ID   SAMKD_DICDI             Reviewed;         553 AA.
AC   Q55CW1;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Probable inactive serine/threonine-protein kinase samkD;
DE   AltName: Full=SAM domain-containing protein kinase D;
GN   Name=samkD; Synonyms=SAMK-D, smkD; ORFNames=DDB_G0270680;
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   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
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; AAFI02000005; EAL72690.1; -; Genomic_DNA.
DR   RefSeq; XP_646370.1; XM_641278.1.
DR   AlphaFoldDB; Q55CW1; -.
DR   SMR; Q55CW1; -.
DR   PaxDb; Q55CW1; -.
DR   EnsemblProtists; EAL72690; EAL72690; DDB_G0270680.
DR   GeneID; 8617325; -.
DR   KEGG; ddi:DDB_G0270680; -.
DR   dictyBase; DDB_G0270680; samkD.
DR   HOGENOM; CLU_492983_0_0_1; -.
DR   InParanoid; Q55CW1; -.
DR   OMA; KESSCRT; -.
DR   PhylomeDB; Q55CW1; -.
DR   Reactome; R-DDI-111932; CaMK IV-mediated phosphorylation of CREB.
DR   Reactome; R-DDI-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   Reactome; R-DDI-442729; CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde.
DR   Reactome; R-DDI-9619229; Activation of RAC1 downstream of NMDARs.
DR   PRO; PR:Q55CW1; -.
DR   Proteomes; UP000002195; Chromosome 1.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..553
FT                   /note="Probable inactive serine/threonine-protein kinase
FT                   samkD"
FT                   /id="PRO_0000362033"
FT   DOMAIN          24..90
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          134..393
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         140..148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   553 AA;  65038 MW;  FA2381454C403DA2 CRC64;
     MEKSIESISS STLNILDNKN YKKWDNETVC KWLLNNIKTI QKVSIEIFQA NEIIGKDLEF
     LTDKILLKMG VGIRDILNFK FEYQILKNCY NNNNNNNHIT INNFNYNFNN FKININKDLL
     KVVVNAPIIN INEYQYIETI SKNKFCEIEK YKKSQTKVNE YIIIKKIIKN STLNEEKLIN
     EIDTIYLLDH PNLIKIIGYC KDKNYFYIGM KYYETFKFKQ SNISKFGKNF EQVIRKISFK
     ILSAIDYLHS LEPPIIHGNI NAKNILLDNE NNEPILIDFG LSYKSIDLLT NQKTQFISPC
     FITPEYFYKK TKNKISKEAD IFSFGSTISN MIKGGTDFKE DEEGFEELKR TFAGVLTSRD
     KVSFDYRSLF TEINKDEPCF RPSSKELLKS FWFVEPPQPS FKTSEITTNL LIYYLKKYGC
     YIIRDGVAMV SLNFNENIYS TSSIIGSEFS HQPKINEKHK YFKEINQFYS KILSESFQAK
     IGWYLLNLNN EFKDKPYFKN IFLSFSTSDK LEINSVADLN LKLTIFFYNS ITMSLIYQTI
     YQKPKSFKIV DYL