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Y9955_DICDI
ID   Y9955_DICDI             Reviewed;         916 AA.
AC   Q55GU0;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Probable serine/threonine-protein kinase DDB_G0267514;
DE            EC=2.7.11.1;
GN   ORFNames=DDB_G0267514;
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; AAFI02000003; EAL73210.1; -; Genomic_DNA.
DR   RefSeq; XP_647094.1; XM_642002.1.
DR   AlphaFoldDB; Q55GU0; -.
DR   SMR; Q55GU0; -.
DR   STRING; 44689.DDB0229955; -.
DR   PaxDb; Q55GU0; -.
DR   EnsemblProtists; EAL73210; EAL73210; DDB_G0267514.
DR   GeneID; 8615898; -.
DR   KEGG; ddi:DDB_G0267514; -.
DR   dictyBase; DDB_G0267514; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_317952_0_0_1; -.
DR   InParanoid; Q55GU0; -.
DR   OMA; MGEDYTE; -.
DR   PRO; PR:Q55GU0; -.
DR   Proteomes; UP000002195; Chromosome 1.
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   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
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.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..916
FT                   /note="Probable serine/threonine-protein kinase
FT                   DDB_G0267514"
FT                   /id="PRO_0000355167"
FT   DOMAIN          662..916
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          283..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        784
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         668..676
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         689
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   916 AA;  103257 MW;  8BEC703A476F7C06 CRC64;
     MKGGGFYQNQ YLVPNVYFGN SSPVIAPIGG NALNNNNNNN NNNNNNGNNN NGININISNF
     QHQQHQIHQQ HFGGLSPNMN QNHIIQHISH HQHQQAQQIQ IIQNNNQPQP QQHQIQHQQQ
     QQQQIQQQIQ QQQIQQQQIQ QQQIQQQQQQ QIQQQQQQSK MNFIRGHHQR NSSFDEFSLS
     DVSVGSFKDM GWEEIYFCYH HFTQMDEGKG YLKSFQQLIR YITGLYPDIS PSPNSQFLFS
     LGLLYPNALP QVQSPNMILS LTLKQMIETY SYTKSMVYSG SGSGGGNSGS GGGNSGSGGS
     SGNGTSGSGG SNNGSTIIIN NTNLNNINNN NNTNNNNTNN INIPSTPPIL RSLANGASST
     NINIRKFSPQ QACHIIDVFN SVKDNKTGGV STLKLSLFGA DASLLPLTTL PFHEFVQYIG
     LNIIPFENLF KPPPPPSSQL QSSPPIESQH LFLSEIDELT NNNQNNQNNN QQQQQYQQQQ
     HHQQQQQQYQ QQPQPQPQPQ HQPFIYFEDT SNNNSPLDGN FNNSFGLFNN NNVVNHSPLG
     NNILNNIQQF NNQNNNQNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN HNNNNHNNNN
     NNNNQNNIFN HNQNQNNHLI NNHSPNQYNN QGNILKNSGS VVEPPSQQQQ YFSDIEISFS
     ELKISSKLGE GTFGVVYKGL WRGSSVAIKQ IKINEDVNNQ VLEEFRKELT ILSRLRHPNI
     VLLMAACTAP PNLCFITEYL PGGSLYDALH SKKIKMNMQL YKKLAIQIAQ GMNYLHLSGV
     IHRDIKSLNL LLDEHMNVKI CDFGLSKLKS KSTEMTKSIG SPIWMSPELL MGEDYTEKVD
     VYAFGIILWE LGTGELPYSG LDSVQLALAV TTKSLRPPIP NAWPYQLSHL IQACWHQDPL
     KRPSFTEILN LLNEIP
 
 
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