ID G8GIJ5_9HIV1 Unreviewed; 450 AA.
AC G8GIJ5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:AER92959.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AER92959.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AER92959.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AER92959.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HIV101664 {ECO:0000313|EMBL:AER92959.1};
RG PharmAccess African Studies to Evaluate Resistance (PASER);
RA Sigaloff K.C.E.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AER92959.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HIV101664 {ECO:0000313|EMBL:AER92959.1};
RX PubMed=22448003; DOI=10.1093/infdis/jis261;
RG the PharmAccess African Studies to Evaluate Resistance (PASER);
RA Sigaloff K.C., Hamers R.L., Wallis C.L., Kityo C., Siwale M., Ive P.,
RA Botes M.E., Mandaliya K., Wellington M., Osibogun A., Stevens W.S.,
RA van Vugt M., Rinke de Wit T.F.;
RT "Second-line antiretroviral treatment successfully resuppresses drug-
RT resistant HIV-1 after first-line failure: prospective cohort in Sub-Saharan
RT Africa.";
RL J. Infect. Dis. 205:1739-1744(2012).
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; JN132276; AER92959.1; -; 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 41..110
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 164..354
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AER92959.1"
FT NON_TER 450
FT /evidence="ECO:0000313|EMBL:AER92959.1"
SQ SEQUENCE 450 AA; 51016 MW; B8142BB84CE40E1B CRC64;
GGGNTLSETG AEGEGNVSFX FPQITLWQRP VVTVKIEGQL KEALLDTGAD DTVLEDINLP
GKWKPKMIGG IGGFIKVKQY DQISIEICGK KAIGTVLVGP TPVNIIGRNM LTQIGCTLNF
PISPIETVPV KLKPGMDGPK VKQWPLTEEK IKALTEICTD MEKEGKISRI GPENPYNTPI
FAIKKKDSTK WRKLVDFREL NKRTQDFWEV QLGIPHPAGL KKKKSVTILD VGDAYFSVPL
DKEFRKYTAF TIPSTNNETP GIRYQYNVLP QGWKGSPAIF QSSMTKILEP FRKQNPEIVI
CQYVDDLYVG SDLEIGQHRT KIEELREHLL KWGFYTPDKK HQKEPPFLWM GYELHPDKWT
VQPIKLPEKE SWTVNDIQKL VGKLNWASQI YPGIKVRQLC KCLRGTKALT EVVPLTQEAE
LELSENREIL REPVHLVYYD PSKDLIAVNQ
//
