ID   RADA_HALWD              Reviewed;         343 AA.
AC   Q18EU1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=HQ_3429A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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; AM180088; CAJ53526.1; -; Genomic_DNA.
DR   RefSeq; WP_011572623.1; NC_008212.1.
DR   AlphaFoldDB; Q18EU1; -.
DR   SMR; Q18EU1; -.
DR   STRING; 362976.HQ_3429A; -.
DR   EnsemblBacteria; CAJ53526; CAJ53526; HQ_3429A.
DR   GeneID; 4194566; -.
DR   KEGG; hwa:HQ_3429A; -.
DR   eggNOG; arCOG00415; Archaea.
DR   HOGENOM; CLU_041732_0_0_2; -.
DR   OMA; TFRIYLR; -.
DR   Proteomes; UP000001975; 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; 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   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; Reference proteome.
FT   CHAIN           1..343
FT                   /note="DNA repair and recombination protein RadA"
FT                   /id="PRO_1000048383"
FT   BINDING         107..114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00348"
SQ   SEQUENCE   343 AA;  37279 MW;  9480A613D0ED6AED CRC64;
     MPEDELEDLP GVGPATSDKL VDAGFESYQA IAVASPAEMS NTADVGESTA SDIINAARDA
     ADVGGFETGA AVLQRREEIG KLSWKIPEVD ELLGGGIETQ SITEVYGEFG AGKSQVTHQM
     AVNVQLPPEH GGLGGAAIFV DSEDTFRPER IDDMLRGLDD EIITDLLERR EIEGTPGDDE
     TMKALLDSFL DHIHVAKAFN SNHQILLAEK AKELARDNQD SGFPVRLLCV DSLTAHFRAE
     YVGRGSLAER QQKLNKHLHD LMRIGDLYNT AVLVTNQVAS NPDSYFGDPT QPIGGNILGH
     TSTFRMYLRK SKNDKRIVRL VDAPNLADGE AVMRVKDAGL KPE