ID A0A2A3N262_CAPSP Unreviewed; 454 AA.
AC A0A2A3N262;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498};
GN Name=radA {ECO:0000256|HAMAP-Rule:MF_01498};
GN ORFNames=CDC50_07910 {ECO:0000313|EMBL:PBN45939.1};
OS Capnocytophaga sputigena.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1019 {ECO:0000313|EMBL:PBN45939.1, ECO:0000313|Proteomes:UP000218560};
RN [1] {ECO:0000313|EMBL:PBN45939.1, ECO:0000313|Proteomes:UP000218560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H6490 {ECO:0000313|EMBL:PBN45939.1,
RC ECO:0000313|Proteomes:UP000218560};
RA Gulvik C.A.;
RT "Capnocytophaga spp. assemblies.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in repairing double-strand DNA breaks, probably
CC involving stabilizing or processing branched DNA or blocked replication
CC forks. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC -!- DOMAIN: The middle region has homology to RecA with ATPase motifs
CC including the RadA KNRFG motif, while the C-terminus is homologous to
CC Lon protease. {ECO:0000256|HAMAP-Rule:MF_01498}.
CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01498}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PBN45939.1}.
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DR EMBL; NIBW01000002; PBN45939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3N262; -.
DR Proteomes; UP000218560; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR CDD; cd01121; RadA_SMS_N; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01498; RadA_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004504; DNA_repair_RadA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR041166; Rubredoxin_2.
DR PANTHER; PTHR32472; DNA REPAIR PROTEIN RADA; 1.
DR PANTHER; PTHR32472:SF10; DNA REPAIR PROTEIN RADA-LIKE PROTEIN; 1.
DR Pfam; PF13481; AAA_25; 1.
DR Pfam; PF13541; ChlI; 1.
DR Pfam; PF18073; Rubredoxin_2; 1.
DR PRINTS; PR01874; DNAREPAIRADA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01498};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01498};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01498};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01498};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Zinc {ECO:0000256|ARBA:ARBA00022771};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 70..216
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 352..454
FT /note="Lon-protease-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT MOTIF 253..257
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 454 AA; 50193 MW; A45A22806E5D97FE CRC64;
MAKLKTAYFC QNCGAQYSKW QGQCYTCKQW NTIVEEVVQK DTAPAWQEKE SPIKNKAPKY
IPISQIDTQQ EARLNSNNHE LNNVLGGGIV PGSVTLLGGE PGIGKSTLLL QIALNLPYRT
LYVSGEESEK QIKMRADRIP HKLDNCFILT ETKTQNIFQQ IKELLPEIVI IDSIQTLQSD
YIEASAGSIS QIRECTSELI KFAKTTHTPV ILIGHITKDG QIAGPKILEH MVDTVLQFEG
DRNHVYRILR SLKNRFGSTS ELGIYEMLSN GLREVNNPSE ILISKTDETI SGTSIAATLE
GMRPLMIEIQ ALVSTAVYGT PQRSTTGFNA KRLNMLLAVL EKRAGFRLGA KDVFLNITGG
ITIDDPATDL GVAMAILSSN EDIAIDKDVC FAGEVGLGGE IRPVQRVEQR ITEAEKLGFN
TIFVSKYNKI AFKNTKIKVI TVAKIEDAIQ ELFG
//
