ID A0A453CQF8_AEGTS Unreviewed; 711 AA.
AC A0A453CQF8;
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=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:AET2Gv20923800.51, 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:AET2Gv20923800.51}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A453CQF8; -.
DR EnsemblPlants; AET2Gv20923800.51; AET2Gv20923800.51; AET2Gv20923800.
DR Gramene; AET2Gv20923800.51; AET2Gv20923800.51; AET2Gv20923800.
DR Proteomes; UP000015105; Chromosome 2D.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR021720; Malectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48006; LEUCINE-RICH REPEAT-CONTAINING PROTEIN DDB_G0281931-RELATED; 1.
DR PANTHER; PTHR48006:SF65; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF11721; Malectin; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 307..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 365..645
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 660..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 711 AA; 77335 MW; 42289881BF8BFDD7 CRC64;
MPQSIFDLPM LSYLFLGNNS LSGSLPATKS PLLANLDFSY NHLSGSFPSW VSQKNLQLNL
VANDFVIDSS NNSVLPFGLN CLQRNTPCSL GSPQSSSLAV DCGGSRTISG SDNAMYQADN
ANLGAASHYV GGAPIWGVSS SGRFMDPPNG SYIIYSSRQF QNTLDSGLFQ TARMSPSSLR
YYGIGLENGN YTVTLQFAEF DSPDPQAWKS RARRVFDIYL QGERREQNFD IRKAAGGKSF
VVVKKQYVVP VVKNFLEIHL FWAGKGTCCI PTQGYYGPAI SALSATPNFI PTVHYSVDKK
SSSKTGVIVG VVIGVAVCLL AALAGVFVWR QKRKKMLLEL EELYTIVGRP NVFSYSELRS
ATENFDSSNL LGAGGYGSVY KGKLSDGRVV AVKQLSESSN QGKVQFATEI ETISRVQHRN
LVKLYGCCLE SKTPLLVYEC LENGSLDHAL FGKGGLNLDW PRRFEICLGI ARGIAYLHEE
SSVRIVHRDI KASNVLLDAD LNPKISDFGL AKLYDDKKTH VSTKVAGTFG YLAPEYAMRG
HMTEKIDVFA FGVVALEIVA GESNHHTTLE EETTYIFEKV WDLYENGNPL DFVDPKLLKF
NSEEVLRVIR VALICTQGSP HRRPSMSRVV SMLTGDADMA GEEVIKPSYI TEWQVKAGSS
SSYTGTSSQA GLSSSSTTQQ SSGGGHAAGG DATPATGNPS PIFTSIIDEG R
//
