RADA_METVO
ID RADA_METVO Reviewed; 322 AA.
AC O73948;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA repair and recombination protein RadA;
GN Name=radA;
OS Methanococcus voltae.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=2188;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RA Reich C.I., Buldak G.L., McNeil L.K.;
RT "The RadA protein from the archaeon Methanococcus voltae: a functional
RT homolog of eukaryotic Rad51.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-254.
RX PubMed=9922255; DOI=10.1128/jb.181.3.907-915.1999;
RA Sandler S.J., Hugenholtz P., Schleper C., DeLong E.F., Pace N.R.,
RA Clark A.J.;
RT "Diversity of radA genes from cultured and uncultured archaea: comparative
RT analysis of putative RadA proteins and their use as a phylogenetic
RT marker.";
RL J. Bacteriol. 181:907-915(1999).
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 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC O73948; O73948: radA; NbExp=2; IntAct=EBI-15585834, EBI-15585834;
CC -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family.
CC {ECO:0000305}.
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DR EMBL; AF008421; AAC23499.1; -; Genomic_DNA.
DR EMBL; AF090200; AAD16066.1; -; Genomic_DNA.
DR PDB; 1T4G; X-ray; 2.00 A; A=1-322.
DR PDB; 1XU4; X-ray; 2.40 A; A=1-322.
DR PDB; 2B21; X-ray; 2.40 A; A=1-322.
DR PDB; 2F1H; X-ray; 2.70 A; A=1-322.
DR PDB; 2F1I; X-ray; 2.90 A; A=1-322.
DR PDB; 2F1J; X-ray; 2.30 A; A=1-322.
DR PDB; 2FPK; X-ray; 2.10 A; A=1-322.
DR PDB; 2FPL; X-ray; 2.30 A; A=1-322.
DR PDB; 2FPM; X-ray; 2.00 A; A=1-322.
DR PDB; 2GDJ; X-ray; 2.50 A; A=63-322.
DR PDB; 2I1Q; X-ray; 1.90 A; A=1-322.
DR PDB; 3FYH; X-ray; 1.90 A; A=1-322.
DR PDB; 3NTU; X-ray; 1.90 A; A=4-322.
DR PDB; 4DC9; X-ray; 2.60 A; A/B/C/D/E/F=61-322.
DR PDB; 4QKQ; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=61-322.
DR PDBsum; 1T4G; -.
DR PDBsum; 1XU4; -.
DR PDBsum; 2B21; -.
DR PDBsum; 2F1H; -.
DR PDBsum; 2F1I; -.
DR PDBsum; 2F1J; -.
DR PDBsum; 2FPK; -.
DR PDBsum; 2FPL; -.
DR PDBsum; 2FPM; -.
DR PDBsum; 2GDJ; -.
DR PDBsum; 2I1Q; -.
DR PDBsum; 3FYH; -.
DR PDBsum; 3NTU; -.
DR PDBsum; 4DC9; -.
DR PDBsum; 4QKQ; -.
DR AlphaFoldDB; O73948; -.
DR SMR; O73948; -.
DR DIP; DIP-29120N; -.
DR BRENDA; 3.6.4.B7; 3268.
DR EvolutionaryTrace; O73948; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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.
FT CHAIN 1..322
FT /note="DNA repair and recombination protein RadA"
FT /id="PRO_0000150099"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:3NTU"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:2I1Q"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:2I1Q"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3FYH"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:2I1Q"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4DC9"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:2I1Q"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:2I1Q"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:2I1Q"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2I1Q"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2I1Q"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 141..152
FT /evidence="ECO:0007829|PDB:2I1Q"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:2I1Q"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:2I1Q"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:2I1Q"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:2I1Q"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:2I1Q"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:4QKQ"
FT HELIX 227..247
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3NTU"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1XU4"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:2I1Q"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:2I1Q"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2I1Q"
SQ SEQUENCE 322 AA; 35189 MW; 8A9F5EFB927344B6 CRC64;
MSDNLTDLPG VGPSTAEKLV EAGYIDFMKI ATATVGELTD IEGISEKAAA KMIMGARDLC
DLGFKSGIDL LKQRSTVWKL STSSSELDSV LGGGLESQSV TEFAGVFGSG KTQIMHQSCV
NLQNPEFLFY DEEAVSKGEV AQPKAVYIDT EGTFRPERIM QMAEHAGIDG QTVLDNTFVA
RAYNSDMQML FAEKIEDLIQ EGNNIKLVVI DSLTSTFRNE YTGRGKLAER QQKLGRHMAT
LNKLADLFNC VVLVTNQVSA KPDAFFGMAE QAIGGHIVGH AATFRFFVRK GKGDKRVAKL
YDSPHLPDAE AIFRITEKGI QD
