CSK2A_THEAN
ID CSK2A_THEAN Reviewed; 348 AA.
AC Q4U925; Q8WPV4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Casein kinase II subunit alpha;
DE EC=2.7.11.1;
DE AltName: Full=TaCKIIalpha;
DE Short=CK II;
GN ORFNames=TA10630;
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INITIATION SITE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12891701; DOI=10.1002/jcp.10291;
RA Biermann R., Schnittger L., Beyer D., Ahmed J.S.;
RT "Initiation of translation and cellular localization of Theileria annulata
RT casein kinase IIalpha: implication for its role in host cell
RT transformation.";
RL J. Cell. Physiol. 196:444-453(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara;
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. The alpha chain contains the catalytic site (By
CC similarity). {ECO:0000250}.
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 -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12891701}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI76678.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ315847; CAC86226.1; -; Genomic_DNA.
DR EMBL; CR940353; CAI76678.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q4U925; -.
DR SMR; Q4U925; -.
DR STRING; 5874.XP_953303.1; -.
DR VEuPathDB; PiroplasmaDB:TA10630; -.
DR eggNOG; KOG0668; Eukaryota.
DR InParanoid; Q4U925; -.
DR OrthoDB; 1098380at2759; -.
DR Proteomes; UP000001950; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR017441; Protein_kinase_ATP_BS.
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; 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; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..348
FT /note="Casein kinase II subunit alpha"
FT /id="PRO_0000232676"
FT DOMAIN 55..340
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 61..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 170
FT /note="H -> P (in Ref. 1; CAC86226)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="R -> G (in Ref. 1; CAC86226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 41295 MW; 3EFE3CBEE38F78DC CRC64;
MDQMEVPDND KNRKYPTKDL KIILPKTYAD VNSKKGPEYW DYENITLKWN VPDSYEIVRK
IGRGKFSEVF EGLNTVTKDK CVIKILKPVK KKKIKREIKI LQNLRGGPNI IKLLDIVKDP
QSRTPSLIFE HVNNTDFKTL YPTLTIQDIK YYIYQLLKAM NYCHSQGIMH RDIKPHNVMI
DHEKKILRLI DWGLAEFYHP EQEYSVRVAT RYYKGPELLV DMRYYDYSLD IWSIGCMLAG
IIFKKEPFFY GHDNYDQLVK IAKVLGTEDL HRYFEKYGLK FAPAYQEILG NHSKKPWTKF
VHHENQHLVS PEVMDLLDRM LVYDHTKRIT PLEAMEHPFF NEIKNNSV
