Y8646_DICDI
ID Y8646_DICDI Reviewed; 1221 AA.
AC Q54LU8;
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 serine/threonine-protein kinase DDB_G0286465;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0286465;
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; AAFI02000085; EAL64257.1; -; Genomic_DNA.
DR RefSeq; XP_637732.1; XM_632640.1.
DR AlphaFoldDB; Q54LU8; -.
DR STRING; 44689.DDB0231182; -.
DR PaxDb; Q54LU8; -.
DR PRIDE; Q54LU8; -.
DR EnsemblProtists; EAL64257; EAL64257; DDB_G0286465.
DR GeneID; 8625597; -.
DR KEGG; ddi:DDB_G0286465; -.
DR dictyBase; DDB_G0286465; -.
DR eggNOG; ENOG502SF4Y; Eukaryota.
DR HOGENOM; CLU_268677_0_0_1; -.
DR InParanoid; Q54LU8; -.
DR Reactome; R-DDI-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-DDI-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-DDI-9020702; Interleukin-1 signaling.
DR Reactome; R-DDI-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-DDI-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-DDI-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR PRO; PR:Q54LU8; -.
DR Proteomes; UP000002195; Chromosome 4.
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:0072354; F:histone kinase activity (H3-T3 specific); IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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..1221
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0286465"
FT /id="PRO_0000362066"
FT DOMAIN 186..627
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 448
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 192..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1221 AA; 139876 MW; A1FFDA8F4497612B CRC64;
MTLRLDTSLK RGASRNIPPI PTFSSVSNEN LSSSPYTSSS YYSSNCESLD SIGDISIDSS
VYSSSEIEFV GNGDKKKNFI NNNNNNNGNK YDFSNLLETP KLKFSPSTGR TKNNNNNNNN
NINNNNYKKN DNQKKNFKYI EDNESDYLDD ENDEENVDID LSILNVNFKI INENNSQNNN
NNKYQINNNM QKTGGRNGSV FFVNNNNNSN NNNNNNNNNN NNNNNNNNNN NNNNNNNDNS
NNKNNFKNNN TSYTHNSNKN NNENKNTFAI KQQLVSTPKN KLSQTYREKV ILEHLNILIE
SNKACNFPKL INWYKAAPTS NLSNVNNNNS NNNNNNSNNN ITNSRYGSNY EDIYDDNYYD
EVDDYDSGKE EEESTKTITK TITTTTASIK PNIQYMHLIL EYANMGTLKE YGKDNNFEFT
ISQMKSLLFQ VIYSLAISQK EFEFVHNDLH FGNVLLTSFP VDKKYIVYQD KLDNGEFNNW
IVGGDFIVKI SDFGLSRIKL PSNEIIYNQR NDRSKEFCFY SDLYSFSSLL NKIKIKESPS
SSSTTSTSTS QVLIKSDSDS SSSASSSSSS SSSSSSSSSS SLPKSKNKSN RSKDNQSKLD
PEKRLLTKLK KSMKDLPPYK LLDHPFFDSL KVCPNDCLPL NSIRISTNGI VPKEFPKPLS
PIFEKNNIIS IPSSPISTTT TTFPTTPTIK STTKKISKTI VIPSSPSLAL PPNLSVKSPF
APPSKKQLQQ YQQQQKQQTI SMFKYDDEEE KEEEEKEKEK EKEKEKEKEE EGEEGNIPKE
KLILKMTPKP YIFIHHFSPN SLGPLSPPSS TSSTLLGALS QEKFEKKQRQ IQDSEKVNKN
EEENQTKDDA DNISPPLPHA IKKSIYNNKN NHQKISTNTI IKTPIKAPIK TITQIPTETP
NKIPNKTISQ SNPVIIRDET PQKGIPFEKK VVSTPLIYKE RPHFVFLKKA KLSSNSNNKE
NIINFHNNNN NNNNNNNNNN NNNNNNNNNN NNNKDSYNEK GNATSYCNGD DDDDDFKIDH
KENVVSGFLI EKDHEFIGDK ENSKEKQKVS KRVQDKAWQE LNAFLRKNPT QGVSRIKSTD
YPALSDLFPK KKRCSENNFV FEKEKKQEKE NKEKENKEKE KKQLEKQKQL EREKLEKDRL
EKDRLEKEQQ EKDCLEREKF LENERLEKEQ EREKLEKEIK ILVVSKKNRT NPLQKDYDRY
IKKVGSSLTE KRASKPMNDN I
