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 05-JUL-2004 (Rel. 44, Last annotation update) DE Carbon catabolite derepressing protein kinase (EC 2.7.1.-). GN Name=SNF1; OS Candida glabrata (Yeast) (Torulopsis glabrata). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5478; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 90030 / NCCLS 84; RX MEDLINE=97101049; 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). 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 protein kinase family. SNF1 CC subfamily. 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; 1H0U. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW ATP-binding; Carbohydrate metabolism; Nuclear protein; KW Phosphorylation; Serine/threonine-protein kinase; Transferase. 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 Proton acceptor (By similarity). FT MOD_RES 194 194 Phosphothreonine (by autocatalysis) (By FT 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 //