ID G3FA37_9HIV1 Unreviewed; 345 AA. AC G3FA37; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 17-JUN-2020, entry version 45. DE SubName: Full=Pol protein {ECO:0000313|EMBL:AEN55660.1}; DE Flags: Fragment; GN Name=pol {ECO:0000313|EMBL:AEN55660.1}; OS Human immunodeficiency virus 1. OC Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus. OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AEN55660.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:AEN55660.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=K1 {ECO:0000313|EMBL:AEN55660.1}; RX PubMed=22044422; DOI=10.1111/j.1537-2995.2011.03415.x; RG NHLBI Retrovirus Epidemiology Donor Study-II (REDS-II); RG International Component; RA Zeng P., Wang J., Huang Y., Guo X., Li J., Wen G., Yang T., Yun Z., He M., RA Liu Y., Yuan Y., Schulmann J., Glynn S., Ness P., Jackson J.B., Shan H.; RT "The human immunodeficiency virus-1 genotype diversity and drug resistance RT mutations profile of volunteer blood donors from Chinese blood centers."; RL Transfusion 52:1041-1049(2012). CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130, CC Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:83828; EC=2.7.7.49; CC Evidence={ECO:0000256|SAAS:SAAS01256919}; CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family. CC {ECO:0000256|RuleBase:RU004064}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JF505552; AEN55660.1; -; Genomic_DNA. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR CDD; cd05482; HIV_retropepsin_like; 1. DR Gene3D; 2.40.70.10; -; 1. DR Gene3D; 3.30.70.270; -; 2. DR InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR001995; Peptidase_A2_cat. DR InterPro; IPR021109; Peptidase_aspartic_dom_sf. DR InterPro; IPR034170; Retropepsin-like_cat_dom. DR InterPro; IPR018061; Retropepsins. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR000477; RT_dom. DR Pfam; PF00077; RVP; 1. DR Pfam; PF00078; RVT_1; 1. DR SUPFAM; SSF50630; SSF50630; 1. DR PROSITE; PS50175; ASP_PROT_RETROV; 1. DR PROSITE; PS00141; ASP_PROTEASE; 1. DR PROSITE; PS50878; RT_POL; 1. PE 3: Inferred from homology; KW Aspartyl protease {ECO:0000256|RuleBase:RU004064}; KW Hydrolase {ECO:0000256|RuleBase:RU004064, ECO:0000256|SAAS:SAAS01262043}; KW Multifunctional enzyme {ECO:0000256|SAAS:SAAS01254940}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS01262069}; KW Protease {ECO:0000256|RuleBase:RU004064}; KW RNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS01262051}; KW Transferase {ECO:0000256|SAAS:SAAS01262065}. FT DOMAIN 22..91 FT /note="Peptidase A2" FT /evidence="ECO:0000259|PROSITE:PS50175" FT DOMAIN 145..335 FT /note="Reverse transcriptase" FT /evidence="ECO:0000259|PROSITE:PS50878" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AEN55660.1" FT NON_TER 345 FT /evidence="ECO:0000313|EMBL:AEN55660.1" SQ SEQUENCE 345 AA; 39394 MW; 6582C6249A086881 CRC64; SFPQITLWQR PLVTIKIGGQ MKEALLDTGA DDTVLEDINL PGKWKPKMIG GIGGFIKVRQ YDQILIEICG KKAIGTVLVG PTPVNIIGRN MLTQLGCTLN FPISPIDTVP VTLKPGMDGP RVKQWPLTEE KIKALTEICK EMEEEGKISR IGPENPYNTP VFAIKKKDST KWRKLVDFRE LNKRTQDFWE VQLGIPHPAG LKKKKSVTVL DVGDAYFSVP LDESFRKYTA FTIPSINNET PGIRYQYNVL PQGWKGSPAI FQCSMTKILE PFRKKNPEMV IYQYMDDLYV GSDLEIGQHR TKIEELRDHL LSWGFTTPDK KHQKEPPFLW MGYELHPDRW TVQPI //