ID A0A453NCU0_AEGTS Unreviewed; 1050 AA.
AC A0A453NCU0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:AET6Gv20331500.2, 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:AET6Gv20331500.2}
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; A0A453NCU0; -.
DR SMR; A0A453NCU0; -.
DR STRING; 200361.A0A453NCU0; -.
DR EnsemblPlants; AET6Gv20331500.2; AET6Gv20331500.2; AET6Gv20331500.
DR Gramene; AET6Gv20331500.2; AET6Gv20331500.2; AET6Gv20331500.
DR OrthoDB; 358380at2759; -.
DR Proteomes; UP000015105; Chromosome 6D.
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 CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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:SF29; RECEPTOR-LIKE PROTEIN KINASE HSL1; 1.
DR Pfam; PF00560; LRR_1; 10.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00369; LRR_TYP; 6.
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; 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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW 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}; Signal {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..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..1050
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019348595"
FT TRANSMEM 690..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 773..1050
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 802
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1050 AA; 115131 MW; D60039D5C0EDFF74 CRC64;
MQTLQLPNKT HSKISHIPSL GLALVLLICL AAPTSSCTEQ EKGFLLQFLA GLSQDGGLAA
SWHHGTDCCQ WEGITCRQDR TITDVLLASK GLEGHISGSL GNLTGLQHLN LSHNSLSGGL
PLELVSSSII VLDISFNQLN GTLLELPTST AAWPLKVLNI SSNLFTGQLQ STTWKVMKNL
VTLNASNNSF TGQIPTHFCN TSPSFSVLDL CFNRFSGSIP QGLGGCSKLR ELRAGYNNLS
GTVPDEVFNA TSLEYLSFSN NDLHGVLDGA HILNLRNLST LDLGGNNFGG NIPDSIGQLK
KLEELHLDNN KLSGELPSAL SNCTNLITID LKKNNFNGQL TKVNFSNLPN LKTLDLLENN
FTGTIPETIY SCSNLTALRL TRNHLDGQLS PRIGDLKYLS FLSLAENSFR NITNALRILK
SCRNLTTLLI GGNFRGELMP EDDILDGFQN LQVLAINGCS LLGKIPRWLS KITNLEMLFL
HSNQLTGPIP DWISSLNFLF CLDISNNSLT GEIPTALMDM HMLKSEMTKV HLDPSIFELP
VYTGPSFQYQ YRVPTAFPKS LDLSNNKFTG EIPLNIGQLK GLLSVNLSFN DLTGQIPQSI
CKLTKLQELD LSSNNLTGGI PAALSNLNFL SAFNISHNDL EGPIPSGGQF NTFQNSSFDG
NPKLCGTVLT EKCRPGSTPL VPRKQGDKKA IFAIAFGVFF GGIAILLLLG RLLVSVGMKG
FTGKNRWENN EGNEGTSFYS SSVQTLVAMR MPQGKGEENK LQFTDIVKAT NNFDKENIIG
CGGYGLVYKA ELPDGSKLAI KKLYDEMCLM EREFTAEVDA LSMAQHENLV PLWGYCIQGN
SRFLIYSYME NGSLDDWLHN RDDGASSFLD WPTRLKIAQG ASLGLSYIHD VCEPHIVHRD
IKSSNILLDK EFKAYVADFG LARLILPNKT HVTTELVGTM GYIPPEYGQA WVATLRGDIY
SFGVVLLELL TGSRPVPVLS TSKELVPWVR QMRSEGKQTE VLDPTLRGRG YEEQMLKVLE
TACKCVDNNQ FRRPAITEVV SSLASIEADP
//