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Database: UniProt
Entry: C8BUI0_9HIV1
LinkDB: C8BUI0_9HIV1
Original site: C8BUI0_9HIV1 
ID   C8BUI0_9HIV1            Unreviewed;       381 AA.
AC   C8BUI0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:ACU67568.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:ACU67568.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ACU67568.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ACU67568.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1003-103001p-46a {ECO:0000313|EMBL:ACU67568.1};
RX   PubMed=19116249; DOI=10.1128/JVI.01960-08;
RA   Kearney M., Maldarelli F., Shao W., Margolick J.B., Daar E.S.,
RA   Mellors J.W., Rao V., Coffin J.M., Palmer S.;
RT   "Human immunodeficiency virus type 1 population genetics and adaptation in
RT   newly infected individuals.";
RL   J. Virol. 83:2715-2727(2009).
CC   -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC       {ECO:0000256|RuleBase:RU004064}.
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DR   EMBL; GQ286960; ACU67568.1; -; 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   CDD; cd01645; RT_Rtv; 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          59..128
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   DOMAIN          182..372
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACU67568.1"
FT   NON_TER         381
FT                   /evidence="ECO:0000313|EMBL:ACU67568.1"
SQ   SEQUENCE   381 AA;  43101 MW;  4FDED61A10536C0A CRC64;
     SEQTRANSPT SRELQVWGGD NNSPTEAGAD RQGDVSFGFP QITLWQRPLV TVKIGGQLRE
     ALLDTGADDT VLEEINLPGK WKPKMIGGIG GFIKVKQYDQ IPIEICGHKA EGTVLVGPTP
     VNIIGRNLLT QIGCTLNFPI SPIETVPVKL KPGMDGPKVK QWPLTEEKIK ALVEICTEME
     KEGKISKIGP ENPYNTPVFA IKKKDSTKWR KLVDFRELNK KTQDFWEVQL GIPHPAGLKK
     KKSVTVLDVG DAYFSVPLDK DFRKYTAFTI PSINNETPGI RYQYNVLPQG WKGSPAIFQS
     SMTKILEPFR KQNPDIVIYQ YMDDLYVGSD LEIGQHRAKI EELRQHLLRW GFTTPDKKHQ
     KEPPFLWMGY ELHPDKWTVQ P
//
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