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 03-APR-2013, entry version 95. 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 mitosporic Nakaseomyces. 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 -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBCELLULAR LOCATION: Nucleus membrane; Peripheral membrane CC protein (By similarity). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK CC Ser/Thr protein kinase family. SNF1 subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 30-303, 437-609. DR GeneID; 2891294; -. DR GenomeReviews; CR380959_GR; CAGL0M08910g. DR KEGG; cgr:CAGL0M08910g; -. DR HOGENOM; HOG000233016; -. DR KO; K12761; -. DR OMA; RIDIRAI; -. DR OrthoDB; EOG4Q5CXQ; -. DR BRENDA; 2.7.11.1; 1113. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_cat_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR013896; Ubiquitin-assoc_dom. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF08587; UBA_2; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Kinase_like; 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; KW ATP-binding; Carbohydrate metabolism; Complete proteome; Kinase; KW Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; KW 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. FT NP_BIND 45 53 ATP (By similarity). FT COMPBIAS 6 17 Poly-His. FT ACT_SITE 161 161 Proton acceptor (By similarity). FT BINDING 68 68 ATP (By similarity). FT MOD_RES 194 194 Phosphothreonine; by autocatalysis (By FT similarity). FT CONFLICT 69 69 I -> S (in Ref. 1; AAB48642). FT CONFLICT 85 85 E -> D (in Ref. 1; AAB48642). FT CONFLICT 446 446 Missing (in Ref. 1; AAB48642). FT CONFLICT 497 497 E -> H (in Ref. 1; AAB48642). FT CONFLICT 511 511 K -> N (in Ref. 1; AAB48642). 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 //