ID   SNF1_CANTR              Reviewed;         619 AA.
AC   O94168;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Carbon catabolite-derepressing protein kinase;
DE            EC=2.7.11.1;
GN   Name=SNF1;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   PubMed=10525743; DOI=10.1007/s002030050768;
RA   Kanai T., Ogawa K., Ueda M., Tanaka A.;
RT   "Expression of the SNF1 gene from candida tropicalis is required for growth
RT   on various carbon sources, including glucose.";
RL   Arch. Microbiol. 172:256-263(1999).
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; AB024535; BAA75889.1; -; Genomic_DNA.
DR   AlphaFoldDB; O94168; -.
DR   SMR; O94168; -.
DR   VEuPathDB; FungiDB:CTMYA2_056000; -.
DR   VEuPathDB; FungiDB:CTRG_05385; -.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..619
FT                   /note="Carbon catabolite-derepressing protein kinase"
FT                   /id="PRO_0000086668"
FT   DOMAIN          52..303
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         58..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         207
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   619 AA;  70323 MW;  0FCF1FC3DCE706D7 CRC64;
     MSEQNQGQPD QQHSGDHQHH HHHHHHHHHS QQPAQPIPID PNVNPANRIG RYQIIKTLGE
     GSFGKVKLAQ HVGTGQKVAL KIINRKTLAK SDMQGRVERE ISYLRLLRHP HIIKLYDVIK
     SKDEIIMVIE FAGKELFDYI VQRGKMPEDE ARRFFQQIIA AVEYCHRHKI VHRDLKPENL
     LLDDQLNVKI ADFGLSNIMT DGNFLKTSCG SPNYAAPEVI SGKLYAGPEV DVWSSGVILY
     VMLCGRLPFD DEFIPALFKK ISNGVYTLPN YLSPGAKHLL TRMLVVNPLN RITIHEIMED
     EWFKQDMPDY LLPPDLSKIK TSKIDIDEDV ISALSVTMGY DRDEIISVIE KANREAAAGG
     ATPTNQSKST NEVLDAYLLM KENHTLVKDL KKSKSENIES FLSLSPPPSS SFPNPGSTSS
     APGVQQSLTY QTLATVPDLS TLPNSTIAIL PTSLPSIHRA YMMETKVNDP QQQIPAPQPT
     KKLKTRWHFG IRSRSYPLDV MGEIYRALKN LGAEWAKPTE EELWTIRVRW KYDSTPQLRV
     WQRTNLMKMQ IQLFQLEPNN YLVDFKFDGW EQTSDESKND ASLDYKQQDL DEVGSFSAYP
     FLHLATRLIM ELAVNSQSG