RADA_DESA1
ID RADA_DESA1 Reviewed; 328 AA.
AC B8D610;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=DNA repair and recombination protein RadA {ECO:0000255|HAMAP-Rule:MF_00348};
GN Name=radA {ECO:0000255|HAMAP-Rule:MF_00348}; OrderedLocusNames=DKAM_1215;
OS Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS 1221n) (Desulfurococcus kamchatkensis).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus.
OX NCBI_TaxID=490899;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n;
RX PubMed=19114480; DOI=10.1128/jb.01525-08;
RA Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Complete genome sequence of the anaerobic, protein-degrading
RT hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL J. Bacteriol. 191:2371-2379(2009).
CC -!- FUNCTION: Involved in DNA repair and in homologous recombination. Binds
CC and assemble on single-stranded DNA to form a nucleoprotein filament.
CC Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand
CC exchange between homologous DNA molecules. {ECO:0000255|HAMAP-
CC Rule:MF_00348}.
CC -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00348}.
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DR EMBL; CP001140; ACL11541.1; -; Genomic_DNA.
DR RefSeq; WP_012608882.1; NC_011766.1.
DR AlphaFoldDB; B8D610; -.
DR SMR; B8D610; -.
DR STRING; 490899.DKAM_1215; -.
DR EnsemblBacteria; ACL11541; ACL11541; DKAM_1215.
DR GeneID; 7171290; -.
DR KEGG; dka:DKAM_1215; -.
DR eggNOG; arCOG00415; Archaea.
DR HOGENOM; CLU_041732_0_0_2; -.
DR OMA; TFRIYLR; -.
DR Proteomes; UP000006903; 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 CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00348; RadA_arch; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR011938; DNA_recomb/repair_RadA.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02236; recomb_radA; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..328
FT /note="DNA repair and recombination protein RadA"
FT /id="PRO_1000133406"
FT BINDING 118..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00348"
SQ SEQUENCE 328 AA; 36461 MW; 2ABCD6BAE1327185 CRC64;
MSEEKETIKE RSSGFISVRD IPGVGSSIAD KLEAAGYLSA WSIVVARAEE LAERTGLPVL
TVQKIIENAR KMLGITFKTA REVKQERLNI GKITTGSKSL DELLGGGVET KTITEFFGEY
GSGKTQICHQ LSVNVQLTPE KGGLNGRAVY IDTEGTFRWE RIEAMARALG LDPDKVMDNI
YYMRAYNSDH QIAIVDELFT FVPKNDVRLV ILDSVTSHFR AEYPGREHLA ERQQKLNSHL
HQLMRLAEAY NVAVVVTNQV MARPDVFYGD PTTAVGGHVL AHTPGVRIQL RKSKGNKRIA
RVVDAPHLPE GEVVFVITEE GIRDSEEE
