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Database: UniProt
Entry: C4NDP5_9HIV1
LinkDB: C4NDP5_9HIV1
Original site: C4NDP5_9HIV1 
ID   C4NDP5_9HIV1            Unreviewed;       328 AA.
AC   C4NDP5;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:ACQ72396.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:ACQ72396.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ACQ72396.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ACQ72396.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B305 {ECO:0000313|EMBL:ACQ72396.1};
RA   Kawashima Y., Pfafferott K., Frater J., Matthews P., Payne R., Addo M.,
RA   Gatanaga H., Fujiwara M., Hachiya A., Koizumi H., Kuse N., Oka S., Duda A.,
RA   Prendergast A., Crawford H., Leslie A., Brumme Z., Brumme C., Allen T.,
RA   Brander C., Kaslow R., Tang J., Hunter E., Allen S., Mulenga J., Branch S.,
RA   Roach T., John M., Mallal S., Ogwu A., Shapiro R., Prado J.G., Fidler S.,
RA   Weber J., Pybus O.G., Klenerman P., Ndung'u T., Phillips R., Heckerman D.,
RA   Harrigan P.R., Walker B.D., Takiguchi M., Goulder P.;
RT   "Adaptation of HIV-1 to human leukocyte antigen class I.";
RL   Nature 458:641-645(2009).
CC   -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC       {ECO:0000256|RuleBase:RU004064}.
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DR   EMBL; FJ498478; ACQ72396.1; -; 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          78..147
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   DOMAIN          201..328
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   REGION          8..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACQ72396.1"
FT   NON_TER         328
FT                   /evidence="ECO:0000313|EMBL:ACQ72396.1"
SQ   SEQUENCE   328 AA;  36691 MW;  CAF8BA0E3B40184E CRC64;
     FFRENLAFPQ GKAREFPPEQ TRANSPTRAN SSTSRELQVR GDNSRSEAGA ERQGTLNFPQ
     ITLWQRPLVS IKVGGQIKEA LLDTGADDTV LEEINLPGKW KPKMIGGIGG FIKVRQYDQI
     LIEICGKKAI GAVLVGPTPV NIIGRNMLTQ LGCTLNFPIS PIETVPVKLK PGMDGPKVKQ
     WPLTEEKIKA LKEICDEMEK EGKITKIGPE NPYNTPVFAI KKKDSTKWRK LVDFRELNKR
     TQDFWEVQLG IPHPAGLKKK KSVTVLDVGD AYFSVPLDES FRKYTAFTIP SINNETPGIR
     YXYNVLPQGW KGSPAIFQAS MTKILEPF
//
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