ID A0A453HH09_AEGTS Unreviewed; 965 AA.
AC A0A453HH09;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
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:AET4Gv20189700.1, 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:AET4Gv20189700.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR AlphaFoldDB; A0A453HH09; -.
DR SMR; A0A453HH09; -.
DR STRING; 200361.A0A453HH09; -.
DR EnsemblPlants; AET4Gv20189700.1; AET4Gv20189700.1; AET4Gv20189700.
DR Gramene; AET4Gv20189700.1; AET4Gv20189700.1; AET4Gv20189700.
DR OMA; GELHFLT; -.
DR OrthoDB; 356101at2759; -.
DR Proteomes; UP000015105; Chromosome 4D.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 5.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR48056:SF20; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 4.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51450; LRR; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..965
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019194039"
FT TRANSMEM 606..628
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 668..957
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 697
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 965 AA; 104924 MW; 6803F47DE55F7473 CRC64;
MRIHIIFCLQ LTILLSLSVS STCQTDPQTE ALLQFKASLA DPLNYLQTWT NATSPCQFHG
IQCNAGLVTE ISLSSMNLSG TISPSIAALS GLERLDLDTN SLSGAVPSEL ISCTQLRLLN
LSWNTLTREL PDFSALTELE SLDVANNGFS GRFPAWVGDM TGLVYLSIGC NNYDQGEMPP
SIGNLKNLTY LYLSNCSLRG AIPDSVFELT LLETLDLSLN NLAGEIPRAI GNLKKVWKIE
LYKNSLTGEL PPELGRLAEL REIDVSRNQL SGGIPAAFAK LKNLEVIQLY RNNLSGAIPA
EWAELRSLKS FSVYENRFTG EFPANFGRFS SLESVDISEN GFVGPFPRHF CNGKSLQFLL
ALQNGFSGEV PEEYSECKTL QRFRINKNQL TGSIPERLWG LPAVTIIDVS DNGFTGTISP
LIGEAQNLNQ LWVQNNRLSG TIPAETGRLG QLQKLYLSNN SFSGTIPSQI GNLAQLTALH
LEDNALGGAL PADIGSCSRL VEIDVSRNEL TGPIPASLSL LSSLNSLNIS RNAITGMIPA
QLQALKLSSV DFSANRLTGS VPPGLLVIAG DEAFAGNPGL CVHGWSELGA CNTNDHHRDG
LARKSLVVLP VIVSVMVLLV VGILFVSYRS FKLEEQRRRD LERGDGCDQW KLESFHPPEL
DADEICGVGE ENLVGSGGTG RVYRLQLKDG GGTVAVKRLW KGDAARVMAA EMSILGTIRH
RNVLKLHACL SRGELNFIVY EYMPRGNLYQ ALRREAKGGG GEPELDWPRR CRVALGAAKG
LMYLHHDCTP AVIHRDIKST NILLDEDYEA KIADFGIARV AAGNSEEFSC FAGTHGYLAP
ELAYSLKVTE KTDVYSFGVV LMELVTGRSP IDARFGEGKD IVFWLSSKLG AQRLDDVVDP
RLAASSAKGK EEMLRVLKIA MLCTTKLPAG RPAMRDVVNM LTDACAGSCS PRGNPPVWSC
SKSAR
//
