ID A0A087YCV0_POEFO Unreviewed; 1371 AA.
AC A0A087YCV0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
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:ENSPFOP00000015853.1, 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:ENSPFOP00000015853.1}
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 -!- 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; AYCK01000200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01000201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 48698.ENSPFOP00000015853; -.
DR Ensembl; ENSPFOT00000015875.1; ENSPFOP00000015853.1; ENSPFOG00000015511.1.
DR eggNOG; KOG4279; Eukaryota.
DR GeneTree; ENSGT00940000159155; -.
DR OMA; DYPKACQ; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0042742; P:defense response to bacterium; IEA:Ensembl.
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:SF332; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 5; 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 3: Inferred from homology;
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:0000256|ARBA:ARBA00022777};
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}; Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 675..933
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1239..1273
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1292..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1371 AA; 154073 MW; 75CB5A14C8E45F99 CRC64;
MMNQDQEGIS FPVPSFGAGP HREAVSGEHS SSNSGGGGGG IPAAGTFWQD PLVGGSGHSP
TSGDSPVETG GLLSAGKSCK SRPVTVAYVV NGEASQQNNA ESMALQCLKD ACDRVGSKLD
TVNFSKLDFG ETTVLDRFYN AALDIAVVEM TDAFRQPSLF YHLGVRESFS MANNIILYCD
TNSESLQSLQ EIICQKNTTC SANYTFIPYM VTPHNKVYCC ESSLMKGLTE LMQPSFEMLL
GPICMPLLDR FIQLLKVSQA NSHQYFRETI LNEIRKAREL YTGVELSAEL SRIQQRLDNV
ECLSVDVVIN LLLTYRDIQD YESIVKLVET LEKLPTFDPM AHPHVKFHYA FALNRRNLPG
DRQKALDIML PLVEGEEQVA SDIYCMVGRI YKDMFLESHF TDTQSRDKGT LWFKKGFESE
PTLHSGINYA VLLLAAGHQF DSSFELRKVG VKLSSLLGKK GSLDKLQSYW DVGFFLGASI
LACDNTRVIQ ASEKLFKLKA PIWYLRSLVE TILIYQHFKK PGSEPPAPRQ ELVDFWMDFL
VESTKKDVSS VRFPVLILEP TKVYQPSYLS INKDVEDNTV SIWHVAPDDK NKGIHEWNFV
ATSVRGVSIS KFDERSAFLY VLHNAEDFQI YFCTEMHCKR FCDLVNSITE EAFKCPDEGD
CDTDALEYDY EYDEHGERVI LGKGTFGVVY AGRDLSNQVR IAIKEIPERD SRYSQPLHEE
IALHKHLKHK NIVQYLGSIS ENGFIKIFME QVPGGSLSAL LRSKWGPLKN NEPTIGFYTR
QILEGLKYLH DNLIAHRDIK GDNVLINTYS GVLKISDFGT SKRLAGINPC TETFTGTLQY
MAPEIIDKGP RGYGKPADIW SLGCTIIEMA TGKPPFYELG EPQAAMFKVG MFKIHPEIPD
TMSPEAKAFI LRCFEPDPDR RSTAVDLLTD EFLTVTSRRK KSRTGLAAPS SGSEYLRSIS
LPVPVVVEDT SSSSEYGSVS PDNDLNTNPF SFKPSVKCYS ERDIKGQRPL FLSIPVENFE
DHSAPPSPDE KDTGFFMLRK DSERRATLNR ILTEDQDKVV GNLMEALTQG SEEMKLKAQH
ISTLVVSLAG FVRVADRKII ATTLSQLKLE LDFDSTAISQ LQVVLFSFQD AVNKVLRNHN
IKPHWMFALD NIIRKAVQTA ITILVPELRP HFSLASESDA ADQDDFDDDV EPVRNSTHQS
RVPAVVAQDD TVATSGVSTL SSTVSHESHN AQRSVNMELG RMKLETNRLL EELLQKEREY
QAILQQVLEE REQEIRLLRM RSEPAEPPTA SESLQDRRRE AGERHEDPEL TGWLRLSGAD
QDAIDRILNE EYTLNDILHY VTRDDLKSLR LRGGVLCKLW KAITDFRQKP A
//