ID   CDC22_MEDSA             Reviewed;         294 AA.
AC   Q05006;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Cell division control protein 2 homolog 2;
DE            EC=2.7.11.22;
GN   Name=CDC2B;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Trifolieae;
OC   Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Stem;
RX   MEDLINE=94035174; PubMed=8220475;
RX   DOI=10.1046/j.1365-313X.1993.04010061.x;
RA   Hirt H., Pay A., Boegre L., Meskiene I., Heberle-Bors E.;
RT   "cdc2MsB, a cognate cdc2 gene from alfalfa, complements the G1/S but
RT   not the G2/M transition of budding yeast cdc28 mutants.";
RL   Plant J. 4:61-69(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   -!- ENZYME REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC       the enzyme, while phosphorylation at Thr-161 activates it (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Found in most organs including root, young
CC       leaf, stem, vegetative meristem and flower bud.
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; X70707; CAA50038.1; -; mRNA.
DR   PIR; S31332; S31332.
DR   HSSP; P24941; 1H06.
DR   BRENDA; 2.7.11.22; 815.
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: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                                2.
FT                                /FTId=PRO_0000085754.
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;  33886 MW;  C2E5D6A67AAF2C3D CRC64;
     MEQYEKVEKI GEGTYGVVYK ARDRATNETI ALKKIRLEQE DEGVPSTAIR EISLLKEMQH
     RNIVRLQDVV HSEKRLYLVF EYLDLDLKKF MDSSPEFAKD QRQIKMFLYQ ILCGIAYCHS
     HRVLHRDLKP QNLLIDRSSN AVKLADFGLA RAFGIPVRTF THEVVTLWYR APEILLGSRH
     YSTPVDVWSV GCIFAEMINQ RPLFPGDSEI DELFKIFRIT GTPNEETWPG VTSLPDFKSA
     FPKWPAKDLA TQVPNLEPAG LDLLSSTCRL DPTRRITARG ALEHEYFKDI KFVP
//