ID   Y255_ENCCU              Reviewed;         516 AA.
AC   Q8SSH1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Probable serine/threonine-protein kinase ECU02_0550;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=ECU02_0550;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   PREDICTION OF FUNCTION.
RX   PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA   Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA   Barton G.J.;
RT   "The complement of protein kinases of the microsporidium Encephalitozoon
RT   cuniculi in relation to those of Saccharomyces cerevisiae and
RT   Schizosaccharomyces pombe.";
RL   BMC Genomics 8:309-309(2007).
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; AL590442; CAD25086.1; -; Genomic_DNA.
DR   RefSeq; NP_584582.1; NM_001040771.1.
DR   AlphaFoldDB; Q8SSH1; -.
DR   SMR; Q8SSH1; -.
DR   STRING; 284813.Q8SSH1; -.
DR   GeneID; 858572; -.
DR   KEGG; ecu:ECU02_0550; -.
DR   VEuPathDB; MicrosporidiaDB:ECU02_0550; -.
DR   HOGENOM; CLU_531021_0_0_1; -.
DR   InParanoid; Q8SSH1; -.
DR   OMA; FIPRCED; -.
DR   OrthoDB; 683807at2759; -.
DR   Proteomes; UP000000819; Chromosome II.
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   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   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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..516
FT                   /note="Probable serine/threonine-protein kinase ECU02_0550"
FT                   /id="PRO_0000384425"
FT   DOMAIN          4..230
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        120
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   516 AA;  58646 MW;  3E5ADB0C9D0858EE CRC64;
     MERYKLRQVI GEGASSTVYS GVSARGEEVA VKVVPRKGRS TGMVYREIEM LSTIKHENIV
     GIVGRFESKK HVYMVEELCD FNLVSFLNEY EVDEDVALKI LRMILCGLRH IHSLGIIHRD
     LKLGNILLKG NTVKICDFGL SCYVEENNSE FCGTMDYLAP EVVDGKKYSF GVDMWSAGVV
     FYVLLTKKKF CESLDSLECS EELRDLLEKL LERDESKRAD ASEALMHRSF SRFIPRCEDF
     RGLPGFERGT KYGVLRKAGD SVELGSIRID ARRGKRHGGG RKHGDLGCLC GEEFTYSVYV
     DSEEIEPAFI TNGQLKTLGL LTAHVKAMRE KTPKIIIDDD GNKFYYMFSG GFVYVGKELT
     LRARGGKYEM SRRSGEKTYL EAVPDFLYEA IGGLEARCKA IDKEVCWFSR ESPVLIDCSS
     HQQFSMSCIS QVSEMSIRNR VEYDYIESTG WCIRDGLNFL FLMNDGEMFE VLCPDLAVRY
     RGRLLFIDDR LPMKLKRSLK GISPFLRSLC DGCYMS