ID A0F6M6_9HIV1 Unreviewed; 499 AA.
AC A0F6M6;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ABJ94079.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ABJ94079.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ABJ94079.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ABJ94079.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1182.48-4204-20030723 {ECO:0000313|EMBL:ABJ94079.1};
RX PubMed=16928764; DOI=10.1128/JVI.00712-06;
RA Baxter J.D., Schapiro J.M., Boucher C.A., Kohlbrenner V.M., Hall D.B.,
RA Scherer J.R., Mayers D.L.;
RT "Genotypic changes in human immunodeficiency virus type 1 protease
RT associated with reduced susceptibility and virologic response to the
RT protease inhibitor tipranavir.";
RL J. Virol. 80:10794-10801(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different
CC cleavage modes: 1. sequence-specific internal cleavage of RNA. Human
CC immunodeficiency virus type 1 and Moloney murine leukemia virus
CC enzymes prefer to cleave the RNA strand one nucleotide away from the
CC RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides
CC from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides
CC away from the primer terminus.; EC=3.1.26.13;
CC Evidence={ECO:0000256|ARBA:ARBA00023415};
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000256|RuleBase:RU004064}.
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DR EMBL; DQ878436; ABJ94079.1; -; 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 Gene3D; 3.30.70.270; -; 3.
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 InterPro; IPR010659; RVT_connect.
DR InterPro; IPR010661; RVT_thumb.
DR PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1.
DR PANTHER; PTHR41694:SF5; RIBONUCLEASE H; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF06815; RVT_connect; 1.
DR Pfam; PF06817; RVT_thumb; 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 Virus entry into host cell {ECO:0000256|ARBA:ARBA00023195};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 20..89
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 143..333
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABJ94079.1"
FT NON_TER 499
FT /evidence="ECO:0000313|EMBL:ABJ94079.1"
SQ SEQUENCE 499 AA; 57148 MW; DEC4FB7D9CA91F33 CRC64;
PQITLWQRPI VTIRIGGQLI EALLDTGADD TVLEEMNLPG RWKPKIVGGI GGFVKVKQYD
QIPIEICGHK XLSTVLVGPT PVNVXGRNVM TQLGCTLNFP ISPIETVPVK LKPGMDGPKV
KQWPLTEEKI KALVEICXEL EEAGKISKIG PENPYNTPVF AIKKKNSTKW RKVVDFRELN
KRTQDFWEVQ LGIPHPAGLE KKKSVTVLDV GDAYFSIPLD EEFRKYTAFT IPSINNETPG
VRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNPEIVIY QYVDDLYXSS DLEIEQHRAK
IDELRQYLWK WGFYTPDRKH QKEPPFLWMG YELHPEKWTV QPIVLPEKDS WTVNDIQKLV
GKLNWASQIY PGIKVKQLCK LLRGAKALTE VIPLTKEAEL ELAENREILK EPVHGVYYDP
SKXLIAEIQK QGQGQWTYQI YQDPFKNLKT GKYARTRGAH TNDVKQLTEV VQKIATESIV
IWGKTPKFRL PIQKETWGS
//
