ID A0A1I6CU76_9RHOB Unreviewed; 455 AA.
AC A0A1I6CU76;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-OCT-2025, entry version 32.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|NCBIfam:TIGR00416};
GN Name=radA {ECO:0000256|HAMAP-Rule:MF_01498};
GN ORFNames=SAMN04515673_101383 {ECO:0000313|EMBL:SFQ96794.1};
OS Poseidonocella sedimentorum.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Poseidonocella.
OX NCBI_TaxID=871652 {ECO:0000313|EMBL:SFQ96794.1, ECO:0000313|Proteomes:UP000199302};
RN [1] {ECO:0000313|EMBL:SFQ96794.1, ECO:0000313|Proteomes:UP000199302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMM 9023,NRIC 0796,JCM 17311,KCTC 23692
RC {ECO:0000313|Proteomes:UP000199302};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent ATPase involved in processing of recombination
CC intermediates, plays a role in repairing DNA breaks. Stimulates the
CC branch migration of RecA-mediated strand transfer reactions, allowing
CC the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA
CC in the presence of ADP but not other nucleotides, has ATPase activity
CC that is stimulated by ssDNA and various branched DNA structures, but
CC inhibited by SSB. Does not have RecA's homology-searching function.
CC {ECO:0000256|RuleBase:RU003555}.
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, ECO:0000256|RuleBase:RU003555}.
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DR EMBL; FOYI01000001; SFQ96794.1; -; Genomic_DNA.
DR RefSeq; WP_092076035.1; NZ_FOYI01000001.1.
DR AlphaFoldDB; A0A1I6CU76; -.
DR STRING; 871652.SAMN04515673_101383; -.
DR OrthoDB; 9803906at2; -.
DR Proteomes; UP000199302; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IEA:UniProtKB-UniRule.
DR CDD; cd01121; RadA_SMS_N; 1.
DR FunFam; 3.40.50.300:FF:000050; DNA repair protein RadA; 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 NCBIfam; TIGR00416; sms; 1.
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; Zn_ribbon_LapB; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Reference proteome {ECO:0000313|Proteomes:UP000199302};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003555};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}.
FT DOMAIN 67..216
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 352..455
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 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 455 AA; 47355 MW; 88314419DFAEF141 CRC64;
MAKSAPSFAC ADCGATTSKW AGRCESCGAW NTIHEETPLS AGPSGHALSA VKGRTITLSG
LDTREDPPKR TQAGVEELDR VLGGGLVPAS AILLGGDPGI GKSTLLLQAA ARFARGGLKT
LYISGEEAAE QVRMRAQRLG LTESPVQLAA ETNLRDILTT LEAERPQLAI IDSIQTMWSD
QVGAAPGSVS QVRAAAHELT RFAKTRGVAI ILVGHVTKEG QIAGPRVVEH MVDTVLYFEG
ERGHPFRILR AVKNRFGPAD EIGVFEMTGR GLAEVRNPSA LFLSERGTPA PGSAVFAGVE
GTRPLLVEFQ ALVSPSPHAQ ARRAVVGWDS GRLSMILAVL EARCGIPYAG LDVYLNVAGG
MKVTEPAADL AVAAALLSAR EDSALPDGAV IFGEISLSGA LRPVTQAENR LKEAKKLGFT
SAILPAGGKA GDGSGLALNR VTDLAGFVGE MFGAG
//
