ID A0A059CYG0_EUCGR Unreviewed; 781 AA.
AC A0A059CYG0;
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};
DE Flags: Fragment;
GN ORFNames=EUGRSUZ_C04350 {ECO:0000313|EMBL:KCW82965.1};
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:KCW82965.1};
RN [1] {ECO:0000313|EMBL:KCW82965.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW82965.1};
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 -!- 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};
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DR EMBL; KK198755; KCW82965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059CYG0; -.
DR STRING; 71139.A0A059CYG0; -.
DR EnsemblPlants; KCW82965; KCW82965; EUGRSUZ_C04350.
DR Gramene; KCW82965; KCW82965; EUGRSUZ_C04350.
DR eggNOG; ENOG502QQEW; Eukaryota.
DR InParanoid; A0A059CYG0; -.
DR OMA; DQTRINC; -.
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; cd00028; B_lectin; 1.
DR CDD; cd01098; PAN_AP_plant; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
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; 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 InterPro; IPR024171; SRK-like_kinase.
DR PANTHER; PTHR47976; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD2-5; 1.
DR PANTHER; PTHR47976:SF47; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF01453; B_lectin; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..781
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001574904"
FT DOMAIN 18..145
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 504..781
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 781
FT /evidence="ECO:0000313|EMBL:KCW82965.1"
SQ SEQUENCE 781 AA; 87252 MW; 02BD5899FBC0975A CRC64;
MASVILGILL VLVPLPLSAE AQTGSNLTLG NSLTVNDRNS SWLSPSGEFA FGFRRMGAGA
HLLAIWFEKI EDKTIVWSAN GDNLAPEGSK VQLTANGGLV LTDPRGRELW SSNLNATGLV
YAAMLDTGNF ILASASHVNL WDSFSRPTDT ILPTQQLDLD AVVRARYSKM NYSNGRFIFT
LQTDGNLVLY ATPTPLVVSD AYWATGTRGN GFRLIFNQSG QVYLTDRNGK LLNKVTSDEV
PTSVFYQRAI LEYDGVFRQY IHPKMANSSS GWAMVWSMVS SPVPSNICTS MNRDTGTGAC
GFNSYCTRGD DQIQRPRCHC LPGYTLLDST NEMNGCRQDF APQSCDESKP ETDQFVLREM
LNTGWPMSNY ERSESQTEHW CRQACLADCF CAVAFFKDRK CWKKRTPLSN GRMDPGVGGK
ALVKVRINNS TSKATGNRQK KSKNLTLMII ESVLLSSCVF VSLLTCVIYR SSRSRDYKFL
QPVQINQATG TRTYTYWELQ EATDGFKEEL GRGAFGAVYK GVLGSEDTNF VAVKVLMAWT
GESEKEFERE VSATGQTNHK NLMQLLGFCN EGQHRLLVYE FMSNGSLADF LFGSSRPSWY
KRVEIACDVA RGLSYLHEEC TRHIIHCDIK PQNILLDGSL TAKISDFGLA KLLMANQTRT
TTGVRGTRGY LAPEWFRNMP ISSKVDVYSF GILLVELICC RKNYELKAEI EAQIVMVDWV
YNCYHNGSVL QLVESDEEAS RDIKMVKRLV MIALWCIQED PALRPTMKKT TQMLEGAVEV
P
//
