(data stored in ACNUC8465 zone)

SWISSPROT: Q6FK01_CANGA

ID   Q6FK01_CANGA            Unreviewed;       767 AA.
AC   Q6FK01;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 110.
DE   RecName: Full=Serine/threonine-protein kinase RAD53 {ECO:0000256|PIRNR:PIRNR000661};
DE            EC=2.7.12.1 {ECO:0000256|PIRNR:PIRNR000661};
GN   OrderedLocusNames=CAGL0M02233g {ECO:0000313|CGD:CAL0137271,
GN   ECO:0000313|EMBL:CAG62419.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62419.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Controls S-phase checkpoint as well as G1 and G2 DNA
CC       damage checkpoints. Phosphorylates proteins on serine, threonine,
CC       and tyrosine. Prevents entry into anaphase and mitotic exit after
CC       DNA damage via regulation of the Polo kinase CDC5.
CC       {ECO:0000256|PIRNR:PIRNR000661}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000256|PIRNR:PIRNR000661}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR000661}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CHEK2 subfamily.
CC       {ECO:0000256|PIRNR:PIRNR000661}.
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DR   EMBL; CR380959; CAG62419.1; -; Genomic_DNA.
DR   RefSeq; XP_449443.1; XM_449443.1.
DR   ProteinModelPortal; Q6FK01; -.
DR   STRING; 284593.XP_449443.1; -.
DR   EnsemblFungi; CAG62419; CAG62419; CAGL0M02233g.
DR   KEGG; cgr:CAGL0M02233g; -.
DR   CGD; CAL0137271; CAGL0M02233g.
DR   EuPathDB; FungiDB:CAGL0M02233g; -.
DR   eggNOG; KOG0615; Eukaryota.
DR   eggNOG; ENOG410YA63; LUCA.
DR   HOGENOM; HOG000074515; -.
DR   InParanoid; Q6FK01; -.
DR   KO; K02831; -.
DR   OMA; HLPFNGK; -.
DR   OrthoDB; EOG092C2FDZ; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0009202; P:deoxyribonucleoside triphosphate biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0000077; P:DNA damage checkpoint; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:EnsemblFungi.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:EnsemblFungi.
DR   GO; GO:0042326; P:negative regulation of phosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0008104; P:protein localization; IEA:EnsemblFungi.
DR   InterPro; IPR020636; Ca/CaM-dep_Ca-dep_prot_Kinase.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR016256; Ser/Thr_kinase_Rad53.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   PANTHER; PTHR24347; PTHR24347; 1.
DR   Pfam; PF00498; FHA; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000661; Ser/Thr_PK_RAD53; 1.
DR   SMART; SM00240; FHA; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49879; SSF49879; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FK01.
DR   SWISS-2DPAGE; Q6FK01.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000661,
KW   ECO:0000256|SAAS:SAAS00426447};
KW   Cell cycle {ECO:0000256|PIRNR:PIRNR000661};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   DNA damage {ECO:0000256|PIRNR:PIRNR000661};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000661, ECO:0000256|SAAS:SAAS00426445};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000661,
KW   ECO:0000256|SAAS:SAAS00426483};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR000661};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000661,
KW   ECO:0000256|SAAS:SAAS00315853};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000661,
KW   ECO:0000256|SAAS:SAAS00426482};
KW   Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000661}.
FT   DOMAIN       65    115       FHA. {ECO:0000259|PROSITE:PS50006}.
FT   DOMAIN      188    457       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   DOMAIN      576    639       FHA. {ECO:0000259|PROSITE:PS50006}.
SQ   SEQUENCE   767 AA;  86732 MW;  AF6CE2ADADC268F2 CRC64;
     MMETQPTQQA TQATQKYLID NFTQEQIKKN SVYRVICTSG QIPIKDMEVD VEQIAKKKES
     IKKIWTFGRN NACDYHLGNI SRLSNKHFQI LLGEDGNLLL RDISTNGTWL NNQRIEKDRN
     HLLSQGDEIT VGLGVSSDII SLVIFINEKF RDYLEEVRQE LSSQGLKVSS KSNANPNINL
     TGIYKDFSIN DEVVGTGAFA TVKKAVERNT GKTFAVKIIN KRKVVGNMDG VSRELEVLQK
     LNHPRIVSLK AFYEDEANYY MVMEFISGGD LMDFVAAHGA VGEEAGREIS RQILEAIQYI
     HSKGISHRDL KPDNILIEQD DPVLVKITDF GLAKVQGNGS IMKTFCGTLA YVAPEVIGGF
     TGATGEEETE EERIEYSSLV DMWSMGCLVF VILTGHLPFS GSTQEQLYEQ IRKGSYHEGP
     LKDFRISDEA RDFIDGLLQV DQSKRMTVDD ALNHPWIKQC SSQFDANSMS SQVSLSQSMS
     QQKALESLDD AQYEFLKAQK KLQQDEPIND KLKDFKVPTQ PPTRFTQPKV INPIENIKKY
     TKSVKKKGSG KFMTFKPLPE SVIQESFEIK QGINPFFIGR SDDCNCRIDD NRLSRVHCFI
     LKKRHPIGKS IYESPAQGLD DIWYCHSGSN DSYVNDIRMT PGKKYLLQEG DEIKIIKDKQ
     KDFVIGFQVE LNDTTGLFNN GLGIPNEERS VTSQTEDELK LVSRLAKIMA AQRSSTKEAN
     ETMDQNRNLL KKVHSVSLSQ SITDPSRKVK RAKLDQTDHN AENMQFF
//

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