430 LIB1_ 1_67 K0RV_Q9TTC1 _3mutA 19011 LIB1_ 1_2 SFV1_P23074 -Pro 20592 LIB2_ EA_2 0 FFV_O93209 17431 LIB1_ 1_68 K0RV_Q9TTC1 _3mutA 19012 LIB1_ 1_20 SFV1_P23074 -Pro 20593 LIB2_ EA_2 1 FFV_O93209 17432 LIB1_ 1_69 K0RV_Q9TTC1 _3mutA 19013 LIB1_ 1_21 SFV1_P23074 -Pro 20594 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB2_ EA_2 2 FFV_O93209 17433 LIB1_ 1_7 KORV_Q9TTC1 _3mutA 19014 LIB1_ 1_22 SFV1_P23074 -Pro 20595 LIB2_ EA_2 3 FFV_O93209 17434 LIB1_ 1_70 KORV_Q9TTC1 _3mutA 19015 LIB1_ 1_23 SFV1_P23074 -Pro 20596 LIB2_ EA_2 4 FFV_O93209 17435 LIB1_ 1_71 KORV_Q9TTC1 _3mutA 19016 LIB1_ 1_24 SFV1_P23074 -Pro 20597 LIB2_ EA_2 5 FFV_O93209 17436 LIB1_ 1_72 KORV_Q9TTC1 _3mutA 19017 LIB1_ 1_25 SFV1_P23074 -Pro 20598 LIB2_ EA_2 6 FFV_O93209 17437 LIB1_ 1_73 KORV_Q9TTC1 _3mutA 19018 LIB1_ 1_26 SFV1_P23074 -Pro 20599 LIB2_ EA_2 7 FFV_O93209 17438 LIB1_ 1_74 KORV_Q9TTC1 _3mutA 19019 LIB1_ 1_27 SFV1_P23074 -Pro 20600 LIB2_ EA_2 8 FFV_O93209 17439 LIB1_ 1_75 KORV_Q9TTC1 _3mutA 19020 LIB1_ 1_28 SFV1_P23074 -Pro 20601 LIB2_ EA_3 FFV_O93209 17440 LIB1_ 1_76 KORV_Q9TTC1 _3mutA 19021 LIB1_ 1_29 SFV1_P23074 -Pro 20602 LIB2_ EA_4 FFV_O93209 17441 LIB1_ 1_77 KORV_Q9TTC1 _3mutA 19022 LIB1_ 1_3 SFV1_P23074 -Pro 20603 LIB2_ EA_5 FFV_O93209 17442 LIB1_ 1_78 KORV_Q9TTC1 _3mutA 19023 LIB1_ 1_30 SFV1_P23074 -Pro 20604 LIB2_ EA_6 FFV_O93209 17443 LIB1_ 1_79 KORV_Q9TTC1 _3mutA 19024 LIB1_ 1_31 SFV1_P23074 -Pro 20605 LIB2_ EA_7 FFV_O93209 17444 LIB1_ 1_8 KORV_Q9TTC1 _3mutA 19025 LIB1_ 1_32 SFV1_P23074 -Pro 20606 LIB2_ EA_8 FFVJ393209 17445 LIB1_ 1_80 KORV_Q9TTC1 _3mutA 19026 LIB1_ 1_33 SFV1_P23074 -Pro 20607 LIB2_ EA_9 FFV_O93209 17446 LIB1_ 1_81 KORV_Q9TTC1 _3mutA 19027 LIB1_ 1_34 SFV1_P23074 -Pro 20608 LIB1_ 1_1 FFV_O93209-Pro 17447 LIB1_ 1_82 KORV_Q9TTC1 _3mutA 19028 LIB1_ 1_35 SFV1_P23074 -Pro 20609 LIB1_ 1_10 FFV_O93209-Pro 17448 LIB1_ 1_83 KORV_Q9TTC1 _3mutA 19029 LIB1_ 1_37 SFV1_P23074 -Pro 20610 LIB1_ 1_100 FFV_O93209-Pro 17449 LIB1_ 1_84 KORV_Q9TTC1 _3mutA 19030 LIB1_ 1_38 SFV1_P23074 -Pro 20611 LIB1_ 1_101 FFV_O93209-Pro 17450 LIB1_ 1_85 KORV_Q9TTC1 _3mutA 19031 LIB1_ 1_39 