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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
 
 
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