ID   CERK_CAEEL              Reviewed;         549 AA.
AC   Q9TZI1;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Ceramide kinase 1;
DE            EC=2.7.1.138;
GN   Name=cerk-1 {ECO:0000312|WormBase:T10B11.2};
GN   ORFNames=T10B11.2 {ECO:0000312|WormBase:T10B11.2};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Catalyzes the phosphorylation of ceramide to form ceramide 1-
CC       phosphate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine
CC         1-phosphate + H(+); Xref=Rhea:RHEA:17929, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674,
CC         ChEBI:CHEBI:456216; EC=2.7.1.138;
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
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DR   EMBL; FO080731; CCD66240.1; -; Genomic_DNA.
DR   PIR; T33517; T33517.
DR   RefSeq; NP_491977.1; NM_059576.4.
DR   AlphaFoldDB; Q9TZI1; -.
DR   SMR; Q9TZI1; -.
DR   BioGRID; 37868; 1.
DR   DIP; DIP-25504N; -.
DR   STRING; 6239.T10B11.2; -.
DR   EPD; Q9TZI1; -.
DR   PaxDb; Q9TZI1; -.
DR   PeptideAtlas; Q9TZI1; -.
DR   EnsemblMetazoa; T10B11.2.1; T10B11.2.1; WBGene00020398.
DR   GeneID; 172423; -.
DR   KEGG; cel:CELE_T10B11.2; -.
DR   UCSC; T10B11.2; c. elegans.
DR   CTD; 172423; -.
DR   WormBase; T10B11.2; CE18241; WBGene00020398; cerk-1.
DR   eggNOG; KOG1115; Eukaryota.
DR   GeneTree; ENSGT00940000168717; -.
DR   HOGENOM; CLU_472760_0_0_1; -.
DR   InParanoid; Q9TZI1; -.
DR   OMA; CEQWIQV; -.
DR   OrthoDB; 681139at2759; -.
DR   PhylomeDB; Q9TZI1; -.
DR   Reactome; R-CEL-1660662; Glycosphingolipid metabolism.
DR   UniPathway; UPA00222; -.
DR   PRO; PR:Q9TZI1; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00020398; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0001729; F:ceramide kinase activity; IBA:GO_Central.
DR   GO; GO:0102773; F:dihydroceramide kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001727; F:lipid kinase activity; IBA:GO_Central.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0006672; P:ceramide metabolic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.10330; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Lipid metabolism; Nucleotide-binding;
KW   Reference proteome; Sphingolipid metabolism; Transferase.
FT   CHAIN           1..549
FT                   /note="Ceramide kinase 1"
FT                   /id="PRO_0000421274"
FT   DOMAIN          162..316
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   ACT_SITE        235
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         172..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         205..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         233..236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         277..279
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         500..502
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
SQ   SEQUENCE   549 AA;  62425 MW;  DE95737555534EEB CRC64;
     MPNSKKSKKG GDQQHVTIVP VEPVKGENVD TVAYSSRSRI SGESGHLIAD VQSPHAKKHR
     IIFDRDHNVF EFRLLDGSAK HIIVYRLDEL LSTTCYPFKI KNGVPIIPTK PTTSDKTLYF
     NFVYKKDKQK WRLKQIPVIF YTTSERDYWH SLIDTTLRRV KNRPKNIIIF INPFGGNGKA
     QKIFKDNVDA FFWLTPGLRY KVVLTERANH ARDYIVEMPP EQWSAIDGLV SVGGDGLFNE
     LLSGALLRTQ TDAGRNIDNP SSHLVTPHIR FGIIGAGSAN SIVSTVHETN DHATSAVHIA
     IGSECNVDVC TVHQHQKLIR ISANAISYGW LGDVLRDSEE YRCLGPIRYQ WSALRTTIRH
     PIYRGMVQFS LSHKENVNPK DQLPPCLEPC PVCMKPQGND KYDYHWHAEF THVICCVIPT
     VTPFTPYGLA PFTGIGDGTL DLALVPRISR FHNMQFMRKV AMYGGKQLYE LDPSLNCYRV
     TKWSYQPDAD QEDPGVWNLD GEILEQPKDE PLHFKLHPQL ISFFGRDAAM VKPTKRSFIK
     KRKSSIVYQ