ID A9UI05_9HIV1 Unreviewed; 343 AA. AC A9UI05; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 15-FEB-2017, entry version 58. DE SubName: Full=Pol protein {ECO:0000313|EMBL:ABX84078.1}; DE Flags: Fragment; GN Name=pol {ECO:0000313|EMBL:ABX84078.1}; OS Human immunodeficiency virus 1. OC Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; OC Lentivirus; Primate lentivirus group. OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ABX84078.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:ABX84078.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NV38 {ECO:0000313|EMBL:ABX84078.1}; RX PubMed=18572440; DOI=10.1089/aid.2008.0051; RA McConnell M.J., Docobo-Perez F., Mata R.C., Fernandez-Cuenca F., RA Viciana P., Lopez-Cortes L.F., Trastoy M., Pachon J., Perez-Romero P.; RT "Molecular epidemiology of HIV type 1 in newly diagnosed patients in RT southern Spain."; RL AIDS Res. Hum. Retroviruses 24:881-887(2008). 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; EU288123; ABX84078.1; -; 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 InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR034170; HIV_retropepsin_like. DR InterPro; IPR001995; Peptidase_A2_cat. DR InterPro; IPR021109; Peptidase_aspartic_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, KW ECO:0000256|SAAS:SAAS00034670}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00499946}; KW Protease {ECO:0000256|RuleBase:RU004064}; KW RNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS00500019}; KW Transferase {ECO:0000256|SAAS:SAAS00500401}. FT DOMAIN 17 86 Peptidase A2. {ECO:0000259|PROSITE: FT PS50175}. FT DOMAIN 140 330 Reverse transcriptase. FT {ECO:0000259|PROSITE:PS50878}. FT NON_TER 1 1 {ECO:0000313|EMBL:ABX84078.1}. FT NON_TER 343 343 {ECO:0000313|EMBL:ABX84078.1}. SQ SEQUENCE 343 AA; 39213 MW; C0E064714E6E3565 CRC64; TLWQRPLVTI KIGGQLKEAL LDTGADDTVL EEMDLPGRWK PKMIGGIGGF IKVRQYDQIP IEICGHKAIG TVLIGPTPVN IIGRNLLTQL GCTLNFXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXCTEMEKE GKITKIGPEN PYNTPVFAIK KKDSTKWRKL VDFRELNKRT QDFWEVQLGI PHPAGLKKKK SVTVLDVGDA YFSVPLDKEF RKYTAFTIPS INNETPGIRY QYNVLPQGWK GSPAIFQSSM TKILEPFRKQ NPEIVIYQYM DDLYVGSDLE IGQHRXKIEE SRHHLLRWGF TTPDKKHQKE PPFLWMGYEL HPDKWTVQPI VLP //