RADA_PICTO
ID RADA_PICTO Reviewed; 323 AA.
AC Q6L126;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=PTO0741;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT43326.1; -; Genomic_DNA.
DR RefSeq; WP_011177542.1; NC_005877.1.
DR AlphaFoldDB; Q6L126; -.
DR SMR; Q6L126; -.
DR STRING; 263820.PTO0741; -.
DR EnsemblBacteria; AAT43326; AAT43326; PTO0741.
DR GeneID; 2845061; -.
DR KEGG; pto:PTO0741; -.
DR PATRIC; fig|263820.9.peg.776; -.
DR eggNOG; arCOG00415; Archaea.
DR HOGENOM; CLU_041732_0_0_2; -.
DR OMA; TFRIYLR; -.
DR OrthoDB; 30130at2157; -.
DR Proteomes; UP000000438; 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..323
FT /note="DNA repair and recombination protein RadA"
FT /id="PRO_0000150101"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00348"
SQ SEQUENCE 323 AA; 35657 MW; 1FC6827E640BD6F1 CRC64;
MEKNDKEKRE LTIEDLPGVG DATAEKLRES GYDDIMTIAV ASPKDLAEIS GIAEGAAIKI
INAARKYADV GNFETGEEIL NKRKEIKKLT TGSSNLDNLL GGGLETQSIT EFFGEFGSGK
TQIMHQLAVN ATMPVEKNGF DSDVLIIDTE NTFRPERIIQ MARAKDLDPD QTLERIHVAR
AYNSHHQILL AEKAADMARE YKIRLLIVDS LTSHFRSEYV GRGSLAERQQ LLNRHMHDLL
KFGTIYNAVI AVTNQVSANP AVFFGDPMNP IGGNIVGHTA TFRIYLRKAK AGKRIARLID
SPYLPEGETV ITITESGITD GEK