SFV1_P23074 -Pro 20612 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_102 FFV_O93209-Pro 17451 LIB1_ 1_86 KORV_Q9TTC1 _3mutA 19032 LIB1_ 1_4 SFV1_P23074 -Pro 20613 LIB1_ 1_103 FFV_O93209-Pro 17452 LIB1_ 1_87 KORV_Q9TTC1 _3mutA 19033 LIB1_ 1_40 SFV1-P23074 -Pro 20614 LIB1_ 1_104 FFV_O93209-Pro 17453 LIB1_ 1_88 KORV_Q9TTC1 _3mutA 19034 LIB1_ 1_41 SFV1_P23074 -Pro 20615 LIB1_ 1_105 FFV_O93209-Pro 17454 LIB1_ 1_89 KORV_Q9TTC1 _3mutA 19035 LIB1_ 1_42 SFV1_P23074 -Pro 20616 LIB1_ 1_106 FFV_O93209-Pro 17455 LIB1_ 1_9 KORV_Q9TTC1 _3mutA 19036 LIB1_ 1_43 SFV1_P23074 -Pro 20617 LIB1_ 1_107 FFV_O93209-Pro 17456 LIB1_ 1_90 KORV_Q9TTC1 _3mutA 19037 LIB1_ 1_44 SFV1_P23074 -Pro 20618 LIB1_ 1_108 FFV_O93209-Pro 17457 LIB1_ 1_91 KORV_Q9TTC1 _3mutA 19038 LIB1_ 1_45 SFV1_P23074 -Pro 20619 LIB1_ 1_109 FFV_O93209-Pro 17458 LIB1_ 1_92 KORV_Q9TTC1 _3mutA 19039 LIB1_ 1_46 SFV1_P23074 -Pro 20620 LIB1_ 1_11 FFV_O93209-Pro 17459 LIB1_ 1_93 KORV_Q9TTC1 _3mutA 19040 LIB1_ 1_47 SFV1_P23074 -Pro 20621 LIB1_ 1_110 FFV_O93209-Pro 17460 LIB1_ 1_94 KORV_Q9TTC1 _3mutA 19041 LIB1_ 1_48 SFV1_P23074 -Pro 20622 LIB1_ 1_111 FFV_O93209-Pro 17461 LIB1_ 1_95 KORV_Q9TTC1 _3mutA 19042 LIB1_ 1_49 SFV1_P23074 -Pro 20623 LIB1_ 1_112 FFV_O93209-Pro 17462 LIB1_ 1_96 KORV_Q9TTC1 _3mutA 19043 LIB1_ 1_50 SFV1-P23074 -Pro 20624 LIB1_ 1_113 FFV_O93209-Pro 17463 LIB1_ 1_97 KORV_Q9TTC1 _3mutA 19044 LIB1_ 1_51 SFV1_P23074 -Pro 20625 LIB1_ 1_114 FFV_O93209-Pro 17464 LIB1_ 1_98 KORV_Q9TTC1 _3mutA 19045 LIB1_ 1_52 SFV1_P23074 -Pro 20626 LIB1_ 1_115 FFV_O93209-Pro 17465 LIB1_ 1_99 KORV_Q9TTC1 _3mutA 19046 LIB1_ 1_53 SFV1_P23074 -Pro 20627 LIB1_ 1_116 FFV_O93209-Pro 17466 LIB2_ EA_1 KORV_Q9TTC1 _3mutA 19047 LIB1_ 1_54 SFV1_P23074 -Pro 20628 LIB1_ 1_117 FFV_O93209-Pro 17467 LIB2_ EA_1 0 KORV_Q9TTC1 _3mutA 19048 LIB1_ 1_55 SFV1-P23074 -Pro 20629 LIB1_ 1_118 FFV_O93209-Pro 17468 LIB2_ EA_1 1 KORV_Q9TTC1 _3mutA 19049 LIB1_ 1_56 SFV1_P23074 -Pro 20630 LIB1_ 1_119 FFV_O93209-Pro 17469 LIB2_ EA_1 2 KORV_Q9TTC1 _3mutA 19050 LIB1_ 1_57 SFV1_P23074 -Pro 20631 LIB1_ 1_12 FFV_O93209-Pro 17470 LIB2_ EA_1 3 KORV_Q9TTC1 _3mutA 19051 LIB1_ 