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Database: UniProt
Entry: H9CZJ3_9PLVG
LinkDB: H9CZJ3_9PLVG
Original site: H9CZJ3_9PLVG 
ID   H9CZJ3_9PLVG            Unreviewed;       373 AA.
AC   H9CZJ3;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:AFD62149.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:AFD62149.1};
OS   Human immunodeficiency virus.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC   Primate lentivirus group.
OX   NCBI_TaxID=12721 {ECO:0000313|EMBL:AFD62149.1};
RN   [1] {ECO:0000313|EMBL:AFD62149.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=111277910-271210CY {ECO:0000313|EMBL:AFD62149.1};
RX   PubMed=22559065; DOI=10.1089/aid.2012.0040;
RA   Yabar C.A., Acuna M., Gazzo C., Salinas G., Cardenas F., Valverde A.,
RA   Romero S.;
RT   "New Subtypes and Genetic Recombination in HIV Type 1-Infecting Patients
RT   with Highly Active Antiretroviral Therapy in Peru (2008-2010).";
RL   AIDS Res. Hum. Retroviruses 28:1712-1722(2012).
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}.
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DR   EMBL; JQ430989; AFD62149.1; -; Genomic_RNA.
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; RNA-DIRECTED DNA POLYMERASE-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-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004064};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022771};
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   Viral release from host cell {ECO:0000256|ARBA:ARBA00023113};
KW   Virion maturation {ECO:0000256|ARBA:ARBA00023113};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023195};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
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   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFD62149.1"
FT   NON_TER         373
FT                   /evidence="ECO:0000313|EMBL:AFD62149.1"
SQ   SEQUENCE   373 AA;  42542 MW;  45C4D88535112D61 CRC64;
     PQITLWQRPF VTVKVGGLLR EALLDTGADD TIFQDINLPG KWTPKMVGGI GGFLKVRQYD
     QVPIEIXGHK AICPVLVGPT PVNVLGRNLM TQIGCTLNFP ISSIETVPVK LKPGMDGPKV
     KQWPLTEEKI KALTEICTEM EKEGKISKIG PENPYNTPVF AIKKKNGTKW RKVVDFRELN
     KRTQDFWEVQ LGIPHPAGLK RNKSVTVLDV GDAYFSIPLX KEFRKYTAFT IPSINNETPG
     TRYQYNVLPQ GWKGSPAIFQ NSMTKILEPF RKRNPDLVIY QYVDDLYVGS DLEIGQHRTK
     IEELREHLLR WGLVTPDEKH QKEPPFLWMG YELHPDKWTV QPIKLPEKDS WTXNDIQKLV
     GKLNWASQIY AGI
//
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