ID A0A087Y5K0_POEFO Unreviewed; 600 AA.
AC A0A087Y5K0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 7 {ECO:0000256|ARBA:ARBA00017660};
DE EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000013303.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000013303.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; AYCK01013645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01013646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01013647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01013648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01013649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01013650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007570652.1; XM_007570590.2.
DR RefSeq; XP_016536450.1; XM_016680964.1.
DR AlphaFoldDB; A0A087Y5K0; -.
DR STRING; 48698.ENSPFOP00000013303; -.
DR Ensembl; ENSPFOT00000013321.2; ENSPFOP00000013303.1; ENSPFOG00000013167.2.
DR GeneID; 103150840; -.
DR KEGG; pfor:103150840; -.
DR CTD; 6885; -.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00940000157785; -.
DR OrthoDB; 653199at2759; -.
DR Proteomes; UP000028760; 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 CDD; cd14058; STKc_TAK1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR049637; MAP3K7.
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; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF038168; MAPKKK7; 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}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 27..282
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 437..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 600 AA; 67182 MW; AF5FEB2E10FC28EB CRC64;
MSQTLPPSDM LETPPGYPFE EINYEDIEVE EVVGRGAFGV VCKAKWKGKD VAIKTIESES
ERKAFIVELR QLSRVNHPNI VKLYGSCKSP VCLVMEYAEG GSLYNVLHGA EPLPYYTASH
AMSWCYQCSQ GVAYLHGMKP KALIHRDLKP PNLLLVAGGT VLKICDFGTA CDIQTHMTNN
KGSAAWMAPE VFEGSNYSEK CDVFSWGIIL WEVITRRKPF DEIGGPAFRI MWAVHNGTRP
PLIKNLPKPI ESLMTRCWSK DPSQRPSMEE IVKIMTHLMK YFPGSDEPLQ YPYQYSDEAQ
SNSANSTVSY MDYTGTSTSN RSDVNMEHSD SQGSNDTIKI TPQFAPHFKP KGDPLRTLPL
SRGGSVESLP ARTQCFASSD SKRMSADLSE LEPTMQITPA ARSQYKPGHR KTASFGTILD
VPKIVVTATC EAQRRRSVQD LPAIGTESSQ GSRSSSRSSS PSVRPPDKSN SRSYFPHDDP
TDTNGSDNSI PMAYLTLDHQ LQPLAPCPNS KESMAVFEQH CKMAQEYLKV QTEIALLIQR
KTELIAELDQ DEKDQQNTSR LVQEHKKLLE ENKSLSTYYQ KCKKQLELIR VQQQKRQGTS
//
