Y9849_DICDI
ID Y9849_DICDI Reviewed; 848 AA.
AC Q54XX5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0278535;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0278535;
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. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68440.1; -; Genomic_DNA.
DR RefSeq; XP_642427.1; XM_637335.1.
DR AlphaFoldDB; Q54XX5; -.
DR SMR; Q54XX5; -.
DR STRING; 44689.DDB0229849; -.
DR PaxDb; Q54XX5; -.
DR PRIDE; Q54XX5; -.
DR EnsemblProtists; EAL68440; EAL68440; DDB_G0278535.
DR GeneID; 8621632; -.
DR KEGG; ddi:DDB_G0278535; -.
DR dictyBase; DDB_G0278535; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_020450_0_0_1; -.
DR InParanoid; Q54XX5; -.
DR OMA; NCEEAFS; -.
DR PhylomeDB; Q54XX5; -.
DR Reactome; R-DDI-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-DDI-170968; Frs2-mediated activation.
DR Reactome; R-DDI-3295583; TRP channels.
DR Reactome; R-DDI-392517; Rap1 signalling.
DR Reactome; R-DDI-430116; GP1b-IX-V activation signalling.
DR Reactome; R-DDI-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-DDI-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DDI-5673000; RAF activation.
DR Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DDI-5675482; Regulation of necroptotic cell death.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-9013424; RHOV GTPase cycle.
DR PRO; PR:Q54XX5; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ANK repeat; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..848
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0278535"
FT /id="PRO_0000355160"
FT REPEAT 181..212
FT /note="ANK 1"
FT REPEAT 218..248
FT /note="ANK 2"
FT REPEAT 252..285
FT /note="ANK 3"
FT REPEAT 289..320
FT /note="ANK 4"
FT REPEAT 324..353
FT /note="ANK 5"
FT DOMAIN 378..441
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 529..799
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 650
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 535..543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 848 AA; 94576 MW; 93B088846C85ED4A CRC64;
MNKSSSASTV PPHSTPHTAH STSSSSLPPL SSTHHTNTSS TSNNNNNSNN NHNHNHHHTT
AATTTTSTTG TGTTAATTST STSSTIPINT AGIHTSNSNL ATATNTPSSS PQVSTSVERR
FWMNDRGSRR SSTSLTQQPL TMNRSSNKLH AAVSARDLTR LKQRLSQPRK AKIELAEYDS
MDQTPLCAAL RNGSHDIVRE ILFFYQSNKM DINDQDKSGY TPLHVAASHC DDQILMLLLN
YEGINVNITN EDKNSALHYF CQKFRSPNCQ EPFSIFLKKG VNVNAQNKNG ETPLHKSIFN
NTVRLLMVNM LLDAGAEVNV LNSRGESPLH FAVRLGREDL VSVLVKAGAD ITIKGNEKKT
CYELSLTIGN QRVINFLKNV QDIFNWLKSI DLEQYWLNFV KEEIFMDLLL DIDERTLDSL
GITYSGHRLK IIRNCRILRD QQLLSTANSN VTTGSGSSGS TTTTTTTTTT TSGCGGLNVP
ENKKVTQLSI ESLKSNPPNS MDSTGSISSD DLKESLTNLE HWVIDHSELE YTLKLGSGSS
GKVYKGLYKG KEVAVKVLKS ITTQSQLEEF KKEFQIMGSI RSQFMVTFYG ACIEPKLCMV
MEYCSRDSLY HVMNTKKYDI GWDRFFQFTM QMTLGVQCLH NWTPQIVHRD FKSLNLLVNE
DWECKVSDFG LSRFNTADNL ETLSKIRGTF AYCSPEVAVG NGSLYTTKSD IYSIGIVFWE
LVTRVINGEY SRPYSEYSHI KMDFQIMLNS KEGLRPTLPQ NTPPGLEALY KQCVNQEQTL
RPSCEEIIET LNRLRHEYMS SKTTWDSLIR KLPSLSPPPQ PTTTTTTTTS SSTSTNNINN
NINNNNNT
