Y2550_DICDI
ID Y2550_DICDI Reviewed; 1397 AA.
AC Q54D75;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable cyclin-dependent serine/threonine-protein kinase DDB_G0292550;
DE EC=2.7.11.22;
GN ORFNames=DDB_G0292550;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- 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; AAFI02000190; EAL61254.1; -; Genomic_DNA.
DR RefSeq; XP_629621.1; XM_629619.1.
DR AlphaFoldDB; Q54D75; -.
DR SMR; Q54D75; -.
DR STRING; 44689.DDB0229424; -.
DR PaxDb; Q54D75; -.
DR EnsemblProtists; EAL61254; EAL61254; DDB_G0292550.
DR GeneID; 8628684; -.
DR KEGG; ddi:DDB_G0292550; -.
DR dictyBase; DDB_G0292550; -.
DR eggNOG; KOG0600; Eukaryota.
DR HOGENOM; CLU_254571_0_0_1; -.
DR InParanoid; Q54D75; -.
DR OMA; YPSQYNY; -.
DR PRO; PR:Q54D75; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1397
FT /note="Probable cyclin-dependent serine/threonine-protein
FT kinase DDB_G0292550"
FT /id="PRO_0000362047"
FT DOMAIN 4..287
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 412..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1397 AA; 158111 MW; 2604DAB60C955BCE CRC64;
MNSFQIIELI GSGSYGKVYK AIHNLSKCTV ALKIISVMNI ENGLPVEVKY LMKLRDCKNI
VHLIEYFYSN DDKLVMVFEY LEYDLWKFIS PKNKYMTLSC TKFFIHQLLE GLDELHSQKI
MHLDIKPSNL LINPRFDLKI ADFGFTTYIG NPHLAHQVIS LFYRPPELLM GSRNYGPEVD
IWSVGCIIVE MLTGFYMFAG SNDSLQLELI FKTFGTPTEK NWPGISKLSG YSPYLGSKSK
KYPSKSLKDI SKFKSFSNST LDIILRMLTL CPKNRISTKE ALNHPWFFED PIASPPLDDI
INCLVSRPVK ISKQHQKTNN CNNNNGSYDI IPPNSILVPK RSSSQQAALQ TQQVVDVDLQ
YLILKAEQQQ IQYQKLVLQT SVPNHIYKEV YEVNQLLKQY ILRLKQQKVN LNNNNLNNNN
NNLYGNNNHN NNNNNNNNNN NNNNNNNYNN NNNNHNNNYN HDNNNNNNYN NNNYKNNNNS
NNNFSFNNSN NNNNNNNNNN RNNRNNNNNN NNNNNNNNYN NNSNNNSYNN NFNNGFNNND
NINDDNNNNN SYNNVNNNNI NNNNNNNNGF NGFNNYGNNF NNSNNNGNQF GANNNSFNNT
DFSNDSNYGS YCNGLMDLIN NNSMYNGGNY YMNNASFHQR IQEHIQKIQQ QQLQQMEDQQ
QEKLNFRDYH PLSIPSQHHN TSSSDTHNNN NNNYNNNNNN NNNINNNNIN SIHNQSSDHN
HFIPNNGFTN ENNNNHCINN MNNSNNNNNN NIGNIGSNGG SINEMGNNNN NNNNNNNNNN
NNNNNNNNIN ANHNRNNNNG SNDFSDFNGN QMVINSYNNN SNNNGNINGN NNNGNGNING
IIGNNNNNNS NNNNNTSFNG NRTTTTTTTS SNFNNINNNN NNSNNNNKNN NNKNNNNNNN
NNNNNNNNNN NNNNNNNSNN NSINNNTNNN NNNNNNNNGN GLTSSYANHF QYNHPPFNIS
NAPHPIPFLN NQSIPNSNYQ FLNRFSFSNY SNNNSNGLAN NYQNPFGHGA TNSNNNNSGN
NDHVFGHNTF NFNQNNNNNN NNNNNNNNNN NNNNNNNSNN NSNNNNYNSN NNDNSNSNSN
NNNNNNNNNN NSLFNNFNTH NNSINRGNNS FDSFNNGFNH LKNNNNNINN NNNDINNNNN
NNNNNNNNNG ITKNNTQFGP NILSSTQTSH NSPVSLTPIS VSSSSFSNYS PTSFSSSSME
SLSSSSEFLS SESLSFTNSN QFSPLLNSAS QDINNNSRSS RHRSKLNIDT KGNNNNNNNN
KNNNNNNNNN NNNNNNNNNN NNNSNNINND NNNNSNNNSN SNNNNSNSNN NNNSNNNNNN
SFGLKRYVDD NEEQLLANQK KKKNIKSSPL PSASSSQQSQ TQQQHQIQQQ SQTQQQSQTQ
KIENNDGLSV ENPIVLD
