ID G8GIM6_9HIV1 Unreviewed; 459 AA.
AC G8GIM6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:AER92990.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AER92990.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AER92990.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AER92990.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HIV102945 {ECO:0000313|EMBL:AER92990.1};
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:AER92990.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HIV102945 {ECO:0000313|EMBL:AER92990.1};
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; JN132323; AER92990.1; -; 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 73..142
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 196..386
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AER92990.1"
FT NON_TER 459
FT /evidence="ECO:0000313|EMBL:AER92990.1"
SQ SEQUENCE 459 AA; 51856 MW; 72D89007529A6D4C CRC64;
TAEPIVRGRS RKFSPERIGA NSPTSRDLRD GGRDSPPPEA GAEGQGTXLT FSFPQITLWQ
RPLVTVKIGG QLREALLDTG ADDTVLEEID LPGKWKPKMI GGIGGFIKVK QYDQVPIEIC
GKKAIGAVLV GPTPVNIIGR NMLTQIGCTL NFPISPIETV PVKLKPGMDG PKVKQWPLTE
EKIKALTEIC TELEREGKIS KIGPENPYNT PIFAIKKKDS TKWRKLXDFR ELNKRTQDFW
EVQLGIPHPG GLKKNKSVTV LDVGDAYFSV PLHESFRKYT AFTIPSTNNE TPGIRYQYNV
LPQGWKGSPA IFQSSMTKIL EPFRSRNPEI IIYQYVDDLY VASDLEIGQH RAKIEELRAH
LWKWGFYTPD KKHQKEPPFL WMGYELHPDK WTVQPIQLPE KESWTVNDIQ KLVGKLNWAS
QIYAGIKVKQ LCKLLRGAKS LTEVVTMTRE AELELAENR
//
