RADB_THEKO
ID RADB_THEKO Reviewed; 220 AA.
AC P95547;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=DNA repair and recombination protein RadB;
GN Name=radB; Synonyms=Pk-REC; OrderedLocusNames=TK2231;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=9003328; DOI=10.1007/s004380050337;
RA Rashid N., Morikawa M., Imanaka T.;
RT "A RecA/RAD51 homologue from a hyperthermophilic archaeon retains the major
RT RecA domain only.";
RL Mol. Gen. Genet. 253:397-400(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; D83176; BAA11830.2; -; Genomic_DNA.
DR EMBL; AP006878; BAD86420.1; -; Genomic_DNA.
DR PIR; T46872; T46872.
DR RefSeq; WP_011251181.1; NC_006624.1.
DR PDB; 2CVF; X-ray; 2.60 A; A/B=1-220.
DR PDB; 2CVH; X-ray; 2.20 A; A/B=1-220.
DR PDBsum; 2CVF; -.
DR PDBsum; 2CVH; -.
DR AlphaFoldDB; P95547; -.
DR SMR; P95547; -.
DR STRING; 69014.TK2231; -.
DR EnsemblBacteria; BAD86420; BAD86420; TK2231.
DR GeneID; 3235434; -.
DR KEGG; tko:TK2231; -.
DR PATRIC; fig|69014.16.peg.2186; -.
DR eggNOG; arCOG00417; Archaea.
DR HOGENOM; CLU_041732_2_0_2; -.
DR InParanoid; P95547; -.
DR OMA; GNTLEHW; -.
DR OrthoDB; 93716at2157; -.
DR PhylomeDB; P95547; -.
DR BRENDA; 3.6.1.8; 5246.
DR EvolutionaryTrace; P95547; -.
DR Proteomes; UP000000536; 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; 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 SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02237; recomb_radB; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA recombination; DNA-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..220
FT /note="DNA repair and recombination protein RadB"
FT /id="PRO_0000150119"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2CVF"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:2CVH"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:2CVH"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2CVH"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2CVH"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:2CVH"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:2CVH"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:2CVH"
FT HELIX 128..145
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2CVH"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:2CVF"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2CVF"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:2CVH"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:2CVH"
SQ SEQUENCE 220 AA; 24544 MW; 8821A1274F4F0A35 CRC64;
MLSTGTKSLD SLLGGGFAPG VLTQVYGPYA SGKTTLALQT GLLSGKKVAY VDTEGGFSPE
RLVQMAETRG LNPEEALSRF ILFTPSDFKE QRRVIGSLKK TVDSNFALVV VDSITAHYRA
EENRSGLIAE LSRQLQVLLW IARKHNIPVI VINQVHFDSR TEMTKPVAEQ TLGYRCKDIL
RLDKLPKPGL RVAVLERHRF RPEGLMAYFR ITERGIEDVE
