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ADDB_CALS4
ID   ADDB_CALS4              Reviewed;        1159 AA.
AC   Q8RCZ1;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=TTE0263;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
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}.
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DR   EMBL; AE008691; AAM23559.1; -; Genomic_DNA.
DR   RefSeq; WP_011024732.1; NC_003869.1.
DR   AlphaFoldDB; Q8RCZ1; -.
DR   SMR; Q8RCZ1; -.
DR   STRING; 273068.TTE0263; -.
DR   EnsemblBacteria; AAM23559; AAM23559; TTE0263.
DR   KEGG; tte:TTE0263; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000000555; 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; -; 4.
DR   Gene3D; 3.90.320.10; -; 1.
DR   HAMAP; MF_01452; AddB_type1; 1.
DR   InterPro; IPR014140; DNA_helicase_suAddB.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02773; addB_Gpos; 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;
KW   Reference proteome.
FT   CHAIN           1..1159
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379226"
FT   REGION          1140..1159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         784
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1102
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1105
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1111
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ   SEQUENCE   1159 AA;  135216 MW;  35B36BA20D413B1E CRC64;
     MSIRFIYGRA GSGKTYFCLE EIKHKLNDGA NHPLILLVPE QFTFEAEKYL LDMIERDEKM
     RAQVLSFKTL ANRVFVEVGG LARQHMKACG KSMVIYKVLE ENKEKLKVYS KASRQQGFVK
     KISEAITEFK RFDVTPFQLI DASEKIEKLG LKEKLEDLAL IYSSFEEVLH KNYIDEEDEL
     DLLSKKLEKS LQFEGAEFWI DGFTGFTPKQ YKVIEKLLKK ASRVSVTLTL DPSIDSIDPT
     HLFYTTKKTE EKLIKICETN GISVEEPVNL NKGIPKRFEH NKELAFLEKN FFSHPYEIYN
     EETKNISIFK ATNMYSEVEE VARDIARLIR DEHMRYSDIV VATKDLKRYY KLVKAIFSHY
     GIPHFIDLKI NITNNPIIVY VISIFEIYLK NWSYESVFRY LKTGFTGIDK EEINLLENYV
     LANGIKGNKW KERWEYRIDY KTDSLLMEER EKQIINKVNE VRERVYLPLE KFYTRFSHSK
     NVKEACEVLY DFLVENKLPE KIEKFIEEFK NRGEFDTANQ YAQIWDIVVD VLDQMVEVLG
     EEKISLEQFA RLISIGFDEY QIASIPPALD EVLVTSVDRM KSHNSKVLYL LGANDGVFPA
     SSFEEGIFSD EERNLLSSLD LELDRDTKAK VFEEQFLVYT ALTSASEFLK ISYPIADHEG
     RSLRPSIIIS RLRRIFPKIK VSTNIVEMDT DEENLNRVTV PLPTFNEMIK SFKKWNITGK
     IHPIWLEVYK WYRTKDEWKK KLEDTLEGFV YDNQIKRIPP LKIKKLYGEE MEFSVSRLEK
     YAACPFAYFV QYGLKAKERK IYGFEPPDLG IFMHNVLNEI AKALEKEELT WQEIDKEWCN
     DAVDIIVEEM VDKIPGYILK SSSRYRYLAN RLKRVLSKAV WIISEHMKRS SFVPLGHEVA
     FGENQKYPPI KIVLSNGEEI KLIGRIDRVD VLEKEGETYV RIIDYKSGDK TLDLSDVLYG
     LELQLLVYLD AILESAFEGK ANLSPAGIFY FKIDDPIVRA DKDISDEELY KEIMKRLRLE
     GFVLKSLDII REMDKLIEGT SYVIPASINK DGTIGKNTKG LTEEQFEILR KFVKKKSKKL
     AEEMLQGDIS ILPYKKEKET ACQYCPYSSI CKFETNFKGN DYRRIESKEE KLWSIFEEEV
     KEDGSQVDGR TEGSDNNEG
 
 
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