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Database: UniProt
Entry: A0A200Q5A5_9MAGN
LinkDB: A0A200Q5A5_9MAGN
Original site: A0A200Q5A5_9MAGN 
ID   A0A200Q5A5_9MAGN        Unreviewed;       813 AA.
AC   A0A200Q5A5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Protein kinase domain {ECO:0000313|EMBL:OVA05680.1};
GN   ORFNames=BVC80_263g9 {ECO:0000313|EMBL:OVA05680.1};
OS   Macleaya cordata.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Macleaya.
OX   NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA05680.1, ECO:0000313|Proteomes:UP000195402};
RN   [1] {ECO:0000313|EMBL:OVA05680.1, 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:OVA05680.1};
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:OVA05680.1}.
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DR   EMBL; MVGT01003032; OVA05680.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A200Q5A5; -.
DR   STRING; 56857.A0A200Q5A5; -.
DR   InParanoid; A0A200Q5A5; -.
DR   OrthoDB; 5473383at2759; -.
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:0030247; F:polysaccharide 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; IPR044652; LRK10L-1.1/1.2/1.3/1.4/1.5.
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   InterPro; IPR032872; WAK_assoc_C.
DR   InterPro; IPR025287; WAK_GUB.
DR   PANTHER; PTHR46008; LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-LIKE 1.4; 1.
DR   PANTHER; PTHR46008:SF47; LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-LIKE 1.4 ISOFORM X1; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF14380; WAK_assoc; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OVA05680.1};
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   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          371..651
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         399
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   813 AA;  90178 MW;  0F67C334C1161BE9 CRC64;
     MHPQYQYRHQ LLSSFPPLIF IFLLIFLIHI NNLMIIFSSA QDDHERYKSC SRPFECGDFT
     ASYPFWGQDR PEYCGHPDFK LDCIKNIPSI NDTASQRYSI LSMNNETQIL NIALMDILEG
     ICPAQSSSSS SSSNFISNFP LLEFTSASQN LTLLYGCTLN LQSLMQGAVF NFTCSVNRVP
     RDLYITGFVG PITPGIESMG NCNKDSVVVP VLKTAAAEFW RNPSNEGVGG VVRKGFEVRW
     IMDDTPCRRC VHSGGQCGYT DPSNPFICFC SNGRRSETSC PPSGSAASPP TSISAGFVVI
     LLLCSSFLIY RRRRSNKLLL ISSSSPILLS KNTSSSKTNS KINMDYEKGS SNFSGVQIFT
     YTELQEATNN FDASKELGDG GFGTVYYGIL KDGRQVAVKR LFENNYKRVE QFMNEVEILT
     MLRHQNLVTL YGSTSHNSRE LLLVYEFIAN GTVADHLHGA RAKPGQLNWP SRMNIAMESA
     SALTYLHASD IIHRDVKTTN ILLDKYFGVK VADFGLSRLF PTNVTHVSTA PQGTPGYVDP
     EYYQCYQLTD KSDVYSFGVV LIELISSKPA VDTNRHRYEI NLASMAINKI RNGELHEMVD
     PNLGFETDQV VRRMIISVAE LAFRCLQQQR EMRPSMVEVL EVLKGIKSEV YTVENAEVVD
     IPADDIGLLD DIPMISPDST TTTSKDTITL EQAKSAIFSD EKFEEAEEKH DKSLGLFVQG
     GKKSGSGGAV GRAVGAGRVD RAGGAIARVA KEWKPVMKST KVAEKEILKK EDVAQTYAVF
     EICKLKDDDD VIVDDDAHVI PKMESNLGVT QCG
//
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