ID A0A0K3ATZ5_CAEEL Unreviewed; 1481 AA.
AC A0A0K3ATZ5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN Name=nsy-1 {ECO:0000313|EMBL:CTQ86493.1,
GN ECO:0000313|WormBase:F59A6.1b};
GN ORFNames=CELE_F59A6.1 {ECO:0000313|EMBL:CTQ86493.1}, F59A6.1
GN {ECO:0000313|WormBase:F59A6.1b};
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:CTQ86493.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CTQ86493.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CTQ86493.1,
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=2.7.11.25;
CC Evidence={ECO:0000256|ARBA:ARBA00000478};
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=2.7.11.25; Evidence={ECO:0000256|ARBA:ARBA00000106};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529}.
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; BX284602; CTQ86493.1; -; Genomic_DNA.
DR RefSeq; NP_001300554.1; NM_001313625.1.
DR SMR; A0A0K3ATZ5; -.
DR EPD; A0A0K3ATZ5; -.
DR EnsemblMetazoa; F59A6.1b.1; F59A6.1b.1; WBGene00003822.
DR AGR; WB:WBGene00003822; -.
DR WormBase; F59A6.1b; CE50862; WBGene00003822; nsy-1.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003822; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR ExpressionAtlas; A0A0K3ATZ5; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06624; STKc_ASK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046872; DRHyd-ASK.
DR InterPro; IPR046873; HisK-N-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR043969; MAP3K_PH.
DR InterPro; IPR025136; MAP3K_TRAF-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11584:SF369; APOPTOTIC SIGNAL-REGULATING KINASE 1, ISOFORM C; 1.
DR PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF19039; ASK_PH; 1.
DR Pfam; PF20309; DRHyd-ASK; 1.
DR Pfam; PF20302; HisK-N-like; 1.
DR Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:CTQ86493.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Proteomics identification {ECO:0007829|EPD:A0A0K3ATZ5,
KW ECO:0007829|PeptideAtlas:A0A0K3ATZ5};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:CTQ86493.1}.
FT DOMAIN 650..911
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1264..1291
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 24..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1481 AA; 167566 MW; DA2168F431E6CE3A CRC64;
MSNDVCPLPL PPRGAPPPTA YHASRMAATS SSTNGSFEKS AIPGNARKLH VVIVIDQKVQ
KNLRVREMAL KDVQKVADTL NVNLTRIDFD KLDFGETETL DLFYNADVAL VDVTVTHQQP
SLCYHIGVRE SMGQSYNMIL TYWSPDPEYH IMDALKKTHA HLPMIVYIHH QDSNQLQSYD
KNNNDDDSKP PFARTNVPAK TITFQHRMKQ VLKSVQVEAS AHSREKFMSD LRKAREITDG
DQKNDYLDKM RTRLDNPDVL HPDTVSLMML SYRDNQNYGG MIRLVDDLKR IPDCLKVVDT
PVIRYQYAFA LNRRNKDGDR DLALNTVLSL VEGTTENEEK NGPLSPDVVC LAGRIYKDKF
IASNYEDRES LNSAIEWYRR AFEMSPLEYS GINLTTLLRA SGEHFENNLE MQQIAVVLNS
LLGRKGALQN LMEYWDVATY FEVSVLAENY QKACEAALMM VKLKPPVWYL KSTMENIKLI
NRCAATISPI EKEKQQFLFW SEFFMEATEA DTDISCPRYP VLILELNKEF TPSYLTLNNE
EGTVILSHVL ENSQQKKIHQ SELRGIHRWH FARNNIKAVT ESKRDDRQLF LYVHENSDDF
NLLFPTKAHC KKAYDDMKSM ADVADGNYQG RVLSNPDNEK IRFEYELSNS NERVVLGKGT
YGTVYAARDM DTQRQIVVKE IEVKYDEEVQ PLMEEISLHS TLCHANIVQY LGCDLVGKDG
SNDHFLIFME HVPGGSLSSL LRSKWGPMNE NAMNYYGKQI LEGLKYLHEL KIVHRDIKGD
NVLVNTYSGV CKISDFGTCK RLAGLNPVTE TFTGTLQYMA PEVIDHGQRG YGAPADIWSF
GCTMVEMATG RPPFVEMQNP QAAMFRVGMF KTHPPIPTEI TEKCRNFIKS CFLPEACDRP
SAKDLLQDPF IYHNHHSTRS GSINKKPATK IELNHDKEKK EKSKNQREML RSTSHIGGMG
VVERSPPTPE PMSATLTAGF SHVHSQTVSN ALSTAREEKK LHLKIDHARN RTFSSSSPVP
DGQSSAGTNM SHPGFQLSQP SSPIVDDTNH PHLIVSPISL NTMGSPLSSA ALLNRTISDE
SSNSSSRFFM LQKDSERRRS LGQFMQDYKD LIIDSWSTLL IKQSDTELVV TVYMLEMLLD
GMRDFLLKKD NTKMQKMIDD IRGLLDYDTA KIGQINLALY HFSDSIQPVL RRLDIKPHWM
FALSNLITSA VQCAISILSP DLSLLLHAQD NLPSTSSIVA IRNSSLSEGE ALIESRPPSR
EERVREDRKE LRTLQEENEI LIERLLQVER ELNAQLKSGI TRANRFRDFA MYRNTYPPFR
TPPVAHAPPT PPFSASCGAQ PSGTFTNQPP SFASIKPIAQ KIIMPPGTEN NYQVTRVQEE
LVSWLRGLEI DERSIALIAS EAYTKSDMMD FVTRDELLSI GVGGGSSCRI MRAIGEVRER
QRRQPVFLSP MRSRDDSLDD YHSSSADDMY TGAAAETSSG N
//
