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Database: UniProt
Entry: G2WPS8_YEASK
LinkDB: G2WPS8_YEASK
Original site: G2WPS8_YEASK 
ID   G2WPS8_YEASK            Unreviewed;       564 AA.
AC   G2WPS8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=K7_DBF20 {ECO:0000313|EMBL:GAA27071.1};
GN   ORFNames=SYK7_072461 {ECO:0000313|EMBL:GAA27071.1};
OS   Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=721032 {ECO:0000313|EMBL:GAA27071.1, ECO:0000313|Proteomes:UP000001608};
RN   [1] {ECO:0000313|EMBL:GAA27071.1, ECO:0000313|Proteomes:UP000001608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608};
RX   PubMed=21900213; DOI=10.1093/dnares/dsr029;
RA   Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., Watanabe D.,
RA   Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., Kajiwara S.,
RA   Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., Masubuchi T.,
RA   Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., Ogata T., Ohta A.,
RA   Sato M., Shibasaki S., Takatsume Y., Tanimoto S., Tsuboi H., Nishimura A.,
RA   Yoda K., Ishikawa T., Iwashita K., Fujita N., Shimoi H.;
RT   "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai no.
RT   7.";
RL   DNA Res. 18:423-434(2011).
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         Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. COT1 subfamily. {ECO:0000256|ARBA:ARBA00038271}.
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DR   EMBL; DG000052; GAA27071.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2WPS8; -.
DR   HOGENOM; CLU_000288_67_4_1; -.
DR   Proteomes; UP000001608; Chromosome XVI.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd21776; MobB_Sid2p-like; 1.
DR   CDD; cd05600; STKc_Sid2p_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24356:SF417; CELL CYCLE PROTEIN KINASE DBF2-RELATED; 1.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          169..469
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          470..547
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          20..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   564 AA;  65900 MW;  4060165364836E40 CRC64;
     MFSRSDREVD DLAGNMSHLG FHDLNIPKPT SPQAQHRPAR KSENGRLTPG LPRSYKPYDS
     DDQDTFKNRI SLNHSPKKLP KDFHERASQS KTQRVVNVCQ LYFLDYYCDM FDYVISRRQR
     TKQVLRYLEQ QRSVKNVSNK VLNEEWALYL QREHEVLRKR RLKPKHKDFQ ILTQVGQGGY
     GQVYLAKKKD SDEICALKIL NKKLLFKLNE TNHVLTERDI LTTTRSDWLV KLLYAFQDPE
     SLYLAMEFVP GGDFRTLLIN TRILKSGHAR FYISEMFCAV NALHELGYTH RDLKPENFLI
     DATGHIKLTD FGLAAGTVSN ERIESMKIRL EEVKNLEFPA FTERSIEDRR KIYHNMRKTE
     INYANSMVGS PDYMALEVLE GKKYDFTVDY WSLGCMLFES LVGYTPFSGS STNETYENLR
     YWKKTLRRPR TEDRRAAFSD RTWDLITRLI ADPINRVRSF EQVRKMSYFA EINFETLRIS
     SPPFIPQLDD ETDAGYFDDF TNEEDMAKYA DVFKRQNKLS AMVDDSAVDS KLVGFTFRHR
     DGKQGSSGIL YNGSEHSDPF STFY
//
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