ID B7TEF5_9HIV1 Unreviewed; 935 AA.
AC B7TEF5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ACJ25612.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ACJ25612.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ACJ25612.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACJ25612.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1199 {ECO:0000313|EMBL:ACJ25612.1};
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:ACJ25612.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1199 {ECO:0000313|EMBL:ACJ25612.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ199552; ACJ25612.1; -; Genomic_DNA.
DR MEROPS; A02.001; -.
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: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:0008270; F:zinc ion binding; 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 CDD; cd01645; RT_Rtv; 1.
DR Gene3D; 1.10.10.200; -; 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; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR017856; Integrase-like_N.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR003308; Integrase_Zn-bd_dom_N.
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:SF3; RNA-DIRECTED DNA POLYMERASE-RELATED; 1.
DR Pfam; PF02022; Integrase_Zn; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF00665; rve; 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; SSF46919; N-terminal Zn binding domain of HIV integrase; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50876; ZF_INTEGRASE; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
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 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:ARBA00023296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00450}.
FT DOMAIN 72..141
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 195..385
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 585..708
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT DOMAIN 714..755
FT /note="Integrase-type"
FT /evidence="ECO:0000259|PROSITE:PS50876"
FT DOMAIN 765..915
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 10..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACJ25612.1"
FT NON_TER 935
FT /evidence="ECO:0000313|EMBL:ACJ25612.1"
SQ SEQUENCE 935 AA; 105962 MW; 3ACCE7E2F8DFFA6C CRC64;
FFRENLAFPE GEAREFPSEQ TRANSPTSRE LQIRGDNPRS EAGAERQGTL NFPQITLWQR
PLVSIKVGGQ IKEALLDTGA DDTVLEEINL PGKWKPKMIG GIGGFIKVRQ YDQILIEICG
KKAIGTVLVG PTPVNIIGRN MLTQLGCTLN FPISPIETVP VKLKPGMDGP KVKQWPLTEE
KIKALTAICE EMEKEGKITK IGPDNPYNTP VFAIKKKDST KWRKLVDFRE LNKRTQDFWE
VQLGIPHPAG LKKKKSVTVL DVGDAYFSVP LDKDFRKYTA FTIPSINNET PGIRYQYNVL
PQGWKGSPAI FQCSMTKILE PFRAKNPEIV IYQYMDDLYV GSDLEIGQHR AKIEELRGHL
LKWGFTTPDK KHQKEPPFLW MGYELHPDKW TVQPIQLPEK DSWTVNDIQK LVGKLNWASQ
IYPGIKVKHL CKLLRGAKAL TEIVPLTEEA ELELAENREI LKEPVHGVYY DPSKDLIAEI
QKQGNDQWTY QIYQEPFKNL KTGKYAKRRT AHTNDVKQLT EAVQKIAMES IVIWGKTPKF
RLPIQKETWE TWWTDYWQAT WIPEWEFVNT PPLVKLWYQL EKEPIAGAET FYVDGAANRE
TKMGKAGYVT DRGRQKIVPL TETTNQKTEL QAIQLALQDS GSEVNIVTDS QYALGIIQAQ
PDKSESELVN QIIEQLIKKE RVYLSWVPAH KGIGGNEQVD KLVSSGIRKV LFLDGIDKAQ
EEHEKYHSNW RAMASEFNLP PIVAKEIVAS CDKCQLKGEA IHGQVDCSPG IWQLDCTHLE
GKVILVAVHV ASGYIEAEVI PAETGQETAY YILKLAGRWP VKVIHTDNGS NFTSAAVKAA
CWWAGIQQEF GIPYNPQSQG VVESMNKELK KIIGQVRDQA EHLRTAVQMA VFIHNFKRKG
GIGGYSAGER IIDIIATDIQ TKELQKQIIN IQKFR
//
