ID A0A1R2CQL3_9CILI Unreviewed; 359 AA. AC A0A1R2CQL3; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 11-DEC-2019, entry version 16. DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127}; DE EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127}; GN ORFNames=SteCoe_6250 {ECO:0000313|EMBL:OMJ91270.1}; OS Stentor coeruleus. OC Eukaryota; Alveolata; Ciliophora; Postciliodesmatophora; Heterotrichea; OC Heterotrichida; Stentoridae; Stentor. OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ91270.1, ECO:0000313|Proteomes:UP000187209}; RN [1] {ECO:0000313|EMBL:OMJ91270.1, ECO:0000313|Proteomes:UP000187209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ91270.1}; 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-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=2.7.11.24; CC Evidence={ECO:0000256|SAAS:SAAS01125144}; 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 ECO:0000256|SAAS:SAAS01125154}; 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:OMJ91270.1}. 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; MPUH01000085; OMJ91270.1; -; Genomic_DNA. DR OrthoDB; 741207at2759; -. DR Proteomes; UP000187209; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. 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|RuleBase:RU000304, ECO:0000256|SAAS:SAAS00574094}; KW Kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574086}; KW Magnesium {ECO:0000256|RuleBase:RU361165}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00574135}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00574114}; KW Transferase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574095}. FT DOMAIN 13..301 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" SQ SEQUENCE 359 AA; 41488 MW; F24D498E984992D4 CRC64; MSEDIETHIL RKYEILQKLG KGAYGIVWKA IDKKTREVIA LKKVFDAFQN ATDAQRTFRE IMFLQELNGH ENIIRLLNVI RAENDRDIYL VFDFMETDLH AVIRANILEE IHKQYVTYQI LKALKYMHTG QLLHRDLKPS NILLNSECLV KVADFGLARS VASQEEGSNA VLTDYVATRW YRAPEILLGS TKYSKAVDMW SLGCIIGEML HGKPIFPGTS TLNQLDRILE LTGRPSAEDI ESIQSNLAST MLDSLPPGRA KTYHDFFPSA SDDALDLVRK LLQFNPSKRL TIEQCLRHPY VAQFHNPDDE PACNRTITIS INDDKKFSIR EYRDRIYTDI SKKKKEIRRR HLQARGYYH //