Y9877_DICDI
ID Y9877_DICDI Reviewed; 941 AA.
AC Q54QI2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Serine/threonine-protein kinase DDB_G0283821;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0283821;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL65525.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL65525.1};
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] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17659086; DOI=10.1186/gb-2007-8-7-r144;
RA Sawai S., Guan X.-J., Kuspa A., Cox E.C.;
RT "High-throughput analysis of spatio-temporal dynamics in Dictyostelium.";
RL Genome Biol. 8:R144.1-R144.15(2007).
CC -!- FUNCTION: May play a role in responding to changes in cAMP levels.
CC {ECO:0000269|PubMed:17659086}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250, ECO:0000305};
CC -!- DISRUPTION PHENOTYPE: Cells have an aberrant response to waves of cAMP
CC stimulation. {ECO:0000269|PubMed:17659086}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. {ECO:0000269|PubMed:17659086}.
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DR EMBL; AAFI02000057; EAL65525.1; -; Genomic_DNA.
DR RefSeq; XP_638889.1; XM_633797.1.
DR AlphaFoldDB; Q54QI2; -.
DR SMR; Q54QI2; -.
DR STRING; 44689.DDB0229877; -.
DR PaxDb; Q54QI2; -.
DR EnsemblProtists; EAL65525; EAL65525; DDB_G0283821.
DR GeneID; 8624287; -.
DR KEGG; ddi:DDB_G0283821; -.
DR dictyBase; DDB_G0283821; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_312033_0_0_1; -.
DR InParanoid; Q54QI2; -.
DR OMA; CTYSAID; -.
DR Reactome; R-DDI-75153; Apoptotic execution phase.
DR PRO; PR:Q54QI2; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022357; MIP_CS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00221; MIP; 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; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..941
FT /note="Serine/threonine-protein kinase DDB_G0283821"
FT /id="PRO_0000361652"
FT DOMAIN 13..265
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 270..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 941 AA; 103673 MW; 70ECBDC796AF5B9C CRC64;
MDTIKETDSF SKYQIGEAVG KGAFGKVFKA LNAETGDFCA IKQIEKTIIS EKQLPSIIQE
IKLLQTLQHP NIVKFIESYE TSRYLYFALE FIEGGSLAKI AKRYGCFQEP LLSRYFSQVL
KGLAYLHEKG VIHRDIKSDN ILITKEGVIK LADFGSCTYS AIDRKLTVVG TPFWMAPEVI
QMDMNARSTA CDIWSLGCTL LEMLTGNPPY WDLGTMPAMF AMVNNPHPPI PNNISADLKH
FLLACFVRDI NKRPTASQLL EHPWIKQHIH EPSQSQPASS PEPSRIKSSG SGSKLSINTY
AEGYDVESDD DTTNSNNGSD HDRIQQLESQ KKEMTETIKR LKLHFLRAMK EKKVMKDMIS
QLVTERDEYM IKLGLTPPPL PPILANATLN SKSSLDSSNE LLNKESSQGN LLGSGGSGSP
YTNHTRSSSA PLTAPGKIIS THQIHSPSLS NSSASASTSG VSNNKERGSS ILTNDFFHPP
SDDDQHSPTN DLFLHEHFEK NLKVTASSSP SSLSKNSRLT TKFELESDNN TNNNNNNNNN
NNNINITTTT TTTTTTPASN QNLGAYYQSS GNLHLYTNQN NLTNNNINNT NNNNNNNNNN
NNNNNLGSNT NVDMYLRTSS EKTHLSITQP VSLSGALSYG DHLNPSVTIG GHNSLKQKGS
GKTSIPVLQK EPSNKSLNSL NNNNVNNNNN NNNNNNNNNN NNNNNNNNNN NNNNTNSNSN
NNTNNINSTN NINTNNINNV LGTSPSRKIS NSDQFTPNRK SSQPIAPSFS LLNQSLDRNP
NSNNNNNNNN NNSNNNNNNN NNNNNNLNSG SNSFNNNSPI SSFTNNNNNN ESGDEYDDDS
DIIEDEQSSN SSLSFNNSNV PQVESVVVNV QPPRVGDECK VKCGDGWYDA VVDLVSGSTF
VVTIKPFKIK REVSHSDVTL APLQFPVTAT KKKKFSLFNR K
