CDC2B_ANTMA
ID CDC2B_ANTMA Reviewed; 280 AA.
AC Q38773;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cell division control protein 2 homolog B;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE Flags: Fragment;
GN Name=CDC2B;
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 -!- ACTIVITY REGULATION: Phosphorylation at Tyr-2 inactivates the enzyme,
CC while phosphorylation at Thr-148 activates it. {ECO:0000250}.
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; X97638; CAA66234.1; -; mRNA.
DR PIR; T17116; T17116.
DR AlphaFoldDB; Q38773; -.
DR SMR; Q38773; -.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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..280
FT /note="Cell division control protein 2 homolog B"
FT /id="PRO_0000085746"
FT DOMAIN <1..274
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING <1..5
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 148
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 280 AA; 32167 MW; EB4F3715A4FFE6CC CRC64;
AYGVVYKARD IETNEDIALK KIRLEQEDEG VPSTAIREIS LLKEMHHENI VNLKDVVHRE
KRLYLVFEYL DLDLKKHMDS CPEFSQDLHM VKMFLCQILR GVAYCHSHRV LHRDLKPQNL
LIDRGSNTIK LADFGLARAF GIPVRTFTHE VVTLWYRAPE VLLGSRHYST PVDVWSVGCI
FAEMVNQKPL FPGDSEIDEL HKIFRIIGTP NEDIWPGVTS LPDFKSSFPK WPPKELATIV
PNLGATGLDL LCKMLQLDPS KRITAKKALE HEYFKDIVLP