Reviewed, UniProtKB/Swiss-Prot Q00646 (CDC2_EMENI)

Names and origin

Protein names

Recommended name:
    Cell division control protein 2
    EC=2.7.11.22
    EC=2.7.11.23
Alternative name(s):
    Cyclin-dependent protein kinase

Gene names

Name:	nimX
ORF Names:	AN4182

Organism

Emericella nidulans (Aspergillus nidulans) [Complete proteome]

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Plays a key role in the control of the eukaryotic cell cycle. It is required in higher cells for entry into S-phase and mitosis By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
Enzyme regulation	Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-180 activates it By similarity.
Subunit structure	Forms a stable but non-covalent complex with a regulatory subunit (SUC1) and with a cyclin.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 323	323	Cell division control protein 2		PRO_0000085719
Regions
	Domain	4 – 306	303	Protein kinase
	Nucleotide binding	10 – 18	9	ATP By similarity
Sites
	Active site	147	1	Proton acceptor By similarity
	Binding site	34	1	ATP By similarity
Amino acid modifications
	Modified residue	14	1	Phosphothreonine By similarity
	Modified residue	15	1	Phosphotyrosine By similarity
	Modified residue	180	1	Phosphothreonine; by CAK By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q00646-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3178CAFBDDC32224	FASTA	323	36,779
	10 20 30 40 50 60 MENYQKIEKI GEGTYGVVYK ARELTHPNRI VALKKIRLEA EDEGVPSTAI REISLLKEMN 70 80 90 100 110 120 DPNIVRLLNI VHADGHKLYL VFEFLDLDLK KYMEALPVSE GGRGRALPDG STLSRNLGLG 130 140 150 160 170 180 DAMVKKFMAQ LIEGIRFCHS HRVLHRDLKP QNLLIDRDGN LKLADFGLAR AFGVPLRTYT 190 200 210 220 230 240 HEVVTLWYRS PEILLGGRQY STGVDMWSCG AIFAEMCTRK PLFPGDSEID EIFKIFRILG 250 260 270 280 290 300 TPDETIWPGV TSFPDFKPTF PKWKREDIQN VVPGLEEDGL DLLEALLEYD PARRISAKQA 310 320 CMHPYFQHGS SYYSGRARRN GFH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A single p34cdc2 protein kinase (encoded by nimXcdc2) is required at G1 and G2 in Aspergillus nidulans." Osmani A.H., van Peij N., Mischke M., O'Connell M.J., Osmani S.A. J. Cell Sci. 107:1519-1528(1994) [PubMed: 7962194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mycelium.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U07169 mRNA. Translation: AAA20597.1. AACD01000068 Genomic DNA. Translation: EAA59281.1.
RefSeq	XP_661786.1.
3D structure databases
SMR	Q00646. Positions 1-307.
ModBase	Search...
Genome annotation databases
GeneID	2873604.
KEGG	ani:AN4182.2.
Phylogenomic databases
PhylomeDB	Q00646.
Enzyme and pathway databases
BRENDA	2.7.11.22. 3859. 2.7.11.23. 3859.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDC2_EMENI

Accession

Primary (citable) accession number: Q00646
Secondary accession number(s): Q5B5J8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)