ID E0WDM7_9HIV1 Unreviewed; 580 AA.
AC E0WDM7;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Gag-pol fusion polyprotein {ECO:0000313|EMBL:CBH29290.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:CBH29290.1};
OS HIV-1 CRF02_AG:08GQ060.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC Human immunodeficiency virus 1; HIV-1 recombinants.
OX NCBI_TaxID=690066 {ECO:0000313|EMBL:CBH29290.1};
RN [1] {ECO:0000313|EMBL:CBH29290.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=08GQ060 {ECO:0000313|EMBL:CBH29290.1};
RA Djoko C.F., Wolfe N.D., Vidal N., Tamoufe U., Montavon C., Lebreton M.,
RA Pike B.L., Fair J., Mbacham W.F., Benito A., Rimoin A.W., Saylors K.,
RA Mpoudi-Ngole E., Grillo M.P., Peeters M.;
RT "HIV Type 1 pol Gene Diversity and Genotypic Antiretroviral Drug Resistance
RT Mutations in Malabo, Equatorial Guinea.";
RL AIDS Res. Hum. Retroviruses 26:1027-1031(2010).
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; FN557327; CBH29290.1; -; 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 Gene3D; 3.30.70.270; -; 3.
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; IPR010659; RVT_connect.
DR InterPro; IPR010661; RVT_thumb.
DR PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1.
DR PANTHER; PTHR41694:SF5; RIBONUCLEASE H; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF06815; RVT_connect; 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 Virus entry into host cell {ECO:0000256|ARBA:ARBA00023195};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 76..145
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 199..389
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 13..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CBH29290.1"
FT NON_TER 580
FT /evidence="ECO:0000313|EMBL:CBH29290.1"
SQ SEQUENCE 580 AA; 66371 MW; 7CE72DE9383FCDAE CRC64;
FFRENLAFQQ GEARKFSSEQ TGTNSPTSRE LWDXGRDNLL SEAGTGGQGT ISSLNFPQIT
LWQRPLVTVR IGGQLIEALL DTGADDTVLE EINLLGKWKP KMIGGIGGFI KVRQYDQIPI
EICGKKAIGT VLVGPTPVNI IGRNMLTQIG CTLNFPISPI ETVPVKLKPG MDGPKVKQWP
LTEEKIRALT EICTDMEKEG KISRIGPENP YNTPVFAIKK KDSTKWRKLV DFRELNKRTQ
DFWEVQLGIP HPAGLKKKKS VTVLDVGDAY FSVPLDKDFR KYTAFTIPSV NNETPGIRYQ
YNVLPQGWKG SPAIFQASMT KILEPFRIKN PEIVIYQYMD DLYVGSDLEI GQHRAKIEEL
REHLLTWGFT TPDKKHQKEP PFLWMGYELH PDKWTVQPIQ LPEKDSWTVN DIQKLVGKLN
WASQIHAGIK VKQLCKLLRG AKALTDIVTL TEEAELELAE NREILKEPVH GVYYDPTKDL
VAEIQKQGQD QWTYQIYQEP FKNLKTGKYA KRRTAHTNDV KQLAAVVQKV AIESIVIWGK
TPKFRLPIQR ETWETWWTEY WQATWIPEWE FVNTPPLVKL
//
