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Database: UniProt
Entry: A0A452ZIJ8_AEGTS
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ID   A0A452ZIJ8_AEGTS        Unreviewed;      1305 AA.
AC   A0A452ZIJ8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
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:AET1Gv20795900.31, 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:AET1Gv20795900.31}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) to UniProtKB.
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EnsemblPlants; AET1Gv20795900.15; AET1Gv20795900.15; AET1Gv20795900.
DR   EnsemblPlants; AET1Gv20795900.26; AET1Gv20795900.26; AET1Gv20795900.
DR   EnsemblPlants; AET1Gv20795900.27; AET1Gv20795900.27; AET1Gv20795900.
DR   EnsemblPlants; AET1Gv20795900.31; AET1Gv20795900.31; AET1Gv20795900.
DR   EnsemblPlants; AET1Gv20795900.32; AET1Gv20795900.32; AET1Gv20795900.
DR   Gramene; AET1Gv20795900.15; AET1Gv20795900.15; AET1Gv20795900.
DR   Gramene; AET1Gv20795900.26; AET1Gv20795900.26; AET1Gv20795900.
DR   Gramene; AET1Gv20795900.27; AET1Gv20795900.27; AET1Gv20795900.
DR   Gramene; AET1Gv20795900.31; AET1Gv20795900.31; AET1Gv20795900.
DR   Gramene; AET1Gv20795900.32; AET1Gv20795900.32; AET1Gv20795900.
DR   Proteomes; UP000015105; Chromosome 1D.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05171; PIKKc_ATM; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   InterPro; IPR038980; ATM_plant.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR044107; PIKKc_ATM.
DR   PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR   PANTHER; PTHR37079:SF4; SERINE_THREONINE-PROTEIN KINASE ATM; 1.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          188..841
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          949..1261
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          1273..1305
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
FT   REGION          142..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          696..730
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1305 AA;  149018 MW;  9E44F0AFDA95D212 CRC64;
     MVHSRGINTQ LVEQTLLGMD KYSTVPLEDS DIWQTDGQPY EQWLCTLVSS LISHCDDIIL
     RLCRSLVFLK VEAAELLLAS ALVNIAGNMD SNSGICGLIS SKVEKIIFCD SNYMMKSVKL
     FLDALNVVRS FYVTERARAS PYNTRASPSP YNTPKDGSRS ARSKSRSPAA TPSSSWRKVY
     WLSVDYLVAA RAAQRCSCDF ATLMYVELWC EEQFNKLDLG PPDFSQQESL APHIGLLVEA
     FTHINEPDSI YGITLANEVA SQIIRYEHEG NWSSALEYYD LLVRSTPKEN LANFAGTVLT
     GPSVSSKAEE NLLNWKMHKG LMRSLQKTGC SHVLDIYSQG LTNQKACLQQ DSEFVDIQYE
     AAWRAGNWDF SFFVPYSSQP SSRSRDYCLF NENLHSCLRA LQNGDSEQFQ GKLSHSKMDL
     VLALSNASKE STKYIHSTVL KLQMLDHLSM AWELRWKFCP DQAPKSNVGT EEFNLVPAVP
     KRNQLELLSK EWNFILCQTE RNLDLFEPFL AFRRGLLKIL GSEEHLIEHL FQSASALRKG
     LRFSLAAASL YELKELCCHR DQQTVPSTYF LSKLEEAKLL RAQGQHDMAI GLGKYILKNH
     TDERNKSDVY RLVGKWLAET RSSNSRTIIE DYLNHSVALD KKYMSRQCRT HFHLAHYTYN
     LFKSYEERLS SNEWQAALRL RKYKTKELDT LLKRLKNSSK AEKSDYGAKI QELQKQLALD
     REEAQKIQDD RDEFLSLALE GYQRSLVVGG KYDLQVVFRL VSLWFNLFSR KQVVDSMIKT
     TKEVQSYKFI PLVYQIASRL GSSKDAQGST NFQNALASLL KKMAIDHPYH TICQLLALAN
     GDRVKDKQRS RSSFVVDMDK KLAAENLLKE LSSFHGALIR QMKQMVEIYI RLAELETRKE
     DTNKKISLPR EFRSICQLEL AKVPVVTATI PVDPNCRYEE GTFPHFSGLV DSITIMNGIN
     APKVIQCIGS DGNRYRQLAK SGNDDLRQDA VMEQFFSLVN MFLQNHRDTS ERRLRIRTYN
     VVPFTPSAGV VEWVNRTVPL GDYLLDSNRI GGAHARYGTG DWTFLQCREH LACEKDKRKA
     FFKICDNFRP VMHHFFIERF LQPADWFQSR LAYTRSVAAS SMVGYIVGLG DRHSMNILID
     EDTAEVVHID LGVAFEQGLM LKTPERVPFR LTRDIIDGMG VTGTEGVFKR CCEKTLSVMR
     ENKEALLTII EVFIHDPLYK WALSPLKALQ RQKETEYNDS CLDDSQEACE GNKDAARAIL
     RVKQKLDGYE DGEMRSVEGQ VQQLIQDAVD TDRLCQMFPG WAPWL
//
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