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Database: UniProt
Entry: C4NDF5_9HIV1
LinkDB: C4NDF5_9HIV1
Original site: C4NDF5_9HIV1 
ID   C4NDF5_9HIV1            Unreviewed;       326 AA.
AC   C4NDF5;
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:ACQ72306.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:ACQ72306.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ACQ72306.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ACQ72306.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B169 {ECO:0000313|EMBL:ACQ72306.1};
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; FJ498374; ACQ72306.1; -; 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          80..149
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   DOMAIN          203..326
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   REGION          8..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACQ72306.1"
FT   NON_TER         326
FT                   /evidence="ECO:0000313|EMBL:ACQ72306.1"
SQ   SEQUENCE   326 AA;  36146 MW;  091CE416AC2BE91C CRC64;
     FFRENLAFPQ GEAGKFSSEQ TRANSPTSRA NSPSSREFQV RGDNSRSEAG AEGQGNTLNF
     PQITLWQRPL VSIKVGGQIK EALLDTGADD TVLEDINLPG KWKPRMIGGI GGFIKVRQYE
     EIPIEICGKK AIGTVLVGPT PVNIIGRNIL TQLGCTLNFP ISSIKTVPVK LKPGMDGPKV
     KQWPLTEEKI KALTAICEEM EKEGKITKIG PENPYNTPIF AIKKKDSTKW RKLVDFRELN
     XRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSIPLD ESFRKYTAFT IPSINNATPG
     IRYQYNVLPQ GWKGSPAIFQ SSMTKI
//
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