ID A0A1F7W641_9BACT Unreviewed; 412 AA.
AC A0A1F7W641;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|RuleBase:RU003555};
GN ORFNames=A2318_01310 {ECO:0000313|EMBL:OGL98230.1};
OS Candidatus Uhrbacteria bacterium RIFOXYB2_FULL_45_11.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1802421 {ECO:0000313|EMBL:OGL98230.1, ECO:0000313|Proteomes:UP000177331};
RN [1] {ECO:0000313|EMBL:OGL98230.1, ECO:0000313|Proteomes:UP000177331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGL98230.1}.
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DR EMBL; MGFD01000030; OGL98230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7W641; -.
DR STRING; 1802421.A2318_01310; -.
DR Proteomes; UP000177331; 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; 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 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 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|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|RuleBase:RU003555}.
FT DOMAIN 43..192
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 44300 MW; 31B8B8847C063496 CRC64;
MTCDHWGTIK EETEHPSPAT RASGSKAKPK ETTSLKDIKA QDEHVRLSIG EHELDRVLGG
GIVTGSLTLL SGEPGIGKST LVAGMAAKIA STKHDVLYVS GEESAMQLKS RFDRLNADLS
RIKFLEMVSV EELVATLEKE KPTLAIVDSV QTMFSNAVEA QSGSPTLVRY ATSCLLELAK
RTGISLLLVG QVTKDGSVAG PKTLEHLVDT VLSLTGEPSH ELRILEATKN RFGATDEIGV
FEMTSEGLKA VENPSARFLA ERVSVPGSVI ATVREGSRIF LVEVQALVEK SFYGTPVRRA
NGMDQNRLQM LIAILSKRAG LHLGESDVYV NVVGGMQLKE PASDLAVCAA IMSAAKNRID
SEPIVYIGEV GLGGEIRNVM AVEKRVTEAK RVGIEKSVTP KTMKSVKELS SY
//
