ID   CDC2_VIGAC              Reviewed;         294 AA.
AC   Q41639;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 65.
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   Vigna aconitifolia (Mothbean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae;
OC   Vigna.
OX   NCBI_TaxID=3918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root nodule;
RX   MEDLINE=94143490; PubMed=8310070; DOI=10.1104/pp.101.4.1399;
RA   Hong Z., Miao G.-H., Verma D.P.S.;
RT   "p34cdc2 protein kinase homolog from mothbean (Vigna aconitifolia).";
RL   Plant Physiol. 101:1399-1400(1993).
CC   -!- FUNCTION: Plays a key role in the control of the eukaryotic cell
CC       cycle. Component of the kinase complex that phosphorylates the
CC       repetitive C-terminus of RNA polymerase II.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
CC       [DNA-directed RNA polymerase] phosphate.
CC   -!- ENZYME REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC       the enzyme, while phosphorylation at Thr-161 activates it (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; M99497; AAA34241.1; -; mRNA.
DR   PIR; JQ2243; JQ2243.
DR   HSSP; P24941; 1H06.
DR   BRENDA; 2.7.11.22; 18771.
DR   BRENDA; 2.7.11.23; 18771.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0008353; F:RNA polymerase subunit kinase activity; IEA:EC.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   Pfam; PF00069; Pkinase; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00220; S_TKc; 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; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    294       Cell division control protein 2 homolog.
FT                                /FTId=PRO_0000085760.
FT   DOMAIN        4    287       Protein kinase.
FT   NP_BIND      10     18       ATP (By similarity).
FT   ACT_SITE    127    127       Proton acceptor (By similarity).
FT   BINDING      33     33       ATP (By similarity).
FT   MOD_RES      14     14       Phosphothreonine (By similarity).
FT   MOD_RES      15     15       Phosphotyrosine (By similarity).
FT   MOD_RES     161    161       Phosphothreonine; by CAK (By similarity).
SQ   SEQUENCE   294 AA;  33983 MW;  C8AF96B32389E312 CRC64;
     MEQYEKVEKI GEGTYGVVYK ARDRVTNETI ALKKIRLEQE DEGVPSTAIR EISLLKEMQH
     RNIVRLQDVV HSEKRLYLVF EYLDLDLKKH MDSSPEFVKD PRQVKMFLYQ ILCGIAYCHS
     HRVLHRDLKP QNLLIDRRTN SLKLADFGLA RAFGIPVRTF THEVVTLWYR APEILLGSRH
     YSTPVDVWSV GCIFAEMVNR RPLFPGDSEI DELFKIFRIL GTPNEETWPG VTALPDFKST
     FPKWPPKDLA TVVPNLDAAG LNLLSSMLCL DPSKRITARI AVEHEYFKDI KFVP
//