ID RADA_HALSA Reviewed; 343 AA. AC Q9HMM4; O93747; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 24-JUL-2024, entry version 128. DE RecName: Full=DNA repair and recombination protein RadA; GN Name=radA; Synonyms=radA1; OrderedLocusNames=VNG_2473G; OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) OS (Halobacterium halobium). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001. OX NCBI_TaxID=64091; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9922255; DOI=10.1128/jb.181.3.907-915.1999; RA Sandler S.J., Hugenholtz P., Schleper C., DeLong E.F., Pace N.R., RA Clark A.J.; RT "Diversity of radA genes from cultured and uncultured archaea: comparative RT analysis of putative RadA proteins and their use as a phylogenetic RT marker."; RL J. Bacteriol. 181:907-915(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1; RX PubMed=11016950; DOI=10.1073/pnas.190337797; RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R., RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P., RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M., RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J., RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., RA DasSarma S.; RT "Genome sequence of Halobacterium species NRC-1."; RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000). 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 (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG20547.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF090196; AAD16062.1; -; Genomic_DNA. DR EMBL; AE004437; AAG20547.1; ALT_INIT; Genomic_DNA. DR PIR; G84397; G84397. DR PIR; T43802; T43802. DR RefSeq; WP_012289511.1; NC_002607.1. DR AlphaFoldDB; Q9HMM4; -. DR SMR; Q9HMM4; -. DR STRING; 64091.VNG_2473G; -. DR PaxDb; 64091-VNG_2473G; -. DR GeneID; 68694984; -. DR KEGG; hal:VNG_2473G; -. DR PATRIC; fig|64091.14.peg.1915; -. DR HOGENOM; CLU_041732_0_0_2; -. DR InParanoid; Q9HMM4; -. DR OrthoDB; 31129at2157; -. DR PhylomeDB; Q9HMM4; -. DR Proteomes; UP000000554; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. 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; cd19515; archRadA; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR020588; RecA_ATP-bd. DR InterPro; IPR020587; RecA_monomer-monomer_interface. DR NCBIfam; TIGR02236; recomb_radA; 1. DR PANTHER; PTHR22942:SF39; DNA REPAIR PROTEIN RAD51 HOMOLOG 1; 1. DR PANTHER; PTHR22942; RECA/RAD51/RADA DNA STRAND-PAIRING FAMILY MEMBER; 1. DR Pfam; PF14520; HHH_5; 1. DR Pfam; PF08423; Rad51; 2. DR PIRSF; PIRSF005856; Rad51; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00278; HhH1; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF47794; Rad51 N-terminal domain-like; 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_0000150092" FT BINDING 107..114 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT CONFLICT 1..2 FT /note="MP -> MRGAPPTRRYIS (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 8 FT /note="E -> D (in Ref. 1; AAD16062)" FT /evidence="ECO:0000305" FT CONFLICT 15..17 FT /note="ATA -> PTT (in Ref. 1; AAD16062)" FT /evidence="ECO:0000305" FT CONFLICT 23 FT /note="N -> S (in Ref. 1; AAD16062)" FT /evidence="ECO:0000305" FT CONFLICT 30..32 FT /note="SLA -> ILT (in Ref. 1; AAD16062)" FT /evidence="ECO:0000305" FT CONFLICT 75 FT /note="R -> P (in Ref. 1; AAD16062)" FT /evidence="ECO:0000305" FT CONFLICT 132 FT /note="G -> A (in Ref. 1; AAD16062)" FT /evidence="ECO:0000305" FT CONFLICT 263 FT /note="K -> P (in Ref. 1; AAD16062)" FT /evidence="ECO:0000305" FT CONFLICT 266 FT /note="N -> D (in Ref. 1; AAD16062)" FT /evidence="ECO:0000305" SQ SEQUENCE 343 AA; 37423 MW; 847D17052968EF2D CRC64; MPESDLEELP GVGPATAEKL RDNGFDAFQS LAVANSAELS NTADIGESTA ADVIQAAREA ADVGGFETGA TVLERREQIG KLTWNIPEVD DLLGGGVETQ SITEVYGEFG AGKSQVTHQL AVNVQLPTEY GGLHGRAVFI DSEDTFRPER IDDMVRGLSD ETLQAAMEAH EIEGSTDDED TLTELVDAFL DKIHVAKGFN SNHQMLLAEK AKEIASEHED GDWPVRMLTV DSLTAHFRAE YVGRGELADR QQKLNKHLHD LEKVGNLYNA AVLVTNQVQS NPDAFFGDPT KPIGGNILGH KSTFRMYLRK SKNDKRIVKL VDAPNLADGE AVMRVQDEGL KPE //