ID A0A346G274_9HIV1 Unreviewed; 435 AA. AC A0A346G274; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 03-MAY-2023, entry version 17. 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; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC 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., Sokolova O.O., RA Gashnikova M.P., Bekbolotov A.A., Akbekov B.M., Kadyrbekov U.K., RA 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=Endohydrolysis of RNA in RNA/DNA hybrids. Three different CC cleavage modes: 1. sequence-specific internal cleavage of RNA. Human CC immunodeficiency virus type 1 and Moloney murine leukemia virus CC enzymes prefer to cleave the RNA strand one nucleotide away from the CC RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides CC from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides CC away from the primer terminus.; EC=3.1.26.13; CC Evidence={ECO:0000256|ARBA:ARBA00023415}; 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:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW. DR CDD; cd05482; HIV_retropepsin_like; 1. DR Gene3D; 3.30.70.270; -; 2. DR Gene3D; 2.40.70.10; Acid Proteases; 1. DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1. DR InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR043502; DNA/RNA_pol_sf. 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; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR000477; RT_dom. DR InterPro; IPR010661; RVT_thumb. DR PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1. DR PANTHER; PTHR41694:SF3; INTEGRASE-RELATED; 1. DR Pfam; PF00077; RVP; 1. DR Pfam; PF00078; RVT_1; 1. DR Pfam; PF06817; RVT_thumb; 1. DR SUPFAM; SSF50630; Acid proteases; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 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|ARBA:ARBA00022750, KW ECO:0000256|RuleBase:RU004064}; KW DNA integration {ECO:0000256|ARBA:ARBA00023195}; KW DNA recombination {ECO:0000256|ARBA:ARBA00023172}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004064}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Protease {ECO:0000256|RuleBase:RU004064}; KW RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Viral genome integration {ECO:0000256|ARBA:ARBA00023195}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023195}. FT DOMAIN 66..135 FT /note="Peptidase A2" FT /evidence="ECO:0000259|PROSITE:PS50175" FT DOMAIN 189..379 FT /note="Reverse transcriptase" FT /evidence="ECO:0000259|PROSITE:PS50878" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AXN89387.1" FT NON_TER 435 FT /evidence="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 //