ID   RADA_HALVD              Reviewed;         343 AA.
AC   Q48328; D4GYV0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=DNA repair and recombination protein RadA;
GN   Name=radA; OrderedLocusNames=HVO_0104;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DS2 / DSM 5716 / WFD11;
RX   PubMed=8668545; DOI=10.1093/nar/24.11.2125;
RA   Sandler S.J., Satin L.H., Samra H.S., Clark A.J.;
RT   "recA-like genes from three archaean species with putative protein products
RT   similar to Rad51 and Dmc1 proteins of the yeast Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 24:2125-2132(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DS2 / DSM 5716 / WFD11;
RX   PubMed=9157249; DOI=10.1046/j.1365-2958.1997.2651626.x;
RA   Woods W.G., Dyall-Smith M.L.;
RT   "Construction and analysis of a recombination-deficient (radA) mutant of
RT   Haloferax volcanii.";
RL   Mol. Microbiol. 23:791-797(1997).
CC   -!- FUNCTION: Involved in DNA repair and in homologous recombination. Binds
CC       and assembles 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 (Probable). In addition to
CC       its role in homologous recombination plays a critical role in
CC       maintenance and/or replication of some plasmids, but not in plasmid
CC       transformation. {ECO:0000269|PubMed:9157249, ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Decreased growth rate, loss of homologous
CC       recombination, increased sensitivity to DNA damaging agents such as UV
CC       light and ethylmethane sulfonate (EMS). Loss of maintenance and/or
CC       replication of pHH1 and pHV2 (but not pHK2) replicon-containing
CC       plasmids. {ECO:0000269|PubMed:9157249}.
CC   -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family.
CC       {ECO:0000305}.
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DR   EMBL; U45311; AAC44121.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE02303.1; -; Genomic_DNA.
DR   PIR; S71094; S71094.
DR   RefSeq; WP_004045193.1; NC_013967.1.
DR   AlphaFoldDB; Q48328; -.
DR   SMR; Q48328; -.
DR   IntAct; Q48328; 15.
DR   STRING; 309800.C498_18758; -.
DR   EnsemblBacteria; ADE02303; ADE02303; HVO_0104.
DR   GeneID; 8924867; -.
DR   KEGG; hvo:HVO_0104; -.
DR   eggNOG; arCOG00415; Archaea.
DR   HOGENOM; CLU_041732_0_0_2; -.
DR   OMA; TFRIYLR; -.
DR   OrthoDB; 30130at2157; -.
DR   BRENDA; 3.6.4.B7; 2561.
DR   Proteomes; UP000008243; 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; Reference proteome.
FT   CHAIN           1..343
FT                   /note="DNA repair and recombination protein RadA"
FT                   /id="PRO_0000150093"
FT   BINDING         107..114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   343 AA;  37320 MW;  42540896B1B9D832 CRC64;
     MAEDDLESLP GVGPATADKL VESGYDSYQS IAVASPGELS NKADIGSSTA SDIINAARDA
     ADVGGFETGS MVLERRQQIG KLSWQIDEVD ELLGGGLETQ SITEVYGEFG AGKSQITHQL
     AVNVQLPPEQ GGLGGGCIFI DSEDTFRPER IDDMVRGLED EALEATLDDR EMEGSIDDEE
     TIKALVDDFL DKIHVAKAFN SNHQILLAEK AKELAGEHED TEWPVRLLCV DSLTAHFRAE
     YVGRGELAER QQKLNKHLHD LMRIGDLFNT GILVTNQVSS NPDSYFGDPT QPIGGNILGH
     TSTFRIYLRK SKGDKRIVRL VDAPNLADGE AIMRVQDAGL KPE