ID   MSK1_MEDSA              Reviewed;         411 AA.
AC   P51137;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Glycogen synthase kinase-3 homolog MsK-1;
DE            EC=2.7.11.1;
GN   Name=MSK-1;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8401615; DOI=10.1111/j.1365-313x.1993.00847.x;
RA   Paz A., Jonak C., Boegre L., Meskiene I., Mairinger T., Szalay A.,
RA   Heberle-Bors E., Hirt H.;
RT   "The MsK family of alfalfa protein kinase genes encodes homologues of
RT   shaggy/glycogen synthase kinase-3 and shows differential expression
RT   patterns in plant organs and development.";
RL   Plant J. 3:847-856(1993).
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   -!- TISSUE SPECIFICITY: Leaves, petioles, roots, stems and nodes.
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; X68411; CAA48474.1; -; mRNA.
DR   PIR; S37644; S37644.
DR   AlphaFoldDB; P51137; -.
DR   SMR; P51137; -.
DR   BRENDA; 2.7.11.26; 3078.
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   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   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..411
FT                   /note="Glycogen synthase kinase-3 homolog MsK-1"
FT                   /id="PRO_0000086400"
FT   DOMAIN          75..359
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        200
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         81..89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         235
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  46774 MW;  55A0ED4A495A74CC CRC64;
     MASVGVAPTS GFREVLGDGE IGVDDILPEE MSDMKIRDDR EMEATVVDGN GTETGHIIVT
     TIGGRNGQPK QTISYMAERV VGHGSFGVVF QAKCLETGET VAIKKVLQDK RYKNRELQTM
     RLLDHPNVVS LKHCFFSTTE KDELYLNLVL EYVPETVHRV IKHYSKLNQR MPMIYVKLYT
     YQIFRALSYI HRCIGVCHRD IKPQNLLVNP HTHQVKLCDF GSAKVLVKGE PNISYICSRY
     YRAPELIFGA TEYTTAIDVW SVGCVLAELL LGQPLFPGER GVDQLVEIIK VLGTPTREEI
     KCMNPNYTEF KFPQIKAHPW HKIFHKRMPA EAVDLVSRLL QYSPNLRCQA LDCLTHPFFD
     ELRDPNARLP TGRFLPPLFN FKPHELKGVP VETLMKLVPE HARKQCPFLG L