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Database: UniProt
Entry: A0A3B3DA99_ORYME
LinkDB: A0A3B3DA99_ORYME
Original site: A0A3B3DA99_ORYME 
ID   A0A3B3DA99_ORYME        Unreviewed;       419 AA.
AC   A0A3B3DA99;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=mitogen-activated protein kinase kinase {ECO:0000256|ARBA:ARBA00038999};
DE            EC=2.7.12.2 {ECO:0000256|ARBA:ARBA00038999};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000026816.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000026816.1}
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=2.7.12.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00036883};
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=2.7.12.2; Evidence={ECO:0000256|ARBA:ARBA00036524};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00035978};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00038035}.
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DR   AlphaFoldDB; A0A3B3DA99; -.
DR   Ensembl; ENSOMET00000003558.1; ENSOMEP00000026816.1; ENSOMEG00000008936.1.
DR   GeneTree; ENSGT00940000157505; -.
DR   OMA; ANDCTQV; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06619; PKc_MKK5; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48013:SF26; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 5; 1.
DR   PANTHER; PTHR48013; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 5-RELATED; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51745; PB1; 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|RuleBase:RU000304};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|RuleBase:RU000304}.
FT   DOMAIN          1..81
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   DOMAIN          138..391
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   419 AA;  46961 MW;  A12955B28B5F95C4 CRC64;
     MDSSVDSPSL LNFNDLMVAI RDVMPEATVT AFEYEDEVGD RITVRSDEEL KAMLSYYLNT
     VNEQRMNGLL PDPLQIFPRA GKTPGIRNIH GLKVNTRSNP ASDCTHAASD SIANNSLKKS
     SAELKKILTN GQINAQDIHY QELLGHGNGG TVYKAYHVLG KRVLAVKVIP LDITVELQKQ
     IMSELEILYK CDSPYIITFF SAFFVENRIS ICTEFMDGGS LDVYKKIPEH VLGRIAVAVV
     KGLTYLWSLK ILHRDVKPSN MLVNTRGQVK LCDFGVSTQL VNSIAKTYVG TNAYMAPERI
     SGEQYGIHAD VWSVGISFME LALGMFPYPQ IQKNQGSLIP LQLLQCIVDE DPPVLPIGEF
     TEMFVHFITL CMQRNPKERP APNNLMDHPF IIQFNDGNAE VVSMWVCRCL EERRAQQAQ
//
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