ID Q98YC8_9HIV1 Unreviewed; 327 AA.
AC Q98YC8;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 104.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:AAK32617.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AAK32617.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AAK32617.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AAK32617.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12060770; DOI=10.1073/pnas.112177799;
RA Beerenwinkel N., Schmidt B., Walter H., Kaiser R., Lengauer T.,
RA Hoffmann D., Korn K., Selbig J.;
RT "Diversity and complexity of HIV-1 drug resistance: a bioinformatics
RT approach to predicting phenotype from genotype.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8271-8276(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077};
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DR EMBL; AF347541; AAK32617.1; -; 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:InterPro.
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; 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; PTHR33064; POL PROTEIN; 1.
DR PANTHER; PTHR33064:SF35; RIBONUCLEASE H; 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; PS50878; RT_POL; 1.
PE 4: Predicted;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
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};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022750};
KW RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral genome integration {ECO:0000256|ARBA:ARBA00023195};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023195}.
FT DOMAIN 20..89
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 143..327
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAK32617.1"
FT NON_TER 327
FT /evidence="ECO:0000313|EMBL:AAK32617.1"
SQ SEQUENCE 327 AA; 36972 MW; 9BDE086473EE7CAC CRC64;
PQITVWQGPI VTXXIGGQLK EAXXDTGAXX TVLEEMNLPG KWRPKMIGGI GGFIKVRQYD
QXPIEICGHK VVSTXLIGPT PVNVIGRNXM XXLGCTLNFP ISPIETVPVK LKPGMDGPKV
KQWPLTEEKI KALMEICTEL EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
KRTQDXWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD EDFRKYTAFT IPSMNNETPG
IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF XKQNPDLVIY QYVDDLLVGS DLEIGQHXAK
IEELREHLLR WGFYXPDKKH QKEPPFL
//