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Database: UniProt
Entry: A0A0N4UXU0_ENTVE
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Original site: A0A0N4UXU0_ENTVE 
ID   A0A0N4UXU0_ENTVE        Unreviewed;       404 AA.
AC   A0A0N4UXU0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE            EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN   ORFNames=EVEC_LOCUS2074 {ECO:0000313|EMBL:VDD86931.1};
OS   Enterobius vermicularis (Human pinworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX   NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000236601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EVEC_0000236601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDD86931.1, ECO:0000313|Proteomes:UP000274131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00006529}.
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DR   EMBL; UXUI01007313; VDD86931.1; -; Genomic_DNA.
DR   STRING; 51028.A0A0N4UXU0; -.
DR   WBParaSite; EVEC_0000236601-mRNA-1; EVEC_0000236601-mRNA-1; EVEC_0000236601.
DR   Proteomes; UP000038041; Unplaced.
DR   Proteomes; UP000274131; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017421; MAP3K7-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR46716; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7; 1.
DR   PANTHER; PTHR46716:SF1; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000274131};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          16..281
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          284..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   404 AA;  45972 MW;  B9731885A366799C CRC64;
     MDTGNEVVPF IQSDLLKSTN HIGRGGFGEV RGARYCGESV AMKILENNSD LCKKQFINEM
     EQLYRLRHPN IIRVIGQCSC DGKLAFVMEL MTDGSVDDII HQHLRLSYKA DHVISWAYQC
     ADAVSFIHNK GLVHRDLKPN NLLLSDGYRI LKLCDFGTVA AIKTLMTNNL GSPSWMAPEN
     GLQYHVKFQV FRSHSYTDKC DVYSFGITLW EMFTRRRPFD NNATAFSILW QASHGHRPPV
     IRDPCPPVIM ELISDCWNGT PEVRPSMKDV LDILSELRKV FPNGKDPLKS DEEECSEDRD
     PIASQNTRLG NEDALYSDQI EACKELYETE NRLVALYKIK HDLIAKLKRM EETAKLIEKK
     ESLLSQLNTA HERICRLKQA APNRAAKQFF FHRANMGKDG SSGS
//
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