GenomeNet

Database: UniProt
Entry: Q6BB79_9HIV1
LinkDB: Q6BB79_9HIV1
Original site: Q6BB79_9HIV1 
ID   Q6BB79_9HIV1            Unreviewed;       317 AA.
AC   Q6BB79;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:AAT92427.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:AAT92427.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:AAT92427.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AAT92427.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=00cl4.6 {ECO:0000313|EMBL:AAT92427.1};
RX   PubMed=15767575; DOI=10.1073/pnas.0407534102;
RA   Hue S., Pillay D., Clewley J.P., Pybus O.G.;
RT   "Genetic analysis reveals the complex structure of HIV-1 transmission
RT   within defined risk groups.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:4425-4429(2005).
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; AY670006; AAT92427.1; -; 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; -; 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..317
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAT92427.1"
FT   NON_TER         317
FT                   /evidence="ECO:0000313|EMBL:AAT92427.1"
SQ   SEQUENCE   317 AA;  35990 MW;  8E7B5806C2C67F7D CRC64;
     PQITLWQRPL VTIKIGGQLK EALLDTGADN TVLEDIDLPG RWTPKMIGGI GGFIKVRQYE
     EIPIEICGHK TTGTVLVGPT PVNIIGRDLM TQIGCTLNFP ISPIETVPVK LKPGMDGPKV
     KQWPLTEEKI KALVEICTEL EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
     KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD KEFRKYTAFT IPSMNNETPG
     IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNPDIVIY QYMDDLYVGS DLEIGQHRTK
     IEELRQHLLK WGFYTPD
//
DBGET integrated database retrieval system