RADA_METM7
ID RADA_METM7 Reviewed; 322 AA.
AC A6VGG2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=MmarC7_0469;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000745; ABR65538.1; -; Genomic_DNA.
DR RefSeq; WP_011976870.1; NC_009637.1.
DR AlphaFoldDB; A6VGG2; -.
DR SMR; A6VGG2; -.
DR STRING; 426368.MmarC7_0469; -.
DR EnsemblBacteria; ABR65538; ABR65538; MmarC7_0469.
DR GeneID; 5329120; -.
DR KEGG; mmz:MmarC7_0469; -.
DR eggNOG; arCOG00415; Archaea.
DR HOGENOM; CLU_041732_0_0_2; -.
DR OMA; TFRIYLR; -.
DR OrthoDB; 30130at2157; -.
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..322
FT /note="DNA repair and recombination protein RadA"
FT /id="PRO_1000048388"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00348"
SQ SEQUENCE 322 AA; 35197 MW; 2B0268B508F21E72 CRC64;
MADVLTELPG VGPSTAEKLI EAGYLDFMKI ATATIGELTD IEGISEKAAA KMIMAARDLC
DLGFKSGVEL LRQRQSVWRL STGSKELDTV LAGGLESQSV TEFAGMYGSG KTQIMHQSCV
NLQIAGKIYA DLEGVVEEEL EHPKAVYIDT EGTFRPERVV QMAEGLGIDG QLVLDNTFVA
RAYNSDMQML FAEKIEDLIK GGNNIKLVII DSLTSTFRNE FTGRGKLAER QQKLGRHMAT
LNKLADLYNC IVLVTNQVAA KPDAFFGVAE QAIGGHVVGH AATFRFFLRK SKGDKRVAKL
YDSPHLPDSE AVFRITEKGI MD