Y4491_DICDI
ID Y4491_DICDI Reviewed; 1212 AA.
AC Q54PK8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0284491;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0284491;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; AAFI02000066; EAL65172.1; -; Genomic_DNA.
DR RefSeq; XP_638524.1; XM_633432.1.
DR AlphaFoldDB; Q54PK8; -.
DR STRING; 44689.DDB0231198; -.
DR PaxDb; Q54PK8; -.
DR EnsemblProtists; EAL65172; EAL65172; DDB_G0284491.
DR GeneID; 8624617; -.
DR KEGG; ddi:DDB_G0284491; -.
DR dictyBase; DDB_G0284491; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_269659_0_0_1; -.
DR InParanoid; Q54PK8; -.
DR OMA; GGQANIY; -.
DR PRO; PR:Q54PK8; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1212
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0284491"
FT /id="PRO_0000362054"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 865..1182
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 288..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..721
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1035
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 871..879
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 924
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1212 AA; 140458 MW; 1E26895EECFC7BE0 CRC64;
MSDYILSAEI NLPLLKWMTS FKLNSNLFST SRNQSLKSIS EIYRDLQYNI IPPKDEELQN
LWTHLYDLNN YYSNSIEYNQ VEKSLMGLKS KYRNSYLKGY YEIINLFQSI ANDFEKLSSP
ISQTTTTTQI PIISFNKNSV LDAINNRKNE NKENSFKFLS SFESYVPTVE EIKRIYCIDN
KEILIDKSCT LPVEYKLFHS FSLLNLYVYL IIVIRIIKLI GEINRQSSNA SENQEILHLL
KEYSLHIKSI EEFQLQLKLN NLYYQPTKKE IILKYFVEIN SNNNLNNLNN NNDNNLNNNN
SNNNLNNNNN SNSNFNNDNN LNSNINSNDT SISNNNSIIN NNSNNSNTNN NNNNNIINNI
KIFEFSEKEL KYSKRYYSYN EFTLRPAELP NNSLGIETQN LIFYTTSNYN SGNSNSGSNN
SNSSNNNSSS NSLINNSGGN SNSGLIPKIK FNHHRPKDIN PKIVLAVYNN ILSMSKVIDK
KTINSMNEII KNNNNNNNNN SNNNNNNNDE DDSDYEENEF NKEFNNQFEF GSEIIEQDKE
CYICRFRSEF ISFCNYCKCK MICDLCSVNK VCWNCYFKVD KVSGNEQQQQ QQHFIPLEVV
VKLKDRKYPR LIYMLLRSYS FRDLMNTLYQ DRFERDSVIS PKDRFTYKLH KTKLYNFHLV
LPNCKNPFQT KEIQIFDDYS LIIALRLLMN FILSNYIIDQ KEVPPPPTQP SSRPQSPPTV
SPLTPLNNHH HSGGSLLEHA IARNFNNNSV EVVSDDNTSG SGTGGSNSNS NTGGSYNKFN
NNNNNRKNST GSGTNSRNNN SDNEYSYNNN NNNYNNNNNN KIINNNSIVT VENPILWNID
KFILNVIESS IDIEQSLKIP SSCIETEIEP FASGGQANIY MVKHIDWPML SNCPEGSYVF
KQFIETKDSL QLEEDIEREM YEEKIYQTYK TGESVDNFKY NFSNVEQTDK KSLETLFYEE
VDKLKRLQFS DYIIKMPAIS DDNPNKRGML LECATAGSLK TNLLEYRSWK LVIRFMMDIC
LGMIDIHKCQ IIHRDLKPDN ILVFENFNSS EASDENDERQ REFGGLICKI TDLGASIQKE
LVHDNNFTST FHTDDYVPEE YGRFQYDGEK VDIYSFGCTF FEMVTKHRYQ YKHPTPLHRD
FLTTDFQYIP IRIKTLIASL LAEQSQRKQS FNEVYNDLQD IYKNVIPGLP DIPLSPISTN
GSQFCKRCNP QK
