YRL5_CAEEL
ID YRL5_CAEEL Reviewed; 363 AA.
AC Q09595;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Putative serine/threonine-protein kinase R03D7.5;
DE EC=2.7.11.1;
GN ORFNames=R03D7.5;
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z46828; CAA86858.2; -; Genomic_DNA.
DR PIR; T23871; T23871.
DR RefSeq; NP_496356.2; NM_063955.2.
DR AlphaFoldDB; Q09595; -.
DR SMR; Q09595; -.
DR STRING; 6239.R03D7.5; -.
DR EPD; Q09595; -.
DR PaxDb; Q09595; -.
DR EnsemblMetazoa; R03D7.5a.1; R03D7.5a.1; WBGene00010991.
DR GeneID; 187536; -.
DR KEGG; cel:CELE_R03D7.5; -.
DR UCSC; R03D7.5; c. elegans.
DR CTD; 187536; -.
DR WormBase; R03D7.5a; CE35899; WBGene00010991; -.
DR eggNOG; KOG0658; Eukaryota.
DR GeneTree; ENSGT00520000055635; -.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; Q09595; -.
DR OMA; FGCEKFT; -.
DR OrthoDB; 957693at2759; -.
DR PhylomeDB; Q09595; -.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-CEL-399956; CRMPs in Sema3A signaling.
DR Reactome; R-CEL-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR PRO; PR:Q09595; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00010991; Expressed in adult organism and 1 other tissue.
DR ExpressionAtlas; Q09595; baseline and differential.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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..363
FT /note="Putative serine/threonine-protein kinase R03D7.5"
FT /id="PRO_0000086843"
FT DOMAIN 20..304
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 311..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 363 AA; 41304 MW; 46719F28D17667A3 CRC64;
MMNGFGIKNN GEFYSVSLQF GAHKLCGSGR FSNVYCGQMI SPIEKEVAVK NVWSDTETRH
LATSEYPEIQ ILSKLFHPAI SNLLYFYSRN ANDKVINCLV LDYLPQDLAR LRDQGVKFDV
LDAKLYTFQL FCAISHLTSK NIVHMDIKPQ NVVMDRMAGR LKLADFGNAR RLETNEKTGS
AYQVTRFYRP PELLFGCEKF TASIDIWSAT CVAFELFANR VLFKGKDTKD QIVLITGVFG
YPTDDDIKSI GVKRPRVARK DARGIETFTS KMLDSEIYDF MKATLKIDPK KRKSAIDVLK
MPLFDILRSS PPKKRSNGVE MPNLASYTEM HHKREPETEV VADIQTTEKA EKESDSTNEE
LED
