ID A0A6I8TH40_AEDAE Unreviewed; 1480 AA.
AC A0A6I8TH40;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 18-JUN-2025, entry version 20.
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=5570419 {ECO:0000313|EnsemblMetazoa:AAEL008306-PE};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EnsemblMetazoa:AAEL008306-PE, ECO:0000313|Proteomes:UP000008820};
RN [1] {ECO:0000313|EnsemblMetazoa:AAEL008306-PE, ECO:0000313|Proteomes:UP000008820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL008306-PE,
RC ECO:0000313|Proteomes:UP000008820};
RG Aedes aegypti Genome Working Group (AGWG);
RA Matthews B.J.;
RT "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AAEL008306-PE}
RP IDENTIFICATION.
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL008306-PE};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:ARBA00048329};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC Evidence={ECO:0000256|ARBA:ARBA00047559};
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 EnsemblMetazoa; AAEL008306-RE; AAEL008306-PE; AAEL008306.
DR OrthoDB; 275301at2759; -.
DR Proteomes; UP000008820; 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 CDD; cd06624; STKc_ASK; 1.
DR FunFam; 1.10.510.10:FF:000054; Mitogen-activated protein kinase kinase kinase 5; 1.
DR FunFam; 3.30.200.20:FF:000487; Serine/threonine protein kinase, putative; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11584:SF394; APOPTOTIC SIGNAL-REGULATING KINASE 1, ISOFORM C; 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; SSF81901; HCP-like; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008820};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 39..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 230..257
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 42..63
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..992
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1204
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1480 AA; 166163 MW; D69C20B6FC7F1837 CRC64;
MYPSQLHKKP LPSPGINAGS FADSMSNLSD VSSTTAILNN TAGSSVNPSN PANSVSGSQS
GSSRPRMDIA CVIDTTHTQR KAAFEEVKLA CVQVCANLQP LEFEKLDFGE LNTVDSLYSA
DVVVVDLSVW AQQSTLSYHL GVRESFEMKE NIVIYNDADS EATLRMKISC GNYTFVPYRA
VDGAGCVVTN PSKVGYLEEV DSKISLVSKL RKIFQDVEIQ SKAHLREKFL ADLRSLRDQY
AGNVEELQKM LRNMRKRLDD PHVLSKEIVQ TYMLSLRDVQ DYDAMVQLVD DLQTVPNKQH
YINTGNMNYL YAFALNRRNK EGDRDKALKS CTKALEKKEN HFPDMLCLCG RIYKDMFVES
NRTDMGSLKN AITWYRKSFQ IQPNEFAGIN LATLLVIEGK DFSDSELQHI GLTLNNLIGK
KGSLASIKDY WNVATFFEIS VLAENYAKAI QAAECMFRLK PPKWYLKSTI GNITLIDCSR
RKSEESLASI EQQIFQFWME FFIEATNAEP SSTVRFPILI QETQKVLFPS YVSIHMDAEQ
KSIDIVNICQ QHEKDKCRKV HNFNFLASQI KSVSLYKRDE RCAFLYVQQN SDDFQMYFPS
VQCRQQFYDL ILQMTADQNS GFIDLSTETM SDEIKYEYEM DDQARRIMLG RGTYGAVYAA
RDLDTQVKIA VKEVPEKYSH EVQPLHEEIK LHSQLRHRNI VQYWGSKSED NYFKIFMEQV
PGGSLSALLR SKWGPLKDNE ATIAFYSKQI LEGLKYLHEQ KIVHRDIKGD NVLVNTYSGV
VKISDFGTSK RLAGINPVTE TFTGTLQYMA PEVIDQGVRG YGPAADIWSF GCTVVEMATG
KPPFVELGSP QAAMFKVGFY KKHPEIPDEL SPVAKIFIKR CFEVDVDKRA TAAELLEDPF
LSDKHKKMRA SISIPPTTMS AAEFSRSVSM PADRHVSKTL TSQQSSASCN TPSINSEAEN
LAETPSLEIE SIEPPPAGFQ LNRRSSSGGL LSPEVELPTT SSKSPLLAGE ANESDGFYLL
KKDSQRRATL HKVLEHDERK ICQVWMEKIV FDRKEAVDIT QAHLEILIKA LRTYITEQKK
EHLEAAISGL KKNLDFDSTG IDHLHLAMYR FQDAVITVLR SHNIKPHWMF ALDNLVKSAI
QAAIIILSPE LGRNLAGHGH NDDDDEDDDG ENDLNRGDAA RGGIDDDDDD GELSTSGVGT
VNSVTVPKPA KLTRTKMVND QIAALRAENL RLMEDLYESH KMYHGVFKTA LKGQSMNADM
VRALATQLMS VASRQDHNSQ GYASDLAESP VIADEVDSAN NNFLRPTVPT RQSSVRPGLD
RRTPVRVAPF DGVSDSMAAG SQPDTRLDEW LVQHGFNDHV RNTIHFEEFS YEDFIYAMDQ
EDLRRIGLRV GTEVKLWRAI RAHRHRFPQP LWSPSDSRHP ALTPQSYSSS SLVTVLNANG
GSVDEPALKP ISNSNSYDST HSACTTASSE YESCNGFDSS
//
