ID A0A0H5BN33_9HIV1 Unreviewed; 584 AA. AC A0A0H5BN33; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 15-MAR-2017, entry version 10. DE SubName: Full=Gag-pol polyprotein {ECO:0000313|EMBL:CDG41821.1}; DE Flags: Fragment; OS HIV-1 M:CRF08_BC. OC Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; OC Lentivirus; Primate lentivirus group. OX NCBI_TaxID=1385608 {ECO:0000313|EMBL:CDG41821.1}; RN [1] {ECO:0000313|EMBL:CDG41821.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=YN254 {ECO:0000313|EMBL:CDG41821.1}; RA Chen S., Chen Y.Y., Lu W.; RT "Changing subtype dominance and shift in resistance of HIV-1 in the RT southwest border of China."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). {ECO:0000256|SAAS:SAAS00501992}. 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; HG421589; CDG41821.1; -; Genomic_RNA. 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 InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR001995; Peptidase_A2_cat. DR InterPro; IPR021109; Peptidase_aspartic_dom. DR InterPro; IPR034170; Retropepsin-like_cat_dom. DR InterPro; IPR018061; Retropepsins. DR InterPro; IPR000477; RT_dom. DR InterPro; IPR010659; RVT_connect. DR InterPro; IPR010661; RVT_thumb. DR Pfam; PF00077; RVP; 1. DR Pfam; PF00078; RVT_1; 1. DR Pfam; PF06815; RVT_connect; 1. DR Pfam; PF06817; RVT_thumb; 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, KW ECO:0000256|SAAS:SAAS00034670}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00696869}; KW Protease {ECO:0000256|RuleBase:RU004064}; KW RNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS00697127}; KW Transferase {ECO:0000256|SAAS:SAAS00697419}. FT DOMAIN 72 141 Peptidase A2. {ECO:0000259|PROSITE: FT PS50175}. FT DOMAIN 195 385 Reverse transcriptase. FT {ECO:0000259|PROSITE:PS50878}. FT NON_TER 1 1 {ECO:0000313|EMBL:CDG41821.1}. FT NON_TER 584 584 {ECO:0000313|EMBL:CDG41821.1}. SQ SEQUENCE 584 AA; 67204 MW; 82ACDA6F31FF5E9F CRC64; FFRENLACPQ GEAREFPPEQ TRANSPASRE LQVRGDNPSS EAGTERQGTL NFPQITLWQR PLVSIKIGGQ IKEALLDTGA DDTVLEEINL PGKWKPKMIG GIGGFIKVRQ YEQIPIEICG KRATGTVLVG PTPVNIIGRN MLTQLGCTLN FPISPIETVP VKLKPGMDGP KVKQWPLTEE KIKALTAICD EMEKEGKITK IGPDNPYNTP IFAIKKKDST KWRKLVDFRE LNKRTQDFWE VQLGIPHPAG LKKKRSVTVL DVGDAYFSVP LDKDFRKYTA FTIPSINNAT PGIRYQYNVL PQGWKGSPAI FQCSMTKILE PFRKQNPDIV IYQYMDDLYV GSDLEIGQHR TKIEELREHL LKWGFTTPDK KHQKEPPFLW MGYELHPDKW TVQPIQLPDK DSWTVNDIQK LVGKLNWASQ IYPGIKVRQL CRLLRGAKAL TDIVPLTEEA ELELAENREI LKEPVHGAYY DPSKELIAEI QKQGQDQWTY QIYQEPFKNL KTGKYAKMRT AHTNDVKQLT EAVQKISMES IVIWGKIPKF RLPIQKETWE TWWTDYWQAT WIPEWEFVNT PPLVKLWYQL EKDP //