KC1_PLAF4
ID KC1_PLAF4 Reviewed; 324 AA.
AC O15726;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Casein kinase I;
DE EC=2.7.11.1;
GN Name=CK1;
OS Plasmodium falciparum (isolate Dd2).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57267;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9334178; DOI=10.1074/jbc.272.42.26132;
RA Barik S., Taylor R.E., Chakrabarti D.;
RT "Identification, cloning, and mutational analysis of the casein kinase 1
RT cDNA of the malaria parasite, Plasmodium falciparum. Stage-specific
RT expression of the gene.";
RL J. Biol. Chem. 272:26132-26138(1997).
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 -!- DEVELOPMENTAL STAGE: Stage-specific expression in the parasite, in the
CC order trophozoite > ring >> schizont.
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; AF017139; AAB70009.1; -; mRNA.
DR AlphaFoldDB; O15726; -.
DR SMR; O15726; -.
DR BRENDA; 2.7.11.1; 4889.
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; IDA:CACAO.
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_0000192851"
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; 37832 MW; 93A53AAC11187EFD CRC64;
MEIRVANKYA LGKKLGSGSF GDIYVAKDIV TMEEFAVKLE STRSKHPQLL YESKLYKILG
GGIGVPKVYW YGIEGDFTIM VLDLLGPSLE DLFTLCNRKF SLKTVRMTAD QMLNRIEYVH
SKNFIHRDIK PDNFLIGRGK KVTLIHIIDF GLAKKYRDSR SHTSYPYKEG KNLTGTARYA
SINTHLGIEQ SRRDDIEALG YVLMYFLRGS LPWQGLKAIS KKDKYDKIME KKISTSVEVL
CRNASFEFVT YLNYCRSLRF EDRPDYTYLR RLLKDLFIRE GFTYDFLFDW TCVYASEKDK
KKMLENKNRF DQTADQEGRD QRNN
