RADA_METS5
ID RADA_METS5 Reviewed; 324 AA.
AC A4YCN4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Msed_0009;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP94186.1; -; Genomic_DNA.
DR RefSeq; WP_011921155.1; NC_009440.1.
DR AlphaFoldDB; A4YCN4; -.
DR SMR; A4YCN4; -.
DR STRING; 399549.Msed_0009; -.
DR EnsemblBacteria; ABP94186; ABP94186; Msed_0009.
DR GeneID; 5105025; -.
DR GeneID; 59456560; -.
DR KEGG; mse:Msed_0009; -.
DR eggNOG; arCOG00415; Archaea.
DR HOGENOM; CLU_041732_0_0_2; -.
DR OMA; TFRIYLR; -.
DR Proteomes; UP000000242; 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..324
FT /note="DNA repair and recombination protein RadA"
FT /id="PRO_1000120512"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00348"
SQ SEQUENCE 324 AA; 35544 MW; 6F25EB4F0F17FFD8 CRC64;
MADQVEEKKR IKTVKDLSGV GQAVLNKLTE AGYSTLESIA VASPQDLSTA AGIPITTAQR
IIKEARDALD IRFKTALEIE QERASVKKIT TGSQALDGLL GGGIETRTMT ELFGEFGSGK
TQICHQVSVN VQLPPERGGL SGKALYIDTE GTFRTERIKA MASALGLEPK EVLQNIMSIR
AINTDHQIAI VEELQDIIAK DNSIKLVVVD SITSHFRAEY SGRENLAVRQ QKLNRHLHQL
VRLAEIYDLA VIVTNQVMAR PDMFYGDPTV AVGGHTLYHV PGIRVQIKKS RGNRRIARMV
DAPHLPEGEV VFSITNTGIR DAEE
