ID   Y8487_DICDI             Reviewed;         636 AA.
AC   Q54Y06;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Probable cyclin-dependent serine/threonine-protein kinase DDB_G0278487;
DE            EC=2.7.11.22;
GN   ORFNames=DDB_G0278487;
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).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17259634; DOI=10.1099/mic.0.2006/000562-0;
RA   Serafimidis I., Bloomfield G., Skelton J., Ivens A., Kay R.R.;
RT   "A new environmentally resistant cell type from Dictyostelium.";
RL   Microbiology 153:619-630(2007).
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   -!- DEVELOPMENTAL STAGE: Up-regulated in aspidocytes, a resistant cell type
CC       induced by a range of toxins including heavy metals and antibiotics.
CC       {ECO:0000269|PubMed:17259634}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000023; EAL68416.1; -; Genomic_DNA.
DR   RefSeq; XP_642396.1; XM_637304.1.
DR   AlphaFoldDB; Q54Y06; -.
DR   SMR; Q54Y06; -.
DR   STRING; 44689.DDB0229294; -.
DR   PaxDb; Q54Y06; -.
DR   PRIDE; Q54Y06; -.
DR   EnsemblProtists; EAL68416; EAL68416; DDB_G0278487.
DR   GeneID; 8621601; -.
DR   KEGG; ddi:DDB_G0278487; -.
DR   dictyBase; DDB_G0278487; clkB.
DR   eggNOG; KOG0600; Eukaryota.
DR   HOGENOM; CLU_430502_0_0_1; -.
DR   InParanoid; Q54Y06; -.
DR   OMA; IEEPICK; -.
DR   PhylomeDB; Q54Y06; -.
DR   PRO; PR:Q54Y06; -.
DR   Proteomes; UP000002195; Chromosome 3.
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; ISS:dictyBase.
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:0004674; F:protein serine/threonine kinase activity; ISS:dictyBase.
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   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..636
FT                   /note="Probable cyclin-dependent serine/threonine-protein
FT                   kinase DDB_G0278487"
FT                   /id="PRO_0000362064"
FT   DOMAIN          64..343
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..555
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         70..78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   636 AA;  73679 MW;  96FCE039D9FB05D6 CRC64;
     MPSQSNNVIT SSTASSSMSS SSNSSDASST SSSNTNNAHS SNNQFVSGQL NLVGNTHTKI
     NDNYEIISKI GEGISGSVFK AIKKGTEEMV ALKNFKGWTE GDRASKEECS LLQQLRHIPY
     ITPVIDIYTN FETSEYIIVF PYFEHDLSGL LSEHRLSIPQ VKCYFKQLLE GINEIHNAGV
     MHRDIKAANL LVNNKGSLFI GDLGTATSYT KRSVFSSKVV TLWYRAPELL LGSTQYGPEI
     DMWSIGCVLI ELVTSRNFLP GSSEQQQLEA ICKLCGTPTD EIWPNVSQLQ NFNQISHLPV
     YPSRLRTVFK NFSNDFIELL EGLLTLNPKK RLTAEQALQS PFFTNHPLPF KPENMPGYQP
     IHVLEAVQKR VQQQQELEQQ KKQEEQKKQQ EEQKKLEDQK KQEEQKKQED LLKRQRLLKR
     QQELKKQQDE QRQQELIKKQ QEQEQLRLKV EHEKQRQEQE RLRLIQQEQE RLKRQQQEHE
     QRLQREQQQQ LNQLQQQKES PLNNSYGKIN LKRSLDLVND IRNYCTSETE SEYESDEEDF
     YTEEEVEDYS SDEEDDYYNA QSNKSLYTPI KAMIQQHNNN QQHQQQYPYS QQQQEPISSN
     PFLQPPKKQR TASTGFNNNN GNNNNNNNLS TPLTIH