KC1_TOXGO
ID KC1_TOXGO Reviewed; 324 AA.
AC Q6QNM1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Casein kinase I;
DE EC=2.7.11.1;
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Donald R.G.K., Liberator P.A., Zhong T.;
RT "Coccidian parasite casein kinase I as a chemotherapeutic target for anti-
RT protozoal agents.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. It can phosphorylate a large number of proteins (By
CC similarity). {ECO:0000250}.
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. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR EMBL; AY532160; AAS46019.1; -; mRNA.
DR AlphaFoldDB; Q6QNM1; -.
DR SMR; Q6QNM1; -.
DR EnsemblProtists; TGME49_240640-t26_1; TGME49_240640-t26_1; TGME49_240640.
DR VEuPathDB; ToxoDB:TGARI_240640; -.
DR VEuPathDB; ToxoDB:TGCAST_240640; -.
DR VEuPathDB; ToxoDB:TGCOUG_240640; -.
DR VEuPathDB; ToxoDB:TGDOM2_240640; -.
DR VEuPathDB; ToxoDB:TGFOU_240640; -.
DR VEuPathDB; ToxoDB:TGGT1_240640; -.
DR VEuPathDB; ToxoDB:TGMAS_240640; -.
DR VEuPathDB; ToxoDB:TGME49_240640; -.
DR VEuPathDB; ToxoDB:TGP89_240640; -.
DR VEuPathDB; ToxoDB:TGPRC2_240640; -.
DR VEuPathDB; ToxoDB:TGRH88_030510; -.
DR VEuPathDB; ToxoDB:TGRUB_240640; -.
DR VEuPathDB; ToxoDB:TGVAND_240640; -.
DR VEuPathDB; ToxoDB:TGVEG_240640; -.
DR OMA; IFDWTFL; -.
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; IPR030509; CK1.
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 PANTHER; PTHR11909:SF409; PTHR11909:SF409; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..324
FT /note="Casein kinase I"
FT /id="PRO_0000192854"
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 324 AA; 37960 MW; 06DAA7D90C55E31F CRC64;
MEVRVGGKYR LGRKIGSGSF GDIYIGANIL TGDEVAIKLE SIKSKHPQLL YESKLYKLLA
GGIGIPMVHW YGIEGDYNVM VIDLLGPSLE DLFSICNRKL SLKTVLMLAD QMLNRIEFVH
SKNFIHRDIK PDNFLIGRGK KMSVVYIIDF GLAKKYRDPK TQQHIPYREG KNLTGTARYA
SINTHLGIEQ SRRDDLEALG YVLMYFNRGS LPWQGLKATT KKDKYDKIME KKMSTPIEIL
CKHFPFEFIT YLNYCRSLRF EDRPDYAYLR RLFKDLFFRE GYQYDFIFDW TFINTEKDRA
SRRSQQVYVE DNRQVEENQN ELPM