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Database: UniProt
Entry: A0A200Q0W5_9MAGN
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ID   A0A200Q0W5_9MAGN        Unreviewed;      2097 AA.
AC   A0A200Q0W5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=BVC80_8671g3 {ECO:0000313|EMBL:OVA04103.1};
OS   Macleaya cordata.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Macleaya.
OX   NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA04103.1, ECO:0000313|Proteomes:UP000195402};
RN   [1] {ECO:0000313|EMBL:OVA04103.1, 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:OVA04103.1};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:OVA04103.1}.
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DR   EMBL; MVGT01003398; OVA04103.1; -; Genomic_DNA.
DR   STRING; 56857.A0A200Q0W5; -.
DR   InParanoid; A0A200Q0W5; -.
DR   OrthoDB; 501776at2759; -.
DR   Proteomes; UP000195402; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR   CDD; cd00028; B_lectin; 2.
DR   CDD; cd01098; PAN_AP_plant; 2.
DR   CDD; cd14066; STKc_IRAK; 3.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 3.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR021820; S-locus_recpt_kinase_C.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR32444:SF158; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF01453; B_lectin; 3.
DR   Pfam; PF11883; DUF3403; 2.
DR   Pfam; PF08276; PAN_2; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 3.
DR   Pfam; PF00954; S_locus_glycop; 3.
DR   SMART; SM00108; B_lectin; 2.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00473; PAN_AP; 2.
DR   SMART; SM00220; S_TKc; 3.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 3.
DR   PROSITE; PS50927; BULB_LECTIN; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50948; PAN; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 3.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Kinase {ECO:0000313|EMBL:OVA04103.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW   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        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        428..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1696..1721
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..148
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          341..415
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          496..776
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          929..965
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          994..1274
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1309..1429
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          1623..1698
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          1777..2057
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1732..1753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2097 AA;  235473 MW;  B81AEF2F2B5DF1AE CRC64;
     MEDLPFFIFC YTFTVSVLLD ISFAVDAITQ NHSISDVGRQ TLVSSGGSFE LGFFSPGSSK
     SRYLGLWYKN IPSPVVWVAN RNNPITDSSG VLKIGSDGNI VLVNGTENVV WSSNSSIPTL
     VNPIALLLDS GNLVLRDERS SNSDTHIWQS FDYPCDTLLP GMKHGWSLKE NKNWSLSSWK
     SIDDPSPGDF IYSVDHVGLP QFVLRKGSEI QFRSGNYDGA RFGGDPEIKI TPVFKPKFVF
     NPNEVYYTFE DIYPTITRFV LNQSGSIDHL KWNDESREWI PLITLHRDNC DNYAACGANA
     ACNINDTPMC HCLKGFTPKS PQESIAFDLS AGCIRSSPLN CSKGEGFEKF TRMKLPDKSE
     VLNTSNRCDR ECLARCSCTA YAVTAVTSCA VWFGDLVDIR EYIKGGATDL YIRMAANELD
     SNSKKMKIII VSVVLGTFLL GSISWFIIWK KRRANRGVAG IHISNQDRDY TDKSQEEDLE
     LHIFDFATIA AATNNFSFAN KIGEGGFGPV YKGQLSTGQE IAVKTLAKDS GQGINEFKNE
     VMLIAKLQHR NLVRILGCCI QGEDRMLIYE YMPNKSLDTF IFDKTRGISL NWRERFDIIV
     GIARGLLYLH QDSRLRIVHR DLKASNILLD GNMNPKISDF GAAKTFIGDQ TEANTKRVVG
     TYGYMSPEYA IDGLFSMKSD VFSYGVIVLE IVSGKKNRGF YHPDHDLNLL GHVWKLWNEG
     KALELMDEKM ETPVPLPMSE VLRCIHVGLL CVQQRPVDRP TMSSVVLMLG SDTATLPQPK
     QPGFSTESYL WQSFDYPCDT LLPGMKLGWS SKETRNWSLS SWKNADDPSP GDFTYGIDPG
     GLPQIVLRKG SKIQFRSGNY DGVQFGGEPE LKITRAFKPI FIFKRDEVYY TFEDINPAIT
     RFVLSPTGSP DHFKWNDGSR VWVTIFTSHR DNCDTYAACG AHGICNIIDS RMCKCLKGFT
     PKSPQEDYTD EGQEEDLELH IFGFATIEAA TNNFAFANKI GEGGFGPVYK GQLSMGQEIA
     VKRLAKDSGQ GITAFKSEVM LIAKLQHRNL VRLLGCCIQG EERMLIYEYM PNKSLDAFIF
     DKRKDISLNW RKRFDIIVGI ARGLLYLHQD SRLRIIHRDL KASNILLDSD MNPKISDFGA
     AKTFRGDQTE ANTKRVVGTY GYMSPEYAID GLFSMKSDIF SFGVVVLEIV SGKKNRGFYH
     PDHDLNLLGH VWKLWNEGKA LELMDAKMET PFPLPMSEVL RCIHVGLLCV QQRPEDRPTM
     SSVVLMLASD TATLPKPKQP GFSTERFLTD LESSSCDTGN ELTVTAFEVD TIAPDQSIRG
     NQTLVSAGGS FELGFFTPGN SRNQYLGMWF KVMPSTVVWV ANRNEPITDS SGVLKISTDG
     NIVLLNGTED VVWSSNSSRR VVNPVAQLLE TGNLVLRDES SSNSDSYTWQ SFDYPCDTLL
     PGMKIGWSLK AVRNWSLSSW KNSDDPSPGD FTYSVDPRGL PQLVLRKGSE IQFRSGPWDD
     GTRFGEDAER QNSIFKPMVV FNKDEVYYIF ENKQKSTISR FLVNQSGTIQ HFRWNDVRHE
     WVPMITLHRD NCDNYAACGA YGACNIIESP NCKCLKGFTP KSPQEWNVND PSAGCIRRST
     LGCKKGEGFV KFTRVKLPDK SQILNTSTEC ERECLTRCSC MAYAKIDVIS NCAVWLGDDL
     IDIREYSEDS SDKKKLVLTI TLVSVVFVIF LLGSISWFII WKKRTAKGEG KKINNQDRDY
     HSQEINQERD HTDESREEDL ELHIFEFLTI AAATNNFSFA NKIGEGGFGP VYKGQLLMGQ
     EIAVKRLAKD SGQGINEFKN EVMLIAKLQH RNLVRLLGCC IQGEERMLIY EYMPNKSLDT
     FIFDKTRGIS LNWGKRLDII MGIARGVLYL HQDSRLRIVH RDLKASNILL DGDMNPKISD
     FGAAKTFIGD QTEANTKRVV GTYGYMSPEY AIDGLFSIKS DVFSFGVLVL EIVSGKKNRG
     FYHPDHDLNL LGHVWKLWNE GKASELMDEN METPVPLPLS EVLRCIHVGL LCVQQRPENR
     PTMSSVVLML GSDTATLPQP KQPGFSTERF LIDNESSSSE KKLYTGNEIT LTTLEGR
//
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