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Y0436_DICDI
ID   Y0436_DICDI             Reviewed;         967 AA.
AC   Q54FR9;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable serine/threonine-protein kinase DDB_G0290621;
DE            EC=2.7.11.1;
GN   ORFNames=DDB_G0290621;
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; AAFI02000164; EAL62171.1; -; Genomic_DNA.
DR   RefSeq; XP_635698.1; XM_630606.1.
DR   AlphaFoldDB; Q54FR9; -.
DR   SMR; Q54FR9; -.
DR   STRING; 44689.DDB0220436; -.
DR   PaxDb; Q54FR9; -.
DR   PRIDE; Q54FR9; -.
DR   EnsemblProtists; EAL62171; EAL62171; DDB_G0290621.
DR   GeneID; 8627769; -.
DR   KEGG; ddi:DDB_G0290621; -.
DR   dictyBase; DDB_G0290621; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_306405_0_0_1; -.
DR   InParanoid; Q54FR9; -.
DR   OMA; HINGSYL; -.
DR   PRO; PR:Q54FR9; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; 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; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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..967
FT                   /note="Probable serine/threonine-protein kinase
FT                   DDB_G0290621"
FT                   /id="PRO_0000355154"
FT   DOMAIN          345..610
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          65..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..94
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        467
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         351..359
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         368
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   967 AA;  110461 MW;  2085D96990E562C9 CRC64;
     MNSFEKKILI LKKDDKDSFI ALVKQLSTKE KQILFDTIDS RIRKLQTIYL NKPFNLKFLQ
     TFIKEDSDED DDDEEDEEDE EDSDEEEDDD VVEDDNTKDI GKSRDSDKSI KGKEKGKEKE
     KEEIEIIEQR YETKVIPKKP IYKDQQQELL QQLQLQQLQQ KPISPIKDNS GVSYNTSFSS
     LSSLSMSNST SSSLLSTSLL SASLLSASSS GLSTSSLSSS INNSSNNNSN ISSSPLSSSP
     LTLSSSSSSS SPLQRIQSIQ NLIRSNSLRT SLSSSSSLLP NLIQLQQQQL PPPPPSQQQQ
     QQQQQQQQQN NSMLQQSNNN NISPRTQLLN NTTTLLPNNG LEEIFNDSNK IGEGGQCSIY
     KYMGTAMKRF KPSLSSSLIS KEFENEVLIL ERLNHPNIVK IITYSTIERI ILLEFIDGNS
     LDKYPSQSLP LSPSSSLPNP LKVIQDFQQI VDAMIYLHNE IGIIHFDLKP SNILKNSKNN
     KLKLIDFGIS KFLNNNNQNN NNNSLNMGSY RYSPPELLCN NNQNNNLINK SVDVFSFGIM
     LWECLNWTLP YESLSREQVK QIKTDMERES HLPLDHLPKG IQDLIRLCWK HDPSIRPSFI
     EIRSRLSEII LNNIPSLNGR QFWISSSKYL QQNDDSLINN NNNNNQNNNN QNNNNNNNNN
     NNNNNNNKDE TTSIIIYESI PWLKFKTFLS NHLNIYRQSS TSNSNSSFNL NNNSSRNNQR
     QQQQQNNRNR SVYNNNYNNN NNNIINNNNN NINNNRNRNY NAYYEYIFDY IRYILKVIDE
     KRDEVSVIEF SRFCTFFSPL ISSSLFRSIQ IFCDIPGLYG YCLKKDLILS SSMITLMSKI
     GYLIFIDPNN INQLFLKMKA PTSSSSNKNN NNNNNDNNNP SNFIDFTIRV KIGNYNQRIF
     QCHGHTSSSL SGLIKELQPL IDNNNSGNSS GSSSSKKSNS GFLYQKTPIS EIKDRHINGS
     YLNQNYK
 
 
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