RADA_CENSY
ID RADA_CENSY Reviewed; 398 AA.
AC O93748; A0RU75;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=DNA repair and recombination protein RadA;
GN Name=radA; OrderedLocusNames=CENSYa_0250;
OS Cenarchaeum symbiosum (strain A).
OC Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX NCBI_TaxID=414004;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A;
RX PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT symbiosum.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-398.
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 -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family.
CC {ECO:0000305}.
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DR EMBL; DP000238; ABK76892.1; -; Genomic_DNA.
DR EMBL; AF090197; AAD16063.1; -; Genomic_DNA.
DR AlphaFoldDB; O93748; -.
DR SMR; O93748; -.
DR STRING; 414004.CENSYa_0250; -.
DR EnsemblBacteria; ABK76892; ABK76892; CENSYa_0250.
DR KEGG; csy:CENSYa_0250; -.
DR PATRIC; fig|414004.10.peg.217; -.
DR HOGENOM; CLU_041732_0_0_2; -.
DR OMA; EARICKV; -.
DR Proteomes; UP000000758; 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; 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 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; Reference proteome.
FT CHAIN 1..398
FT /note="DNA repair and recombination protein RadA"
FT /id="PRO_0000150090"
FT REGION 320..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 398 AA; 42742 MW; 4D32116EA2B7EB68 CRC64;
MNIENFDLSD LEGVGPVTKK KLEDSGVHSM MDLVVRGPVE LGEISSMSSE ICEKIVTIAR
KRLAETGAIT KDFASGSEIY KRRQSIGMIT TGTDALDALL GGGIETQAIT EVFGEFGSGK
TQFCHTMCVT TQKPKEEGGL GGGVMYIDTE GTFRPERVVT IAKANNMDPA KLLDGIIVAR
AYNSSHQVLI LEEAGKTIQE ENIKLIISDS TTGLFRSEYL GRGTLASRQQ KLGRYIRLLA
RIAETYNCAV LATNQVSSSP DSFFGDPTRP VGGNVVGHAS TYRIYFRKGG KNKRVAKIID
SPHHPASEAV FELGERGVQD TEEHLKQLDK EAKKAEKEAA KPVKKSKAKA KADGPEGVDA
TPAIEPEGID TAAAEPEDIG TIVSESADAG EPADPELE