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RADB_ARCFU
ID   RADB_ARCFU              Reviewed;         221 AA.
AC   O28184;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=DNA repair and recombination protein RadB;
GN   Name=radB; OrderedLocusNames=AF_2096;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- FUNCTION: Involved in DNA repair and in homologous recombination. May
CC       regulate the cleavage reactions of the branch-structured DNA. Has a
CC       very weak ATPase activity that is not stimulated by DNA. Binds DNA but
CC       does not promote DNA strands exchange (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family. RadB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE000782; AAB89159.1; -; Genomic_DNA.
DR   PIR; H69511; H69511.
DR   AlphaFoldDB; O28184; -.
DR   SMR; O28184; -.
DR   STRING; 224325.AF_2096; -.
DR   EnsemblBacteria; AAB89159; AAB89159; AF_2096.
DR   KEGG; afu:AF_2096; -.
DR   eggNOG; arCOG00417; Archaea.
DR   HOGENOM; CLU_041732_2_0_2; -.
DR   OMA; GNTLEHW; -.
DR   PhylomeDB; O28184; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00350; RadB; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR   InterPro; IPR011939; DNA_repair_and_recomb_RadB.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   Pfam; PF08423; Rad51; 1.
DR   PIRSF; PIRSF003336; RadB; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02237; recomb_radB; 1.
DR   PROSITE; PS50162; RECA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..221
FT                   /note="DNA repair and recombination protein RadB"
FT                   /id="PRO_0000150111"
FT   BINDING         31..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   221 AA;  24936 MW;  B73363A3F7D1966F CRC64;
     MQRMLIPTGS KCIDSLLGGG VETGTVTQIY GHGGTGKTTL CLMLAKNAAE QFKVAYIDTE
     GLSGERVRQI FGDERLFSNV FVYEVYRFRQ QGVAIQEAEK LCRSEKVKLV IVDCFTSLYR
     SELEDDRKQI KIKRELTSQL TFLLGMARKY DVAVVITNQM FTDVGSGVDR PLGGPSLEHL
     SKVIIALERS NELRKATLIK HRWMKEGKSC FYRITDRGIE P
 
 
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