1_58 SFV1_P23074 -Pro 20632 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_120 FFV_O93209-Pro 17471 LIB2_ EA_1 4 KORV_Q9TTC1 _3mutA 19052 LIB1_ 1_59 SFV1_P23074 -Pro 20633 LIB1_ 1_121 FFV_O93209-Pro 17472 LIB2_ EA_1 5 KORV_Q9TTC1 _3mutA 19053 LIB1_ 1_6 SFV1_P23074 -Pro 20634 LIB1_ 1_122 FFV_O93209-Pro 17473 LIB2_ EA_1 6 KORV_Q9TTC1 _3mutA 19054 LIB1_ 1_60 SFV1_P23074 -Pro 20635 LIB1_ 1_13 FFV_O93209-Pro 17474 LIB2_ EA_1 7 KORV_Q9TTC1 _3mutA 19055 LIB1_ 1_61 SFV1_P23074 -Pro 20636 LIB1_ 1_14 FFV_O93209-Pro 17475 LIB2_ EA_1 8 KORV_Q9TTC1 _3mutA 19056 LIB1_ 1_62 SFV1_P23074 -Pro 20637 LIB1_ 1_15 FFV_O93209-Pro 17476 LIB2_ EA_1 9 KORV_Q9TTC1 _3mutA 19057 LIB1_ 1_63 SFV1_P23074 -Pro 20638 LIB1_ 1_16 FFV_O93209-Pro 17477 LIB2_ EA_2 KORV_Q9TTC1 _3mutA 19058 LIB1_ 1_64 SFV1_P23074 -Pro 20639 LIB1_ 1_17 FFV_O93209-Pro 17478 LIB2_ EA_2 0 KORV_Q9TTC1 _3mutA 19059 LIB1_ 1_65 SFV1_P23074 -Pro 20640 LIB1_ 1_18 FFV_O93209-Pro 17479 LIB2_ EA_2 1 KORV_Q9TTC1 _3mutA 19060 LIB1_ 1_66 SFV1_P23074 -Pro 20641 LIB1_ 1_19 FFV_O93209-Pro 17480 LIB2_ EA_2 2 KORV_Q9TTC1 _3mutA 19061 LIB1_ 1_67 SFV1_P23074 -Pro 20642 LIB1_ 1_2 FFV_O93209-Pro 17481 LIB2_ EA_2 3 KORV_Q9TTC1 _3mutA 19062 LIB1_ 1_68 SFV1_P23074 -Pro 20643 LIB1_ 1_20 FFV_O93209-Pro 17482 LIB2_ EA_2 4 KORV_Q9TTC1 _3mutA 19063 LIB1_ 1_69 SFV1_P23074 -Pro 20644 LIB1_ 1_21 FFV_O93209-Pro 17483 LIB2_ EA_2 5 KORV_Q9TTC1 _3mutA 19064 LIB1_ 1_7 SFV1_P23074 -Pro 20645 LIB1_ 1_22 FFV_O93209-Pro 17484 LIB2_ EA_2 6 KORV_Q9TTC1 _3mutA 19065 LIB1_ 1_70 SFV1_P23074 -Pro 20646 LIB1_ 1_23 FFV_O93209-Pro 17485 LIB2_ EA_2 7 KORV_Q9TTC1 _3mutA 19066 LIB1_ 1_71 SFV1_P23074 -Pro 20647 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_24 FFV_O93209-Pro 17486 LIB2_ EA_2 8 KORV_Q9TTC1 _3mutA 19067 LIB1_ 1_72 SFV1_P23074 -Pro 20648 LIB1_ 1_25 FFV_O93209-Pro 17487 LIB2_ EA_3 KORV_Q9TTC1 _3mutA 19068 LIB1_ 1_73 SFV1_P23074 -Pro 20649 LIB1_ 1_26 FFV_O93209-Pro 17488 LIB2_ EA_4 KORV_Q9TTC1 _3mutA 19069 LIB1_ 1_74 SFV1_P23074 -Pro 20650 LIB1_ 1_27 FFV_O93209-Pro 17489 LIB2_ EA_5 KORV_Q9TTC1 _3mutA 19070 LIB1_ 1_75 SFV1_P23074 -Pro 20651 LIB1_ 