ID   CDC2D_ANTMA             Reviewed;         312 AA.
AC   Q38775;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Cell division control protein 2 homolog D;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
GN   Name=CDC2D;
OS   Antirrhinum majus (Garden snapdragon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX   NCBI_TaxID=4151;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Flower;
RX   PubMed=8837502; DOI=10.2307/3870243;
RA   Fobert P.R., Gaudin V., Lunness P., Coen E.S., Doonan J.H.;
RT   "Distinct classes of cdc2-related genes are differentially expressed during
RT   the cell division cycle in plants.";
RL   Plant Cell 8:1465-1476(1996).
CC   -!- FUNCTION: Plays a key role in the control of the eukaryotic cell cycle.
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   -!- DEVELOPMENTAL STAGE: Expression specific to the G2 and M phases.
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; X97640; CAA66236.1; -; mRNA.
DR   PIR; T17118; T17118.
DR   AlphaFoldDB; Q38775; -.
DR   SMR; Q38775; -.
DR   BRENDA; 2.7.11.22; 376.
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:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IEA:UniProtKB-EC.
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..312
FT                   /note="Cell division control protein 2 homolog D"
FT                   /id="PRO_0000085748"
FT   DOMAIN          14..304
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        145
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         20..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         24
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         25
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         179
FT                   /note="Phosphothreonine; by CAK"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  35503 MW;  A38D2177EBF70210 CRC64;
     MAEEKSKSSA MDAFVKLEKV GEGTYGKVYR AMEKSTGKIV ALKKTRLHED EEGVPPTTLR
     EVSLLRMLSR DPHVVRLLDV KQGQNKEGKT VLYLVFEYMD TDLKKYIRSF KQTGESIAPM
     NVKSLMYQLC KGVAFCHGHG VLHRDLKPHN LLMDRKTMML KIADLGLARA YTLPIKKYTH
     EILTLWYRAP EVLLGATHYS PAVDMWSVAC IFAELVTQKA LFPGDSELQQ LLHIFRLLGT
     PNEEIWPGVS TLVDWHEYPQ WTAQPISSAV PGLDEKGLNL LSEMLHYEPS RRISAKKAME
     HPYFDELDKS GL