Y0111_DICDI
ID Y0111_DICDI Reviewed; 1126 AA.
AC Q54VV7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0280111;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0280111;
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; AAFI02000035; EAL67282.1; -; Genomic_DNA.
DR RefSeq; XP_641248.1; XM_636156.1.
DR AlphaFoldDB; Q54VV7; -.
DR SMR; Q54VV7; -.
DR STRING; 44689.DDB0229350; -.
DR PaxDb; Q54VV7; -.
DR EnsemblProtists; EAL67282; EAL67282; DDB_G0280111.
DR GeneID; 8622380; -.
DR KEGG; ddi:DDB_G0280111; -.
DR dictyBase; DDB_G0280111; -.
DR eggNOG; KOG1989; Eukaryota.
DR HOGENOM; CLU_279716_0_0_1; -.
DR InParanoid; Q54VV7; -.
DR OMA; AFEEMKW; -.
DR Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q54VV7; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
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; IPR011417; ANTH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07651; ANTH; 1.
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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1126
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0280111"
FT /id="PRO_0000362038"
FT DOMAIN 16..295
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 314..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..362
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1126
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1126 AA; 126004 MW; C7E026D60EFE7AAB CRC64;
MGNNQGKTLK IGSYHLNFVK QIAEGGFSYV FLVKDSNTSK HYALKRILIR DEDELKGVKH
EISIMKRLTK HKNIVKILDY HKVSDKNNTE MFILMEYCSG GHLVEIMQKR LSSGSKFTDQ
EILKIFQDIC ESVAYMHSQQ PLIIHRDLKV ENVLLDEESG IYKLCDFGSA TEEITRMKNK
TEMQNAEDDI SRHTTLQYRA PEIVDFYRSP VINEKIDIWA LGCLLYKLLF YVTPFEDSGS
LGILNSNYTI PPNHTHSNDL ISLIKIMLNP DPINRPNIFE ITNQLNLLRN QQPLFPSHKS
NILLSYNENN NINNNNNNIN NNNNNNIVNG KNIPKPLPKV VSQTTPTPTP PPPAPSQSPS
PSPSPTVVNN IENNSNGLEH SNSNGNISQP SPTPPKRRAT PGTTPSLQPV SFPPNNSNNS
FDDPFRDSPR TNLSNNPFNV NSNDNSNSSN NNNNNNNNNN NNNNNNGNNI TNEEILNIIT
QLTNNDQTNT FDSGLLLKLK SMKPGKGTMH IIVKRPLKEP LVCFKSLLLV HALLSEGNNI
QFKSDVHDSK DLFNNLYLGW SKQKDRYLQL GELLSHYSLL LYKFILFHQK NYMIDGSFAF
EEMKWGIPES LDSNNHPISI NTIKALFDIM DHLFLVQNNL SDYCINNICS SNSSGSGNVP
ISLLQHCVNI LNSSSYSIFC FISGSIDVLS KQFSDVDMKL ISCVNQFQSM YTRLREQYTK
LAQVPCFSDI FFPTLPNTAP TFTIVRSNSF NRLNSSLSDL NLNNNNNNNN NSNNSNNSNN
SNSGNLSGNA SLNSSFDNIN SSNPFSTEPT FNPFSATTTN TSESGFGNFG LSEPTSNPSP
RYQQSNNNNN NNNNNNGTPI SLTPGSLSPV IGAKKPPLPP NIHHLQQQQH PQQQQQQQQQ
QQQQQQQQQQ QQQQQQQQHP QQQGLRFPHS ASLEDARLYT LILTPSSSPP LSPSTGPTTA
AQQQQQQQQS QHTFDNFNIN GHAPPVPQST QPSFQPHVSF APNVNINNNN NSHVSAPHSL
NSSSSSISSI SNPNLGGIAQ KGSGNSLMPP PLYKPAARGH RRSQSSNGDE VRRRNLLQQQ
LEQNRDFLNH NRLLNKQSRM NNPNNLFDEG DSGFGDGEEE DEGLLN
