ID   RADA_SULIY              Reviewed;         324 AA.
AC   C3N7M8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=YG5714_1966;
OS   Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=439386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.G.57.14 / Yellowstone #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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}.
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; CP001403; ACP46222.1; -; Genomic_DNA.
DR   RefSeq; WP_012711863.1; NC_012622.1.
DR   AlphaFoldDB; C3N7M8; -.
DR   SMR; C3N7M8; -.
DR   EnsemblBacteria; ACP46222; ACP46222; YG5714_1966.
DR   GeneID; 7813047; -.
DR   GeneID; 7939623; -.
DR   GeneID; 8761952; -.
DR   KEGG; siy:YG5714_1966; -.
DR   HOGENOM; CLU_041732_0_0_2; -.
DR   OMA; TFRIYLR; -.
DR   Proteomes; UP000002308; 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.
FT   CHAIN           1..324
FT                   /note="DNA repair and recombination protein RadA"
FT                   /id="PRO_1000205330"
FT   BINDING         114..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00348"
SQ   SEQUENCE   324 AA;  35840 MW;  3437186AD6533918 CRC64;
     MSNEVEQKKS IKTINDLPGI SQTVINKLIE AGYSSLETLA VASPQDLSVA AGIPLSTAQK
     IIKEARDALD IRFKTALEVK KERMNVKKIS TGSQALDGLL AGGIETRTMT EFFGEFGSGK
     TQLCHQLSVN VQLPPEKGGL SGKAVYIDTE GTFRWERIEN MAKALGLDID NVMNNIYYIR
     AINTDHQIAI VDDLQELVSK DPSIKLIVVD SVTSHFRAEY PGRENLAVRQ QKLNKHLHQL
     TRLAEVYDIA VIITNQVMAR PDMFYGDPTV AVGGHTLYHV PGIRIQLKKS RGNRRIARVV
     DAPHLPEGEV VFALTEEGIR DAEE