ID A0A5B8NGG8_9HIV1 Unreviewed; 353 AA. AC A0A5B8NGG8; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 11-DEC-2019, entry version 2. DE SubName: Full=Pol protein {ECO:0000313|EMBL:QDZ37985.1}; DE Flags: Fragment; GN Name=pol {ECO:0000313|EMBL:QDZ37985.1}; OS Human immunodeficiency virus 1. OC Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus. OX NCBI_TaxID=11676 {ECO:0000313|EMBL:QDZ37985.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:QDZ37985.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DR2014-0432 {ECO:0000313|EMBL:QDZ37985.1}; RA Dan Y.; RT "Assessing the Efficacy of Second-Line Antiretroviral Regimen for HIV Drug RT Resistant Patients in Sichuan China: A Retrospective Observational Study."; RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases. 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:SAAS01120264}; 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; MK948197; QDZ37985.1; -; Genomic_DNA. 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_sf. DR InterPro; IPR034170; Retropepsin-like_cat_dom. DR InterPro; IPR018061; Retropepsins. 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:SAAS01057967}; KW Multifunctional enzyme {ECO:0000256|SAAS:SAAS00719445}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS01055310}; KW Protease {ECO:0000256|RuleBase:RU004064}; KW RNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS01055094}; KW Transferase {ECO:0000256|SAAS:SAAS01054657}. FT DOMAIN 20..89 FT /note="Peptidase A2" FT /evidence="ECO:0000259|PROSITE:PS50175" FT DOMAIN 143..333 FT /note="Reverse transcriptase" FT /evidence="ECO:0000259|PROSITE:PS50878" FT UNSURE 166 FT /note="D or N" FT /evidence="ECO:0000313|EMBL:QDZ37985.1" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QDZ37985.1" FT NON_TER 353 FT /evidence="ECO:0000313|EMBL:QDZ37985.1" SQ SEQUENCE 353 AA; 40311 MW; CB1CAADCCC760A03 CRC64; PQITLWQRPL VTIKIGGQXK EALLDTGADD TVLEEMNLPG KWKPKMIGGI GGFIKVRQYE QVXIEICGHK AIGTVLVGPT PVNIIGRNLL TQLGCTLNFP ISPIETVPVK LKPGMDGPKV KQWPLTEEKI KALTEICEEM EKEGKITKIG PDNPYNTPIF AIKKKDSTXW RKLVDFRELN KRTQDFWEVQ LGIPHPAGLK KNKSVTVLDV GDAYFSVPLH EDFRKYTAFT IPSTNNETPG VRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNPDIVIY QYVDDLYVGS DLEIGQHRTK IEELRQHLLR WGFTTPDKKH QKEPPFLWMG YELHPDKWTV QPIQLPEKDS WTV //