ID   A0A1R2CQL3_9CILI        Unreviewed;       359 AA.
AC   A0A1R2CQL3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   18-SEP-2019, entry version 15.
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;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ91270.1};
RN   [1] {ECO:0000313|EMBL:OMJ91270.1}
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.,
RA   Prabakaran S., Witkowska E., Larue G.E., Fisher S., Freeman R.M.,
RA   Gunawardena J., Chu W., Stover N.A., Gregory B.D., Nowacki M.,
RA   Derisi J., Roy S.W., Marshall W.F., 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,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24; 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
CC       protein kinase family. MAP kinase subfamily.
CC       {ECO:0000256|RuleBase:RU361165}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OMJ91270.1}.
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DR   EMBL; MPUH01000085; OMJ91270.1; -; Genomic_DNA.
DR   OrthoDB; 741207at2759; -.
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,
KW   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,
KW   ECO:0000256|SAAS:SAAS00574095}.
FT   DOMAIN       13    301       Protein kinase. {ECO:0000259|PROSITE:
FT                                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
//