RADA_PYRIL
ID RADA_PYRIL Reviewed; 330 AA.
AC Q9UWR5; A1RSF9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=DNA repair and recombination protein RadA;
GN Name=radA; OrderedLocusNames=Pisl_0713;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10672022; DOI=10.1046/j.1432-1327.2000.01108.x;
RA Spies M., Kil Y., Masui R., Kato R., Kujo C., Ohshima T., Kuramitsu S.,
RA Lanzov V.;
RT "The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum
RT is a DNA-dependent ATPase that exhibits two disparate catalytic modes, with
RT a transition temperature at 75 degrees C.";
RL Eur. J. Biochem. 267:1125-1137(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA88984.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB026115; BAA88984.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000504; ABL87891.1; -; Genomic_DNA.
DR RefSeq; WP_011762467.1; NC_008701.1.
DR AlphaFoldDB; Q9UWR5; -.
DR SMR; Q9UWR5; -.
DR STRING; 384616.Pisl_0713; -.
DR EnsemblBacteria; ABL87891; ABL87891; Pisl_0713.
DR GeneID; 4617625; -.
DR KEGG; pis:Pisl_0713; -.
DR eggNOG; arCOG00415; Archaea.
DR HOGENOM; CLU_041732_0_0_2; -.
DR OMA; TFRIYLR; -.
DR OrthoDB; 30130at2157; -.
DR BRENDA; 3.6.4.B7; 5240.
DR Proteomes; UP000002595; 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..330
FT /note="DNA repair and recombination protein RadA"
FT /id="PRO_0000150105"
FT BINDING 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 144
FT /note="P -> A (in Ref. 1; BAA88984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 36799 MW; 32B20F8C9E046647 CRC64;
MSSKKRKDAE VAQARVEITP DLDVEELEGV GRVTGAKLKE RGFFTVRDVA FASVKELAEI
VGNEERAQQI VEAARKMLGL HSFVSALEVY ERRKKIRRIS TGVRALDELL GGGIETRAVT
EVAGEFGSGK TQLCHQLAVM VQLPEERGGL GAKAIYIDTE NTFRPERIMQ IAKARGLDPD
QALNNIFYAR AYSSDHQMIL VDQAKSIIRQ HNVALLIVDS VIAHFRSEFP GRENLAERQQ
KLNKHVADLL RLADAYDVAV VITNQVMAQP DVFFGNPLRP AGGNILAHGA TYRLWLRKSK
ENIRIAKIFD SPYHPEGEVS FRITEEGLVD