RADA_PYRFU
ID RADA_PYRFU Reviewed; 349 AA.
AC O74036;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=DNA repair and recombination protein RadA;
GN Name=radA; OrderedLocusNames=PF1926;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10486005; DOI=10.1007/pl00006570;
RA DiRuggiero J., Brown J.R., Bogert A.P., Robb F.T.;
RT "DNA repair systems in archaea: mementos from the last universal common
RT ancestor?";
RL J. Mol. Evol. 49:474-484(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10903318; DOI=10.1074/jbc.m004557200;
RA Komori K., Miyata T., DiRuggiero J., Holley-Shanks R., Hayashi I.,
RA Cann I.K.O., Mayanagi K., Shinagawa H., Ishino Y.;
RT "Both RadA and RadB are involved in homologous recombination in Pyrococcus
RT furiosus.";
RL J. Biol. Chem. 275:33782-33790(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; AF052597; AAC34998.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL82050.1; -; Genomic_DNA.
DR RefSeq; WP_011013066.1; NC_018092.1.
DR PDB; 1PZN; X-ray; 2.85 A; A/B/C/D/E/F/G=1-349.
DR PDB; 4A6P; X-ray; 1.50 A; A=108-349.
DR PDB; 4A6X; X-ray; 1.55 A; A/B=108-349.
DR PDB; 4B2I; X-ray; 1.30 A; A=108-349.
DR PDB; 4B2L; X-ray; 1.50 A; A=108-349.
DR PDB; 4B2P; X-ray; 1.60 A; A=108-349.
DR PDB; 4B32; X-ray; 1.50 A; A=108-349.
DR PDB; 4B33; X-ray; 1.50 A; A=108-349.
DR PDB; 4B34; X-ray; 1.55 A; A=108-349.
DR PDB; 4B35; X-ray; 1.40 A; A=108-349.
DR PDB; 4B3B; X-ray; 1.19 A; A=108-349.
DR PDB; 4B3C; X-ray; 1.90 A; A=108-349.
DR PDB; 4B3D; X-ray; 1.59 A; A/C=108-349.
DR PDB; 4D6P; X-ray; 1.48 A; A/B=108-349.
DR PDB; 4UQO; X-ray; 1.88 A; A/B=108-349.
DR PDB; 5FOS; X-ray; 1.35 A; A=108-349, C=93-108.
DR PDB; 5FOT; X-ray; 1.19 A; A=108-349.
DR PDB; 5FOU; X-ray; 1.50 A; A=108-349.
DR PDB; 5FOV; X-ray; 1.74 A; A/C=108-349.
DR PDB; 5FOW; X-ray; 1.80 A; A/C=108-349.
DR PDB; 5FOX; X-ray; 1.30 A; A=108-349.
DR PDB; 5FPK; X-ray; 1.34 A; A=108-349.
DR PDB; 5J4H; X-ray; 1.37 A; A=108-349.
DR PDB; 5J4K; X-ray; 1.35 A; A=108-349.
DR PDB; 5J4L; X-ray; 1.13 A; A=108-349.
DR PDB; 5JEC; X-ray; 2.34 A; A/B=108-349.
DR PDB; 5JED; X-ray; 1.33 A; A=108-349.
DR PDB; 5JEE; X-ray; 1.49 A; A=108-349.
DR PDB; 5JFG; X-ray; 1.77 A; A=108-349.
DR PDB; 5KDD; X-ray; 1.99 A; A/B=108-349.
DR PDB; 5L8V; X-ray; 1.50 A; A=108-349.
DR PDB; 5LB2; X-ray; 2.10 A; A=108-349.
DR PDB; 5LB4; X-ray; 1.98 A; A=108-349.
DR PDB; 5LBI; X-ray; 1.43 A; A=108-287, A=301-349.
DR PDB; 5QUB; X-ray; 1.35 A; A=108-349.
DR PDB; 5QUC; X-ray; 1.43 A; A=108-349.
DR PDB; 5QUD; X-ray; 1.30 A; A=108-349.
DR PDB; 5QUE; X-ray; 1.30 A; A=108-349.
DR PDB; 5QUF; X-ray; 1.35 A; A=108-349.
DR PDB; 5QUG; X-ray; 1.48 A; A=108-349.
DR PDB; 5QUH; X-ray; 1.38 A; A=108-349.
DR PDB; 5QUI; X-ray; 1.40 A; A=108-349.
DR PDB; 5QUJ; X-ray; 1.42 A; A=108-349.
DR PDB; 5QUK; X-ray; 1.16 A; A=108-349.
DR PDB; 5QUL; X-ray; 1.28 A; A/B=108-349.
DR PDB; 5QUM; X-ray; 1.93 A; A/B=108-349.
DR PDB; 5QUN; X-ray; 1.24 A; A=108-349.
DR PDB; 5QUO; X-ray; 1.34 A; A=108-349.
DR PDB; 5QUP; X-ray; 1.25 A; A=108-349.
DR PDB; 5QUQ; X-ray; 1.25 A; A=108-349.
DR PDB; 5QUR; X-ray; 1.25 A; A=108-349.
DR PDB; 5QUS; X-ray; 1.25 A; A=108-349.
DR PDB; 5QUT; X-ray; 1.25 A; A=108-349.
DR PDB; 5QUU; X-ray; 1.25 A; A=108-349.
DR PDB; 6TUU; X-ray; 1.74 A; A/B/C/D=108-349.
DR PDB; 6TV3; X-ray; 1.50 A; A=108-349.
DR PDB; 6TW3; X-ray; 1.35 A; A=108-349.
