ID A0A1V0DCJ2_9BACT Unreviewed; 454 AA.
AC A0A1V0DCJ2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|HAMAP-Rule:MF_01498, ECO:0000256|RuleBase:RU003555};
GN Name=radA {ECO:0000256|HAMAP-Rule:MF_01498};
GN ORFNames=AWN76_005710 {ECO:0000313|EMBL:ARA92708.1};
OS Rhodothermaceae bacterium RA.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae.
OX NCBI_TaxID=1779382 {ECO:0000313|EMBL:ARA92708.1, ECO:0000313|Proteomes:UP000055617};
RN [1] {ECO:0000313|EMBL:ARA92708.1, ECO:0000313|Proteomes:UP000055617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA {ECO:0000313|EMBL:ARA92708.1,
RC ECO:0000313|Proteomes:UP000055617};
RA Liew K.J.;
RT "Complete genome of the potential lignocellulosic biomass degrader
RT Rhodothermaceae bacterium RA isolated from the saline hot spring in
RT Malaysia.";
RL Submitted (MAR-2017) 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; CP020382; ARA92708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0DCJ2; -.
DR STRING; 1779382.AWN76_005710; -.
DR KEGG; rbar:AWN76_005710; -.
DR OrthoDB; 9803906at2; -.
DR Proteomes; UP000055617; Chromosome.
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 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; 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 ECO:0000256|RuleBase:RU003555};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01498};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01498,
KW ECO:0000256|RuleBase:RU003555};
KW Reference proteome {ECO:0000313|Proteomes:UP000055617};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01498}; Zinc {ECO:0000256|RuleBase:RU003555};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}.
FT DOMAIN 69..216
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 38..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 98..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01498"
SQ SEQUENCE 454 AA; 49491 MW; 6E371CC60127FC23 CRC64;
MAKTRTQYTC QVCGHTSPQW MGRCPSCEAW SSFVEETLRP ETRHRPAQVD AGRPATRRPL
PLSQVELRAE TRLQTAVGEF DRVMGGGIMQ GSLTLIAGDP GIGKSTLMTE LARFLPDRTI
LYVTGEESAR QVRLRAERLG VTSDNLLLLA ETNLFDILTA MQEAEPDLII VDSIQTVYHP
EMQSAPGSVS QVRACAAALL QATKALDAPT FIVGHVTKEG AIAGPRVLEH MVDTVLYFEG
DRHHAFRILR AVKNRFGSTN EIGVFEMHES GLEEVTNPSE IFLSERRYGV SGATVVCSME
GTRPILVEIQ ALVTPTSYGT PQRNATGFDG RRLQMLLAVL EKREGLRLST HDVFVNVAGG
VRLDEPAVDL GVVVAAASSF RDVPADTGTV LIGEVGLGGE IRTVSRVEPR LKEAAKLGFE
RALVPATNLK GLRPPRGMEV TPVERLHQVL DLVL
//