1_28 FFV_O93209-Pro 17490 LIB2_ EA_6 KORV_Q9TTC1 _3mutA 19071 LIB1_ 1_76 SFV1_P23074 -Pro 20652 LIB1_ 1_29 FFV_O93209-Pro 17491 LIB2_ EA_7 KORV_Q9TTC1 _3mutA 19072 LIB1_ 1_77 SFV1_P23074 -Pro 20653 LIB1_ 1_3 FFV_O93209-Pro 17492 LIB2_ EA_8 KORV_Q9TTC1 _3mutA 19073 LIB1_ 1_78 SFV1_P23074 -Pro 20654 LIB1_ 1_30 FFV_O93209-Pro 17493 LIB2_ EA_9 KORV_Q9TTC1 _3mutA 19074 LIB1_ 1_79 SFV1_P23074 -Pro 20655 LIB1_ 1_31 FFV_O93209-Pro 17494 LIB1_ 1_1 KORV_Q9TTC1 -Pro_3mut 19075 LIB1_ 1_8 SFV1_P23074 -Pro 20656 LIB1_ 1_32 FFV_O93209-Pro 17495 LIB1_ 1_10 KORV_Q9TTC1 -Pro_3mut 19076 LIB1_ 1_80 SFV1_P23074 -Pro 20657 LIB1_ 1_33 FFV_O93209-Pro 17496 LIB1_ 1_100 KORV_Q9TTC1 -Pro_3mut 19077 LIB1_ 1_81 SFV1_P23074 -Pro 20658 LIB1_ 1_34 FFV_O93209-Pro 17497 LIB1_ 1_101 KORV_Q9TTC1 -Pro_3mut 19078 LIB1_ 1_82 SFV1_P23074 -Pro 20659 LIB1_ 1_35 FFV_O93209-Pro 17498 LIB1_ 1_102 KORV_Q9TTC1 -Pro_3mut 19079 LIB1_ 1_83 SFV1_P23074 -Pro 20660 LIB1_ 1_37 FFV_O93209-Pro 17499 LIB1_ 1_103 KORV_Q9TTC1 -Pro_3mut 19080 LIB1_ 1_84 SFV1_P23074 -Pro 20661 LIB1_ 1_38 FFV_O93209-Pro 17500 LIB1_ 1_104 KORV_Q9TTC1 -Pro_3mut 19081 LIB1_ 1_85 SFV1_P23074 -Pro 20662 LIB1_ 1_39 FFV_O93209-Pro 17501 LIB1_ 1_105 KORV_Q9TTC1 -Pro_3mut 19082 LIB1_ 1_86 SFV1_P23074 -Pro 20663 LIB1_ 1_4 FFV_O93209-Pro 17502 LIB1_ 1_106 KORV_Q9TTC1 -Pro_3mut 19083 LIB1_ 1_87 SFV1_P23074 -Pro 20664 LIB1_ 1_40 FFV_O93209-Pro 17503 LIB1_ 1_107 KORV_Q9TTC1 -Pro_3mut 19084 LIB1_ 1_88 SFV1_P23074 -Pro 20665 LIB1_ 1_41 FFV_O93209-Pro 17504 LIB1_ 1_108 KORV_Q9TTC1 -Pro_3mut 19085 LIB1_ 1_89 SFV1_P23074 -Pro 20666 LIB1_ 1_42 FFV_O93209-Pro 17505 LIB1_ 1_109 KORV_Q9TTC1 -Pro_3mut 19086 LIB1_ 1_9 SFV1_P23074 -Pro 20667 LIB1_ 1_43 FFV_O93209-Pro 17506 LIB1_ 1_11 KORV_Q9TTC1 -Pro_3mut 19087 LIB1_ 1_90 SFV1_P23074 -Pro 20668 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_44 FFV_O93209-Pro 17507 LIB1_ 1.110 KORV_Q9TTC1 -Pro_3mut 19088 LIB1_ 1.91 SFV1_P23074 -Pro 20669 LIB1_ 1_45 FFV_O93209-Pro 17508 LIBI-U11 KORV_Q9TTC1 -Pro_3mut 19089 LIB1_ 1_92 SFV1_P23074 -Pro 20670 LIB1_ 1_46 FFV_O93209-Pro 17509 LIB1_ 1_112 KORV_Q9TTC1 -Pro_3mut 19090 