ID   Y2354_DICDI             Reviewed;         495 AA.
AC   Q54DF7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable serine/threonine-protein kinase DDB_G0292354;
GN   ORFNames=DDB_G0292354;
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; AAFI02000189; EAL61301.1; -; Genomic_DNA.
DR   RefSeq; XP_629684.1; XM_629682.1.
DR   AlphaFoldDB; Q54DF7; -.
DR   SMR; Q54DF7; -.
DR   STRING; 44689.DDB0216336; -.
DR   PaxDb; Q54DF7; -.
DR   EnsemblProtists; EAL61301; EAL61301; DDB_G0292354.
DR   GeneID; 8628600; -.
DR   KEGG; ddi:DDB_G0292354; -.
DR   dictyBase; DDB_G0292354; -.
DR   eggNOG; KOG1164; Eukaryota.
DR   HOGENOM; CLU_019279_2_7_1; -.
DR   InParanoid; Q54DF7; -.
DR   OMA; NYEDRPN; -.
DR   PhylomeDB; Q54DF7; -.
DR   PRO; PR:Q54DF7; -.
DR   Proteomes; UP000002195; Chromosome 6.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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..495
FT                   /note="Probable serine/threonine-protein kinase
FT                   DDB_G0292354"
FT                   /id="PRO_0000384441"
FT   DOMAIN          16..275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          293..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..429
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         22..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   495 AA;  55282 MW;  0CBA93FF1D16FD2F CRC64;
     MQNIGFAAGS LIKGRWTVVK KIGQGAFGEI FSGKNIINNE QIAIKVEKVD TKKQVLRLEV
     AVLKKLQLCP YVCRFITCGR HNDYNYMVME LLGENLSELR RKQLDGKFSL GSTLKLGVQM
     IQSLQAVHDL GYLHRDVKPS NFAIGLNPSK RNITYLIDFG LARRFVLASG EVRPARESTG
     FRGTARYASI NSHLSKDLGR RDDLWSIFYV LIEFAEGQLP WRKLKDKDQI GEMKQKYNTP
     DLVKDLPPQF SQFMKHLKSL NYEDRPNYVF LQTLLNDCYT SLGLSESTPF DWEVQTNSGA
     SSSSSNTTQQ QQQQQQQQQQ RNLNQSGLNN SSARLMASPS TIDVEASGKS TQLNNSNNNN
     NNNNKGLGAE NDSSPQPQII RRNSESNSQI ANSSESDNKG SGGGSWNQKS SSPRHKDKNL
     QDDGGEGSQK HLKASNNNNI NNNNNNYNNN NNNNNNSHMN GNGSNSQPID KIELSHQQQK
     SSTTKCCSTS KCSVM