Y3301_DICDI
ID Y3301_DICDI Reviewed; 663 AA.
AC Q54R98;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0283301;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0283301;
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. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000052; EAL65791.1; -; Genomic_DNA.
DR RefSeq; XP_639149.1; XM_634057.1.
DR AlphaFoldDB; Q54R98; -.
DR SMR; Q54R98; -.
DR STRING; 44689.DDB0229335; -.
DR PaxDb; Q54R98; -.
DR EnsemblProtists; EAL65791; EAL65791; DDB_G0283301.
DR GeneID; 8624019; -.
DR KEGG; ddi:DDB_G0283301; -.
DR dictyBase; DDB_G0283301; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_414163_0_0_1; -.
DR InParanoid; Q54R98; -.
DR PhylomeDB; Q54R98; -.
DR Reactome; R-DDI-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DDI-381042; PERK regulates gene expression.
DR PRO; PR:Q54R98; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein 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:0051321; P:meiotic cell cycle; 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 InterPro; IPR017441; Protein_kinase_ATP_BS.
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.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..663
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0283301"
FT /id="PRO_0000362050"
FT DOMAIN 312..586
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 440
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 318..326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 663 AA; 77522 MW; 5F88ADA9F5372B1A CRC64;
MTSQNWKNCF NKKAIEVIEI HRSQETITVE TVNNEDKIKN NISKPKIKVH KKPIIKSISK
LKLQPKFSRY NDIIDYSIDF NCNKNYFLKQ DKVSGNTFIH VFCEKRESKI NLESDIENLK
CLGKETIEAR NNNKEIALFS TLKNQCLGLK IMHELISRNV MFIDDNGKDE LLVKCLEEGR
VDMVKYLITV DINLISKLKR ICQITQLSLE TLQFVELINS EYEKIVEIGL KSAGREYIKL
FFIQFILGNF SKESIIQTID EYKLPPIPKE IEDFFFVYNY QMCDFVKLTE IKPRYLNEIS
KINIYPIGQV SIERRNELGR GGNGTVYSGV LKEIDSQGNE ISIPVAIKIP TQFYKSKLVE
VYKELAIHQK INGICGPKLF GCVKLNVGFG IIIERFDCSL HDYIQNNNID FDLFFELALK
MVITIRNLHK CHLNEIFHRD IKPHNWLVKK TKDELVVVLS DFGLSRENSE TNENTLQKYR
GTSVFIPPEL NDNILYNEKS DIYSLGVSFM MLLYKVVYGK MENPFYEFKI SKMEYFKTVV
ALENFLVPIV PTFLPDSFKE FLFSTMNRIY TCRPNSEECV ERLITLKTEY ENDKTKWQVN
SAIIQKEKSL LTDSIISQQL KLMNQVKKFV QENDKFVFLK KTKLFFSESE IKQYLLSIIK
CQE
