GenomeNet

Database: UniProt
Entry: A0A087YHH3_POEFO
LinkDB: A0A087YHH3_POEFO
Original site: A0A087YHH3_POEFO 
ID   A0A087YHH3_POEFO        Unreviewed;       859 AA.
AC   A0A087YHH3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase kinase 1 {ECO:0000256|PIRNR:PIRNR038172};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038172};
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:ENSPFOP00000017476.2, 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:ENSPFOP00000017476.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: May play a role in the response to environmental stress.
CC       Appears to act upstream of the JUN N-terminal pathway.
CC       {ECO:0000256|PIRNR:PIRNR038172}.
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=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433,
CC         ECO:0000256|PIRNR:PIRNR038172};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC         ECO:0000256|PIRNR:PIRNR038172};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRNR:PIRNR038172};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily. {ECO:0000256|ARBA:ARBA00008874,
CC       ECO:0000256|PIRNR:PIRNR038172}.
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; AYCK01004936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AYCK01004937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007552530.1; XM_007552468.2.
DR   AlphaFoldDB; A0A087YHH3; -.
DR   STRING; 48698.ENSPFOP00000017476; -.
DR   Ensembl; ENSPFOT00000017498.2; ENSPFOP00000017476.2; ENSPFOG00000017317.2.
DR   GeneID; 103138324; -.
DR   KEGG; pfor:103138324; -.
DR   CTD; 11184; -.
DR   eggNOG; KOG0576; Eukaryota.
DR   GeneTree; ENSGT00940000160308; -.
DR   OMA; IQVFWKH; -.
DR   OrthoDB; 152877at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IEA:InterPro.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06613; STKc_MAP4K3_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR021160; MAPKKKK.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR48012:SF15; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 1; 1.
DR   PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF038172; MAPKKKK; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR038172};
KW   Kinase {ECO:0000256|PIRNR:PIRNR038172};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR038172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038172};
KW   Transferase {ECO:0000256|PIRNR:PIRNR038172}.
FT   DOMAIN          26..283
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          527..829
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          331..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..437
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        146
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038172-1"
FT   BINDING         32..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038172-2"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038172-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   859 AA;  96944 MW;  B96EA5D1D3D0037A CRC64;
     MSQHIRMDFH QRAALDISTK NPQDDFEILL RVGGGTYGEV YKARNKQNGE LAAIKVIKME
     PEDDFSIIQQ EIVIVKSCKH PNIVAYYGSY IRANKLWICM EFCGGGSLQD IYHVTGSLSE
     PQIAYVCREM LQGLDYLHAQ KKIHRDIKGA NILLNDQGEV KLADFGISAQ ITATLARRMS
     FIGTPYWMAP EVAAVEIKGG YNELCDVWSV GITAIELAEL QPPLFDVHPL RVLFLMSKSG
     YQPPKLKDKS KWSSNFYNFV KAMLVRNPKK RPSAAKMLSH PFLTQQCLNQ ELTLDLLDKF
     KNPEKHKSCV STEDDDMEVA PPASLRRIQS INKHNRAERT NSDISFEQIY TQRPMKTGSP
     NVTLTPSSGS TGSINSPSRD QDSDSDDYDD VDIPTMQPSG LIMPEDETPP PLPPKPKART
     SSEESMASED DRSRKHGSLC PPAPAPLIRT SSGTHVRPTP HPRASRHSDP PSLPTQIQNI
     PADTVPPELP PKDFRRRKPI SKDLPECPSP VLKKPPVYFK KIFHGCPLKI NCSTTWENPT
     SKEQHLIMGA EEGIYTLNLN GSEATMELLY PGKCSWVYTI NNVLMSVSGK SSQLHSHSLK
     ELYEQARKDQ RMVPLPTHRL LSRKCPVTSK IPDTKGCKTC AVGGNLFLCC ALDSSVVLLQ
     WYEPMHKFML IKHFDFPLPS PLRVFEMVVP PLQEYPMVCI GVSRSCSPST PVNVEYINLN
     SNTSWFFNSG MEKPCPDVVQ VNQLDGNSLL VLMERSVQVV NLEGELKTNR HPPQETIFSH
     DVESIVYFED TLLAVWRHGW QRRTKSFTEV LDEMTDHRKI YRMVKSDRMV VLETRQVEDQ
     LGLSNLYLLE VAENYVLLP
//
DBGET integrated database retrieval system