ID   RADA_METS3              Reviewed;         311 AA.
AC   A5UMW0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=DNA repair and recombination protein RadA {ECO:0000255|HAMAP-Rule:MF_00348};
GN   Name=radA {ECO:0000255|HAMAP-Rule:MF_00348}; OrderedLocusNames=Msm_1333;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC   -!- FUNCTION: Involved in DNA repair and in homologous recombination. Binds
CC       and assemble on single-stranded DNA to form a nucleoprotein filament.
CC       Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand
CC       exchange between homologous DNA molecules. {ECO:0000255|HAMAP-
CC       Rule:MF_00348}.
CC   -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_00348}.
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DR   EMBL; CP000678; ABQ87538.1; -; Genomic_DNA.
DR   RefSeq; WP_004036279.1; NC_009515.1.
DR   AlphaFoldDB; A5UMW0; -.
DR   SMR; A5UMW0; -.
DR   STRING; 420247.Msm_1333; -.
DR   EnsemblBacteria; ABQ87538; ABQ87538; Msm_1333.
DR   GeneID; 5217158; -.
DR   KEGG; msi:Msm_1333; -.
DR   PATRIC; fig|420247.28.peg.1329; -.
DR   eggNOG; arCOG00415; Archaea.
DR   HOGENOM; CLU_041732_0_0_2; -.
DR   OMA; TFRIYLR; -.
DR   Proteomes; UP000001992; Chromosome.
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:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd01123; Rad51_DMC1_radA; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00348; RadA_arch; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR   InterPro; IPR011938; DNA_recomb/repair_RadA.
DR   InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR   InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR033925; Rad51_DMC1_RadA.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   Pfam; PF08423; Rad51; 1.
DR   PIRSF; PIRSF005856; Rad51; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00278; HhH1; 2.
DR   SUPFAM; SSF47794; SSF47794; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02236; recomb_radA; 1.
DR   PROSITE; PS50162; RECA_2; 1.
DR   PROSITE; PS50163; RECA_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA-binding;
KW   Nucleotide-binding.
FT   CHAIN           1..311
FT                   /note="DNA repair and recombination protein RadA"
FT                   /id="PRO_1000048390"
FT   BINDING         104..111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00348"
SQ   SEQUENCE   311 AA;  34258 MW;  536B9CD2BDE8DCCE CRC64;
     MVELEDLPSV GEKTAEKLRD AGFADMMRLA TATPKELSVK AEIGEGVAEK VIEAARKSEK
     IDFETAYDVL ERRRDVGHIS VGSEGFNDLI GGGIETQSIT EVFGEFGSGK SQISHELAVT
     VQLPPEKGGL DGECVFIDTE NTFRPERIEQ IANGFELDID EVLQKIHVAR AFNSSHQILM
     AEKINELIQQ GNNIKLVIVD SLMAHFRAEY VGRESLAVRQ QKLNQHLHAL QQIANTYNVA
     VFITNQVQAK PDSFFGSPTK AIGGHVLGHA STYRIWLKKG LAGKRIARLV DSPHLPEGEC
     VFKIKTEGIV D