ID A0A0G0EXW8_9BACT Unreviewed; 446 AA.
AC A0A0G0EXW8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-NOV-2023, entry version 33.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|RuleBase:RU003555};
GN ORFNames=US24_C0016G0005 {ECO:0000313|EMBL:KKQ11748.1};
OS candidate division WS6 bacterium GW2011_GWC2_36_7.
OC Bacteria; Candidatus Dojkabacteria.
OX NCBI_TaxID=1619091 {ECO:0000313|EMBL:KKQ11748.1, ECO:0000313|Proteomes:UP000034075};
RN [1] {ECO:0000313|EMBL:KKQ11748.1, ECO:0000313|Proteomes:UP000034075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC {ECO:0000256|RuleBase:RU003555}.
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:KKQ11748.1}.
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DR EMBL; LBSF01000016; KKQ11748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0EXW8; -.
DR PATRIC; fig|1619091.4.peg.227; -.
DR Proteomes; UP000034075; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004504; DNA_repair_RadA.
DR InterPro; IPR014774; KaiC-like_dom.
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; PF06745; ATPase; 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|RuleBase:RU003555};
KW DNA damage {ECO:0000256|RuleBase:RU003555};
KW DNA repair {ECO:0000256|RuleBase:RU003555};
KW DNA-binding {ECO:0000256|RuleBase:RU003555};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003555};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003555};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Zinc {ECO:0000256|RuleBase:RU003555};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU003555}.
FT DOMAIN 62..215
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
SQ SEQUENCE 446 AA; 47948 MW; 65AFC2813DE70891 CRC64;
MKYICTACGT ESLKWSGKCP SCGQWGTLEE SEELPVEKSG TKIGTAAKYE SIFQDESKAF
SSDTRISTGY TEVDRVLGTG LIPGEVVLIS GEPGIGKSTL LMQVVLKFSE KKILYVCGEE
SPGQLNSRLV RLANNKSSSK IGQNFMVTED ICAENIVALI EKENFDLIVV DSIQSISSMQ
SRSYPGSISQ VRICGAMLTH VAKIKRIPMF IVGQINKGGD IAGPKVLEHI VDCVLYLEGD
QFNQYRILRG MKNRFGSTNE IGVFEMTGSG LQEVGNPSLV FLENDTKSSG SAIGAVLQGS
RVVFVEVQSL VVERESTGGP MMRVANGIKK PRLDMLCAVM SRKGGVFLGD KDVFVNIVGG
LNINDPCIDL AICAAIKSSA KDKVLDKESV YVGEVGLTGE VRGSWGVSAI IDEAQRVGYK
SAIIGKSKLG KAQDIAVKKI SQITSI
//
