GenomeNet

Database: UniProt
Entry: Q9EH43_9HIV1
LinkDB: Q9EH43_9HIV1
Original site: Q9EH43_9HIV1 
ID   Q9EH43_9HIV1            Unreviewed;       328 AA.
AC   Q9EH43;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:AAF91972.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:AAF91972.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:AAF91972.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AAF91972.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=038B07a {ECO:0000313|EMBL:AAF91972.1};
RX   PubMed=10952598; DOI=10.1128/AAC.44.9.2475-2484.2000;
RA   Bacheler L.T., Anton E.D., Kudish P., Baker D., Bunville J., Krakowski K.,
RA   Bolling L., Aujay M., Wang X.V., Ellis D., Becker M.F., Lasut A.L.,
RA   George H.J., Spalding D.R., Hollis G., Abremski K.;
RT   "Human immunodeficiency virus type 1 mutations selected in patients failing
RT   efavirenz combination therapy.";
RL   Antimicrob. Agents Chemother. 44:2475-2484(2000).
RN   [2] {ECO:0000313|EMBL:AAF91972.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=038B07a {ECO:0000313|EMBL:AAF91972.1};
RA   Abremski K.E., Bacheler L.T., Li J.;
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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; AY001631; AAF91972.1; -; Genomic_RNA.
DR   PIR; S32058; S32058.
DR   MEROPS; A02.001; -.
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..328
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAF91972.1"
FT   NON_TER         328
FT                   /evidence="ECO:0000313|EMBL:AAF91972.1"
SQ   SEQUENCE   328 AA;  37459 MW;  C706AF033FC50E47 CRC64;
     PQITLWQRPL VTVKIGGQLK EALLDTGADD TVLEEMNLPG RWKPKMIGGI GGFIKVRQYD
     QIPIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP ISPIETVPVK LKPGMDGPKV
     KQWPLTEEKI KALMEICTEM EKEGKISKIG PENPYNTPVF AIKKKNSTRW RKLVDFRELN
     KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD KEFRKYTAFT IPSINNETPG
     IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNPDIVIY QYVDDLYVGS DLEIGQHRTK
     IEELRQHLLR WGFYTPDEKH QKEPPFLW
//
DBGET integrated database retrieval system