ID G3FA37_9HIV1 Unreviewed; 345 AA. AC G3FA37; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 29-OCT-2014, entry version 21. 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; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; OC Lentivirus; Primate lentivirus group. 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., RA He M., Liu Y., Yuan Y., Schulmann J., Glynn S., Ness P., Jackson J.B., RA Shan H.; RT "The human immunodeficiency virus-1 genotype diversity and drug RT resistance mutations profile of volunteer blood donors from Chinese RT blood centers."; RL Transfusion 52:1041-1049(2012). CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). {ECO:0000256|SAAS:SAAS00109248}. CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family. CC {ECO:0000256|RuleBase:RU004064}. CC -!- SIMILARITY: Contains peptidase A2 domain. CC {ECO:0000256|SAAS:SAAS00156356}. CC -!- SIMILARITY: Contains peptidase Adomain. CC {ECO:0000256|SAAS:SAAS00156356}. CC -!- SIMILARITY: Contains reverse transcriptase domain. CC {ECO:0000256|SAAS:SAAS00109794}. 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 Gene3D; 2.40.70.10; -; 1. DR InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR018061; Pept_A2A_retrovirus_sg. DR InterPro; IPR001995; Peptidase_A2_cat. DR InterPro; IPR021109; Peptidase_aspartic_dom. 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:RU000453}; KW Hydrolase {ECO:0000256|RuleBase:RU000453, KW ECO:0000256|SAAS:SAAS00156518}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00109382}; KW Protease {ECO:0000256|RuleBase:RU000453}; KW RNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS00109431}; KW Transferase {ECO:0000256|SAAS:SAAS00109069}. FT NON_TER 1 1 {ECO:0000313|EMBL:AEN55660.1}. FT NON_TER 345 345 {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 //