GenomeNet

Database: UniProt
Entry: D0UCW2_9HIV1
LinkDB: D0UCW2_9HIV1
Original site: D0UCW2_9HIV1 
ID   D0UCW2_9HIV1            Unreviewed;       333 AA.
AC   D0UCW2;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 2.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:ACY42114.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:ACY42114.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ACY42114.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ACY42114.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=96122 {ECO:0000313|EMBL:ACY42114.1};
RX   PubMed=19779560; DOI=10.1371/journal.ppat.1000590;
RA   Hughes G.J., Fearnhill E., Dunn D., Lycett S.J., Rambaut A.,
RA   Leigh Brown A.J.;
RT   "Molecular phylodynamics of the heterosexual HIV epidemic in the United
RT   Kingdom.";
RL   PLoS Pathog. 5:E1000590-E1000590(2009).
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; GQ462487; ACY42114.1; -; 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; -; 1.
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   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   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   UNSURE          19
FT                   /note="I or L"
FT                   /evidence="ECO:0000313|EMBL:ACY42114.1"
FT   UNSURE          268
FT                   /note="E or Q"
FT                   /evidence="ECO:0000313|EMBL:ACY42114.1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACY42114.1"
FT   NON_TER         333
FT                   /evidence="ECO:0000313|EMBL:ACY42114.1"
SQ   SEQUENCE   333 AA;  37946 MW;  25BDE77AE2053001 CRC64;
     PQITLWQRPL VTIKXEGQLK EALLDTGADD TVLEEINLPG KWKPKMIGGI GGFIKVRQYE
     QILIEICGKK AIGTVLVGPT PVNIIGRNML TQLGCTLNFP ISPIETVPVK LKPGMDGPKV
     KQWPLTEEKI KALTXICEEM EKEGKITKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
     KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD ENFRKYTAFT IPSINNATPG
     XRYQYNVLPQ GWKGSPAIXQ SSMTKILEPF RTKNPDIVIY QYMDDLYVXS DLEIGQHRXK
     VEELREHLLR WGITTPDKKH QKEPPFLWMG YEL
//
DBGET integrated database retrieval system