CK12_TRYBB
ID CK12_TRYBB Reviewed; 332 AA.
AC B9VVJ6;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Casein kinase I isoform 2 {ECO:0000303|PubMed:19450734};
DE EC=2.7.11.1 {ECO:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830};
GN Name=CK1.2 {ECO:0000303|PubMed:19450734};
GN Synonyms=Tb927.5.800 {ECO:0000303|PubMed:19450734};
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702 {ECO:0000312|EMBL:ACM68937.1};
RN [1] {ECO:0000312|EMBL:ACM68937.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-133 AND 299-ARG--VAL-332.
RC STRAIN=427 {ECO:0000312|EMBL:ACM68937.1};
RX PubMed=19450734; DOI=10.1016/j.molbiopara.2009.03.001;
RA Urbaniak M.D.;
RT "Casein kinase 1 isoform 2 is essential for bloodstream form Trypanosoma
RT brucei.";
RL Mol. Biochem. Parasitol. 166:183-185(2009).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=427 {ECO:0000303|PubMed:27002830};
RX PubMed=27002830; DOI=10.1371/journal.ppat.1005514;
RA Minia I., Clayton C.;
RT "Regulating a Post-Transcriptional Regulator: Protein Phosphorylation,
RT Degradation and Translational Blockage in Control of the Trypanosome
RT Stress-Response RNA-Binding Protein ZC3H11.";
RL PLoS Pathog. 12:e1005514-e1005514(2016).
CC -!- FUNCTION: Serine/threonine protein kinase (PubMed:19450734,
CC PubMed:27002830). May phosphorylate ZC3H11 during unstressed
CC conditions, leading to proteasome-dependent degradation of ZC3H11
CC (PubMed:27002830). {ECO:0000269|PubMed:19450734,
CC ECO:0000269|PubMed:27002830}.
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:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830};
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:0000269|PubMed:19450734,
CC ECO:0000269|PubMed:27002830};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19450734, ECO:0000269|PubMed:27002830};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is about 27 degrees Celsius. Loses activity at 41
CC degrees Celsius. {ECO:0000269|PubMed:27002830};
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the bloodstream form
CC inhibits cell population growth and leads to gross morphological
CC changes and multinucleation (PubMed:19450734). RNAi-mediated knockdown
CC in the procyclic form inhibits cell population growth and decreases
CC ZC3H11 phosphorylation (PubMed:27002830). {ECO:0000269|PubMed:19450734,
CC ECO:0000269|PubMed:27002830}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; FJ608535; ACM68937.1; -; Genomic_DNA.
DR AlphaFoldDB; B9VVJ6; -.
DR SMR; B9VVJ6; -.
DR OMA; IFDWTFL; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:2000058; P:regulation of ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..332
FT /note="Casein kinase I isoform 2"
FT /id="PRO_0000451924"
FT DOMAIN 11..282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 306..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 133
FT /note="D->A: Abolishes protein kinase activity; when
FT associated with 299-R--V-332 DEL."
FT MUTAGEN 299..332
FT /note="Missing: Catalytic active. Abolishes protein kinase
FT activity; when associated with A-133."
FT /evidence="ECO:0000269|PubMed:19450734"
SQ SEQUENCE 332 AA; 38375 MW; 86CCEE3F205983F3 CRC64;
MSVELRVGNR FRIGQKIGSG SFGEIFRGTN IQTGDPVAIK LEQVKTRHPQ LAFEARFYRV
LNAGGGVVGI PNVLYHGVEG EFNVMVIDLL GPSLEDLFSF CGRRLSLKTT LMLAEQMIAR
IEFVHSKSII HRDIKPDNFL MGTGKKGHHV YIIDFGLAKK YRDARTHQHI PYKEGKSLTG
TARYCSINTH IGIEQSRRDD LEGIGYILMY FLRGSLPWQG LKAHTKQEKY ARISDRKQTT
SVETLCRSFP AEFAAYLNYT RSLHFEDKPD YSYLKRLFRE LFVREGYHVD YVFDWTLKRI
HDTLQEGRAD QQQQQQQQQQ RRGSEKEDEH PV
