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 03-AUG-2022, entry version 150.
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 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC 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; DOI=10.1128/iai.64.12.5269-5273.1996;
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., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., 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 interacts
CC and has functional relationship to the regulatory protein SNF4. Could
CC phosphorylate CAT8 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; L78130; AAB48642.1; -; Genomic_DNA.
DR EMBL; CR380959; CAG62709.1; -; Genomic_DNA.
DR RefSeq; XP_449733.1; XM_449733.1.
DR AlphaFoldDB; Q00372; -.
DR SMR; Q00372; -.
DR STRING; 5478.XP_449733.1; -.
DR EnsemblFungi; CAG62709; CAG62709; CAGL0M08910g.
DR GeneID; 2891294; -.
DR KEGG; cgr:CAGL0M08910g; -.
DR CGD; CAL0136473; SNF1.
DR VEuPathDB; FungiDB:CAGL0M08910g; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_3_1; -.
DR InParanoid; Q00372; -.
DR OMA; KALNYEW; -.
DR BRENDA; 2.7.11.1; 1113.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0000144; C:cellular bud neck septin ring; 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:0005774; C:vacuolar membrane; IEA:EnsemblFungi.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0007155; P:cell adhesion; IEA:EnsemblFungi.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEA:EnsemblFungi.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; 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:2000222; P:positive regulation of pseudohyphal growth; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IGI:CGD.
DR GO; GO:2000217; P:regulation of invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; 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_sf.
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;
KW ATP-binding; Carbohydrate metabolism; Kinase; Membrane; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..612
FT /note="Carbon catabolite-derepressing protein kinase"
FT /id="PRO_0000086667"
FT DOMAIN 39..290
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 194
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 69
FT /note="I -> S (in Ref. 1; AAB48642)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="E -> D (in Ref. 1; AAB48642)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="Missing (in Ref. 1; AAB48642)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="E -> H (in Ref. 1; AAB48642)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="K -> N (in Ref. 1; AAB48642)"
FT /evidence="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
