ID A0A452QXS9_URSAM Unreviewed; 1282 AA.
AC A0A452QXS9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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|Ensembl:ENSUAMP00000010574.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000010574.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000010574.1}
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};
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 Ensembl; ENSUAMT00000011886.1; ENSUAMP00000010574.1; ENSUAMG00000008678.1.
DR GeneTree; ENSGT00940000159398; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
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: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; 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:ARBA00022527};
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:UP000291022};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 636..894
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 888..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1156..1183
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 927..946
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1282 AA; 142164 MW; 485765A24DE92C0B CRC64;
SAPPTPPYRL VQAAGGSWRF GWGQGGRSYR PLSVVYVLTR EPQPGVEDEA GAEAEPLPLR
CLREACAQLP GPRPRPQLCT LPFGTLALGD TAALDSFYNA DVVVLEVSSS LAQPSLFYHL
GVRESFSMTN NVLLCSQADL PDLQALREDV FQKNSDCVGS YTLIPYVVTA TGRVLCGDAG
LLRGLADGLV QAGVGTEALL TPLVGRLARL LETTPTDSCG YFRETIRQDI RRARERFCGQ
QLRQELARLQ RRLDSVELLS PDIIMNLLLS YRDVQDYSAI IELVETLQAL PTCDVAEQHN
VCFHYTFALN RRNRPGDREK ALAVLLPLVQ SEGSVAPDLY CMCGRVYKDM FFSSGFQDAG
YREQAYHWYR KAFDVEPSLH SGINAAVLLI AAGQRFEDSE ELRLIGMKLG CLLARKGCVE
KMQYYWDVGF YLGAQILAND LTQVALAAEQ LYKLNAPIWY LVSMMETFLL YQHFRPTLEL
PEGPPHRAHF WLHFLLQSCQ PLKTACTQGD QCLVLVLEMN KVLLPARLEI QGTDPVSAVT
LSLLAEPESQ DVPSSWTFPV ASICGVSSSK RDERCCFLYA LPPAQDVQLC FPSVGHCQWF
CGLIQALVTN PDSTAPAEEA EGVGEVLEFD YEYAETGERL VLGKGTYGVV YAGRERHTRV
RIAIKEIPER DSRFSQPLHE EIALHKRLRH KNIVRYLGSA SQGGYLKIFM EEVPGGSLSS
LLRSVWGPLQ DNESTISFYT RQILQGLGYL HDNRIVHRDI KGDNVLINTF SGLLKISDFG
TSKRLAGITP CTETFTGTLQ YMAPEIIDQG PRGYGKAADI WSLGCTVIEM ATGRPPFHEL
GSPQAAMFQV GMYKVHPPMP TSLSAEAQAF LLRTFEPDPR LRASAQALLG DPFLQPGKRS
RSPGSPRHAL RPTDAPSASP TPSADPTTQP QTFPRPQAPF QHPPSPPKRC LSYGDTSQLR
VPEEPGAEEP TSPEESSGLS LLHQESKRRA MLAAVLEQER RALADGLCPK QEQGPHLGRN
HVEQLLRCLG AHIHTPNRRR LAQELRALQG QLRAQGLGPA LLHGPLFAFP DAVKQILRRR
QIRPHWMFVL DSLLSRAVRV ALAVLGPEVE TEEVPPRSEE SSKEEEPHSK QQETLVQLSR
LPGEPEQAPP PPVVQLGLLR AETDRLRDVL AEKERECQAL VQQALQRVNG EARTCTLATE
PPAALTVDQG LVQWLQELNV DSGTIQMLLN HSFNLRTLLT CATRDDLIYT RIRGGMVCRI
WRAILAQRAG PTAITSGRQE AE
//
