ID G0YBR9_9HIV1 Unreviewed; 434 AA.
AC G0YBR9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:AEJ85173.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AEJ85173.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AEJ85173.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AEJ85173.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=36221 {ECO:0000313|EMBL:AEJ85173.1};
RA Kao C.-F., Fu T.-Y., Yang J.-Y.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEJ85173.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=36221 {ECO:0000313|EMBL:AEJ85173.1};
RX PubMed=21235402; DOI=10.1089/aid.2010.0244;
RA Kao C.F., Chang S.Y., Hsia K.T., Chang F.Y., Yang C.H., Liu H.R., Fu T.Y.,
RA Yang J.Y.;
RT "Surveillance of HIV Type 1 Recent Infection and Molecular Epidemiology
RT Among Different Risk Behaviors Between 2007 and 2009 After the HIV Type 1
RT CRF07_BC Outbreak in Taiwan.";
RL AIDS Res. Hum. Retroviruses 27:745-749(2011).
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; HQ657903; AEJ85173.1; -; 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 CDD; cd01645; RT_Rtv; 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:AEJ85173.1"
FT NON_TER 434
FT /evidence="ECO:0000313|EMBL:AEJ85173.1"
SQ SEQUENCE 434 AA; 49346 MW; 8029EB2FF2C736C0 CRC64;
PQITLWQRPV VTIRIGGQLR EALLDTGADD TVLEEINLPG RWKPKMIGGI GGFIKVRQYD
QVPIEICGHT ATGTVLVGPT PVNIIGRNLL TQLGCTLNFP ISPIDTVPVK LKPGMDGPKV
KQWPLTEEKI KALVEICTEM EKEGKISKIG PENPYNTPIF AIKKKDSTKW RKLVDFRELN
KRTQDFWEVQ LGIPHPAGLQ KRKSVTVLDV GDAYFSVPLD KEFRKYTAFT IPSINNETPG
IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNPDIVIY QYMDDLYVAS DLEIGQHRTK
VEELRXHLXK WGLTTPDKKH QKEPPFLWMG YELHPDKWTV QPIELPEKDS WTVNDIQKLV
GKLNWASQIY XGIKVKQLCK LLRGTKALTE VVPLTAEAEL ELAENREILK EPVYGVYYDP
SKELIAEIQK QGLG
//
