ID A0A058ZZN8_EUCGR Unreviewed; 838 AA.
AC A0A058ZZN8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Receptor-like serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000641};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000641};
GN ORFNames=EUGRSUZ_K01176 {ECO:0000313|EMBL:KCW47377.1};
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:KCW47377.1};
RN [1] {ECO:0000313|EMBL:KCW47377.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW47377.1};
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 -!- 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 ECO:0000256|PIRNR:PIRNR000641};
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 ECO:0000256|PIRNR:PIRNR000641};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|PIRNR:PIRNR000641}.
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DR EMBL; KK198763; KCW47377.1; -; Genomic_DNA.
DR RefSeq; XP_010038719.1; XM_010040417.2.
DR AlphaFoldDB; A0A058ZZN8; -.
DR EnsemblPlants; KCW47377; KCW47377; EUGRSUZ_K01176.
DR GeneID; 104427305; -.
DR Gramene; KCW47377; KCW47377; EUGRSUZ_K01176.
DR KEGG; egr:104427305; -.
DR eggNOG; ENOG502QUNW; Eukaryota.
DR InParanoid; A0A058ZZN8; -.
DR OMA; ENWIFHE; -.
DR OrthoDB; 344059at2759; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00028; B_lectin; 1.
DR CDD; cd01098; PAN_AP_plant; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.90.10.30; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR47976; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD2-5; 1.
DR PANTHER; PTHR47976:SF30; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS50948; PAN; 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|PIRNR:PIRNR000641};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000641};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000641}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641}.
FT DOMAIN 32..161
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 345..435
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 521..794
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 838 AA; 93343 MW; EFF7C10277C4F207 CRC64;
MDAQAQYDNY APLSSSWYNG EETFGEPSRR DPQITVVRPI LLRNRGVDYD GPAYACGFYC
NGVCNNYLFA VFIVILNGGV FGNINDGFPQ VVWSANRNNP VKNGATVQLT SEGDLVLKDA
DQTVAWSTNT SGKSVIGLNL TDSGNLVLLG ANNAPVWQSF DHPMDSLVLR QKLSIGQKLV
PSVSETNWTA QGLLSLSMTR TGLFAQMDTD PPQVYFLVPA NLPYTSDDSN YIKFVNGTLA
LFTNSTLNDS IFINIPPASL FMRLEYDGHL RAYEFDGHQR QWIVADDLLQ KHGDCGYPTV
CGQYGICSSN GQCTCPDSDG DTNYFKQINN RHRNLWCYRE VPLSCDNSQF QSFLELGDLS
YFTYSADPES TPDLANANMV YCKEACAKNC SCKAAFFLKD RDSPTDSGSC YLLTEVFSLM
NLKLPVKSIF YLKVQNISNV VPKSPGSSRT PSFNNRGRTN RLASILGSSL GSVVALIIVI
GVIKVLCRKR EAVDEAEENH LDRIPGVPMK FTYDSLKVIT KDFSKKLGEG GFGSVFEGTL
QDGSKVAVKR LDGLGHIKKS FSAEVETIGS IHHVNLVMLV GFCTENSRRL LVYEYMPNGS
LDKWIFCRSS EYVLNWQQRR KIIYDIAEGL NYLHEGCRRK IVHLDIKPQN ILLDDNFNAK
VADFGLSKLI DRDKSQVVTT MRGTPGYLAP EWLSAAITEK VDVYSFGVVV LEIVSARKVF
DNSQDSESMY LVGAFRRKVE EGRLSDMVNI HSEDMRVNEV EAVNMLRIAG WCLQGDFTKR
PSMSVVMKVL DGLMDVPDDL EYDFSFPPLL KSRAKVLQEE AHFAPSTLLM PSVLSGPR
//
