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Database: UniProt
Entry: A0A443Q3I2_9MAGN
LinkDB: A0A443Q3I2_9MAGN
Original site: A0A443Q3I2_9MAGN 
ID   A0A443Q3I2_9MAGN        Unreviewed;      1262 AA.
AC   A0A443Q3I2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=CKAN_02701200 {ECO:0000313|EMBL:RWR97570.1};
OS   Cinnamomum micranthum f. kanehirae.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX   NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR97570.1, ECO:0000313|Proteomes:UP000283530};
RN   [1] {ECO:0000313|EMBL:RWR97570.1, ECO:0000313|Proteomes:UP000283530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:RWR97570.1};
RX   PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA   Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA   Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA   Leebens-Mack J.H., Tsai I.J.;
RT   "Stout camphor tree genome fills gaps in understanding of flowering plant
RT   genome evolution.";
RL   Nat. Plants 5:63-73(2019).
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   -!- 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:RWR97570.1}.
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DR   EMBL; QPKB01000014; RWR97570.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443Q3I2; -.
DR   STRING; 337451.A0A443Q3I2; -.
DR   Proteomes; UP000283530; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd12087; TM_EGFR-like; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 5.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR   PANTHER; PTHR48005:SF70; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 10.
DR   Pfam; PF13855; LRR_8; 4.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00365; LRR_SD22; 11.
DR   SMART; SM00369; LRR_TYP; 14.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52047; RNI-like; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|EMBL:RWR97570.1};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000313|EMBL:RWR97570.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283530};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:RWR97570.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1262
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019499814"
FT   TRANSMEM        946..971
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1012..1250
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         1040
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1262 AA;  138788 MW;  3A3FA67DB32ED3FF CRC64;
     MAERKKSSLS LLVLSFALLQ LLLFLNVRAI APAPVTQEAA EAQALLTWKA SLENHSLLNS
     WSLLNNSNAT FTESKRNSTC NWLGITCNVA GRITRINLFN ASLRGKLDNL RFSSFSELTI
     LNLSSNALHG TIPAHIGTLT KLNILDLSMN QFFGYLPLSL GNLTKLTTLY IHTNKISGSI
     PQEIGYLKNL INLELSTNLL TGTIPPTLGN LTKLTTLYIH RNNISGSIPQ EIVYLKNLID
     LEMSYNLLTG SIPSTLGNLT KLSTLYIGKN KLSGYIPQEM GNLKNLTDLE MSFNLLTSSI
     PPTLGNLTKL NILYIHNNKI SGPIPREIGY LKNLIDLELS TNLLTGTIPP TLGNLTQLTT
     LYIHENNISG IIPQEVGYLR NLVELAMYKN FLTGSIPPTI GNLTKLTTLY IYENNISGSI
     PQEIGHLKNL IDLELSTNLL IGTIPPTLGN LTKLTTMYID TNNISGSIPQ EIGHLKNLID
     LELSTNLLTG IIPPTLGNLT KLTTLYIHEN NISGSIPQEI GHLKNLIDLE LSINLLTGTI
     PPTLGNLTKL TTLYIHKDNI SGSIPQEIGH LKNLVDLRMS TNLLIGSIPS TIGKLKNLIV
     FAILKNQLSG PIPPELTNLT HLTELYLDEN NFSGHLPENI CHGGSLKKFT ASSNHLIGPI
     PKSLQNCTTL IRVRLENNHL TGNTSKVFGH YPNLIYMDLS YNDLYGELSP KWGECQSLQK
     LQLSGNKIIG KIPPEFGKLS QLKVIGLSSN NLAGEIPKEI GRLSALYSLS LNDNELSGSV
     PLEIGLLSDL EVLDLSMNNL SSHIPEELMS CFKLWSLHMS RNKFSGRIPS QIGNLAMLQS
     LDLSQNSLSK EIPSQLGSLK MLENLNLSHN MLSGHIPPSF EEISSLTSID ISYNNLEGPI
     PRNKAFQQAP FEALSHNKGL CGNASSLQPC NSTFIDKGHL KKVSKVVIII TLSISGLIFL
     LLACIVIFFF LKRRARHTAI ELEEMRHGDA FSIWDFDGRI VYDDIIQATE NFDSNYCIGV
     GGYGSVYKTE LSTGQVVAVK RLHPMEGGST RDQKSFNNEI KALTEIRHRN IVKLVNVVKG
     VASGLSYMHH DCSPPIVHRD ISSNNILLDS ELQACISDFG TSRLLKPDSS NWSSLAGTYG
     YVAPELAYTM EVTEKCDVYS FGVLTFEVLM GKHPGDLIHT LHFSTGQNIL LKDVLDQRLS
     PPSAQTADEV ISVAVVALAC IRANPHSRPN MRNVSQKLSS QRLCTSEPFQ TITLCQLNDL
     DI
//
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