Y9871_DICDI
ID Y9871_DICDI Reviewed; 1024 AA.
AC Q86HG9; Q55AN7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0271682;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0271682;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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 -!- DOMAIN: The protein kinase domain 2 is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000006; EAL71531.1; -; Genomic_DNA.
DR RefSeq; XP_645485.1; XM_640393.1.
DR AlphaFoldDB; Q86HG9; -.
DR SMR; Q86HG9; -.
DR STRING; 44689.DDB0229871; -.
DR PaxDb; Q86HG9; -.
DR PRIDE; Q86HG9; -.
DR EnsemblProtists; EAL71531; EAL71531; DDB_G0271682.
DR GeneID; 8618113; -.
DR KEGG; ddi:DDB_G0271682; -.
DR dictyBase; DDB_G0271682; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_295512_0_0_1; -.
DR InParanoid; Q86HG9; -.
DR PhylomeDB; Q86HG9; -.
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:Q86HG9; -.
DR Proteomes; UP000002195; Chromosome 2.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1024
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0271682"
FT /id="PRO_0000355166"
FT DOMAIN 360..609
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 645..1018
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 187..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 484
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 366..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 651..659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 719
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1024 AA; 115910 MW; 88DCC6508424EABE CRC64;
MATLDLCNNE HLNETESADE EDDQLQTPIK TVVTLKFKEN PDSTSPIQVF QLNIGSNIIG
RGSPSFLNDI KISRRHAEII VSAEVGNVTF NQLGQNHSTL YRKDQTPIKM VRGISNQLLD
DDLISLYDGS IPFSIHIERD NQFMSVCEGN FILTQDAADT NYHINSPTKT ITTTSTTTTT
TETLIKNIDN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNSILSKR SRDNENNHNH QYIHHDKTPL TLQQQQQLQN QQQLHQQQQQ QLQYEQLQQL
QQLQQHQQQQ QHQQQQQQQQ QQQQQQQQQQ QQQQFKKHKR ENTPVIVEDS LKLNIQENEL
LFIKKIGSGA CGEVCQYEWK GTPVAVKTIF KSLLRKDKKE EFEKEVSILK CLRHPNVVLF
MGTCLLNGNL AIITEYLNRG SLRDVLTTMN KSELSLSVKV KMLIDVAQGM NYLHTYSPPI
IHRDLKSLNL LVDNNFNVKV SDFGLSRFIS GGIGSSAKTF CGTLSWIAPE VFNGSGYTTK
VDVYSFGIVL WEILTHKQPS GNISATSLGH PELPSNCPQS FSDLIKECCN RNPDQRPNFS
QILLKLKLMY NQINNNNNNN KIDSSSFHNN NNNCSYNNSN DNNGILVTGG VGGNVSGNVE
SNNNNNNNTL NGAGNVIILN EIKDFTIQPN EITNIKTIIV KDSYSILEGQ YKGKLVSIKQ
INGSINDFEM KQLGVLASIK SPLAVRFIGV VFNTDEYAII SEHVGNNGSL LTLMQNHSNQ
LNWSNTIDLA IQITQSIQYL HKHQPPILHR NITSDCFLLS SLNNNSNQNN NNNNNNNNNN
NNNNNNNNNN NKKNDGGDDN GENTNTTTTT TTTTTTATNI TNELNINEIK IKVHDFGLSR
FNTQENEESL KEIKGNFLYS PPELLSLNTY SNKSDIYSLS IVLYELFETC LTKTYKKPYH
EVTLDFDFQI IHKTSKLNLR PTISNNMPNE ISKILQQGWF SDSVLRPSLD TIIKELLICK
KNLC
