RADA_DEIRA
ID RADA_DEIRA Reviewed; 503 AA.
AC Q9RVC4;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=DNA repair protein RadA {ECO:0000255|HAMAP-Rule:MF_01498};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01498};
DE AltName: Full=Branch migration protein RadA {ECO:0000255|HAMAP-Rule:MF_01498};
GN Name=radA {ECO:0000255|HAMAP-Rule:MF_01498}; OrderedLocusNames=DR_1105;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX DOI=10.1007/s11434-006-2209-7;
RA Zhou Q., Zhang X.J., Xu H., Xu B.J., Hua Y.J.;
RT "RadA: a protein involved in DNA damage repair processes of Deinococcus
RT radiodurans R1.";
RL Chin. Sci. Bull. 51:2993-2999(2006).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=19303848; DOI=10.1016/j.cell.2009.01.018;
RA Slade D., Lindner A.B., Paul G., Radman M.;
RT "Recombination and replication in DNA repair of heavily irradiated
RT Deinococcus radiodurans.";
RL Cell 136:1044-1055(2009).
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:0000255|HAMAP-Rule:MF_01498}.
CC -!- FUNCTION: Plays a role in DNA damage repair (Ref.2). Following severe
CC irradiation (IR, 7 kGy of gamma irradiation), genomic DNA is fragmented
CC and progressively degraded for the first 1.5 hours after IR, in a step
CC promoted by RecA and counterbalanced by DNA Pol I and Pol III. This is
CC followed by massive DNA synthesis and genome reassembly in the next
CC hour. Optimal priming of DNA synthesis requires both RecA and RadA. Pol
CC III initiates DNA synthesis while both Pol I and Pol III are required
CC for its continuation (PubMed:19303848). {ECO:0000269|PubMed:19303848,
CC ECO:0000269|Ref.2}.
CC -!- DOMAIN: Has a putative N-terminal zinc-finger, a middle region with
CC homology to RecA with ATPase motifs including the RadA KNRFG motif,
CC while the C-terminus is homologous to Lon protease (By similarity).
CC Absence of the zinc-finger domain gives a slight increase in
CC sensitivity to gamma and UV irradiation, absence of the Lon protease
CC domain gives slightly increased resistance to gamma and UV irradiation.
CC {ECO:0000255|HAMAP-Rule:MF_01498, ECO:0000269|Ref.2}.
CC -!- DISRUPTION PHENOTYPE: Moderately decreased resistance to gamma and UV
CC irradiation, no effect on H(2)O(2) resistance (Ref.2). Slightly reduced
CC DNA synthesis rate even in the absence of ionizing radiation (IR);
CC after IR chromosome fragment assembly is delayed. Double recA-radA
CC deletion mutants have lower rates of DNA synthesis than the recA
CC deletion alone with or without IR (PubMed:19303848).
CC {ECO:0000269|PubMed:19303848, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01498}.
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DR EMBL; AE000513; AAF10678.1; -; Genomic_DNA.
DR PIR; D75437; D75437.
DR RefSeq; NP_294829.1; NC_001263.1.
DR RefSeq; WP_010887748.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RVC4; -.
DR SMR; Q9RVC4; -.
DR STRING; 243230.DR_1105; -.
DR MEROPS; S16.A04; -.
DR EnsemblBacteria; AAF10678; AAF10678; DR_1105.
DR KEGG; dra:DR_1105; -.
DR PATRIC; fig|243230.17.peg.1301; -.
DR eggNOG; COG1066; Bacteria.
DR HOGENOM; CLU_018264_0_1_0; -.
DR InParanoid; Q9RVC4; -.
DR OMA; FELMRLA; -.
DR OrthoDB; 505485at2; -.
DR Proteomes; UP000002524; Chromosome I.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR CDD; cd01121; Sms; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR041166; Rubredoxin_2.
DR Pfam; PF18073; Rubredoxin_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00416; sms; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..503
FT /note="DNA repair protein RadA"
FT /id="PRO_0000435881"
FT ZN_FING 66..83
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT REGION 118..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..503
FT /note="Lon-protease-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT MOTIF 310..314
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
SQ SEQUENCE 503 AA; 52758 MW; B38D7165D34272EF CRC64;
MERVAVLFRR TCNSENCSKG RRPLRERPLA GLFFCSLPAP LSIPCLSLPG SNPGDFVPKV
KTNYICNSCG YQSAKPLGRC PNCQAWNSFE EEVPTASTSG KSGRGGLGGY GGVKGGKLTP
LSTVGRREEP RTPSGIPELD RVLGGGLVAG GVTLIGGEPG IGKSTLLLQV ADKVASRGGT
VLYVAGEESL EQIRLRADRL GVAADLQMTR DTRAEHIAAL LEEHKPALCI VDSIQTVTVE
GEGAPGGVAQ VRDGTAMLTR AAKETGTATV LVGHVTKDGT VAGPKVMEHI VDTTVFLETV
GAFRLLRSVK NRFGQAGELG VFEMRGEGLI AVDNPSAAFL AERPLDVPGS VVAATVDGQR
PMLLEVQALA SKTPYPNARR VVVGLDPRRV DVVLAVLERR LDLTLGGLDV YVNLAGGLKV
PDPGLDLAVA LAVYSAVVGR ALPQNVAVFG EVGLAGEVRS TQMALRRAEE AGRAGYKRLV
VPPGLDGQAG VKSVEEAVKA VWR
