ID A0A200R3K7_9MAGN Unreviewed; 969 AA.
AC A0A200R3K7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Protein kinase domain {ECO:0000313|EMBL:OVA17292.1};
GN ORFNames=BVC80_1837g90 {ECO:0000313|EMBL:OVA17292.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA17292.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA17292.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA17292.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OVA17292.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MVGT01000438; OVA17292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200R3K7; -.
DR STRING; 56857.A0A200R3K7; -.
DR InParanoid; A0A200R3K7; -.
DR OrthoDB; 384316at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
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; 2.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR48055; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1.
DR PANTHER; PTHR48055:SF57; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 7.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:OVA17292.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:OVA17292.1};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..969
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012035443"
FT TRANSMEM 608..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 686..958
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 715
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 969 AA; 104838 MW; 09807A637A5455B9 CRC64;
MRNLVISLFS VILVLPVLVR SYDPPLNDDV LGLIVFKVDL RDPNSKLISW NEDDDSPCNW
FGVRCNPRNN RVSELVLDGL SLSGKIGRGL LRLQFLRRLS LSKNNFTGSI NPILASMENL
RVMDLSENNL TGSIPDDFFR KCGYLRAVSF ARNKLSGQIP KSLSSCSTLA AVNFSSNQIS
GRLPSEIWSL NGLRSLDLSD NLLEGDIPKG IKGLYNLRAI NLRKNQFTGQ VPDDIGGCSL
LKVIDFSENA LSGSLPDSME KLSMCNFLNL QGNELGGEVP AWIGEMRSLQ TLDLSSNSFT
GSIPDSMGHL QSLKVLNLSE NKFNGVLPES LANCTNLLDL DFSRNSLTGV LPTWIFGLGL
QSVLLSENSL SGKIETPSPS METSYHKLQV LDLSDNGFSG EIPSDIGIFS GLEFLSMSKN
SLLGAVPVSV GELKVVSILD FSDNQLNGSI PSEIGGAVSL KELRLEKNFL AGRIPTQIEK
CSSLTVLILS QNKLVGPIPA TIANLTNLQT VDLSLNSLTG SLPKQLANLP HLLSFNVSHN
HLQGELPAGG FFNTISPSSV SDNPSLCGSV VNRSCPAVLP KPIVLNPNSS SDSSETGSLS
PNLRHKKIIL SISALIAIGA AAVIALGVVA VTVLNLHVRS TSRSAAALAL SGGDDFSRSP
TTDANSGKLV MFSGDPDFSA GAHALLNKDC ELGRGGFGAV YKTVLRDGRP VAIKKLTVSS
LVKSQEDFER EVKKLGKIRH HNLVELEGYY WTPSLQLLIY EFVSGGSLYK QLHEGPGGNI
LSWHERFNII LGTAKSLAHL HQQNIIHYNL KSSNVLIDSN GEPKVGDFGL ARLLPMLDRY
VLSSKIQSAL GYMAPEFACR TVKITEKCDV YGFGVLVLEV VTGKRPVEYM EDDVVVLCDM
VRGALEEGKV EECVDARLQG NFPAEEAIPV MKLGLICTSQ VPSNRPDMGE VVNILELIRC
PSEGQEELE
//