ID   GSK1_MAGOR              Reviewed;         394 AA.
AC   Q3S406;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Glycogen synthase kinase 1 {ECO:0000303|PubMed:28424497};
DE            EC=2.7.11.1 {ECO:0000269|PubMed:30776962};
GN   Name=GSK1 {ECO:0000303|PubMed:28424497};
OS   Magnaporthe oryzae (Rice blast fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=318829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, DISRUPTION
RP   PHENOTYPE, AND SUBCELLULAR LOCATION.
RC   STRAIN=Guyane 11;
RX   PubMed=28424497; DOI=10.1038/s41598-017-01006-w;
RA   Zhou T., Dagdas Y.F., Zhu X., Zheng S., Chen L., Cartwright Z.,
RA   Talbot N.J., Wang Z.;
RT   "The glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is
RT   required for fungal development and pathogenicity in Magnaporthe oryzae.";
RL   Sci. Rep. 7:945-945(2017).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=30776962; DOI=10.1080/15548627.2019.1580104;
RA   Yin Z., Chen C., Yang J., Feng W., Liu X., Zuo R., Wang J., Yang L.,
RA   Zhong K., Gao C., Zhang H., Zheng X., Wang P., Zhang Z.;
RT   "Histone acetyltransferase MoHat1 acetylates autophagy-related proteins
RT   MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and
RT   pathogenicity in Magnaporthe oryzae.";
RL   Autophagy 15:1234-1257(2019).
CC   -!- FUNCTION: Protein kinase that acts downstream of the MPS1 MAPK cascade
CC       as a highly conservative signal modulator that dictates growth,
CC       conidiation and pathogenicity (PubMed:28424497). Phosphorylates HAT1 at
CC       'Ser-8' to block its translocation from the nucleus to the cytoplasm
CC       where HAT1 positively regulates appressorium development and
CC       pathogenicity (PubMed:30776962). {ECO:0000269|PubMed:28424497,
CC       ECO:0000269|PubMed:30776962}.
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:0000269|PubMed:30776962};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28424497}.
CC       Note=Mainly localizes to the cytoplasm at the conidial stage.
CC       {ECO:0000269|PubMed:28424497}.
CC   -!- INDUCTION: Expression is regulated by MPS1 MAP kinase, particularly
CC       under stress conditions. {ECO:0000269|PubMed:28424497}.
CC   -!- DISRUPTION PHENOTYPE: Leads to significant delay in mycelial growth,
CC       complete loss of conidiation and inability to penetrate the host
CC       surface by mycelia-formed appressorium-like structures, consequently
CC       resulting in loss of pathogenicity. {ECO:0000269|PubMed:28424497}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR   EMBL; DQ168585; ABA02071.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3S406; -.
DR   SMR; Q3S406; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051094; P:positive regulation of developmental process; IEA:UniProt.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd14137; STKc_GSK3; 1.
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; IPR039192; STKc_GSK3.
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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Germination; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Stress response; Transferase; Virulence.
FT   CHAIN           1..394
FT                   /note="Glycogen synthase kinase 1"
FT                   /id="PRO_0000453108"
FT   DOMAIN          35..318
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         41..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   394 AA;  45383 MW;  E1DB6459F2E6678B CRC64;
     MSQNRPAAFN TLRMGEVIRE KVQDGITGET RDLQYTQCKI VGNGSFGVVF QTKLSPSNED
     AAIKRVLQDK RFKNRELQIM RIVRHPNIVQ LKAFYYSNGE RRDEVYLNLV QEFVPETVYR
     ASRFFNKMKT TMPILEVKLY IYQLFRALAY IHSQGICHRD IKPQNLLLDP TTGILKLCDF
     GSAKILVENE PNVSYICSRY YRAPELIFGA TNYTTKIDVW STGCVMAELM LGQPLFPGES
     GIDQLVEIIK VLGTPTREQI RTMNPNYMEH KFPQIKPHPF NRVLRKADNN AIDLIARLLE
     YTPTERLGAI DAMVHPFFDD LRNPSTKLPD SRHQTGQVRD LPPLFDFNRH ELSIAPQLNH
     QLVPPHVRPT LAAQGLDIDH FTPMRKEDML ARLD