ID SNF1_CANGA STANDARD; PRT; 611 AA. AC Q00372; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE CARBON CATABOLITE DEREPRESSING PROTEIN KINASE (EC 2.7.1.-). GN SNF1. OS Candida glabrata (Yeast) (Torulopsis glabrata). OC Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales; OC anamorphic Saccharomycetales; Candida. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NCCLS84; RX MEDLINE; 97101049. 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). 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 -!- SUBCELLULAR LOCATION: ASSOCIATED WITH THE NUCLEAR MEMBRANE (BY CC SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC SNF1 SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; -. DR HSSP; P24941; 1AQ1. DR INTERPRO; IPR000719; -. DR INTERPRO; IPR002290; -. DR PFAM; PF00069; pkinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Phosphorylation; Carbohydrate metabolism; Nuclear protein. FT DOMAIN 6 17 POLY-HIS. FT DOMAIN 39 290 PROTEIN KINASE. FT NP_BIND 45 53 ATP (BY SIMILARITY). FT BINDING 68 68 ATP (BY SIMILARITY). FT ACT_SITE 161 161 BY SIMILARITY. FT MOD_RES 194 194 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). SQ SEQUENCE 611 AA; 70049 MW; 89E17812A4900CD0 CRC64; MENKEHHHHH HHHHHHHSNG SYVSNKVSSL ADGSRVGNYQ IVKTLGEGSF GKVKLAYHVT TGQKVALKSI NKKVLAKSDM QGRIDREISY 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 STISIPTSLP QIHRANMLAQ GLPAASKISP LVTKKSKTRW HFGIRSRSYP LDVMGHIYIA LKNLGAEWAN PSEEDLWTIR VRWKYDSDES RLIEDGVKKI PNLMKIVIQL FQIETNNYLV DFKFDGWEST YGDSTISTNM SEDEMSTFSA YPFLHLTTKL IMELAVNSQG N //