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}.
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; 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
//