GenomeNet

Database: UniProt
Entry: Q9EIW9_9HIV1
LinkDB: Q9EIW9_9HIV1
Original site: Q9EIW9_9HIV1 
ID   Q9EIW9_9HIV1            Unreviewed;       328 AA.
AC   Q9EIW9;
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:AAF88909.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:AAF88909.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:AAF88909.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AAF88909.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=000A06n {ECO:0000313|EMBL:AAF88909.1};
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:AAF88909.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=000A06n {ECO:0000313|EMBL:AAF88909.1};
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}.
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DR   EMBL; AY001004; AAF88909.1; -; Genomic_RNA.
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:AAF88909.1"
FT   NON_TER         328
FT                   /evidence="ECO:0000313|EMBL:AAF88909.1"
SQ   SEQUENCE   328 AA;  37256 MW;  BB5517D72015F085 CRC64;
     PQITLWQRPL VTIKIGGQLR EALLDTGADD TVLEEMDLPG RWKPKMIGGI GGFIKVKQYD
     QIPIEICGHK VIGTVLVGPT PVNIIGRNLL TQLGCTLNFP ISPIETVPVK LKPGMDGPKV
     KQWPLTEEKI KALVEICTEM EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
     KKTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD KDFRKYTAFT IPSVNNETPG
     IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RQQNPEIVIY QYMDDLYVGS DLEIGQHGTK
     IEELRNHLLR WGFTTPDKKH QKEPPFLW
//
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