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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