ID C9DKA7_9HIV1 Unreviewed; 397 AA.
AC C9DKA7;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ACW57640.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ACW57640.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ACW57640.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACW57640.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3f0Av5AoFu9RFB8 {ECO:0000313|EMBL:ACW57640.1};
RX PubMed=19835478; DOI=10.1086/644505;
RA Vercauteren J., Wensing A.M., van de Vijver D.A., Albert J., Balotta C.,
RA Hamouda O., Kucherer C., Struck D., Schmit J.C., Asjo B., Bruckova M.,
RA Camacho R.J., Clotet B., Coughlan S., Grossman Z., Horban A., Korn K.,
RA Kostrikis L., Nielsen C., Paraskevis D., Poljak M., Puchhammer-Stockl E.,
RA Riva C., Ruiz L., Salminen M., Schuurman R., Sonnerborg A., Stanekova D.,
RA Stanojevic M., Vandamme A.M., Boucher C.A.;
RT "Transmission of drug-resistant HIV-1 is stabilizing in Europe.";
RL J. Infect. Dis. 200:1503-1508(2009).
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; GQ399474; ACW57640.1; -; 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; -; 2.
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; IPR010661; RVT_thumb.
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 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 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 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:ACW57640.1"
FT NON_TER 397
FT /evidence="ECO:0000313|EMBL:ACW57640.1"
SQ SEQUENCE 397 AA; 45361 MW; E716E252E695C7B2 CRC64;
PQITLWQRPL VNIKIGGQLR EALLDTGADD TVLEEIDLPG RWKPKMIGGI GGFIKVRQYD
QVPIEICGHK TXGTVLIGPT PVNIIGRNLL TQLGCTLNFP ISPIETVPVK LKPGMDGPKV
KQWPLTEEKI KALVEICTEM EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD EEFRKYTAFT IPSTNNETPG
MRYQYNVLPQ GWKGSPAIFQ CSMTKILEPF RKQNPDIVIY QYMDDLYVGS DLEIXQHRAK
IEELRQHLLK WGFTTPDKKH QKDPPFLWMG YELHPDKWTV QPIVLPEKDS WTVNDIQKLV
GKLNWASQIY PGIKVRQLCK LLRGXKSLTE VIPLTXE
//
