ID A0A059DCH0_EUCGR Unreviewed; 946 AA.
AC A0A059DCH0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=EUGRSUZ_A00805 {ECO:0000313|EMBL:KCW88418.1};
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:KCW88418.1};
RN [1] {ECO:0000313|EMBL:KCW88418.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW88418.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK198753; KCW88418.1; -; Genomic_DNA.
DR RefSeq; XP_018727594.1; XM_018872049.1.
DR AlphaFoldDB; A0A059DCH0; -.
DR EnsemblPlants; KCW88418; KCW88418; EUGRSUZ_A00805.
DR GeneID; 104432933; -.
DR Gramene; KCW88418; KCW88418; EUGRSUZ_A00805.
DR eggNOG; ENOG502QVWS; Eukaryota.
DR InParanoid; A0A059DCH0; -.
DR OMA; CPIQSCP; -.
DR OrthoDB; 1214803at2759; -.
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; IBA:GO_Central.
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; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; IPR025875; Leu-rich_rpt_4.
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; PTHR45974:SF216; OS01G0960400 PROTEIN; 1.
DR PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR Pfam; PF00560; LRR_1; 4.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51450; LRR; 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|SAM:SignalP};
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 SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..946
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001570150"
FT TRANSMEM 553..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 618..891
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 946 AA; 104456 MW; 1654C48A139E21B9 CRC64;
MLKLRVPISA LVLSCCYFAY LVEARVTAPS EVNALIAVKS KLVDPMKHLA NWEKGDPCTS
NWTGVLCNGT VGTDGYLHVY EIQLLNMNLS GSIAPAVAQL SRLQILDFMW NELTGSIPKE
IGSIASLRLL LLNGNKLSGS LPDELGYLSK LNRLQVDENQ ISGPIPKSFA SLSSAKHLHL
NNNTISGQIP AELSNISTLL HLLLDNNNLA GYLPQEFSLL PVLRILQLDN NNFNGEIPAS
YGEFPNLAKL SLQNCSLEGS IPDLSQIPNL RFLDLSHNQL SGPIPSNKLS DNMTTIDLSN
NLLDGSIPAN FSYLPSLQRL SLENNSLTGS VPVNIWQNMT STSRKMLIDL QKNSFSDAVG
DLNPPENVTL RLGGNPVCSK GNTTNISRFC GNESGDDGTP GNSANSTSCP PQSCPTDNFF
EYVPSSPVKC LCASPLRIGY RLKSPSFSYF PPYEYPFEVY LTRSLNLELY QLHIDSYTWE
GPRMRMYLKL FPEVNGPRTF NEIEVQRIKG IFTSWDFPGD DLYGPYELLN FTLLGPYKTM
IFPNQKVNIS KGILVAIVLS SIACVTAISA MITFLVTRRK TRYQPSLSRK NLSSKVSMKL
EGVKAFTFRE MAVATDNFNR STQVGQGGYG KVYKGNLYDN TVVAVKRAEE GSLQGQKEFL
TEIKMLSRLH HRNLVSLVGY CNEEGEQMLV YEFMPNGTLR DWLSGKTKEY LNFSMRLRIA
LGSAKGILYL HTEAHPPVFH RDIKASNILL DSKLTAKVAD FGLSRLAPVL DDEGTVPHHV
STIVKGTPGY LDPEYFLTHK LTDKSDVYSL GVVFLELLTG MQPISHGKNI VREVNMAHRA
GMMFSIIDSR MGSYPSECVE RFVALALLCC YDNPEKRPSM LDVVRELESI LKMMPDGDAI
LSETASVYSG KSLPSSSSYA SMDPYISSSV SGSDLISGVV PTVTPR
//
