ID   CSK2A_ENCCU             Reviewed;         319 AA.
AC   Q8SRU0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable casein kinase II subunit alpha homolog;
DE            Short=CK II subunit alpha;
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:P68400};
GN   Name=CKA1; OrderedLocusNames=ECU05_1510;
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   -!- FUNCTION: Catalytic subunit of a constitutively active
CC       serine/threonine-protein kinase complex that phosphorylates a large
CC       number of substrates containing acidic residues C-terminal to the
CC       phosphorylated serine or threonine. {ECO:0000250|UniProtKB:P68400}.
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         Evidence={ECO:0000250|UniProtKB:P68400};
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; Evidence={ECO:0000250|UniProtKB:P68400};
CC   -!- SUBUNIT: Tetramer composed of two alpha chains, one beta chain and one
CC       beta' chain. {ECO:0000250|UniProtKB:P15790}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AL590445; CAD26671.1; -; Genomic_DNA.
DR   RefSeq; NP_597494.1; NM_001041360.1.
DR   AlphaFoldDB; Q8SRU0; -.
DR   SMR; Q8SRU0; -.
DR   STRING; 284813.Q8SRU0; -.
DR   GeneID; 859161; -.
DR   KEGG; ecu:ECU05_1510; -.
DR   VEuPathDB; MicrosporidiaDB:ECU05_1510; -.
DR   HOGENOM; CLU_000288_70_4_1; -.
DR   InParanoid; Q8SRU0; -.
DR   OMA; ACEKRPQ; -.
DR   OrthoDB; 1098380at2759; -.
DR   Proteomes; UP000000819; Chromosome V.
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   CDD; cd14132; STKc_CK2_alpha; 1.
DR   InterPro; IPR045216; CK2_alpha.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24054; PTHR24054; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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..319
FT                   /note="Probable casein kinase II subunit alpha homolog"
FT                   /id="PRO_0000385507"
FT   DOMAIN          37..316
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         43..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   319 AA;  37688 MW;  936EB6555C2A3927 CRC64;
     MVVVTVARSN ADVNEKKDER YWNYECYTIT TGSIEKYQIY QRMGRGKYSE VFEGRKDREK
     IVIKALKPVR KAKICREVLI LRNLSHKNII KLMDVVVDPE SQIYSLIFEY IEHEDYAKIF
     EKLCYKDIVE YSRQILSALS YCHSMGIIHR DIKPQNMVIN QARRELKIID WGLAEFYHPK
     KEYSVRVASR YYKGPELLVD YPYYDYSLDI WSFGCVLAEL VFKKRPFFHG ESNSDQLVKI
     ARILGYTHLK KYVRKYKMAP LNPKYEGVGE RVLLSSFTPP GKTGLYTNAI DLLEKILIYD
     HQDRPTADEC LRHPLFESR