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Database: UniProt
Entry: W6RQW7_CAEEL
LinkDB: W6RQW7_CAEEL
Original site: W6RQW7_CAEEL 
ID   W6RQW7_CAEEL            Unreviewed;       927 AA.
AC   W6RQW7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=dapk-1 {ECO:0000313|EMBL:CDM63494.1,
GN   ECO:0000313|WormBase:K12C11.4d};
GN   ORFNames=CELE_K12C11.4 {ECO:0000313|EMBL:CDM63494.1}, K12C11.4
GN   {ECO:0000313|WormBase:K12C11.4d};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CDM63494.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CDM63494.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CDM63494.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
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         Evidence={ECO:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; BX284601; CDM63494.1; -; Genomic_DNA.
DR   RefSeq; NP_001293417.1; NM_001306488.1.
DR   AlphaFoldDB; W6RQW7; -.
DR   SMR; W6RQW7; -.
DR   PeptideAtlas; W6RQW7; -.
DR   EnsemblMetazoa; K12C11.4d.1; K12C11.4d.1; WBGene00003400.
DR   GeneID; 187322; -.
DR   AGR; WB:WBGene00003400; -.
DR   WormBase; K12C11.4d; CE49601; WBGene00003400; dapk-1.
DR   OrthoDB; 4580305at2759; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00003400; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR   ExpressionAtlas; W6RQW7; baseline and differential.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR   GO; GO:0009605; P:response to external stimulus; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd08782; Death_DAPK1; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020859; ROC_dom.
DR   PANTHER; PTHR24342:SF14; DEATH-ASSOCIATED PROTEIN KINASE DAPK-1; 1.
DR   PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00531; Death; 1.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00005; DEATH; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 3.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   1: Evidence at protein level;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDM63494.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:W6RQW7};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:CDM63494.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDM63494.1}.
FT   REPEAT          170..202
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          203..235
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          236..268
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          269..301
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          341..596
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   DOMAIN          821..891
FT                   /note="Death"
FT                   /evidence="ECO:0000259|PROSITE:PS50017"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..52
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   927 AA;  103132 MW;  4DBB2D94D574D785 CRC64;
     MYREMSARES ARNQTTESAL KEFVEQRDRF PSDSEEDDDS EEEEEEEEEE GLPVTKSLDF
     KKLNLCQASS NTQTSFDDQY DEDSDQSDTD NTIVVMPGSV LSSYLSDPLT NPSASYLFES
     PRPRAADFVY PGQDRYSKLG SVPAYSSTTA FIQLLNDISE THPDLCECAR EETPLHVAAA
     RGHVDCVQAL LDANSPIDAV EQDGKTALII ALENGNVDIA SILITNGCDI NHADHHGDTA
     LHIASKHGLL QAVQTLCHCA VTVDSVNANK KTALHLAAHY GHVDIIRVLL LARADVTLRG
     DDGLTAELVA VAAERLEAHS LLKMVKSQEI REEYISQLYP LDTSLRRIKL KLLGHSQSGK
     TRLVQTLHSS RGISSFLESV TRRISDHYSP SSSMKDDGIH STNGSFVSES NNNSSFDLAA
     AAGSKYAPPH SQYTRGIDVQ TVNINGCGEF SVWEFGGYEP MHTCYDHFVG NADCIHLILY
     RTSDPTEVQY KQILYWMNFL KGRVTPFEPI GHCGFSSRRS KVIIVGTHAT SSLFPQMNQE
     GEYVSSDIEA MLNTVRLRFE THFDMDHRLI LLDATNPSCI GMKTLKMELA KCRTNILAKL
     LKPLAILDTV VNHLNLVRKK HANFPVITWP DFIQLVRNEI NPLTGDAHCR QIVQQLQLIG
     EPAKDTQLHQ WSECSKLVSQ DREAVIRMVG DAVEIRARGP SESATSMFYF MEDLINLVEH
     AAAEVGPGIS LERHFISPKH LKEHREHPAL FPPESMMEMQ QRESLSVKGT QDEEELFTDV
     VCFGSRDVAR HLTLGIDVGV ADLQMASRCE LACLLDPPHA MGRDWSILAV KLQLTDQVPD
     VDSTGQSLSR TDQLLNEWAI HHPEQASVGN LCRILVELGR CDARDALYRT VPLYVFAPLE
     DQFLLETNDS GVVSSCHSSS EHNPINI
//
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