ID A0A200R917_9MAGN Unreviewed; 476 AA.
AC A0A200R917;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Protein kinase domain {ECO:0000313|EMBL:OVA19205.1};
GN ORFNames=BVC80_8637g2 {ECO:0000313|EMBL:OVA19205.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA19205.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA19205.1, 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:OVA19205.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
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:OVA19205.1}.
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DR EMBL; MVGT01000216; OVA19205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200R917; -.
DR STRING; 56857.A0A200R917; -.
DR InParanoid; A0A200R917; -.
DR OrthoDB; 393015at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47973; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 3; 1.
DR PANTHER; PTHR47973:SF19; OS11G0470500 PROTEIN; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01657; Stress-antifung; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51473; GNK2; 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, ECO:0000313|EMBL:OVA19205.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 149..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..125
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 210..476
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 476 AA; 52769 MW; C5BD1FDF6CC47EE0 CRC64;
MINLFMRYES NAFFDQTTLL GNKGVCGNKI SSQANAFNSA TDGLLADLVI ATPRIGGFFA
AAKKELISGS NSFVYGVAQC AVTVSEAGCN DCLTVAHNNI QNCPPNADGR AVDAGCFLRY
SDTAFFLDNQ TIDLTPFLRT GGSSSKKKII IGGVVGGAGF IFAMVIFIIL FEVFRRKPKK
AQRGDILGAT ELRGPVTFGY NDLKSATKNF SEENKLGEGG FGDVYKGTLR NGKIVAVKKL
TFIQSSRAKT DFESEVKLIS NVHHRNLVRL LGCCSKSPEL LLVYEYMANS SLDKFLYGDR
RGSLNWKQRF DIIVGIARGL AYLHNEFHAR IIHRDIKSSN ILLDEDFQPK IADFGLARLL
PEDQSHLSTK FAGTLGYTAP EYAIHGQLSE KVDTYSFGVV ILEIISGRKS NDMRLEPVSQ
YLLEWYETIQ PVEQYRDWVN YLSSFTFQML SSTPKVYATY SGGSRNFLQG ERVNID
//
