ID   RADA_PYRNV              Reviewed;         330 AA.
AC   B1YC14;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Tneu_1953;
OS   Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS   V24Sta) (Thermoproteus neutrophilus).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=444157;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL   Submitted (MAR-2008) 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. {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; CP001014; ACB40868.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1YC14; -.
DR   SMR; B1YC14; -.
DR   STRING; 444157.Tneu_1953; -.
DR   EnsemblBacteria; ACB40868; ACB40868; Tneu_1953.
DR   KEGG; tne:Tneu_1953; -.
DR   eggNOG; arCOG00415; Archaea.
DR   HOGENOM; CLU_041732_0_0_2; -.
DR   OMA; TFRIYLR; -.
DR   Proteomes; UP000001694; 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_1000120513"
FT   BINDING         124..131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00348"
SQ   SEQUENCE   330 AA;  36580 MW;  38AFD507479393B5 CRC64;
     MSSRKKKDAE VAQASVEVNP DLDVEELEGV GRVTGAKLKE RGFFTVRDVA FASVKELAEV
     VGNEERALQI VEAARKMLGL HSFVSALEVY ERRKTIRRIS TGVKALDELL GGGIETRAVT
     EVAGEFGSGK TQLCHQLAVM VQLPEERGGL GAKAIYIDTE NTFRPERIMQ IAKARGLDPD
     QALNNIFYAR AYSSDHQMIL VDQAKSIIKQ NNVALLVVDS VIAHFRSEFP GRENLAERQQ
     KLNKHVADLL RLADAYDVAV VITNQVMAQP DVFFGNPLRP AGGNILAHGA TYRLWLRKSK
     ENIRIAKIFD SPYHPEGEVS FRITEEGLVD