ID A0A6I9Y249_9SAUR Unreviewed; 1279 AA.
AC A0A6I9Y249;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
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=MAP3K6 {ECO:0000313|RefSeq:XP_013921092.1};
OS Thamnophis sirtalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Natricinae; Thamnophis.
OX NCBI_TaxID=35019 {ECO:0000313|Proteomes:UP000504617, ECO:0000313|RefSeq:XP_013921092.1};
RN [1] {ECO:0000313|RefSeq:XP_013921092.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) 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 RefSeq; XP_013921092.1; XM_014065617.1.
DR AlphaFoldDB; A0A6I9Y249; -.
DR GeneID; 106548273; -.
DR KEGG; tsr:106548273; -.
DR CTD; 9064; -.
DR OrthoDB; 275301at2759; -.
DR Proteomes; UP000504617; Unplaced.
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:0033554; P:cellular response to stress; IEA:TreeGrafter.
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:000067; Mitogen-activated protein kinase kinase kinase 5; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_013921092.1};
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:UP000504617};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 594..852
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 857..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1145..1179
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1077..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1279 AA; 144446 MW; 1EDE6E9C7606AD16 CRC64;
MEATDSKLGS AGSLWQDTLA MALTPSKPLS PAGSQGCREG GGGGRTRALR VVYVSTEDLE
KPLPFLCLQE ACREFPGTEL ATVPFGTLML GVTDSLDRFY NADVVVVEMS NSLCQPSLFY
HLGVRESFSM TNNILLCCYT DLPELQALRD VIFQKNSDSN GSYTFIPYVV TNQKKVFCCD
VGTMMCLTEL YQSNFNMEAV FNPLTAQLAK LLEGTSVSSS GYFREMIRSD IRKAREMYHG
EQLSRELTSI LQRLDSVECL SLDIVMNFLL SYRDAQDCDA IITLVETLQT LPTCSVAEQH
NICFHYAFAL DRRNQPGDRE KALSVLLPLV EKPEGVAPDL YCMCGRIYKD MFIDSGFTDP
EKRDKAFFWY HKAFLTEPSL HAGINSVVLL IAAGHSFEAS MQLRQIGMKV SCVLGRKGSL
EKMQHYWDVG FYFGASILTG DFDKIIQASE KLYKLNAPVW YVVVTFHLVK VGERDVLILD
LSKVLQPSQL SVCNEEIRKS VTLSYIGSLE EEGISTWTFP ASSIRGISIS KCDERCCFLY
VRHTVEDFQL YFPTQNHCRW FFELVHSFMA EMGEEGNWCS SPVELEYDYE YTEAGDRVVL
GKGTYGVVYA GRDRSNQVRI AIKEIPERDS RYSQPLHEEI ALHKRLKHRN IVRYLGSVSQ
NGFLKIFMEE VPGGSLSSLL RSMWGPLKDN EPTIVFYTKQ ILEGLRYLHD NQIIHRDIKG
DNVLINTYSG VLKISDFGTS KRLAGISPST ETFTGTLQYM APEIIDQGPR GYGKPADIWS
LGCTIIEMAT GRPPFFELGS PQAAMFKVGM FKIHPEVPSS MSDEAKDFIL KCFEADPDKR
STAAALLQEP FLRNRKKCRS PAVPDEPSVS HKPRRSTSSE GIAESRNRSS SLHSLKVQVE
NIVLSRSASE VNQGNNYLRT PEAVTNVDLN LSASSHEESS CLFLLKKDSE RRATLHKVLT
EELPNIAAAI YEAQEEKVLS LAHISELVSC LKSYIRSPSR KQLAQSLLQL QDHFQSDGLS
FCQVQAPLFA FQDTVKHMLR KLQIKPHWVF ALDNLMGQAV QATFTVLLEE LKVQPQNLQE
ESQNHPGTRE HEEPLLTEQP PSLKKHESDL KDSADTPTSG IGTDTNSWLD SQPPFKSHLP
LMTQLNHLQE ETRRLQWKLV EKQQECQRLL QEALKIMEQD SWALRRPQII EIPPSPTSWD
QEENAGDPHL AEWLEKQGAD KATVSVFCYH GFTLNDLLKL ATIDDLRYTC IRGGMVCRIW
KAIMDHRQNL SQQQLHQQP
//
