(data stored in ACNUC8465 zone)

SWISSPROT: SNF1_CANGA

ID   SNF1_CANGA              Reviewed;         612 AA.
AC   Q00372; Q6FJ61;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   30-AUG-2017, entry version 124.
DE   RecName: Full=Carbon catabolite-derepressing protein kinase;
DE            EC=2.7.11.1;
GN   Name=SNF1; OrderedLocusNames=CAGL0M08910g;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 90030 / DSM 11226 / NCCLS 84;
RX   PubMed=8945576;
RA   Petter R., Kwon-Chung K.J.;
RT   "Disruption of the SNF1 gene abolishes trehalose utilization in the
RT   pathogenic yeast Candida glabrata.";
RL   Infect. Immun. 64:5269-5273(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
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   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., 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: Essential for release from glucose repression. It
CC       interacts and has functional relationship to the regulatory
CC       protein SNF4. Could phosphorylates CAT8 (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
DR   EMBL; L78130; AAB48642.1; -; Genomic_DNA.
DR   EMBL; CR380959; CAG62709.1; -; Genomic_DNA.
DR   RefSeq; XP_449733.1; XM_449733.1.
DR   ProteinModelPortal; Q00372; -.
DR   SMR; Q00372; -.
DR   STRING; 284593.XP_449733.1; -.
DR   EnsemblFungi; CAG62709; CAG62709; CAGL0M08910g.
DR   KEGG; cgr:CAGL0M08910g; -.
DR   CGD; CAL0136473; SNF1.
DR   EuPathDB; FungiDB:CAGL0M08910g; -.
DR   eggNOG; KOG0586; Eukaryota.
DR   eggNOG; ENOG410XNQ0; LUCA.
DR   HOGENOM; HOG000233016; -.
DR   InParanoid; Q00372; -.
DR   KO; K12761; -.
DR   OMA; RWHFGIR; -.
DR   OrthoDB; EOG092C0QJU; -.
DR   BRENDA; 2.7.11.1; 1113.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0005641; C:nuclear envelope lumen; IEA:EnsemblFungi.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:EnsemblFungi.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:EnsemblFungi.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IEA:EnsemblFungi.
DR   GO; GO:0071940; P:fungal-type cell wall assembly; IEA:EnsemblFungi.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:EnsemblFungi.
DR   GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IEA:EnsemblFungi.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:EnsemblFungi.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IEA:EnsemblFungi.
DR   GO; GO:0006468; P:protein phosphorylation; IGI:CGD.
DR   GO; GO:0007124; P:pseudohyphal growth; IEA:EnsemblFungi.
DR   GO; GO:0001302; P:replicative cell aging; IEA:EnsemblFungi.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:EnsemblFungi.
DR   GO; GO:0090606; P:single-species surface biofilm formation; IEA:EnsemblFungi.
DR   GO; GO:0005993; P:trehalose catabolic process; IMP:CGD.
DR   CDD; cd14334; UBA_SNF1_fungi; 1.
DR   InterPro; IPR032270; AMPK_C.
DR   InterPro; IPR028375; KA1/Ssp2_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   InterPro; IPR013896; SNF1_UBA.
DR   Pfam; PF16579; AdenylateSensor; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08587; UBA_2; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF103243; SSF103243; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Q00372.
DR   SWISS-2DPAGE; Q00372.
KW   ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase;
KW   Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    612       Carbon catabolite-derepressing protein
FT                                kinase.
FT                                /FTId=PRO_0000086667.
FT   DOMAIN       39    290       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND      45     53       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   COMPBIAS      6     17       Poly-His.
FT   ACT_SITE    161    161       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING      68     68       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     194    194       Phosphothreonine; by autocatalysis.
FT                                {ECO:0000250}.
FT   CONFLICT     69     69       I -> S (in Ref. 1; AAB48642).
FT                                {ECO:0000305}.
FT   CONFLICT     85     85       E -> D (in Ref. 1; AAB48642).
FT                                {ECO:0000305}.
FT   CONFLICT    446    446       Missing (in Ref. 1; AAB48642).
FT                                {ECO:0000305}.
FT   CONFLICT    497    497       E -> H (in Ref. 1; AAB48642).
FT                                {ECO:0000305}.
FT   CONFLICT    511    511       K -> N (in Ref. 1; AAB48642).
FT                                {ECO:0000305}.
SQ   SEQUENCE   612 AA;  70209 MW;  4532C99E39709238 CRC64;
     MENKEHHHHH HHHHHHHSNG SYVSNKVSSL ADGSRVGNYQ IVKTLGEGSF GKVKLAYHVT
     TGQKVALKII NKKVLAKSDM QGRIEREISY LRLLRHPHII KLYDVIKSKD EIIMVIEYAG
     NELFDYIVQR NKMSEQEARR FFQQIISAVE YCHRHKIVHR DLKPENLLLD EHLNVKIADF
     GLSNIMTDGN FLKTSCGSPN YAAPEVISGK LYAGPEVDVW SCGVILYVML CRRLPFDDES
     IPVLFKNISN GVYTLPKFLS PGASDLIKRM LIVNPLNRIS IHEIMQDEWF KVDLAEYLVP
     QDLKQQEQFN KKSGNEENVE EIDDEMVVTL SKTMGYDKDE IYEALESSED TPAYNEIRNA
     YILIKDNKSL IKDMKQDNNV TQELDTFLSQ SPPTFQQNGD GMKASEDQKK KHSGRRLASS
     VTQQRTFHQP PFMDQSKEED STISILPTSL PQIHRANMLA QGLPAASKIS PLVTKKSKTR
     WHFGIRSRSY PLDVMGEIYI ALKNLGAEWA KPSEEDLWTI RVRWKYDSDE SRLIEDGVKK
     IPNLMKIVIQ LFQIETNNYL VDFKFDGWES TYGDSTISTN MSEDEMSTFS AYPFLHLTTK
     LIMELAVNSQ GN
//

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