ID   Y7566_DICDI             Reviewed;         844 AA.
AC   Q1ZXR2;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Probable serine/threonine-protein kinase DDB_G0267566;
DE            EC=2.7.11.1;
GN   ORFNames=DDB_G0267566;
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:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AAFI02000003; EAS66945.1; -; Genomic_DNA.
DR   RefSeq; XP_001134482.1; XM_001134482.1.
DR   AlphaFoldDB; Q1ZXR2; -.
DR   SMR; Q1ZXR2; -.
DR   STRING; 44689.DDB0231559; -.
DR   PaxDb; Q1ZXR2; -.
DR   EnsemblProtists; EAS66945; EAS66945; DDB_G0267566.
DR   GeneID; 8615936; -.
DR   KEGG; ddi:DDB_G0267566; -.
DR   dictyBase; DDB_G0267566; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_337544_0_0_1; -.
DR   InParanoid; Q1ZXR2; -.
DR   PhylomeDB; Q1ZXR2; -.
DR   PRO; PR:Q1ZXR2; -.
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   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
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   ANK repeat; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Repeat; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..844
FT                   /note="Probable serine/threonine-protein kinase
FT                   DDB_G0267566"
FT                   /id="PRO_0000362062"
FT   REPEAT          335..367
FT                   /note="ANK 1"
FT   REPEAT          371..400
FT                   /note="ANK 2"
FT   DOMAIN          508..773
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        634
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         514..522
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         539
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   844 AA;  97296 MW;  1DCC0AEF9268D953 CRC64;
     MNIKFDMFVK DSNSIDSEEL LNNYLTLNVV SQELLIQNAQ KPLTPLSIEI GKTRTINKNI
     KSKLNFIMPS FCEYYELEGN YILYFKKLKI FEDFIIYKDQ SIPISNQMEI KIGKGKVLVN
     GKKISIKDEE IKNNFIRDLN FLSSIKNFRN QYSHGNEIEA VESISKKENS INSLVIPTFI
     KFLGEIIIKT KDTIKFKNLM VLSDNFNILD DVIYQVENNE LNLKNSKNSV VYKSIKKSIP
     IYLLSKVFEH TEFYILEKNN SILNFFCKKR IEDFNENSED KEFNSTSEND SHESSIDLKC
     SSEVSQIKIE RFHEYVSLFS KCISKNVDIN HKNDKGDTAL HNTIKNLKKE SGPMVAALLS
     CGANANIRNN KHKVPLHFAI EFGDESIIKI LLAFGAKPFL EDSISFSERD PGKIYKELNK
     SGQVLKILYE IGVITKLFDN FSVLQHVKTF ILLEILFQNS MNILKSDIFS SILNNIFNQN
     IVRFKLIIQN LKEPPLSKFK KIEKFDRSEL GKLIGKGANG KVYELHYNFG GVEKHCAVKE
     IKVDKYRVGA VLKEIESTAL SQSPFTVGIY GYFEDEKNNF LYIFLEYCPN GNLFDIINKE
     KMKSFDEFFS YAFGVVHCTH DIHSNPKGAL IHRDIKASNF LVDKNNLVKI GDFGTARFDC
     TLNLSSLKNG AGTVCFQAPE ASRGKATIQS DIYSLGVVLF ELCGAIPYKN YNYFFPFGDL
     KYLRVASAVS NYLRPILHPV IPQPLSDLIY SMLNHNEYDR PTSFEVFQKL KKVQEDYESN
     KEEWNSIFNT IDMKEDQQFH HERQEKVALM IKKKYLLTRP ITESLVNHYD NIVFNIDYSI
     SLNF