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
//