LIB1_ 1_93 SFV1_P23074 -Pro 20671 LIB1_ 1_47 FFV_O93209-Pro 17510 LIB1_ 1_113 KORV_Q9TTC1 -Pro_3mut 19091 LIB1_ 1_94 SFV1_P23074 -Pro 20672 LIB1_ 1_48 FFV_O93209-Pro 17511 LIB1_ 1_114 KORV_Q9TTC1 -Pro_3mut 19092 LIB1_ 1_95 SFV1-P23074 -Pro 20673 LIB1_ 1_49 FFV_O93209-Pro 17512 LIB1_ 1.115 KORV_Q9TTC1 -Pro_3mut 19093 LIB1_ 1.96 SFV1_P23074 -Pro 20674 LIB1_ 1_50 FFV_O93209-Pro 17513 LIB1_ 1_116 KORV_Q9TTC1 -Pro_3mut 19094 LIB1_ 1_97 SFV1_P23074 -Pro 20675 LIB1_ 1_51 FFV_O93209-Pro 17514 LIB1_ 1_117 KORV_Q9TTC1 -Pro_3mut 19095 LIB1_ 1_98 SFV1_P23074 -Pro 20676 LIB1_ 1_52 FFV_O93209-Pro 17515 LIB1_ 1_118 KORV_Q9TTC1 -Pro_3mut 19096 LIB1_ 1_99 SFV1_P23074 -Pro 20677 LIB1_ 1_53 FFV_O93209-Pro 17516 LIB1_ 1_119 KORV_Q9TTC1 -Pro_3mut 19097 LIB2_ EA_1 SFV1.P23074 -Pro 20678 LIB1_ 1_54 FFV_O93209-Pro 17517 LIB1_ 1_12 KORV_Q9TTC1 -Pro_3mut 19098 LIB2_ EA_1 0 SFV1_P23074 -Pro 20679 LIB1_ 1_55 FFV_O93209-Pro 17518 LIB1_ 1_120 KORV_Q9TTC1 -Pro_3mut 19099 LIB2_ EA_1 1 SFV1.P23074 -Pro 20680 LIB1_ 1_56 FFV_O93209-Pro 17519 LIB1_ 1_121 KORV_Q9TTC1 -Pro_3mut 19100 LIB2_ EA_1 2 SFV1_P23074 -Pro 20681 LIB1_ 1_57 FFV_O93209-Pro 17520 LIB1_ 1_122 KORV_Q9TTC1 -Pro_3mut 19101 LIB2_ EA_1 3 SFV1_P23074 -Pro 20682 LIB1_ 1_58 FFV_O93209-Pro 17521 LIB1_ 1_13 KORV_Q9TTC1 -Pro_3mut 19102 LIB2_ EA_1 4 SFV1_P23074 -Pro 20683 LIB1_ 1_59 FFV_O93209-Pro 17522 LIB1_ 1.14 KORV_Q9TTC1 -Pro_3mut 19103 LIB2_ EA.1 5 SFV1_P23074 -Pro 20684 LIB1_ 1_6 FFV_O93209-Pro 17523 LIB1_ 1_15 KORV_Q9TTC1 -Pro_3mut 19104 LIB2_ EA_1 6 SFV1-P23074 -Pro 20685 LIB1_ 1_60 FFV_O93209-Pro 17524 LIB1. 1_16 KORV.Q9TTC1 -Pro_3mut 19105 LIB2. EA_1 7 SFV1.P23074 -Pro 20686 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_61 FFV_O93209-Pro 17525 LIB1_ 1_17 KORV_Q9TTC1 -Pro_3mut 19106 LIB2_ EA_1 8 SFV1_P23074 -Pro 20687 LIB1_ 1_62 FFV_O93209-Pro 17526 LIB1_ 1_18 KORV_Q9TTC1 -Pro_3mut 19107 LIB2_ EA_1 9 SFV1_P23074 -Pro 20688 LIB1_ 1_63 FFV_O93209-Pro 17527 LIB1_ 1_19 KORV_Q9TTC1 -Pro_3mut 19108 LIB2_ EA_2 SFV1_P23074 -Pro 20689 LIB1_ 1_64 FFV_O93209-Pro 17528 LIB1_ 1_2 KORV_Q9TTC1 -Pro_3mut 19109 LIB2_ EA_2 0 SFV1_P23074 -Pro 