ID A0A3B4TUQ9_SERDU Unreviewed; 1323 AA.
AC A0A3B4TUQ9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Mitogen-activated protein kinase kinase kinase 5 {ECO:0000313|Ensembl:ENSSDUP00000010049.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000010049.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000010049.1}
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};
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DR Ensembl; ENSSDUT00000010241.1; ENSSDUP00000010049.1; ENSSDUG00000007290.1.
DR GeneTree; ENSGT00940000159155; -.
DR OMA; ICLAHSK; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; IEA:InterPro.
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; 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 PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
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 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}.
FT DOMAIN 667..925
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1228..1259
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1201..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 696
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1323 AA; 148217 MW; A80D3BFB6F67DBE0 CRC64;
MSQDQDGISL PVPCFSACPG IESLRGESTS SSSGGGGGGG GASGIPAAGS FWQDSVIGSG
GLSPTAGSCP MDGGGLLSTG KSCKNRPVTV AYVVNGEASQ QNNAESMALQ CLKDACDTVG
SKLETVNFSK LDFGETTVLD RFYNADLAVV EMTDAFRQPS LFYHLGVRES FSMANNIILY
CDTNSESLQS LQVTNYTFIP YMVTPHNKVY CCESSLMKGL TELMQPSFEM LLGPICMPLL
DRFIQLLKVS QANSHQYFRE TILNEIRKAR ELYTGMELAA ELSRIQQRLD NVECLSVDIV
INLLLTYRDI QDYESIVKLV ETLEKLPTFD PVAHPHVKFH YAFALNRRNL PGDRQKALDI
MLPLVQDEEQ VASDIYCLVG RIYKDMFLES HFTDTQSRDN GTLWFKKGFE SEPTLHSGIN
YAVLLLAAGH QFDTSFELRK VGVKLSSLLG KKGSLDKLQS YWDVGFFLGA SILACDNTRV
IRASEKLFKL KAPIWYLRSL VETILIYQHF KKPGMEQPAP KQELVDFWMD FLVEATKKDV
SSVRFPVLIL EPTKVYQPSY LSINKDVDDN TVSIWHVAPD DKHKGIHEWN FSATSVRGVS
ISKFDERSAF LYVLHNAEDF QIYFCTEMHC KRFCDLVNSI TEETWKGPEE GDCDTDALEY
DYEYDEHGER VVLGKGTFGV VYAGRDLSNQ VRLAIKEIPE RDSRYSQPLH EEIALHKHLK
HKNIVQYLGS ISENGFIKIF MEQVPGGSLS ALLRSKWGPL KNNEPTIGFY TRQILEGLKY
LHDNQIAHRD IKGDNVLINT YSGVLKISDF GTSKRLAGIN PCTETFTGTL QYMAPEIIDK
GPRGYGKPAD IWSLGCTIIE MATGKPPFYE LGEPQAAMFK VGMFKIHPEI PESMSLEAKA
FILRCFEPDP DRRATAFDLL TDEFLTVTSR KKKSKSTLSP GSEYLRSISL PVPVVVEDTS
SSSEYGSVSP DNDLNTNPFI FKPSVKCYSE RDVKGPRSLF LSIPVENFED HSAPPSPDEK
DSGFFMLRKD SERRATLHHI LTEDRDKVVA NLMEALTQGS EEMKLKPQLI STLVVSLADF
VRMADRKIIA NTLSQLKLEL DFDSSAISQL QVVLFGFQDA VNKVLRNHNI KPHWMFALDN
IIRKAVQTAI TILVPELRPH FSLASESDPA DQEDVDDDTE PEGNSAHQSR APPIAAHDDT
VATSGVSTLS STVSHESHNA QRSVSMELGR MKLETNRLLE QLLEKEREYQ AILQLVLEER
EQEIRLLRLR SEPAGLYSDF ISTLTVGYTS LTCTAATILN EEYTLNDILH DVTRDDLKSL
RLR
//
