ID   Y9333_DICDI             Reviewed;         392 AA.
AC   Q54US6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Probable inactive serine/threonine-protein kinase DDB_G0280855;
GN   ORFNames=DDB_G0280855;
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   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MAP kinase 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; AAFI02000039; EAL66969.1; -; Genomic_DNA.
DR   RefSeq; XP_640945.1; XM_635853.1.
DR   AlphaFoldDB; Q54US6; -.
DR   SMR; Q54US6; -.
DR   STRING; 44689.DDB0229333; -.
DR   PaxDb; Q54US6; -.
DR   EnsemblProtists; EAL66969; EAL66969; DDB_G0280855.
DR   GeneID; 8622749; -.
DR   KEGG; ddi:DDB_G0280855; -.
DR   dictyBase; DDB_G0280855; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   HOGENOM; CLU_620278_0_0_1; -.
DR   PhylomeDB; Q54US6; -.
DR   Reactome; R-DDI-193648; NRAGE signals death through JNK.
DR   Reactome; R-DDI-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-DDI-2871796; FCERI mediated MAPK activation.
DR   Reactome; R-DDI-4086398; Ca2+ pathway.
DR   Reactome; R-DDI-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR   Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-DDI-9007892; Interleukin-38 signaling.
DR   PRO; PR:Q54US6; -.
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; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..392
FT                   /note="Probable inactive serine/threonine-protein kinase
FT                   DDB_G0280855"
FT                   /id="PRO_0000358906"
FT   DOMAIN          46..349
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         52..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   392 AA;  46078 MW;  C43B2225A24001A9 CRC64;
     MEIKDIIINS NLMLPPPTIL TINNKDDYTS FTFKGKSISV PRKQRITKKT IYACDINGTM
     FQTYNMDTNR LLIIKKISLL QFKNHLQGRM MLRNCHYQRF FNHHPFVSGF KVSKRKSLNI
     KTKNLIESPV DDGTDLYFEF DQSDFTLYQM IRSDKAASRK QCPYVLYQLL TTIKYINSAG
     VIHRSLDPKT IAVNKEYKTK LFDFSFSIST DYPTDIFFKD YEETPWPYRS PETIIMLKEF
     SFECDVWSIG VIFAELILGE QLFRGESKQS LLIEISELIG TPTYDECKES TNGFARNFIL
     NIPLKSRHGG IKKRIPNATE EEIEILEGML CWNPKKRWPI ERIIQHPYFQ NYCHIEQYKC
     DKKFSLGSPY VFHRLNAKEI KKIIEDEFVT QP