20690 LIB1_ 1_65 FFV_O93209-Pro 17529 LIB1_ 1_20 KORV_Q9TTC1 -Pro_3mut 19110 LIB2_ EA_2 1 SFV1_P23074 -Pro 20691 LIB1_ 1_66 FFV_O93209-Pro 17530 LIB1_ 1_21 KORV_Q9TTC1 -Pro_3mut 19111 LIB2_ EA_2 2 SFV1_P23074 -Pro 20692 LIB1_ 1_67 FFV_O93209-Pro 17531 LIB1_ 1_22 KORV_Q9TTC1 -Pro_3mut 19112 LIB2_ EA_2 3 SFV1_P23074 -Pro 20693 LIB1_ 1_68 FFV_O93209-Pro 17532 LIB1_ 1_23 KORV_Q9TTC1 -Pro_3mut 19113 LIB2_ EA_2 4 SFV1_P23074 -Pro 20694 LIB1_ 1_69 FFV_O93209-Pro 17533 LIB1_ 1_24 KORV_Q9TTC1 -Pro_3mut 19114 LIB2_ EA_2 5 SFV1_P23074 -Pro 20695 LIB1_ 1_7 FFV_O93209-Pro 17534 LIB1_ 1_25 KORV_Q9TTC1 -Pro_3mut 19115 LIB2_ EA_2 6 SFV1_P23074 -Pro 20696 LIB1_ 1_70 FFV_O93209-Pro 17535 LIB1_ 1_26 KORV_Q9TTC1 -Pro_3mut 19116 LIB2_ EA_2 7 SFV1_P23074 -Pro 20697 LIB1_ 1_71 FFV_O93209-Pro 17536 LIB1_ 1_27 KORV_Q9TTC1 -Pro_3mut 19117 LIB2_ EA_2 8 SFV1_P23074 -Pro 20698 LIB1_ 1_72 FFV_O93209-Pro 17537 LIB1_ 1_28 KORV_Q9TTC1 -Pro_3mut 19118 LIB2_ EA_3 SFV1_P23074 -Pro 20699 LIB1_ 1_73 FFV_O93209-Pro 17538 LIB1_ 1_29 KORV_Q9TTC1 -Pro_3mut 19119 LIB2_ EA_4 SFV1_P23074 -Pro 20700 LIB1_ 1_74 FFV_O93209-Pro 17539 LIB1_ 1_3 KORV_Q9TTC1 -Pro_3mut 19120 LIB2_ EA_5 SFV1_P23074 -Pro 20701 LIB1_ 1_75 FFV_O93209-Pro 17540 LIB1_ 1_30 KORV_Q9TTC1 -Pro_3mut 19121 LIB2_ EA_6 SFV1_P23074 -Pro 20702 Linke r ID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO Linke rID RT Name SEQ ID NO LIB1_ 1_76 FFV_O93209-Pro 17541 LIB1_ 1_31 KORV_Q9TTC1 -Pro_3mut 19122 LIB2_ EA_7 SFV1_P23074 -Pro 20703 LIB1_ 1_77 FFV_O93209-Pro 17542 LIB1_ 1_32 KORV_Q9TTC1 -Pro_3mut 19123 LIB2_ EA_8 SFV1_P23074 -Pro 20704 LIB1_ 1_78 FFV_O93209-Pro 17543 LIB1_ 1_33 KORV_Q9TTC1 -Pro_3mut 19124 LIB2_ EA_9 SFV1_P23074 -Pro 20705 LIB1_ 1_79 FFV_O93209-Pro 17544 LIB1_ 1_34 KORV_Q9TTC1 -Pro_3mut 19125 LIB1_ 1_1 SFV3L_P2740 1_2mut 20706 LIB1_ 1_8 FFV_O93209-Pro 17545 LIB1_ 1_35 KORV_Q9TTC1 -Pro_3mut 19126 LIB1_ 1_10 SFV3L_P2740 1_2mut 20707 LIB1_ 1_80 FFV_O93209-Pro 17546 LIB1_ 1_37 KORV_Q9TTC1 -Pro_3mut 19127 LIB1_ 1.100 SFV3L_P2740 1_2mut 20708 LIB1_ 1_81 FFV_O93209-Pro 17547 LIB1_ 1_38 KORV_Q9TTC1 -Pro_3mut 19128 LIB1_ 1.101 SF...

