CSK2A_MAIZE
ID CSK2A_MAIZE Reviewed; 332 AA.
AC P28523;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Casein kinase II subunit alpha;
DE EC=2.7.11.1;
DE AltName: Full=CK II;
DE AltName: Full=CK2-alpha;
GN Name=ACK2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73 Inbred;
RX PubMed=1756176; DOI=10.1016/0167-4781(91)90230-j;
RA Dobrowolska G., Boldyreff B., Issinger O.-G.;
RT "Cloning and sequencing of the casein kinase 2 alpha subunit from Zea
RT mays.";
RL Biochim. Biophys. Acta 1129:139-140(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=9564028; DOI=10.1093/emboj/17.9.2451;
RA Niefind K., Guerra B., Pinna L.A., Issinger O.G., Schomburg D.;
RT "Crystal structure of the catalytic subunit of protein kinase CK2 from Zea
RT mays at 2.1-A resolution.";
RL EMBO J. 17:2451-2462(1998).
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.
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 (possible).
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; X61387; CAA43659.1; -; mRNA.
DR PIR; S19726; S19726.
DR RefSeq; XP_008668648.1; XM_008670426.1.
DR PDB; 1DAW; X-ray; 2.20 A; A=2-328.
DR PDB; 1DAY; X-ray; 2.20 A; A=2-328.
DR PDB; 1DS5; X-ray; 3.16 A; A/B/C/D=1-332.
DR PDB; 1F0Q; X-ray; 2.63 A; A=1-332.
DR PDB; 1J91; X-ray; 2.22 A; A/B=1-332.
DR PDB; 1JAM; X-ray; 2.18 A; A=1-332.
DR PDB; 1LP4; X-ray; 1.86 A; A=1-332.
DR PDB; 1LPU; X-ray; 1.86 A; A=1-332.
DR PDB; 1LR4; X-ray; 2.00 A; A=1-332.
DR PDB; 1M2P; X-ray; 2.00 A; A=2-326.
DR PDB; 1M2Q; X-ray; 1.79 A; A=2-328.
DR PDB; 1M2R; X-ray; 1.70 A; A=2-328.
DR PDB; 1OM1; X-ray; 1.68 A; A=1-332.
DR PDB; 1ZOE; X-ray; 1.77 A; A=1-332.
DR PDB; 1ZOG; X-ray; 2.30 A; A=1-332.
DR PDB; 1ZOH; X-ray; 1.81 A; A=1-332.
DR PDB; 2OXD; X-ray; 2.30 A; A=1-332.
DR PDB; 2OXX; X-ray; 2.30 A; A=1-332.
DR PDB; 2OXY; X-ray; 1.81 A; A/B=1-332.
DR PDB; 2PVH; X-ray; 2.20 A; A=1-332.
DR PDB; 2PVJ; X-ray; 1.70 A; A=1-332.
DR PDB; 2PVK; X-ray; 1.90 A; A=1-332.
DR PDB; 2PVL; X-ray; 1.90 A; A=1-332.
DR PDB; 2PVM; X-ray; 2.00 A; A=1-332.
DR PDB; 2PVN; X-ray; 2.00 A; A=1-332.
DR PDB; 2QC6; X-ray; 1.85 A; A=1-332.
DR PDB; 3BE9; X-ray; 2.00 A; A=1-332.
DR PDB; 3FL5; X-ray; 2.30 A; A=1-332.
DR PDB; 3KXG; X-ray; 1.70 A; A=2-328.
DR PDB; 3KXH; X-ray; 1.70 A; A=2-328.
DR PDB; 3KXM; X-ray; 1.75 A; A=2-328.
DR PDB; 3KXN; X-ray; 2.00 A; A=2-328.
DR PDB; 3PVG; X-ray; 1.50 A; A=2-332.
DR PDB; 3PWD; X-ray; 2.20 A; A=1-332.
DR PDB; 3PZH; X-ray; 1.92 A; A=1-332.
DR PDB; 4ANM; X-ray; 1.70 A; A=2-332.
DR PDB; 4DGM; X-ray; 1.65 A; A=2-327.
DR PDB; 4DGN; X-ray; 1.75 A; A=2-327.
DR PDB; 4RLK; X-ray; 1.24 A; A=1-332.
DR PDB; 5TS8; X-ray; 1.45 A; A=1-332.
