ID A0A0G1XY76_9BACT Unreviewed; 389 AA.
AC A0A0G1XY76;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA repair protein RadA {ECO:0000256|RuleBase:RU003555};
DE Flags: Fragment;
GN ORFNames=UY82_C0032G0005 {ECO:0000313|EMBL:KKW35961.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWC2_53_7.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1618986 {ECO:0000313|EMBL:KKW35961.1, ECO:0000313|Proteomes:UP000033865};
RN [1] {ECO:0000313|EMBL:KKW35961.1, ECO:0000313|Proteomes:UP000033865}
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:KKW35961.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCRN01000032; KKW35961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1XY76; -.
DR PATRIC; fig|1618986.3.peg.371; -.
DR Proteomes; UP000033865; 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 22..170
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKW35961.1"
SQ SEQUENCE 389 AA; 40856 MW; 79AFEE276FC19695 CRC64;
ASAVAEAKAA DVVRLDSADL KSAERRATTI GELDRVLGGG VVAGSLVLLS GEPGIGKSTL
AAMVGSAFGK AKPIIYASGE ESAPQLSGRL KRLGVELNRI AYVGTTSVER VAKTIEKERP
PLAIVDSVQT LTSSVLDFAA GGTSLVRYAT NVLLETAKQT GVPILLVGQV TKDGSVAGPK
TLEHLVDVVL MLEGKSGYLT RLLRAGKNRF GSTEEVGIFE MREEGLVGVA NPSAHFLEER
AQTPGSIVTA TLEGSRVFLV EVQALVETSV FANPLRRATG FSEKRLLMLS AILSRRAGVK
LADKDIYVNV VGGLRLTEPA ADLAACLAIA GALEKVSLKA QTIVFGEVGL GGELRKVPGM
ERREKEAKRL GFETVISPAT AKTLKELLS
//
