ID B7TF47_9HIV1 Unreviewed; 673 AA.
AC B7TF47;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ACJ25854.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ACJ25854.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ACJ25854.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACJ25854.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PS450 {ECO:0000313|EMBL:ACJ25854.1};
RX PubMed=18596105; DOI=10.1128/JVI.00580-08;
RA Matthews P.C., Prendergast A., Leslie A., Crawford H., Payne R.,
RA Rousseau C., Rolland M., Honeyborne I., Carlson J., Kadie C., Brander C.,
RA Bishop K., Mlotshwa N., Mullins J.I., Coovadia H., Ndung'u T., Walker B.D.,
RA Heckerman D., Goulder P.J.;
RT "Central role of reverting mutations in HLA associations with human
RT immunodeficiency virus set point.";
RL J. Virol. 82:8548-8559(2008).
RN [2] {ECO:0000313|EMBL:ACJ25854.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PS450 {ECO:0000313|EMBL:ACJ25854.1};
RA Matthews P., Prendergast A., Goulder P.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
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; FJ199837; ACJ25854.1; -; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; 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:0046718; P:viral entry into host cell; 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 Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
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; PF00075; RNase_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 SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50879; RNASE_H_1; 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:ARBA00022908};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
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:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022670, 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:ARBA00023296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 72..141
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 195..377
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 567..673
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 12..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACJ25854.1"
FT NON_TER 673
FT /evidence="ECO:0000313|EMBL:ACJ25854.1"
SQ SEQUENCE 673 AA; 76950 MW; 4BBBAC3D39F2961D CRC64;
FFRENLAFPQ GKAREFPSEQ TRANSPTSRE LPVQGDNPHS EAGAARQGTL NFPQITLWQR
PLVSIKVGGQ IREALLDTGA DDTVLEDINL PGKWKPKMIG GIGGFIKVRQ YDQIVIEICG
KKAIGTVLVG PTPVNIIGRN MLTQLGCTLN FPISPIETVP VKLKPGMDGP KVKQWPLTEE
KIKALTAICE EMEKEGKITK IGPENPYNTP IFAIKKKDST KWRKLVDFRE LNKRTQDFWE
VQLGIPHPAG LKKKKSVTVL DVGDAYFSVP LDEGFRKYTA FTIPSINNET PGIRYQYNVL
PQGWKGSPAX LEPFRTQNPD IVIYQYMDDL YVGSDLEIGQ HRAKIEELRA HLLKWGFTTP
DKKHQKEPPF LWMGYELHPD KWTVQPIKLP EKESWTVNDI QKLVGKLNWA SQIYPGIKVR
QLCKLLXLTE EAELELAENR EILREPVHGV YYDPSKDLIA EIQKQGDDQW TYQIYQEPFK
NLKTGKYAKR RTAHTNDVKQ LTEAVQKIAT ESIVIWGKTP KFRLPIQKET WEIWWTDYWQ
ATWIPEWEFV NTPPLVKLWY QLEKEPIAEA ETFYVDGAAN RETKIGKAGY VTDRGRQKIV
SLHETTNQKA ELQAIQLALQ DSGSEVNIVT DSQYALGIIQ AQPDKSDSEL VNQIIEQLIN
KERVYLSWVP AHK
//