Claims

1. A gene modifying polypeptide comprising:a retroviral reverse transcriptase (RT) domain;an StlCas9 nickase domain, wherein the RT domain is C-terminal of theCas9 nickase domain; anda linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker comprises an amino acid sequence of Table 6, or a sequence having at least 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto.

2. A gene modifying polypeptide comprising:a retroviral reverse transcriptase (RT) domain having an amino acid sequence of Table 1, or an amino acid sequence with at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto;an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; anda linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker comprises an amino acid sequence of Table 5, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto.

3. A gene modifying polypeptide comprising:a retroviral reverse transcriptase (RT) domain which is a PERV RT domain;an StlCas9 nickase domain, wherein the RT domain is C-terminal of theCas9 nickase domain; anda linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of any of SEQ ID NOs: 10301, 10304, 10305, 10307, or 10314 or a sequence having at least 75%, 80%, 85%, 90%, 95%,97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto.

4. A gene modifying polypeptide comprising:a retroviral reverse transcriptase (RT) domain which is a BAEVM RT domain;an StlCas9 nickase domain, wherein the RT domain is C-terminal of theCas9 nickase domain; anda linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of any of SEQ ID NOs: 10302, 10308, 10310, or 10312, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto.

5. A gene modifying polypeptide comprising:a retroviral reverse transcriptase (RT) domain which is a WMSV RT domain;an StlCas9 nickase domain, wherein the RT domain is C-terminal of theCas9 nickase domain; anda linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10303, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1,2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto.

6. A gene modifying polypeptide comprising:a retroviral reverse transcriptase (RT) domain which is a MLMS RT domain;an StlCas9 nickase domain, wherein the RT domain is C-terminal of theCas9 nickase domain; anda linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10306, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto.

7. A gene modifying polypeptide comprising:a retroviral reverse transcriptase (RT) domain which is a AVIRE RT domain;an StlCas9 nickase domain, wherein the RT domain is C-terminal of theCas9 nickase domain; anda linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of any of SEQ ID NOs: 10309 or 10313, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto.

8. A gene modifying polypeptide comprising:a retroviral reverse transcriptase (RT) domain which is a XMRV6 RT domain;an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; anda linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10311, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto.

9. A gene modifying polypeptide comprising:a retroviral reverse transcriptase (RT) domain which is a MLVFF RT domain;an StlCas9 nickase domain, wherein the RT domain is C-terminal of the Cas9 nickase domain; anda linker disposed between the RT domain and the Cas9 nickase domain, wherein the linker has an amino acid sequence of SEQ ID NO: 10315, or a sequence having at least 75%, 80%, 85%, 90%, 95%, 97%, 98%, or 99% identity thereto, or an amino acid sequence having up to 1, 2, or 3 amino acid sequence differences (e.g., substitutions) relative thereto.

10. A nucleic acid molecule encoding a gene modifying polypeptide according to any of the preceding claims.

11. A cell comprising:i) a gene modifying polypeptide of any of claims 1-9 orii) a nucleic acid encoding the gene modifying polypeptide.

12. A system comprising:i) a gene modifying polypeptide of any of claims 1-9, ora nucleic acid molecule encoding the gene modifying polypeptide, andii) a template RNA that comprises:a) a gRNA spacer that is complementary to a portion of a target nucleic acid sequence;b) a gRNA scaffold (e.g., a StlCas9 gRNA scaffold) that binds the Cas9 nickase domain of the gene modifying polypeptide;c) a heterologous object sequence; and d) a primer binding site (PBS) sequence.

13. A lipid nanoparticle formulation comprising the system of claim 12.

14. A method for modifying a target nucleic acid molecule in a cell, the method comprising contacting the cell with the system of claim 12, thereby modifying the target nucleic acid molecule.

15. A method for modifying a target nucleic acid molecule in a tissue, the method comprising contacting the tissue with the system of claim 12, thereby modifying the target nucleic acid molecule.

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