ID CDC21_MEDSA Reviewed; 291 AA.
AC P24923;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 08-NOV-2023, entry version 109.
DE RecName: Full=Cell division control protein 2 homolog 1;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE Flags: Fragment;
GN Name=CDC2A;
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].
RX PubMed=2000373; DOI=10.1073/pnas.88.5.1636;
RA Hirt H., Pay A., Gyoergyey J., Bako L., Nemeth K., Boegre L.,
RA Schweyen R.J., Heberle-Bors E., Dudits D.;
RT "Complementation of a yeast cell cycle mutant by an alfalfa cDNA encoding a
RT protein kinase homologous to p34cdc2.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1636-1640(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=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 -!- ACTIVITY REGULATION: Phosphorylation at Thr-11 or Tyr-12 inactivates
CC the enzyme, while phosphorylation at Thr-158 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; M58365; AAB41817.1; -; mRNA.
DR PIR; A39107; A39107.
DR AlphaFoldDB; P24923; -.
DR SMR; P24923; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07835; STKc_CDK1_CdkB_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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:SF548; 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; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN <1..291
FT /note="Cell division control protein 2 homolog 1"
FT /id="PRO_0000085753"
FT DOMAIN 1..284
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 124
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 7..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 291 AA; 33481 MW; E5D4F43E592D22B5 CRC64;
GENVEKIGEG TYGVVYKARD RVTNETIALK KIRLEQEDEG VPSTAIREIS LLKEMQHRNI
VRLQDVVHSD KRLYLVFEYL DLDLKKHMDS SPEFIKDPRQ VKMFLYQMLC GIAYCHSHRV
LHRDLKPQNL LIDRRTNSLK LADFGLARAF GIPVRTFTHE VVTLWYRAPE ILLGSRHYST
PVDVWSVGCI FAEMANRRPL SPGDSEIDEL FKIFRILGTP NEDTWPGVTS LPDFKSTFPR
WPSKDLATVV PNLEPAGLDL LNSMLCLDPT KRITARSAVE HEYFKDIKFV P
//
