ID A0A059CAX8_EUCGR Unreviewed; 795 AA.
AC A0A059CAX8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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_E04143 {ECO:0000313|EMBL:KCW75394.1};
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:KCW75394.1};
RN [1] {ECO:0000313|EMBL:KCW75394.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW75394.1};
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; KCW75394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059CAX8; -.
DR EnsemblPlants; KCW75394; KCW75394; EUGRSUZ_E04143.
DR Gramene; KCW75394; KCW75394; EUGRSUZ_E04143.
DR InParanoid; A0A059CAX8; -.
DR OMA; NRCHAEL; -.
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; 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; 2.
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}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|PIRNR:PIRNR000641}.
FT DOMAIN 27..150
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 339..425
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 479..756
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 795 AA; 89362 MW; 995C6B805A7DFFE8 CRC64;
MALSATGLKG TISDIRSKIP VQCPSTIYRI TASSPLVQNQ TLVSSSQIFE LGFFTPNRSA
KQYLGIWYKN MPSSKKVWVA NRDKPIGHTD KSASLKISND GNLKLLDGQQ NTLWSTHVMA
KSNYSTAFLS DYGNFVLRDR NANNLWESFD EPTDTLLPNM KIGVNTKTGN KRNLISWKGE
NDPSFGSFVV ELTSERPPQL FTRNGSSPYW RSGQWDTTRF IGIPAMDNTY FDVKQDIVQG
TSYYTNNNHN NSIFGYLFIS FEGTLKVDSW TNNRWSTKWN APAPTNPCEI YGKCGPFGVC
NQFSSPICRC LEGFKPISDE EWNRGNWTRG CLRELELNCQ KSASTAASTT VKKDRFWKIT
QMKLPDSADY SSIDDAERCQ SWCLGNCTCL AYSYVNAIGC MAWSKDLLDT LQLSTGGEDL
FIRLVDASAG KFGKMTIPRL FTSEELLRDT AWKEQMKEDD TSKLVFYDFD SIRLATDNFN
VKNKLGQGGF GPVYKGKLND GKEIAAKRLS SSSGQGIAEF KNEILLISKL QHRNLVRLLG
CCIEGEEKIL VYEYLPNKSL DTFLFDSKEK AKLSWSVRFH IIQGVARGLL YLHRDSCLRV
IHRDLKVSNI LLDEKMNPKI SDFGLSRMFE GTQVLVNTHK VVGTLGYMSP EYAMGGIFSE
KSDVYSFGVL LLEIISGKKN TSLDYPGQNL NLLAYAWHLW CEGRGSDLID EGIADAFSVL
EVMRCIQLGL LCTQDHATDR PNMLAVVLML NGESNLSQPK QPTYTFSRSL AHEVPSQEES
IRSMNTITIT TVEGR
//