CDC2_MAIZE
ID CDC2_MAIZE Reviewed; 294 AA.
AC P23111;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cell division control protein 2 homolog;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=p34cdc2;
GN Name=CDC2;
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].
RX PubMed=2014258; DOI=10.1073/pnas.88.8.3377;
RA Colasanti J., Tyers M., Sundaresan V.;
RT "Isolation and characterization of cDNA clones encoding a functional
RT p34cdc2 homologue from Zea mays.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3377-3381(1991).
CC -!- FUNCTION: Plays a key role in the control of the eukaryotic cell cycle.
CC Component of the kinase complex that phosphorylates the repetitive C-
CC terminus of RNA polymerase II.
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=2.7.11.22;
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=2.7.11.22;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC the enzyme, while phosphorylation at Thr-161 activates it.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; M60526; AAA33479.1; -; mRNA.
DR PIR; A40444; A40444.
DR PIR; B40444; B40444.
DR RefSeq; NP_001105342.1; NM_001111872.1.
DR AlphaFoldDB; P23111; -.
DR SMR; P23111; -.
DR STRING; 4577.GRMZM2G008327_P01; -.
DR PaxDb; P23111; -.
DR EnsemblPlants; Zm00001eb001260_T001; Zm00001eb001260_P001; Zm00001eb001260.
DR GeneID; 542270; -.
DR Gramene; Zm00001eb001260_T001; Zm00001eb001260_P001; Zm00001eb001260.
DR KEGG; zma:542270; -.
DR MaizeGDB; 60686; -.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR OrthoDB; 1010560at2759; -.
DR BRENDA; 2.7.11.22; 6752.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; P23111; baseline and differential.
DR Genevisible; P23111; ZM.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Kinase; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..294
FT /note="Cell division control protein 2 homolog"
FT /id="PRO_0000085752"
FT DOMAIN 4..287
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 127
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 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 161
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000250"
SQ SEQUENCE 294 AA; 33834 MW; 5063ECFCC2D5FFDD CRC64;
MEQYEKVEKI GEGTYGVVYK ALDKATNETI ALKKIRLEQE DEGVPSTAIR EISLLKEMNH
GNIVRLHDVV HSEKRIYLVF EYLDLDLKKF MDSCPEFAKN PTLIKSYLYQ ILHGVAYCHS
HRVLHRDLKP QNLLIDRRTN ALKLADFGLA RAFGIPVRTF THEVVTLWYR APEILLGARQ
YSTPVDVWSV GCIFAEMVNQ KPLFPGDSEI DELFKIFRIL GTPNEQSWPG VSCLPDFKTA
FPRWQAQDLA TVVPNLDPAG LDLLSKMLRY EPSKRITARQ ALEHEYFKDL EVVQ
