ID A0A1R2CF40_9CILI Unreviewed; 411 AA. AC A0A1R2CF40; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 19-JAN-2022, entry version 22. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MPUH01000171; OMJ87638.1; -; Genomic_DNA. DR OrthoDB; 741207at2759; -. 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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:RHEA. 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 Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 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 /note="ATP" 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 //