ID   M3XVZ9_MUSPF            Unreviewed;      1124 AA.
AC   M3XVZ9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE            EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000003249.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000003249.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
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; AEYP01047676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01047677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M3XVZ9; -.
DR   STRING; 9669.ENSMPUP00000003249; -.
DR   Ensembl; ENSMPUT00000003314.1; ENSMPUP00000003249.1; ENSMPUG00000003281.1.
DR   eggNOG; KOG4279; Eukaryota.
DR   GeneTree; ENSGT00940000159562; -.
DR   HOGENOM; CLU_003687_1_0_1; -.
DR   InParanoid; M3XVZ9; -.
DR   OMA; MQPNWDS; -.
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: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; 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:SF363; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 15; 1.
DR   PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF19039; ASK_PH; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          444..700
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          710..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          928..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          956..975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          983..1014
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         473
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1124 AA;  127412 MW;  4FD6AFEC29A6A270 CRC64;
     MQPNWDTILG PLCVPLVDRF ISLLKDIHVT SCAYYKETLL NDIRKAREKY QGDELAKELA
     RIRLRLDNTE VLTADIIVNL LLSYRDIQDY DAMVKLVETL EMLPTCDLAD QHNIKFHYAF
     ALNRRNSPGD REKALQVVLQ ILQSCDHPAP DMFCLCGRIY KDIFLDSDCK DDTSRDNAIE
     WYRKGFELQS SLYSGINLAV LLMVAGQQFE TSMELRKIGV RLNSLLGRKG SLEKMNNYWD
     VGQFFSVSML ASDVGKAVQA AERLFRLKPP AWYLRSLVQN LLLIQRFKKP AIEHSPRQER
     LNFWLDMIFE ATNEVTNGLR FPVLVIEPTK VYQPSYVSLN SEAEEKTVSL WHVSPTEMKQ
     IHEWNFTASS IRGISISKFD ERCCFLYVHD NSDDFQIYFS TEDQCSRFCS LVKEMISNSA
     GSTVELEGDT DGDTLEYEYD HDVNGDRVVL GKGTYGIVFA GRDLSNQVRI AIKEIPERDS
     RYSQPLHEEI ALHKYLKHRN IVQYLGSVSE DGYIKIFMEQ VPGGSLSALL RSKWGPVKEP
     TIKFYTRQIL EGLKYLHENQ IVHRDIKGDN VLVNTYSGVV KISDFGTSKR LAGVNPCTGT
     FAGTLQYMAP EIIDQGPRGY GAPADIWSLG CTIIEMATSR PPFHELGEPQ AAMFKVGMFK
     IHPEIPEALS PDARAFILSC FEPDPHKRAT AAELLQAGFL RQVNKGKKNR IAFKPAESPR
     GTALALPMPG EPMGSSSSEH GSVSPDSDAQ LDIFFEKARA SKHRLSHLLS VPDESSASSP
     EDRDPGLFLL RKDSERRAIL YKILWEEQNQ VASYLQECVA QSSEDLHLSV GHIKQIIGIL
     RDFIRSPEHR VMASTISKLK ADLDFDSSSI SQIHLVLFGF QDAVNKILRN HLIRPHWMFA
     MDNIIRRAVQ VAVTILIPEL RAHFEPALET EGVDKDTDEA EEDYPQADLP GRQAHVAFRG
     SSPPSAGAPQ PQQLQHQHLS LQLGELRQET NRLLEHLVQK EREYQNLLRQ TLEQKTRELY
     HLQLQFRPTD TTENPASPPG SQGQSTDPEL VDWLQLQGAD ESTIEKIVEE GYTLSDILNN
     ITKEDLRHLR LRGGLLCRLW TAVTQYRRRA QGSPTSQDEA EPVG
//