ID   CDC2_EMENI              Reviewed;         323 AA.
AC   Q00646; Q5B5J8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Cell division control protein 2;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=Cyclin-dependent protein kinase;
GN   Name=nimX; ORFNames=AN4182;
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mycelium;
RX   MEDLINE=95051110; PubMed=7962194;
RA   Osmani A.H., van Peij N., Mischke M., O'Connell M.J., Osmani S.A.;
RT   "A single p34cdc2 protein kinase (encoded by nimXcdc2) is required at
RT   G1 and G2 in Aspergillus nidulans.";
RL   J. Cell Sci. 107:1519-1528(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC 4;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
CC   -!- FUNCTION: Plays a key role in the control of the eukaryotic cell
CC       cycle. It is required in higher cells for entry into S-phase and
CC       mitosis (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
CC       [DNA-directed RNA polymerase] phosphate.
CC   -!- ENZYME REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC       the enzyme, while phosphorylation at Thr-180 activates it (By
CC       similarity).
CC   -!- SUBUNIT: Forms a stable but non-covalent complex with a regulatory
CC       subunit (SUC1) and with a cyclin.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; U07169; AAA20597.1; -; mRNA.
DR   EMBL; AACD01000068; EAA59281.1; -; Genomic_DNA.
DR   RefSeq; XP_661786.1; -.
DR   HSSP; P24941; 1H00.
DR   SMR; Q00646; 1-307.
DR   GeneID; 2873604; -.
DR   KEGG; ani:AN4182.2; -.
DR   BRENDA; 2.7.11.22; 3859.
DR   BRENDA; 2.7.11.23; 3859.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0008353; F:RNA polymerase subunit kinase activity; IEA:EC.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_pkinase-rel.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   Pfam; PF00069; Pkinase; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00220; S_TKc; 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    323       Cell division control protein 2.
FT                                /FTId=PRO_0000085719.
FT   DOMAIN        4    306       Protein kinase.
FT   NP_BIND      10     18       ATP (By similarity).
FT   ACT_SITE    147    147       Proton acceptor (By similarity).
FT   BINDING      34     34       ATP (By similarity).
FT   MOD_RES      14     14       Phosphothreonine (By similarity).
FT   MOD_RES      15     15       Phosphotyrosine (By similarity).
FT   MOD_RES     180    180       Phosphothreonine; by CAK (By similarity).
SQ   SEQUENCE   323 AA;  36779 MW;  3178CAFBDDC32224 CRC64;
     MENYQKIEKI GEGTYGVVYK ARELTHPNRI VALKKIRLEA EDEGVPSTAI REISLLKEMN
     DPNIVRLLNI VHADGHKLYL VFEFLDLDLK KYMEALPVSE GGRGRALPDG STLSRNLGLG
     DAMVKKFMAQ LIEGIRFCHS HRVLHRDLKP QNLLIDRDGN LKLADFGLAR AFGVPLRTYT
     HEVVTLWYRS PEILLGGRQY STGVDMWSCG AIFAEMCTRK PLFPGDSEID EIFKIFRILG
     TPDETIWPGV TSFPDFKPTF PKWKREDIQN VVPGLEEDGL DLLEALLEYD PARRISAKQA
     CMHPYFQHGS SYYSGRARRN GFH
//