ID   TOS3_YEAS7              Reviewed;         560 AA.
AC   A6ZU08;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Serine/threonine-protein kinase TOS3;
DE            EC=2.7.11.1;
DE   AltName: Full=Target of SBF protein 3;
GN   Name=TOS3; ORFNames=SCY_1891;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: One of the three SNF1 protein kinases (with SAK1 and ELM1)
CC       which are required for growth on nonfermentable carbon sources and
CC       nonpreferred sugars and for response to environmental stress. Activates
CC       SNF1 by phosphorylation of its activation-loop 'Thr-210'. Required for
CC       the regulation by SNF1 of the transcription of a large set of genes,
CC       the modification the activity of metabolic enzymes, and the control of
CC       various nutrient-responsive cellular developmental processes.
CC       Phosphorylates also GAL83, MIG1 and SIP2 (By similarity).
CC       {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   -!- DOMAIN: The C-terminus (residues 351 to 560) is required for efficient
CC       SNF1 pathway signaling. {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AAFW02000099; EDN61946.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZU08; -.
DR   SMR; A6ZU08; -.
DR   EnsemblFungi; EDN61946; EDN61946; SCY_1891.
DR   HOGENOM; CLU_484098_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 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; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Stress response; Transferase.
FT   CHAIN           1..560
FT                   /note="Serine/threonine-protein kinase TOS3"
FT                   /id="PRO_0000333464"
FT   DOMAIN          50..344
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         56..64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   560 AA;  62064 MW;  199E5F98B78C29BF CRC64;
     MVLLKEPVQP LPRSSLLYNN ASNSSSRIKE TRKVKLLYNP LTKRQILNNF EILATLGNGQ
     YGKVKLARDL GTGALVAIKI LNRFEKRSGY SLQLKVENPR VNQEIEVMKR CHHENVVELY
     EILNDPESTK VYLVLEYCSR GPVKWCPENK MEIKAVGPSI LTFQQSRKVV LDVVSGLEYL
     HSQGITHRDI KPSNLLISSN GTVKISDFGV AMSTATGSTN IQSSHEQLLK SRALGTPAFF
     APELCSTEKE YSCSSAIDIW SLGVTIYCLL FGKLPFNANS GLELFDSIIN KPLEFPSYEE
     MLNGATSGIT MEEYTDAKDL LKKLLQKDPD KRIKLADIKV HPFMCHYGKS DAASVSTNLE
     TFHELKVSPP SSCKRVELVS LPVNSSFASL DSVYMENFDH NNLRTGADRN STYSPSIYDA
     NTLSPSAYHN IGSRESSYSS FSSFTSSTAF ASQISIQDAP AIGDQQCLIG ESGSSLRVNS
     CEFPQYTTMS PVGEYPFEST EASLSSTLTP VGNVPQRIKA HLVEGKSNSK DDLRIEADAS
     LVFEASDAQR TRRRMSLYKL