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Database: UniProt
Entry: A0A3B3HZB6_ORYLA
LinkDB: A0A3B3HZB6_ORYLA
Original site: A0A3B3HZB6_ORYLA 
ID   A0A3B3HZB6_ORYLA        Unreviewed;      1275 AA.
AC   A0A3B3HZB6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE            EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN   Name=si:ch211-1i11.3 {ECO:0000313|Ensembl:ENSORLP00000036931.1};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000036931.1, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000036931.1, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000036931.1,
RC   ECO:0000313|Proteomes:UP000001038};
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA   Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA   Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA   Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA   Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA   Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome evolution.";
RL   Nature 447:714-719(2007).
RN   [2] {ECO:0000313|Ensembl:ENSORLP00000036931.1}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000036931.1};
RG   Ensembl;
RL   Submitted (NOV-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   AlphaFoldDB; A0A3B3HZB6; -.
DR   Ensembl; ENSORLT00000045928.1; ENSORLP00000036931.1; ENSORLG00000014582.2.
DR   GeneTree; ENSGT00940000159398; -.
DR   Proteomes; UP000001038; Chromosome 16.
DR   Bgee; ENSORLG00000014582; Expressed in animal zygote and 12 other cell types or tissues.
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: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:SF391; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 6; 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:ARBA00022527};
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:UP000001038};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          577..835
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          902..927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1139..1166
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         606
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1275 AA;  144300 MW;  BF7523EDE8C3236D CRC64;
     MTLRCRSWAP AAARTEENLS LKCLKEACAD AHATLKTFSF ETVSLGTTDI LDSFYNADVA
     VVQMSDTFCQ PSLFYHLGVR ESFCMTNNII LYCYKQDGDL QALKEQCGSY TFIPYMVSPQ
     GKLIAWDSTI MTCIKEWMQP SLKLEPLLTP LVERLVHLLN NVHIQSSEYF RESIRHEIRI
     ARERFSGPAL SEELGRIQQR LDSVDLLTPD IILNLLLSYR DIQDYDAMIK LVETLNNLPM
     CMVARHQNIK FHYIFALNRR NHPGDRAKAL QEILPIVESG NNVASDVYCL CGRIYKDMFM
     SSMFTDVPSR DRACFWYGKA FEMEPTLHSG INSVVLLMAA GHEFETSIEL RKIGVTISTL
     LGRKGSLEKM THYWDVGFYL GANILVKEYR KVIEASEKLY RLKAPVWFVC SLMETYILYR
     QFAKLPETRS PKQDTVDFWM ELLLQSSKPT ISTDCYPVLI LEPSKLFQPA IVSVSKEDES
     RTVHLKHVTS VKKGLHQWTF PASAIRGVSA SKIDERSCFL YVHYNSDDFQ LCFPSETHCK
     SFCELVNSLI QLAENPSQNR EHLSGGVLEF VYETNENGDK VVLGKGTYGV VYAGRDLSNQ
     VRIAIKEIPE KDSTYSQPLH EEIALHKRLK HRNIVQYLGS VSQDGFIKIF MEEVPGGSLS
     SLLRSKWGPL KDNEPTIIFY TKQVLEGLKY LHDNQIVHRD IKGDNVLINT YSGVLKISDF
     GTSKRLAGIN PCTETFAGTL QYMAPEIIDQ GPRGYGKPAD IWSLGCTIIE MATGKTPFHE
     LGSPQAAMFK VGMFKIHPKV PECMSDEAKG FIMSCFEPNP DNRATAAELL MDTFLKSPGK
     KKLKVLQKLE SDDSINSADY QRSLSVPISI LVEDTDSYSG SVDMPSSLDL RKHKSVFQAN
     EISESPPSTS GFLLKPNGSS VDMSSPASSE ENIGLFMLRK DSERRATLHR ILTDSLNHVV
     SNIQQSLPQC DDRCLTADHI IKLVTCLRDN IRSPNRQQLT RGLLELRSTL LASGIPVNNL
     QVVLFNFQDA VKKVLKQQQV KPHWMFALDN LLRQAVQDAI TVLLPELKIQ LQSSFEFEDT
     PLEGQPADPD TPVVLAPDQL GEPADTLRAA TKKENLLTVD LSSPTHIILD GNCTLSEKLR
     DLRIETRRLL SQLSEKEQEY QMLLRNSMRR KRQHIDALRK ETVAEDKELA SRKNSKPETK
     ALVRWLKSIQ VDQDTIDKLL AHEFTLDCLL FMACREDLGY CGLRGGMLCR LWAAITAHRK
     THLSTHNEMC EDTLL
//
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