ID A0F6W0_9HIV1 Unreviewed; 499 AA.
AC A0F6W0;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ABJ94188.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ABJ94188.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ABJ94188.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ABJ94188.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1182.48-5011-20040722 {ECO:0000313|EMBL:ABJ94188.1};
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};
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DR EMBL; DQ878545; ABJ94188.1; -; 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:InterPro.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
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; 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..333
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABJ94188.1"
FT NON_TER 499
FT /evidence="ECO:0000313|EMBL:ABJ94188.1"
SQ SEQUENCE 499 AA; 57229 MW; E09D6F929583C8F8 CRC64;
PQITLWQRPI ITVKIGGQLR EVLMDTGADD TVLEDINLPG RWKPKIVGGI GGFVXVKQYD
EVPIEICGHK TVGTVLVGPT PVDVIGRNLL SQIGCTLNFP ISPIETVPVK LKPGMDGPKV
KQWPLTEEKI KALVEICTEL EEDGKISKIG PENPYNTPVF AIKKKNSDKW RKVADFRELN
KRTQDFWEVQ LGIPHPAGLQ KKKSVTILDV GDAYFSIPLH EDFRKYTAFT IPSINNETPG
IRYQYNVLPQ GWKGSPAIFQ CSMTKILEPF KKQNPEIVIC QYMDDLYVAS DLEIGQHRTK
IEELRQHLWK WGFYTPDRKY QKEPPFLWMG YELHPDKWTV QPIVLPEKDS WTXNDIQKLV
GKLNWASQIY PGIKVKQLCK LLRGTKSLTE VVPLTEEAEL ELAENREILK EPVHGVYYDP
SKDLIAEIQK QGEGQWTYQI YQEEHKNLKT GKYAKMRSTH TNDIKQLTEA VQKIATESIV
IWGKTPKFRL PIQKETWDT
//
