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ADDB_GEOTN
ID   ADDB_GEOTN              Reviewed;        1167 AA.
AC   A4IKW6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01452};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01452};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01452};
DE   AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000255|HAMAP-Rule:MF_01452};
GN   Name=addB {ECO:0000255|HAMAP-Rule:MF_01452}; OrderedLocusNames=GTNG_0588;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC   -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC       and an ATP-dependent, dual-direction single-stranded exonuclease.
CC       Recognizes the chi site generating a DNA molecule suitable for the
CC       initiation of homologous recombination. The AddB nuclease domain is not
CC       required for chi fragment generation; this subunit has 5' -> 3'
CC       nuclease activity. {ECO:0000255|HAMAP-Rule:MF_01452}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP-
CC       Rule:MF_01452}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01452}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABO65970.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000557; ABO65970.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A4IKW6; -.
DR   SMR; A4IKW6; -.
DR   STRING; 420246.GTNG_0588; -.
DR   EnsemblBacteria; ABO65970; ABO65970; GTNG_0588.
DR   KEGG; gtn:GTNG_0588; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   Proteomes; UP000001578; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 3.
DR   HAMAP; MF_01452; AddB_type1; 1.
DR   InterPro; IPR014140; DNA_helicase_suAddB.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR02773; addB_Gpos; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; DNA damage; DNA repair; Exonuclease; Hydrolase; Iron;
KW   Iron-sulfur; Metal-binding; Nuclease; Nucleotide-binding.
FT   CHAIN           1..1167
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379192"
FT   DOMAIN          1..359
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   DOMAIN          282..588
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         803
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1125
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1128
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1134
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ   SEQUENCE   1167 AA;  133929 MW;  23C00BCE7F5445C0 CRC64;
     MSLRFLLGRS GSGKTTACLE EIRRQLQEDP KGRTIVYLVP EQMTFQCEYA LIHTEGTEGM
     IRAQVFSFPR LAWRVLQETG GMNRYHVHDV GVQMMIRKII EQRKQELKLF GRAADKSGFV
     EQLHEMIAEC KRYCLTPDEL RRHAGVLESG SGQPGRRLLA DKLSDVALVY EELERSLLGH
     YLDSEDYLRL LVEHIPRSSY LHGADIYIDG FHHFSPQEYM VIEQLLHRCR RVTVCLTADR
     PYDVGMPDEL DLFYLPAQTY RQLRELALAN DIMIESPVVL SVNRRHQDKA LAHLEEQFHR
     RPLLPYEAET DAICLYEAAN RRAEIEAVAR EIIRLVRDEG ARYRDIALII RQTEAYRDLV
     KTVFFDFDIP YFMDEKEPMH YHPLIELVRA ALETVVTRWR YEAVFRAVKT DLLFPVDGDL
     AMWREAADKL ENYVLAHGVK GEKWTSDERW TYRRYQALDG LNVPQTDEER QFEDKLNEWR
     EALAAPLRRL ERRLRRAADG RGLCTALYLF LEELQIPKKL EQMSAQAEAD GRLVEARQHE
     QAWNAVVDLL DQYVEMLGAE PLPLAEFAKI IEAGLDRLEF ALVPPAIDQV IVAQLDRSRL
     IDVKYAFIIG VNDGVIPAKV KDEGLVAEVE REQLRELGVA LAPGGREQLF YDPFFVYLAL
     ACPSRRLYVT YPLADGEGKA LMPSPLIKQL VQLFPRVSVH LCGNDPFDAP EEKPETFVTV
     PRATQTYLIS QLRAWKRNYG IDPLWWDVYN VLISHPEWRA RVEQAVSGLF YTNQAVLKRE
     WSRRLYGKKI QASVSRMEQF QKCPYAHFAS HGLRLKERNV FRLEAPDVGQ LFHAAIKQIA
     DRVREQHLDW KQLSRSECER LSAEAVERIA PLIQQQVLSS SNRYEYMKRK LKNVVARTTH
     VLSEHARASG FAPVGFELSF GPGGDLPPLR FQLRDGTVME LVGRIDRVDK AESSQGVLLR
     IIDYKSSAKT LDLTEVYYGL ALQMFTYLDI VLTYAEQLVG EPALPAGVLY FHIHNPIIQA
     KQWLDNEMEV ARKLLEPFRM RGLLLADAET IRLMDSQTEN GQWSLIVPAQ LTRTGAIHSR
     SSVASASDFA ALRQHVRRLF VDIGGQIADG VVSIAPYKLK NKTACEFCAF KPVCQFDEAL
     SGNGYRKLTP QTKDAVIETL GKREEES
 
 
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