Y9296_DICDI
ID Y9296_DICDI Reviewed; 460 AA.
AC Q54V83;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable serine/threonine-protein kinase kinase DDB_G0280557;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0280557;
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=2.7.11.1;
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=2.7.11.1;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000037; EAL67080.1; -; Genomic_DNA.
DR RefSeq; XP_641048.1; XM_635956.1.
DR AlphaFoldDB; Q54V83; -.
DR SMR; Q54V83; -.
DR STRING; 44689.DDB0229296; -.
DR PaxDb; Q54V83; -.
DR EnsemblProtists; EAL67080; EAL67080; DDB_G0280557.
DR GeneID; 8622606; -.
DR KEGG; ddi:DDB_G0280557; -.
DR dictyBase; DDB_G0280557; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_620278_0_0_1; -.
DR InParanoid; Q54V83; -.
DR PhylomeDB; Q54V83; -.
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:Q54V83; -.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..460
FT /note="Probable serine/threonine-protein kinase kinase
FT DDB_G0280557"
FT /id="PRO_0000358905"
FT DOMAIN 102..416
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 154..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 460 AA; 53835 MW; F646E3861D2AD685 CRC64;
MEINKIIEIN NNNNNNNNKI IENNNDNKKI IEINNNNNDN NKIIEINDNN NNNIKDKILK
KENKDSILMK PPPIFITPAN KDDTITVFHQ GHIISIPRKL KINLKSITDC GPDGVMFRAK
NEDSKEEVIV KKISVFLMKD DKMARKLLRN LLFQRHFQQH PLVSTFQSVF KRKSSENYLI
SNKNNRNNVR LPLLQQKGDD DIYFEYLLPE FTLLQMIHNK LLTEYNIMIF LYQLLTVVKF
MHSAGVIHRD IDPSAITIDQ NQCLKLTEFY FCFPSNCPVD LFFNDYDTSS FIYRAPETIW
RNTTYTTAID VWNIGVIFGE MILGKRLFKT QDFEDHLISI SKLIGNPTAE DLSIVLSKSI
FQYMEKIPKS TLTPSVGIKR RFKGASKDQI ELLQGMLCWD PRKRMTIDQL LAHKYFSTIH
DESMQIKCNE IFNLKYYPDF YKMKSDLVKK SIENEFLTPC
