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RADA_AERPE
ID   RADA_AERPE              Reviewed;         319 AA.
AC   P0CW92; Q8X233; Q8X263; Q8X264; Q8X265; Q8X266; Q8X267; Q9YFY1;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=DNA repair and recombination protein RadA;
GN   Name=radA; OrderedLocusNames=APE_0119;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(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; BA000002; BAA79030.1; -; Genomic_DNA.
DR   PIR; D72766; D72766.
DR   AlphaFoldDB; P0CW92; -.
DR   SMR; P0CW92; -.
DR   STRING; 272557.APE_0119; -.
DR   EnsemblBacteria; BAA79030; BAA79030; APE_0119.
DR   KEGG; ape:APE_0119; -.
DR   PATRIC; fig|272557.25.peg.81; -.
DR   eggNOG; arCOG00415; Archaea.
DR   OMA; TFRIYLR; -.
DR   Proteomes; UP000002518; 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; Reference proteome.
FT   CHAIN           1..319
FT                   /note="DNA repair and recombination protein RadA"
FT                   /id="PRO_0000150088"
FT   BINDING         111..118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   319 AA;  35320 MW;  714F88859D619E25 CRC64;
     MGEDKREIKD ITDLPGVGPT TAQKLMEAGY TTLEAIAAAT PQEVSQATGI PILTAQKIVD
     AAREALNIDF KTAYDLKIES MNIKKITTGS RNLDELLGGG IETKTITELF GEFGSGKTQI
     CHQLSVNVQL PEDKGGLEGK AVYVDTEGTF RWERIEQMAR GVGLDPDEVM KNIYWIRAIN
     SHHQIAIVDK LFTMVKNDNI KLVVVDSVTS HFRAEFPGRE NLAMRQQLLN RHLHQLMRLA
     DIFNVAVVIT NQVMARPDVF YGDPTQAVGG HVLGHAPGVR VYLKKSRGNK RIARVVDAPH
     LPEGETVFAI TEWGIRDPE
 
 
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