ID A0A059CAI8_EUCGR Unreviewed; 837 AA.
AC A0A059CAI8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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_E04137 {ECO:0000313|EMBL:KCW75387.1};
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:KCW75387.1};
RN [1] {ECO:0000313|EMBL:KCW75387.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW75387.1};
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|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|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; KK198757; KCW75387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059CAI8; -.
DR EnsemblPlants; KCW75387; KCW75387; EUGRSUZ_E04137.
DR Gramene; KCW75387; KCW75387; EUGRSUZ_E04137.
DR InParanoid; A0A059CAI8; -.
DR OMA; VANKENP; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR CDD; cd00028; B_lectin; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd01098; PAN_AP_plant; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 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; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR32444:SF240; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF08276; PAN_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00954; S_locus_glycop; 1.
DR PIRSF; PIRSF000641; SRK; 1.
DR SMART; SM00108; B_lectin; 1.
DR SMART; SM00473; PAN_AP; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000641};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|PIRNR:PIRNR000641};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000641};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000641};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|PIRNR:PIRNR000641}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..837
FT /note="Receptor-like serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001569080"
FT DOMAIN 22..145
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 334..420
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 521..798
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 837 AA; 93385 MW; 53A28535085CD435 CRC64;
MTLHLCSLLV ISLLQALQSS TIYSITASSP LVQNQTLVSR SQIFELGFFT PNGSAKQYVG
IWYKNMTPSK VVWVANRDKP IGHTDKSASL IIGNDGNLKL LDGQQNTVWS TNVMAKSNYS
AAHLSDYGNF VLQDRNANIL WESFDEPTDT LLPNMKIGVN VKTGKKRNLI SWKGEDDPSF
GSFVVGMTSE TPPQLFTWNG LSPYWRSGQW DKTRFIGIPA MDGTYFDVQQ DIVQGTSYYI
NNNHNNSIFG YTFISSEGTL NGVLWANNGW LTYWRAPKPN NPCEIYGKCG PFGVCNQISS
PICRCLEGFK PISDEEWNRG NWTRGCLREL ELNCQKSAST AASTTVKKDR FWKITQMKLP
DSADYSLIDD AERCQSWCLE NCTCLAYSFV NAIGCMTWSK DLLDTLQLST GGEELFIRLV
DTSAGVVADT GVPTRTKLII SLSTISGIIL FGASISVCCL SKWRGKLRKM TIPRLFRSVA
AAIRSEKLLR ETASKEQMKE DDASKVVVYD FDSIRLATDN FDAKNKLGQG GFGPVYKGKL
SNGKEIAAKR LSSSSGQGIA EFKNEILLIS KLQHRNLVRL LGSCTEREEK ILVYEYLPNK
SLDAFLFDSE KKAKLSWVVR FRIIEGVARG LLYLHRDSCL RVIHRDLKVS NILLDEKMNP
KISDFGLARM FESSQVLVNT HKVVGTLGYM SPEYAMGGAF SEKSDVYSFG VLLLEIISSK
KNTSLDYPGQ HLNLLAYAWH LWCEGRGLDL MDAAIANAFS ALEVMRCIQV GLLCTQDHAI
DRPNMSAVVL MLNGESELSQ PKQPAYTFQR LLAQQVQSQE GSIRSMNTIS ITTVEGR
//
