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 02-SEP-2026, entry version 157. 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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; CC -!- CATALYTIC ACTIVITY: CC Reaction=[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed CC RNA polymerase] + ADP + H(+); 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 FunCoup; P23111; 3492. DR STRING; 4577.P23111; -. DR PaxDb; 4577-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 InParanoid; P23111; -. DR OrthoDB; 1732493at2759; -. DR BRENDA; 2.7.11.22; 6752. DR Proteomes; UP000007305; Chromosome 1. DR ExpressionAtlas; P23111; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC. 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:0000086; P:G2/M transition of mitotic cell cycle; IBA:GO_Central. DR CDD; cd07835; STKc_CDK1_CdkB_like; 1. DR FunFam; 3.30.200.20:FF:000187; Cell division control protein 2; 1. DR FunFam; 1.10.510.10:FF:000280; Cell division control protein 2 homolog; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR050108; CDK. 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; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF549; CYCLIN-DEPENDENT KINASE A-1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 //