ID C9DN12_9HIV1 Unreviewed; 413 AA.
AC C9DN12;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ACW58595.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ACW58595.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ACW58595.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACW58595.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=9KQheN2T7TzvVkU {ECO:0000313|EMBL:ACW58595.1};
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; GQ400538; ACW58595.1; -; 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 UNSURE 10
FT /note="I or L"
FT /evidence="ECO:0000313|EMBL:ACW58595.1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACW58595.1"
FT NON_TER 413
FT /evidence="ECO:0000313|EMBL:ACW58595.1"
SQ SEQUENCE 413 AA; 47073 MW; 7C2DCEE491F333DE CRC64;
PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEISLPG RWKPKMIGGI GGFIKVRQYD
XXXIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP ISPIETXPVK LKPGMDGPKV
KQWPLTEEKI KALXEICTEM EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLXDFRELN
KKTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD KEFRKYTAFT IPSINNETPG
IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNPEIVIY QYMDDLYVGS DLEIGQHRTK
IEELRQHLLR WGFTTPDKKH QKEPPFLWMG YELHPDKWTV QPIQLPEKDS WTVNDIQKLV
GKLNWASQIY AGIKVKQLCK LLRGXKALTE VVPLTKEAEI ELAENREILK EPV
//
