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Database: UniProt
Entry: A0A2U9AX14_SCOMX
LinkDB: A0A2U9AX14_SCOMX
Original site: A0A2U9AX14_SCOMX 
ID   A0A2U9AX14_SCOMX        Unreviewed;      1410 AA.
AC   A0A2U9AX14;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE            EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN   ORFNames=SMAX5B_002535 {ECO:0000313|EMBL:AWO96176.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWO96176.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWO96176.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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; CP026243; AWO96176.1; -; Genomic_DNA.
DR   STRING; 52904.ENSSMAP00000005832; -.
DR   Proteomes; UP000246464; Chromosome 1.
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:0000313|EMBL:AWO96176.1};
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:UP000246464};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:AWO96176.1}.
FT   DOMAIN          718..976
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          979..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1280..1329
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        44..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         747
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1410 AA;  158221 MW;  864ED2AA73593244 CRC64;
     MSCESRGPVA FGFSGRSRTG GRVEWRGATR NVVRGESGGG DAPGELTTTK NQEPNATETT
     RSSPRTCAEL RPRTTGEQTM FTTERRRMSR RMSLHELKRR DPVRVSAGSF WQDSDAVELG
     AGGAGRQLVS PRSRTRDVSV AYIVNEDASV PQTEENLSLK CLKEACADAH AAFKSVSFER
     ISQGTTDILD CFYNAGKYVA VVEMSDSFCQ PSLFYHLGVR ESFSMTNNII LYCYKPDGDL
     QAIKEQCGSY TFIPYVVSPQ GKVFACDASM MTGIKELMQP SFQLEPLLTP LVESLVHLLS
     NVHIQSSEYF RESIRHEIRM ARERFSGQAL SEELGHIQKR LDSVELLTPD IVMNLLLSYR
     DIQDYDAIIN LVETLNHLPM CLVARHPNIQ FHYIFALNRR NRPGDRAKAL EAILPIVESG
     GKVASDVYCL CGRIYKDIFM SSGFTDQSNR DQACYWYGKA FETEPTLHSG INNVVLLMAA
     GHEFDTSIEL RKIGVTLSTL LGRKGSLEKM RDYWDVGFYL GANILVNEHR KVIEASEKLY
     RLKAPIWYVA SIMETYILYR QFSKPPVVRY PKQDTVDFWM ELLLQTCKPT VSTDRCPVLV
     LEPSKVLQPA IVCVSEEDES RTVQLKHVTP LKKGLHQWTF PASAIRGVSA SKIDERSCFL
     YVHYNSDDFQ LCFPSELHCT GFCELVNSLL QQAEDSAIQD LDRQTEGILE YIYETSENCD
     KVVLGKGTYG VVYAGRDLSN QVRIAIKEIP EKDSTYSQPL HEEIALHKRL KHRNIVQYLG
     SVSQDGFIKI FMEEVPGGSL SSLLRSKWGP LKDNEATIIF YTKQILEGLK YLHDNQIVHR
     DIKGDNVLIN TYSGVLKISD FGTSKRLAGI NPCTETFAGT LQYMAPEIID QGPRGYGKPA
     DIWSLGCTII EMATGKPPFH ELGSPQAAMF KVGMFKIHPK VPECMSDEAK GFIMNSFVPN
     PDDRATAAEL LMDAFIRSSP RKRAKAPQES ELQSPLSTDY HRSLSVPISI LVEDTDSYSG
     SIDLSCSLDL RRPHYALRVH EVSESPPSTG GFLPIPEDSP SDMSSPASTE ENIGLFMLRK
     DSERRATLHR VLTDYNGHVI SNIQESVPQY GKGSSLTADH ITKLIGCLRD NIHSPDRKQL
     TSDLLDLRAT LLAATVPLNS LQTVLFSFQD AVKKVLKQQQ VKPHWMFALD NLLRQAVQDA
     ISVLLPELKL QLQSSFEIED STPEEQSADP STPVVYVPDQ LGAPADLQPS SPTCEITPTA
     DPYSPTDLVL NTSCPHSEKL RELRLETKRL LGQLSEKETE YQELLKTSVQ RKQEQIDALR
     KTAVTEEKKQ NPEVKALVRW LKSVPVDQDT IDKLLTHEFT LDCLLHMASR DDLMYCGIKG
     GTLCRIWEAI AVRRKTQLSK HDEDSEDTLL
//
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