ID   A0A1R2CF40_9CILI        Unreviewed;       411 AA.
AC   A0A1R2CF40;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   03-MAY-2023, entry version 26.
DE   RecName: Full=Mitogen-activated protein kinase {ECO:0000256|ARBA:ARBA00012411, ECO:0000256|RuleBase:RU361165};
DE            EC=2.7.11.24 {ECO:0000256|ARBA:ARBA00012411, ECO:0000256|RuleBase:RU361165};
GN   ORFNames=SteCoe_10563 {ECO:0000313|EMBL:OMJ87638.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ87638.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ87638.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ87638.1};
RA   Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA   Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA   Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA   Sood P.;
RT   "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT   introns.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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=2.7.11.24; Evidence={ECO:0000256|RuleBase:RU361165};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361165};
CC   -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC       phosphorylation. {ECO:0000256|RuleBase:RU361165}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. MAP kinase subfamily. {ECO:0000256|RuleBase:RU361165}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMJ87638.1}.
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DR   EMBL; MPUH01000171; OMJ87638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R2CF40; -.
DR   OrthoDB; 5474493at2759; -.
DR   Proteomes; UP000187209; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd07834; STKc_MAPK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR   PANTHER; PTHR24055:SF561; MITOGEN-ACTIVATED PROTEIN KINASE 7; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01351; MAPK; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361165};
KW   Magnesium {ECO:0000256|RuleBase:RU361165};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000187209};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361165}.
FT   DOMAIN          39..330
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   411 AA;  47565 MW;  09696E9BB7DD3FD5 CRC64;
     MDRGKSGNRY GVSELGGPSG QFRKSTKVIG STFLLDERYQ IQDTLGSGAY GVVVSARDTR
     TGEIVAIKKI EKAFEHSTYT KRTLRELKIM RLLEHENIIR IKSIQLPRSR EEFDDIYVIV
     ELMETDLSSI IKSPQPLSDE HVQFFLYQIL RGLKFMHSAA ILHRDLKPRN LLVNANCDLK
     ICDFGLARPV IGDMKVNTSQ MTDYVATRWY RAPELLLTYK TYTSAMDVWS VGCIFGELLL
     RKPLLPGTDA NQQLEIIFNL IGTPSAEDIQ KIPHPRSREK VLRMPKRPEK DFNTIFRDAN
     PHAMDLLRRL LTFDPDKRIT VDQALEHPYL EGLHYPDDEP TTHPVSLFDF EYERQILTMK
     DLKDLMYDEI LLYHFNDKKQ EYVKAKAEYV ATHQPTLSFL RTNDESDEEM A
//