ID A0A346G274_9HIV1 Unreviewed; 435 AA. AC A0A346G274; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 16-JAN-2019, entry version 3. DE SubName: Full=Pol protein {ECO:0000313|EMBL:AXN89387.1}; DE Flags: Fragment; GN Name=pol {ECO:0000313|EMBL:AXN89387.1}; OS Human immunodeficiency virus 1. OC Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus. OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AXN89387.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:AXN89387.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KYR_Bishkek91 {ECO:0000313|EMBL:AXN89387.1}; RA Totmenin A.V., Ivlev V.V., Astakhova E.M., Zyryanova D.P., RA Sokolova O.O., Gashnikova M.P., Bekbolotov A.A., Akbekov B.M., RA Kadyrbekov U.K., Gashnikova N.M.; RT "HIV-1 Genetic Diversity and Drug Resistance in Bishkek region of RT Kyrgyzstan."; RL Submitted (JAN-2018) 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- CC COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:61560, 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; MG798970; AXN89387.1; -; Genomic_DNA. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:InterPro. 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 InterPro; IPR010661; RVT_thumb. DR Pfam; PF00077; RVP; 1. DR Pfam; PF00078; RVT_1; 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: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 66 135 Peptidase A2. {ECO:0000259|PROSITE: FT PS50175}. FT DOMAIN 189 379 Reverse transcriptase. FT {ECO:0000259|PROSITE:PS50878}. FT NON_TER 1 1 {ECO:0000313|EMBL:AXN89387.1}. FT NON_TER 435 435 {ECO:0000313|EMBL:AXN89387.1}. SQ SEQUENCE 435 AA; 49405 MW; 35A9E1D66B58A586 CRC64; REARKFSSEQ TRTISPTSRE LWDGGRDNPL PETRTERQGT AASFNFPQIT LWQRPLVTVR VGGQVKEALL DTGADDTVLE DIDLPGKWKP KMIGGIGGFI KVKQYDQILI EICGKRAIGT VLIGPTPVNI IGRNMLTQIG CTLNFPISPI ETVPVALKPG MDGPKVKQWP LTEEKIKALT EICMEMEKEG KISKIGPENP YNTPIFAIKK KDGTKWRKLV DFRELNKRTQ DFWEVQLGIP HPAGLKRQRS VTVLDVGDAY FSVPLDESFR KYTAFTIPST NNETPGIRYQ YNVLPQGWKG SPAIFQSSMT KILEPFRLKN PEIVIYQYMD DLYVGSDLEI GQHRIKIEEL RAHLLSWGFT TPDKKHQKEP PFLWMGYELH PDKWTVQPIV LPEKDSWTVN DIQKLVGKLN WASQIYPGIK VKQLCKLLRG AKALT //