ID   Y2777_DICDI             Reviewed;         639 AA.
AC   Q54SC4;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable serine/threonine-protein kinase DDB_G0282777;
DE            EC=2.7.11.1;
GN   ORFNames=DDB_G0282777;
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:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL66248.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAFI02000047; EAL66248.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_640115.1; XM_635023.1.
DR   AlphaFoldDB; Q54SC4; -.
DR   SMR; Q54SC4; -.
DR   STRING; 44689.DDB0230125; -.
DR   PaxDb; Q54SC4; -.
DR   EnsemblProtists; EAL66248; EAL66248; DDB_G0282777.
DR   GeneID; 8623649; -.
DR   KEGG; ddi:DDB_G0282777; -.
DR   dictyBase; DDB_G0282777; -.
DR   PRO; PR:Q54SC4; -.
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; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   SUPFAM; SSF56112; SSF56112; 2.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..639
FT                   /note="Probable serine/threonine-protein kinase
FT                   DDB_G0282777"
FT                   /id="PRO_0000362049"
FT   DOMAIN          233..588
FT                   /note="Protein kinase"
FT   REGION          601..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          7..122
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        439
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         239..247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   639 AA;  75155 MW;  41E7C6C99B71D741 CRC64;
     MDISGFLKEN KESLKDLKED DINEILEDYE IDNINDPKQK IRFFKQVENT RKRLKIEEKN
     RMLEEDINRM YEEEKNRMLE EEKKEFLIKV EEEKKEFLTK VEEEKQKLKT EVEDLKSIIL
     TSSTKNGDLK GTTSYSELFK IKNSLKLIEE NCEFKDWNIP SGIELKKHVI NLDDCNQEST
     MQSKLDEYFK DFNKKRKLII TNGTKIKINS IISNRYCDYF INQKGFPFEP YWMHMVGDIK
     KGSISSDTNL DQVLKYIDII VEKSNHHVLN RPMFGFLMNK TKIKFVKYDI ENNKYYITID
     YDLRIGFQYL SNIMIYLEQF IRNIPNSLQT ILKNHTNDSV EFYYGATSSV FIVNKEFVYK
     WFNYPYFFQT EVKYLTFIDG IEGTPSIKQQ NQTENWIQIS PRGQLIKNLE GKPIDISFYT
     KVFCRNTQKH TSREVIHRDI RLSNLLMDSG GDPLLVDFGF ANFTENEEFY QGTMNTASNR
     IYNILINNRT NHAFSVVESD DLESLVKVYI MENEQAVKRT IKSIPNSEIG LFRTMWEFFN
     TECFPQYSTL FQQAQNINYE ELKNEFIKID KIKNTTTTSN NNQNHTNIHK NTIANTTSYT
     NTLETSTTNP NTNTTTSDTN TSTTSTTNTN TTTSNTITA