DR PDB; 6QS5; X-ray; 1.96 A; A=2-326.
DR PDBsum; 1DAW; -.
DR PDBsum; 1DAY; -.
DR PDBsum; 1DS5; -.
DR PDBsum; 1F0Q; -.
DR PDBsum; 1J91; -.
DR PDBsum; 1JAM; -.
DR PDBsum; 1LP4; -.
DR PDBsum; 1LPU; -.
DR PDBsum; 1LR4; -.
DR PDBsum; 1M2P; -.
DR PDBsum; 1M2Q; -.
DR PDBsum; 1M2R; -.
DR PDBsum; 1OM1; -.
DR PDBsum; 1ZOE; -.
DR PDBsum; 1ZOG; -.
DR PDBsum; 1ZOH; -.
DR PDBsum; 2OXD; -.
DR PDBsum; 2OXX; -.
DR PDBsum; 2OXY; -.
DR PDBsum; 2PVH; -.
DR PDBsum; 2PVJ; -.
DR PDBsum; 2PVK; -.
DR PDBsum; 2PVL; -.
DR PDBsum; 2PVM; -.
DR PDBsum; 2PVN; -.
DR PDBsum; 2QC6; -.
DR PDBsum; 3BE9; -.
DR PDBsum; 3FL5; -.
DR PDBsum; 3KXG; -.
DR PDBsum; 3KXH; -.
DR PDBsum; 3KXM; -.
DR PDBsum; 3KXN; -.
DR PDBsum; 3PVG; -.
DR PDBsum; 3PWD; -.
DR PDBsum; 3PZH; -.
DR PDBsum; 4ANM; -.
DR PDBsum; 4DGM; -.
DR PDBsum; 4DGN; -.
DR PDBsum; 4RLK; -.
DR PDBsum; 5TS8; -.
DR PDBsum; 6QS5; -.
DR AlphaFoldDB; P28523; -.
DR SMR; P28523; -.
DR IntAct; P28523; 1.
DR STRING; 4577.GRMZM5G845755_P02; -.
DR BindingDB; P28523; -.
DR ChEMBL; CHEMBL4514; -.
DR PaxDb; P28523; -.
DR EnsemblPlants; Zm00001eb118100_T001; Zm00001eb118100_P001; Zm00001eb118100.
DR GeneID; 542637; -.
DR Gramene; Zm00001eb118100_T001; Zm00001eb118100_P001; Zm00001eb118100.
DR MaizeGDB; 30032; -.
DR eggNOG; KOG0668; Eukaryota.
DR HOGENOM; CLU_000288_70_4_1; -.
DR OMA; RAYWDYD; -.
DR OrthoDB; 1098380at2759; -.
DR BRENDA; 2.7.11.1; 6752.
DR EvolutionaryTrace; P28523; -.
DR PRO; PR:P28523; -.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; P28523; baseline and differential.
DR Genevisible; P28523; ZM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005956; C:protein kinase CK2 complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..332
FT /note="Casein kinase II subunit alpha"
FT /id="PRO_0000085901"
FT DOMAIN 34..319
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:4RLK"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:4RLK"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:4RLK"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:4RLK"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:4RLK"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4RLK"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4RLK"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 125..144
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4RLK"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4RLK"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:4RLK"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 207..222
FT /evidence="ECO:0007829|PDB:4RLK"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:4RLK"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:4RLK"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:4RLK"
SQ SEQUENCE 332 AA; 39230 MW; 85513A5A5C77235A CRC64;
MSKARVYADV NVLRPKEYWD YEALTVQWGE QDDYEVVRKV GRGKYSEVFE GINVNNNEKC
IIKILKPVKK KKIKREIKIL QNLCGGPNIV KLLDIVRDQH SKTPSLIFEY VNNTDFKVLY
PTLTDYDIRY YIYELLKALD YCHSQGIMHR DVKPHNVMID HELRKLRLID WGLAEFYHPG
KEYNVRVASR YFKGPELLVD LQDYDYSLDM WSLGCMFAGM IFRKEPFFYG HDNHDQLVKI
AKVLGTDGLN VYLNKYRIEL DPQLEALVGR HSRKPWLKFM NADNQHLVSP EAIDFLDKLL
RYDHQERLTA LEAMTHPYFQ QVRAAENSRT RA
