ID A0A2J5I1Y8_9EURO Unreviewed; 1368 AA.
AC A0A2J5I1Y8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=MAP kinase kinase kinase {ECO:0000256|PIRNR:PIRNR037579};
DE EC=2.7.11.- {ECO:0000256|PIRNR:PIRNR037579};
GN ORFNames=BDW42DRAFT_60164 {ECO:0000313|EMBL:PLN83834.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN83834.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|PIRNR:PIRNR037579};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|PIRNR:PIRNR037579}.
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DR EMBL; KZ559516; PLN83834.1; -; Genomic_DNA.
DR OrthoDB; 1440978at2759; -.
DR Proteomes; UP000235023; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IEA:UniProtKB-UniRule.
DR CDD; cd06626; STKc_MEKK4; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017240; MAPKKK_Ssk2/Ssk22.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF32; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037579; MAPKKK_SSK22; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037579};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR037579};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037579};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR037579};
KW Transferase {ECO:0000256|PIRNR:PIRNR037579}.
FT DOMAIN 1042..1330
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1071
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1368 AA; 154285 MW; 70CD1460FAAF9356 CRC64;
MDSQQDAEFP VMEHPDLNNH DSDGSASSDD LVQPPYVRSN SSFTDAFDTA IVHTPTSTIT
SSPPPSTASA IPSWSSTSAS RPRGSSLGAA ALEKIPLPDG HTVPERELRP QRPSGPARTP
SNTYAPQRRP PQFISLQNDR QRSSSVKRNS RRDPNAQYRA QEKAYVQRIR ADPQAWYSRF
DDAQNMNAVA MGDSDLEEPS PSSEVPFDDD TYDPDTQLFL SDDNQPSFEE LKNPKNQERL
EWHSMLASVL KGDVVKQEKQ RLIGSTETKR SAAQNNEIWL GVRARTCGRS VAMQRKIIEE
ARGALSATVE DIIKFQIKGE TEIGKSPIKQ VEDVVEHIER CERLYPTHSE LETAHPRVAS
EEYCSSRDAI FAWHNTTILI NTELSILQKW VGNAELDFSK PRVKPANSDL SDDSSFLDRI
MKEDGLKTLQ GEHNMLHGIG EVIRKAKNTL IDNAESFARR HLPPYIEELL TLINFPSRLI
QEIIRVRLSY AKNMRDPASQ SPILVDQMIS QFQILMRVAV DIKQRYLDIA KPEPGWDLPP
CIDENFDSVV LDAMKYYFRL LNWKLNANKN TFKEAEILEQ DWEFSNDIGR QLEGGDIEVA
EQFSALTAKS IQRLMIHFER ELATRPNEDP ADMDKRYKSV LDSTRIRQRK LYRFARFLRQ
LFENATEYNL PADIAYEFFE SLLVSDHFLI KSNKSVGQKG VYLFGHHALW DRHAEIQAIL
GTHFREEDTP KDSPHVPYIL VVRPEKPLSW AGKEMLVDIL EQPTDLRLGK LRLVVEGTQQ
RLSNARLEFS QLTGVHLDMA IEQRANLGRV NVELNKINKI SFKLSMTIMD SVAFIREQLT
EKGVENHDLI QACYAFATEF GKRSANVDPN RRAMNSARLV DLSLEWVSFV CDDCDAADRK
TFKWAVSALE FAMAITSSRH LISMHDSQFE YLRQKVAGCM SLLISHFDIM GARSSRAAQA
EKQRMEERAG SRKIGAGRIL TDEEASKLVR EQRLAHLTSI EDQRVEEDAK RQALGKVLES
SNEADRSLTV LSASATNVTL RWQQGQFIGG GTFGSVYAAI NLDSNYLMAV KEIRLQDPQL
IPKIAQQIRD EMGVLEVLDH PNIVSYHGIE VHRDKVYIFM EYCSGGSLAS LLEHGRVEDE
TVIQVYALQL LEGLAYLHQA GIVHRDIKPE NILLDHNGII KYVDFGAAKI IARQGRSVLP
MDAFSSTGNK EAIVPKDNAR GKNQKTMTGT PMYMSPEVIR GDSAKLIHRQ GAVDIWSLGC
VILEMATGRR PWSTLDNEWA IMYNIAQGSQ PALPSRDQLG DLGIDFLRRC FECDPLKRST
AAELLQHEWI VSIRNQVVLD PTTPGSDNSG SSVSSGSRQS SSYGSFTA
//
