LRK10_WHEAT
ID LRK10_WHEAT Reviewed; 636 AA.
AC P93604;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Rust resistance kinase Lr10 {ECO:0000312|EMBL:AAC49629.1};
DE EC=2.7.11.1;
DE AltName: Full=Probable receptor-like serine/threonine-protein kinase LRK10;
DE Flags: Precursor;
GN Name=LRK10 {ECO:0000312|EMBL:AAC49629.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Thatcher; TISSUE=Leaf;
RX PubMed=9025301; DOI=10.1046/j.1365-313x.1997.11010045.x;
RA Feuillet C., Schachermayr G., Keller B.;
RT "Molecular cloning of a new receptor-like kinase gene encoded at the Lr10
RT disease resistance locus of wheat.";
RL Plant J. 11:45-52(1997).
RN [2]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9700067; DOI=10.1023/a:1006062016593;
RA Feuillet C., Reuzeau C., Kjellbom P., Keller B.;
RT "Molecular characterization of a new type of receptor-like kinase (wlrk)
RT gene family in wheat.";
RL Plant Mol. Biol. 37:943-953(1998).
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=2.7.11.1;
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;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9700067};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the aerial parts of the
CC plant. {ECO:0000269|PubMed:9700067}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U51330; AAC49629.1; -; Genomic_DNA.
DR PIR; T06793; T06793.
DR AlphaFoldDB; P93604; -.
DR SMR; P93604; -.
DR STRING; 4565.Traes_1AS_3A3C86D64.1; -.
DR PRIDE; P93604; -.
DR eggNOG; KOG1187; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P93604; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR045874; LRK10-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27009; PTHR27009; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..636
FT /note="Rust resistance kinase Lr10"
FT /id="PRO_5004161889"
FT TOPO_DOM 25..276
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 339..628
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 466
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 345..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 636 AA; 71023 MW; 0F18F3A29BF1DEDC CRC64;
MSKLLVIALL LLPLINHGIY LATAWDDQDF FKYCPPSKCS QHGPMIRYPL CLESSNTSSS
SSCGCAGRSI WKLACSGQDT ILVHPVLGPY SVSAIDYRRS SMKITPLVDP CLVLQQKLII
SRSSSSPQVD VINDEKPSFD ENFFESSSAT IVHCSREFTP AAAHADSIAG PVSCLSNTTH
FFYLVNSDED MSILPLDCKV VPVSDRGGIS LPHMLKDQMF YNFTETAKKI PSFAETAVSW
DEGDCRECEL SGRRCAFSSQ RDREFCMPDP HGSHIKVIAA TSSVAAFVAL LLTVATVLYL
SLKTRYNAEI HMKVEMFLKT YGTSKPTRYT FSEVKKMARR FKEKVGQGGF GSVYKGELPN
GVPVAVKMLE NSTGEGESFI NEVATIGLIH HANIVRLLGF CSEGMRRALI YEFMPNESLE
KYIFSDDSNI FQNLLVPEKL LDIALGIARG MEYLHQGCNQ RILHFDIKPH NILLDYNFNP
KISDFGLAKL CARDQSIVTL TAARGTMGYI APELYSRNFG GVSYKADVYS FGMLVLEMVS
GRRNSDPRIG SQDDVYLPEW IYEKVINGEE LALTLETTQE EKDKVRQLAM VALWCIQWNP
RNRPSMTKVV NMLTGRLQSL QMPPKPFVSS ENELMS