DR PDB; 6TW4; X-ray; 1.73 A; A=108-349.
DR PDB; 6TW9; X-ray; 1.52 A; A=108-349.
DR PDB; 6XTW; X-ray; 2.31 A; A/B=108-349.
DR PDB; 6XUF; X-ray; 1.24 A; A=108-349.
DR PDB; 6XUJ; X-ray; 1.54 A; A=108-349.
DR PDBsum; 1PZN; -.
DR PDBsum; 4A6P; -.
DR PDBsum; 4A6X; -.
DR PDBsum; 4B2I; -.
DR PDBsum; 4B2L; -.
DR PDBsum; 4B2P; -.
DR PDBsum; 4B32; -.
DR PDBsum; 4B33; -.
DR PDBsum; 4B34; -.
DR PDBsum; 4B35; -.
DR PDBsum; 4B3B; -.
DR PDBsum; 4B3C; -.
DR PDBsum; 4B3D; -.
DR PDBsum; 4D6P; -.
DR PDBsum; 4UQO; -.
DR PDBsum; 5FOS; -.
DR PDBsum; 5FOT; -.
DR PDBsum; 5FOU; -.
DR PDBsum; 5FOV; -.
DR PDBsum; 5FOW; -.
DR PDBsum; 5FOX; -.
DR PDBsum; 5FPK; -.
DR PDBsum; 5J4H; -.
DR PDBsum; 5J4K; -.
DR PDBsum; 5J4L; -.
DR PDBsum; 5JEC; -.
DR PDBsum; 5JED; -.
DR PDBsum; 5JEE; -.
DR PDBsum; 5JFG; -.
DR PDBsum; 5KDD; -.
DR PDBsum; 5L8V; -.
DR PDBsum; 5LB2; -.
DR PDBsum; 5LB4; -.
DR PDBsum; 5LBI; -.
DR PDBsum; 5QUB; -.
DR PDBsum; 5QUC; -.
DR PDBsum; 5QUD; -.
DR PDBsum; 5QUE; -.
DR PDBsum; 5QUF; -.
DR PDBsum; 5QUG; -.
DR PDBsum; 5QUH; -.
DR PDBsum; 5QUI; -.
DR PDBsum; 5QUJ; -.
DR PDBsum; 5QUK; -.
DR PDBsum; 5QUL; -.
DR PDBsum; 5QUM; -.
DR PDBsum; 5QUN; -.
DR PDBsum; 5QUO; -.
DR PDBsum; 5QUP; -.
DR PDBsum; 5QUQ; -.
DR PDBsum; 5QUR; -.
DR PDBsum; 5QUS; -.
DR PDBsum; 5QUT; -.
DR PDBsum; 5QUU; -.
DR PDBsum; 6TUU; -.
DR PDBsum; 6TV3; -.
DR PDBsum; 6TW3; -.
DR PDBsum; 6TW4; -.
DR PDBsum; 6TW9; -.
DR PDBsum; 6XTW; -.
DR PDBsum; 6XUF; -.
DR PDBsum; 6XUJ; -.
DR AlphaFoldDB; O74036; -.
DR SMR; O74036; -.
DR STRING; 186497.PF1926; -.
DR BindingDB; O74036; -.
DR EnsemblBacteria; AAL82050; AAL82050; PF1926.
DR GeneID; 41713747; -.
DR KEGG; pfu:PF1926; -.
DR PATRIC; fig|186497.12.peg.1998; -.
DR eggNOG; arCOG00415; Archaea.
DR HOGENOM; CLU_041732_0_0_2; -.
DR OMA; TFRIYLR; -.
DR OrthoDB; 30130at2157; -.
DR PhylomeDB; O74036; -.
DR BRENDA; 3.6.4.B7; 5243.
DR EvolutionaryTrace; O74036; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA recombination; DNA-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..349
FT /note="DNA repair and recombination protein RadA"
FT /id="PRO_0000150104"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:1PZN"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1PZN"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:1PZN"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1PZN"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:1PZN"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:5FOS"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:5J4L"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5J4L"
FT STRAND 127..139
FT /evidence="ECO:0007829|PDB:5J4L"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:5J4L"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5J4L"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:5J4L"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:5J4L"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:5J4L"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:5J4L"
FT HELIX 208..225
FT /evidence="ECO:0007829|PDB:5J4L"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5J4L"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:5J4L"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5J4L"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:5J4L"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:5QUK"
FT HELIX 253..275
FT /evidence="ECO:0007829|PDB:5J4L"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:5J4L"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:5QUD"
FT STRAND 310..317
FT /evidence="ECO:0007829|PDB:5J4L"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:5J4L"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:5J4L"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:6XUF"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:5J4L"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:5J4L"
SQ SEQUENCE 349 AA; 38399 MW; 726E9DF1D67AB039 CRC64;
MAGEEVKEID EFEELGFEPA TEETPKKKKK EKIIRSIEDL PGVGPATAEK LREAGYDTLE
AIAVASPIEL KEVAGISEGT ALKIIQAARK AANLGTFMRA DEYLKKRATI GRISTGSKSL
DKLLGGGIET QAITEVFGEF GSGKTQLAHT LAVMVQLPPE EGGLNGSVIW IDTENTFRPE
RIREIAQNRG LDPDEVLKHI YVARAFNSNH QMLLVQQAED KIKELLNTDR PVKLLIVDSL
TSHFRSEYIG RGALAERQQK LAKHLADLHR LANLYDIAVF VTNQVQARPD AFFGDPTRPI
GGHILAHSAT LRVYLRKGKG GKRIARLIDA PHLPEGEAVF SITEKGIED
