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Database: UniProt
Entry: A0A059CVZ5_EUCGR
LinkDB: A0A059CVZ5_EUCGR
Original site: A0A059CVZ5_EUCGR 
ID   A0A059CVZ5_EUCGR        Unreviewed;      1093 AA.
AC   A0A059CVZ5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=EUGRSUZ_C03742 {ECO:0000313|EMBL:KCW82341.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW82341.1};
RN   [1] {ECO:0000313|EMBL:KCW82341.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW82341.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR   EMBL; KK198755; KCW82341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059CVZ5; -.
DR   EnsemblPlants; KCW82341; KCW82341; EUGRSUZ_C03742.
DR   Gramene; KCW82341; KCW82341; EUGRSUZ_C03742.
DR   eggNOG; ENOG502QPYS; Eukaryota.
DR   InParanoid; A0A059CVZ5; -.
DR   OMA; QIGMLRG; -.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27008; OS04G0122200 PROTEIN; 1.
DR   PANTHER; PTHR27008:SF591; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00560; LRR_1; 4.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00365; LRR_SD22; 8.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        751..774
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          811..1057
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         839
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1093 AA;  121023 MW;  70E4CD8E3D3230D1 CRC64;
     MQSKETLFIM EKLIFLAFVD VLLVSLLMFQ LVICSSNFTD QEALLHFKSM MEVDPTNNIK
     GGNWTVEANF CEWIGVVCSN RKQRVTALDL SHMGLQGRLS PYLGNLSLLA SLDLRNNSFY
     GMILIEIGHL RRLKELILEL NQFEGNIPPI LTQCQNLEVM SLATNRLTGG IPREFGAFPK
     LQQLNLSSND LRGQIPSFLG NISTLQVIRL VNTTLTGSIP SALFNRSLTW MLALNKNQFS
     GPLPETLTQC KELIILGLSS NRFQGSIPRD IGSLQKLQKL FIAVNNLTGT IPRTIGNISS
     LHKLDIGSNH IEGVIPSEIG NLVNLQLMDL SKNLLTGKVP QEVFNISSLR SLGLRDNSLS
     GSFPSGRDLS LPNLEGLYLA NNGFGGNIPQ YFSNFSNLIL FNVEDNQLSG PIHEGFGNLK
     NLEVFDIGRN QLTGETYGSE LGFLSALSNC PSLRELGLEG NPLCGSIPTA IKNFSSSLQI
     LIARNCQIRG RIPEEMGFLK RLTFLKLSNN ALDCNIPSSI GGLERLQRLY LDNNHLKGPI
     PNEICNLTSL EELLLRQNRI SGSILNCIEN LRSLQKFLIS LNNMTSVIPV SLWGLQELIF
     LNLSLNSFNG ELPLEIGKMR AIESIDLSWN RLTGAIPSSI QEFESLASLN LSMNSFQGSI
     PQSIGHLKGM DFLDLSYNEL SGTIPESLEG LVYLQNLNLS FNKLSGEIPN GGSFGNFSAL
     SFIGNEALCG NAIFQVPRCK VNGMKSSRDK WLHILYIIVP IVSAILLVLV ICLLRKRGNT
     SKKALVSMEN LPRIDHPMIS YRELCLATSN FSESNLLGAG SFSSVYKGTL ANGIDIAVKV
     LNLHIEGALK SFDAECDAFR MIRHRNLVKV ISTCTNANLR ALVLQYVPYG SLEKWLYSSN
     YNLDLHQRVK IMVDVATAIE YLHHGQPEPI VHCDMKPSNI LLNEDLVAQV CDFGIAKILA
     KNKLETQTRT LGTIGYIAPE YGSEGKVSTK GDVYSFGILL LEVITGKKPT GEMFNADVSL
     RQWVGAAIPE RVLDIMDSKI LRTRHQDPTL LKFHSIVLLI LELGLECSKD LPEERMDMKT
     VVVKLNKIKL SLR
//
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