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Database: UniProt
Entry: A0A087YCV0_POEFO
LinkDB: A0A087YCV0_POEFO
Original site: A0A087YCV0_POEFO 
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
//
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