ID A0A453HH69_AEGTS Unreviewed; 1460 AA.
AC A0A453HH69;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, 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};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET4Gv20192700.8, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET4Gv20192700.8}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) 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 -!- SIMILARITY: Belongs to the disease resistance NB-LRR family.
CC {ECO:0000256|ARBA:ARBA00008894}.
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 EnsemblPlants; AET4Gv20192700.8; AET4Gv20192700.8; AET4Gv20192700.
DR Gramene; AET4Gv20192700.8; AET4Gv20192700.8; AET4Gv20192700.
DR Proteomes; UP000015105; Chromosome 4D.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR Gene3D; 1.20.5.4130; -; 1.
DR Gene3D; 1.10.8.430; Helical domain of apoptotic protease-activating factors; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR041118; Rx_N.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF5; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 5; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18052; Rx_N; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Plant defense {ECO:0000256|ARBA:ARBA00022821};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1139..1397
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1031..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1460 AA; 163163 MW; 5CD8EDE27F039800 CRC64;
MSSSLLTTSA MEAPMSSSLG AMGPLLRKLH SLLAPDHRLP KPLKHGIELL KEDLEELSAD
LLEQSMADTP NHKAVYWMDE VRELSYEVED CIDDMMLRHA GDGVKTRAVR SHRVSRVKVY
RLFKSLKPST RVSKITELRT LVLEASERRE RYHLDDCASR SSPVFTRHNP VPGLYGQATD
FLVGIDDLKI KLTKWLTEDA DQQLKVMCID GPAGVGKTTL AKQLYCELGE QFDCWAFVRA
SRTSDTKRLL GDILSQVQHC RLPSYSCEVQ NLIDNLTKYL QDKRYFIVID DLWETTWDIV
KSAFPDGNNY SRIITTAETD GVALECCGSQ SDNILKMKPL GSHASAELFF SIVCGSEHRC
PDQLKEVSYR FIGKCGGLPL ATICIAGLLA SQTDNSELWH HLQKCLCSNL STSPTLEEML
KEVLNLSYSC LPHYLKTCLL YLAMYPEGFT MWKVDLLKQW ISEGFITAKE EKEVEEIADS
YFYELVNKGM IQPEQINHND EVLSCTLHHT VRDLIMYKSK EENFITSIDY SKAITGNSNM
VRRLSLHFSS AKYATKPSGV ILSQSRSLFF FGLLRCLPSD VEFKLLRVLI LDFWGNQYGH
TSLNLTRICS LVHLRYLKIS CDIIVELPAQ MRGLQYMETL EINARLSAVP LDIIHLPSLL
HLSLRDETNL PDGIGRIRSL RTLQYFDLGN NTEDNVLSLG GLMNLQYLHL TYSTVQSDEH
LKRNMVALAS SVIKLVNLKS VILAPGALST AIYHDVLSSV YSPPVFLQGL QKLDLLPPIC
MFSSFPKDIG AVRKLCYLNL VVRELRRNDI DSITGLPALT VLSLYVRQPP AESIIFNNGA
FPALKYFKYM CGVLCLAFQE GALPNVHRLK LGFNARKGQQ YDVLLAGIQH LVNLKKIDGI
IGAAEGAEEP DRSAAESAFK DTIHKHSRFP SYVNVKRVDW VEEENEPRTE VNSSSSKCHE
ILQEQRGVNE TEEDTKQFAD SGVTNQIMQM SPQHMDLCAA DTKLTMPSNN RMSFPEKLHD
NIAAEAVSFS CTTSSGSSPK SSSAPSSHHS LPETYTWDPE GSPWSRALSP PTPRNTSAPQ
SAMHPMLSPE DHISRAEGTW STAYFHPLPL PPSAISQVKA TLSNQPAPKV EMSLVAGQWE
KRKLIGSGTF GDVYEATNRH TGALCAVKAI SIPNDSRSAE SLKQLDQEIK LLSQFKHENI
VQYYGSETIE GHLYIYMEYV HLGSINKYIQ QHCGAITESI VGNFTHHILR GLAFLHGQNI
MHRDIKGANM LIDGNGVVKL ADFGTAKHLS TAAPNLSLKG TPYWMAPEMI RATLVKDVGY
DLAVDIWSLG CTIIEMFNGK PPWSGLEGPA AMFKVLNKDP PLPDNLSHEA KDFLKCCFKR
NPAARPSARE LLTHPFIRNS SHYSKHVQEV IIAGCEEVIR ASCDPSLTRK TTTSGGNDAR
SSESLVSQLT LQPVQHGRKF
//
