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Database: UniProt
Entry: A0A200R5B8_9MAGN
LinkDB: A0A200R5B8_9MAGN
Original site: A0A200R5B8_9MAGN 
ID   A0A200R5B8_9MAGN        Unreviewed;       638 AA.
AC   A0A200R5B8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Protein kinase domain {ECO:0000313|EMBL:OVA17901.1};
GN   ORFNames=BVC80_1835g297 {ECO:0000313|EMBL:OVA17901.1};
OS   Macleaya cordata.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Macleaya.
OX   NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA17901.1, ECO:0000313|Proteomes:UP000195402};
RN   [1] {ECO:0000313|EMBL:OVA17901.1, 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:OVA17901.1};
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:OVA17901.1}.
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DR   EMBL; MVGT01000437; OVA17901.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A200R5B8; -.
DR   STRING; 56857.A0A200R5B8; -.
DR   InParanoid; A0A200R5B8; -.
DR   OrthoDB; 460418at2759; -.
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: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; 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; IPR025287; WAK_GUB.
DR   PANTHER; PTHR46008; LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-LIKE 1.4; 1.
DR   PANTHER; PTHR46008:SF58; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 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:OVA17901.1};
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   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..638
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012125827"
FT   TRANSMEM        279..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          342..620
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         370
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   638 AA;  70739 MW;  9CA9095AF2BC4FE0 CRC64;
     MKIPTIAFLH RCLFFLIFIH LSSSQNTCPN CGSMQVPYPL STSPNCGHPD YTLRCDPHTN
     KLYFDTLNGS SYLVLSIQAS MQRMVVQPSP WMPGRCVTQD MPVSEGLWLN QTLPFNVTSS
     NTIFFFNCSP RLLISPLNCS SASLCHQYLE HSGRVDPNRA HQCVGGLEPC CTFVAGGMPS
     AYKIRLHISG CRAFRSILHL DTEKPASEWE EGLEIQWAPP PEPVCRTQID CSRISTCSNS
     TNKPGVSRCL CIKGYYWEHA LGTCSRNVKH STTRIRLKVG MGVLSFFLLA IALTAITLRN
     SSRFTEQSEL TKAREDMLKA SNGGKSSRMF SLKEVKKATC GFSKDRILGI GGFGEVYKGE
     LQDGTVVAVK SAKVGNIKST NQVLNEVGIL SQVNHKHLVR LLGCCIEAEQ PLMIYEYIPN
     GTLHDHLQGK FSSFLNWKTR LKIALQTAEA LAYLHSSAYT PIYHRDVKST NILLDDDLNA
     KVADFGLSRL ARPGLSHVST CAQGTLGYLD PEYYRNYQLT DKSDVYSYGV VLLELLTSQK
     AIDFSRDEDD VNLAVYVTRL VSNGALMEVV DHQLLGDDPS ASSTLTSMKI FAELALACLR
     EKKAERPSMK DVVEELQCVL AILDQEQVSN AVDVKAVI
//
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