ID A9UI05_9HIV1 Unreviewed; 343 AA. AC A9UI05; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 11-NOV-2015, entry version 50. 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:SAAS00034266}. CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family. CC {ECO:0000256|RuleBase:RU004064}. CC -!- SIMILARITY: Contains 1 reverse transcriptase domain. CC {ECO:0000256|RuleBase:RU000322}. CC -!- SIMILARITY: Contains peptidase A2 domain. CC {ECO:0000256|SAAS:SAAS00287301}. 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 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrolase {ECO:0000256|RuleBase:RU000453, KW ECO:0000256|SAAS:SAAS00034670}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00148904}; KW Protease {ECO:0000256|RuleBase:RU000453}; KW RNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS00148984}; KW Transferase {ECO:0000256|SAAS:SAAS00148918}. FT COILED 134 140 {ECO:0000256|SAM:Coils}. 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 //