(data stored in SCRATCH zone)

SWISSPROT: Q6FJ83_CANGA

ID   Q6FJ83_CANGA            Unreviewed;       462 AA.
AC   Q6FJ83;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 91.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62687.1};
GN   OrderedLocusNames=CAGL0M08404g {ECO:0000313|EMBL:CAG62687.1};
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:CAG62687.1, 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   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000256|SAAS:SAAS00594266}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   EMBL; CR380959; CAG62687.1; -; Genomic_DNA.
DR   RefSeq; XP_449711.1; XM_449711.1.
DR   ProteinModelPortal; Q6FJ83; -.
DR   STRING; 284593.XP_449711.1; -.
DR   EnsemblFungi; CAG62687; CAG62687; CAGL0M08404g.
DR   KEGG; cgr:CAGL0M08404g; -.
DR   EuPathDB; FungiDB:CAGL0M08404g; -.
DR   eggNOG; KOG0616; Eukaryota.
DR   eggNOG; ENOG410XPQQ; LUCA.
DR   HOGENOM; HOG000233033; -.
DR   InParanoid; Q6FJ83; -.
DR   KO; K04345; -.
DR   OMA; KICEADY; -.
DR   OrthoDB; EOG092C0HH3; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:EnsemblFungi.
DR   GO; GO:0010737; P:protein kinase A signaling; IEA:EnsemblFungi.
DR   GO; GO:0007265; P:Ras protein signal transduction; IEA:EnsemblFungi.
DR   InterPro; IPR000961; AGC-kinase_C.
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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
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; Q6FJ83.
DR   SWISS-2DPAGE; Q6FJ83.
KW   ATP-binding {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00593399};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Kinase {ECO:0000256|SAAS:SAAS00593820};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00593601};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00593706};
KW   Transferase {ECO:0000256|SAAS:SAAS00592725}.
FT   DOMAIN      152    406       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   DOMAIN      407    462       AGC-kinase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51285}.
SQ   SEQUENCE   462 AA;  53754 MW;  A8FD95EE67D21653 CRC64;
     MQILGENFKE VEIMDSEYDR RKLEEESAGP PGDEPMGQEN HEQLENHIDK ATESQMSKEL
     VVEDDQYDQG SHNIDYEARN KEEHNNGTNR TDGGHTQGTE QSNEQQTESN HEQQQQQRLQ
     QTEQHQQHQM ETVKKPLIYG ANTSGKYTLS DFQILRTLGT GSFGRVHLIR SNHNGRFYAL
     KALKKHTVVK LKQVEHTNDE RRMLSIVSHP FIIRMWGTFQ DSQHVFMVMD YIEGGELFSL
     LRKSQRFPNP VAKFYAAEVC LALEYLHSKE IIYRDLKPEN ILLDKNGHIK ITDFGFAKYV
     PDVTYTLCGT PDYIAPEVVS TKPYNKSVDW WSFGILIYEM LAGYTPFYDA NTMKTYEHIL
     NSELKFPSFF HPDVQDLLSK LITRDLSKRL GNLQNGSEDV KNHPWFSEVV WEKLLARYIE
     TPYEPPIQQG QGDTSQFDRY PEEEINYGVQ GEDPYADLFR EF
//

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