CSK2A_THEPA
ID CSK2A_THEPA Reviewed; 348 AA.
AC P28547; Q4N1S0;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Casein kinase II subunit alpha;
DE Short=CK II;
DE EC=2.7.11.1;
GN OrderedLocusNames=TP04_0659;
OS Theileria parva (East coast fever infection agent).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5875;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1378299; DOI=10.1021/bi00142a004;
RA Ole-Moiyoi O.K., Sugimoto C., Conrad P.A., Macklin M.D.;
RT "Cloning and characterization of the casein kinase II alpha subunit gene
RT from the lymphocyte-transforming intracellular protozoan parasite Theileria
RT parva.";
RL Biochemistry 31:6193-6202(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Muguga;
RX PubMed=15994558; DOI=10.1126/science.1110439;
RA Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT lymphocytes.";
RL Science 309:134-137(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:0000250}.
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=AAA18216.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAN32012.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M92084; AAA18216.1; ALT_INIT; Unassigned_DNA.
DR EMBL; AAGK01000004; EAN32012.1; ALT_INIT; Genomic_DNA.
DR PIR; A43297; A43297.
DR RefSeq; XP_764295.1; XM_759202.1.
DR AlphaFoldDB; P28547; -.
DR SMR; P28547; -.
DR STRING; 5875.XP_764295.1; -.
DR EnsemblProtists; EAN32012; EAN32012; TP04_0659.
DR GeneID; 3501181; -.
DR KEGG; tpv:TP04_0659; -.
DR VEuPathDB; PiroplasmaDB:TpMuguga_04g00659; -.
DR eggNOG; KOG0668; Eukaryota.
DR InParanoid; P28547; -.
DR BRENDA; 2.7.11.1; 6275.
DR Proteomes; UP000001949; Unassembled WGS sequence.
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_0000085905"
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"
SQ SEQUENCE 348 AA; 41213 MW; D840229D5675581F CRC64;
MDQMDLVDTD KSRKYPAKDL KIILPKTYAD VNSKKGPEYW DYENITLKWN VPDSYEIVRK
IGRGKFSEVF EGINTVTKDK CVIKILKPVK KKKIKREIKI LQNLRGGPNI IKLLDIVKDP
QSRTPSLIFE HVNNTDFKTL YPTLSIQDIK YYIYQLLKAM NYCHSQGIMH RDIKPHNVMI
DHEKKILRLI DWGLAEFYHP EQEYSVRVAT RYYKGPELLV DMRYYDYSLD IWSIGCMLAG
IIFKKEPFFY GHDNYDQLVK IAKVLGTEDL HRYFEKYGLK FAPAYQEILG NHSKKPWTKF
VHHENQHLVS PEVMDLLDRM LVYDHTKRIT PLEAMEHPFF NEIKNNSV
