ID A0A200PSL9_9MAGN Unreviewed; 583 AA.
AC A0A200PSL9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Protein kinase domain {ECO:0000313|EMBL:OVA01219.1};
GN ORFNames=BVC80_1649g13 {ECO:0000313|EMBL:OVA01219.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA01219.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA01219.1, 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:OVA01219.1};
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:OVA01219.1}.
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DR EMBL; MVGT01004153; OVA01219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200PSL9; -.
DR STRING; 56857.A0A200PSL9; -.
DR InParanoid; A0A200PSL9; -.
DR OrthoDB; 452324at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45927; LYSM-DOMAIN RECEPTOR-LIKE KINASE-RELATED; 1.
DR PANTHER; PTHR45927:SF15; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OVA01219.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:OVA01219.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..583
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012555308"
FT TRANSMEM 217..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 281..568
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 583 AA; 65524 MW; A14D32D5C5EB7789 CRC64;
MNIQHLFLSS LLLLLLHHLH AQPNITGYTC SPNPSIYPCQ TYVSYRAMAP YFLDLANISD
LFSVSRLMIT NPSNISSPTS PLVPDQSLLI PITCSCNSNY NLSYSNLTYT IKQDDTFYLV
STNHFQNLTT YQSVQLVNPT LTPTLLEIGF QVIFPIFYTL SSIAAKFGSN PQLLIDINGE
KISPFDTVFV PVSRIPNITQ PSVVLPVPSK STERKGVVVG LAIGLGVSGF LLILLILVMG
FRFYKEYWRK NEEEEKEKQH QFRRAKSLNE ENLMADVSDC LDKYRVYGIQ DLREATAGFS
QSSLIQGSVY KGCIGGEFYA IKRMKWNACE ELKILQKVNH GNLVKLEGFS IDPKDGNCYL
VYEYVENGSL YSWLHEDNGV KKKLDWKTRL RIAIDVANGL QYIHEHTRPT VVHKDIKTSN
ILLDGNMRAK IANFGLAKSG CNAITMNIVG TQGYIAPEYL EDGIVTTKMD VFAFGVVLLE
IISGKEAIDE EGKALWTDVN RVLEGREDEK YERLKNWMDL ALVGESCTLE SVRNVLAVAI
ACLQREPSRR PNMVDVVYTL CKSDDLYLDF SEDGLSVTPV SAR
//
