ID   RADB_PYRAB              Reviewed;         229 AA.
AC   Q9V2F6; G8ZFV3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=DNA repair and recombination protein RadB;
GN   Name=radB; OrderedLocusNames=PYRAB01180; ORFNames=PAB2270;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB49042.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ248283; CAB49042.1; ALT_INIT; Genomic_DNA.
DR   EMBL; HE613800; CCE69494.1; -; Genomic_DNA.
DR   PIR; C75199; C75199.
DR   AlphaFoldDB; Q9V2F6; -.
DR   SMR; Q9V2F6; -.
DR   STRING; 272844.PAB2270; -.
DR   EnsemblBacteria; CAB49042; CAB49042; PAB2270.
DR   KEGG; pab:PAB2270; -.
DR   PATRIC; fig|272844.11.peg.131; -.
DR   eggNOG; arCOG00417; Archaea.
DR   HOGENOM; CLU_041732_2_0_2; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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.
FT   CHAIN           1..229
FT                   /note="DNA repair and recombination protein RadB"
FT                   /id="PRO_0000150116"
FT   BINDING         28..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   229 AA;  25694 MW;  12C80418AC9FB039 CRC64;
     MTLTTGVKGL DELLGGGVAR GVILQVYGPF ATGKTTFAMQ VGLLNEGKVA YVDTEGGFSP
     ERLKQMAESR GLDPEKALSK FIIFEPMDLN EQRRIISKLK TVVSDKFSLV VVDSLTAHYR
     AEGSRDHVEL AKQLQVLQWL ARKKNVAVIV VNQVYYDSNT NTLRPIAEHT LGYRTKDILR
     FEKFRVGVRL AVLERHRFRP EGGIVYFKIT DKGIEDVLKA KPENGEENI