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   03-AUG-2022, entry version 98.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Stem;
RX   PubMed=8220475; 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 not
RT   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 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   -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC       the enzyme, while phosphorylation at Thr-161 activates it.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Found in most organs including root, young leaf,
CC       stem, vegetative meristem and flower bud.
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; X70707; CAA50038.1; -; mRNA.
DR   PIR; S31332; S31332.
DR   AlphaFoldDB; Q05006; -.
DR   SMR; Q05006; -.
DR   BRENDA; 2.7.11.22; 3078.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..294
FT                   /note="Cell division control protein 2 homolog 2"
FT                   /id="PRO_0000085754"
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;  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