Y0670_DICDI
ID Y0670_DICDI Reviewed; 641 AA.
AC Q54IF2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0288795;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0288795;
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).
RN [2]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA Skelton J., Ivens A., Bozzaro S.;
RT "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT bacteria in Dictyostelium.";
RL BMC Genomics 9:291-291(2008).
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 -!- INDUCTION: Down-regulated by phagocytic stimuli.
CC {ECO:0000269|PubMed:18559084}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000125; EAL63019.1; -; Genomic_DNA.
DR RefSeq; XP_636525.1; XM_631433.1.
DR AlphaFoldDB; Q54IF2; -.
DR SMR; Q54IF2; -.
DR STRING; 44689.DDB0220670; -.
DR PaxDb; Q54IF2; -.
DR EnsemblProtists; EAL63019; EAL63019; DDB_G0288795.
DR GeneID; 8626810; -.
DR KEGG; ddi:DDB_G0288795; -.
DR dictyBase; DDB_G0288795; -.
DR eggNOG; KOG0690; Eukaryota.
DR HOGENOM; CLU_000288_120_1_1; -.
DR InParanoid; Q54IF2; -.
DR OMA; YYHPFIV; -.
DR PhylomeDB; Q54IF2; -.
DR Reactome; R-DDI-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DDI-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-DDI-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-DDI-165158; Activation of AKT2.
DR Reactome; R-DDI-165159; MTOR signalling.
DR Reactome; R-DDI-165181; Inhibition of TSC complex formation by PKB.
DR Reactome; R-DDI-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-DDI-198693; AKT phosphorylates targets in the nucleus.
DR Reactome; R-DDI-199418; Negative regulation of the PI3K/AKT network.
DR Reactome; R-DDI-203615; eNOS activation.
DR Reactome; R-DDI-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-DDI-389513; CTLA4 inhibitory signaling.
DR Reactome; R-DDI-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-DDI-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-DDI-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DDI-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DDI-6804757; Regulation of TP53 Degradation.
DR Reactome; R-DDI-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-DDI-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-DDI-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DDI-9031628; NGF-stimulated transcription.
DR PRO; PR:Q54IF2; -.
DR Proteomes; UP000002195; Chromosome 5.
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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_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 InterPro; IPR045270; STKc_AGC.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..641
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0288795"
FT /id="PRO_0000355013"
FT DOMAIN 13..144
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 173..430
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 431..503
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 509..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 179..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 641 AA; 71977 MW; 47439819A07CE30F CRC64;
MLKDIYNSLL SKKQEESNMA AWNNEDILET QAQLFFSIKS IKGLKIMDNP IKVYCLASLE
KQSVQTSSIV INKDQSQIEW NEGYTFDVIS SKSILALSIW QGNANVTIAN NSIEGGGSSN
NSKLVGKLYI PFATFKKQFC DQWFPLTGTS QSVSIHVKTS FTNSSKKVTV DDFIFLRMIG
RGAFGQVNLV KKIDTGRLYA MKVIKKDKCL NMNAVGHTFT ERKLLKKYYH PFIVGLKYSF
QTQDSLCMVL DYIGGGELFY HISERETFSE ETARFYIGQI MLAIGFLHEH GVIYRDLKLE
NLLMDLDGNI CLVDLGLCKE GIQEGHVTYT MCGSPEYVAP EIINGTGYSK SVDWWALGTL
FYEMIAGLPP FYSEDPHEMT KLILSSPLKF PPQISKNAAS LVSLLLNRDP SKRLGSGESD
VEEIKAHPFF KNVNWSKLLN KEVDPPFKPH LVGPLDLSYF DPLCTMNSQP INPYTINSNL
SDQDQMAFQG FSYSAPDIFL NNNNNTTTSN TNIGGSGSNS GSAQNSPYNS LRNTPPSIIS
MMKMSGSSGG FERMSPGHFS PISVNKQQQI QQQQQQHHQP PPLLQPQPQF WVQPQHPNHI
PQPMAQLPIL SKLQETTFER RRSLSVNAQT QFTLVLDPNE E
