RADA_SACS2
ID RADA_SACS2 Reviewed; 324 AA.
AC Q55075;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=DNA repair and recombination protein RadA;
GN Name=radA; OrderedLocusNames=SSO0250;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9573041; DOI=10.1101/gad.12.9.1248;
RA Seitz E.M., Brockman J.P., Sandler S.J., Clark A.J., Kowalczykowski S.C.;
RT "RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand
RT exchange.";
RL Genes Dev. 12:1248-1253(1998).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10931349; DOI=10.1046/j.1365-2958.2000.02009.x;
RA Seitz E.M., Kowalczykowski S.C.;
RT "The DNA binding and pairing preferences of the archaeal RadA protein
RT demonstrate a universal characteristic of DNA strand exchange proteins.";
RL Mol. Microbiol. 37:555-560(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.
CC -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family.
CC {ECO:0000305}.
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DR EMBL; U45310; AAC44123.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40589.1; -; Genomic_DNA.
DR PIR; F90166; F90166.
DR PIR; S71093; S71093.
DR RefSeq; WP_009990512.1; NC_002754.1.
DR PDB; 2BKE; X-ray; 3.20 A; A=1-324.
DR PDB; 2DFL; X-ray; 2.90 A; A=1-324.
DR PDB; 2Z43; X-ray; 1.93 A; A/B/C=1-324.
DR PDB; 2ZUB; X-ray; 2.90 A; A/B=1-324.
DR PDB; 2ZUC; X-ray; 3.30 A; A/B=1-324.
DR PDB; 2ZUD; X-ray; 3.20 A; A/B=1-324.
DR PDBsum; 2BKE; -.
DR PDBsum; 2DFL; -.
DR PDBsum; 2Z43; -.
DR PDBsum; 2ZUB; -.
DR PDBsum; 2ZUC; -.
DR PDBsum; 2ZUD; -.
DR AlphaFoldDB; Q55075; -.
DR SMR; Q55075; -.
DR STRING; 273057.SSO0250; -.
DR EnsemblBacteria; AAK40589; AAK40589; SSO0250.
DR GeneID; 44129219; -.
DR KEGG; sso:SSO0250; -.
DR PATRIC; fig|273057.12.peg.244; -.
DR eggNOG; arCOG00415; Archaea.
DR HOGENOM; CLU_041732_0_0_2; -.
DR InParanoid; Q55075; -.
DR OMA; TFRIYLR; -.
DR PhylomeDB; Q55075; -.
DR BRENDA; 3.6.4.B7; 6163.
DR EvolutionaryTrace; Q55075; -.
DR Proteomes; UP000001974; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA recombination; DNA-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..324
FT /note="DNA repair and recombination protein RadA"
FT /id="PRO_0000150107"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 225
FT /note="N -> I (in Ref. 1; AAC44123)"
FT /evidence="ECO:0000305"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:2Z43"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:2Z43"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2DFL"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 184..200
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2Z43"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:2Z43"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2Z43"
FT HELIX 226..247
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:2Z43"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2Z43"
SQ SEQUENCE 324 AA; 35867 MW; AD3CCD9DFF541BCD CRC64;
MSNEVEQKKN 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
