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Database: UniProt
Entry: A0A059BRE6_EUCGR
LinkDB: A0A059BRE6_EUCGR
Original site: A0A059BRE6_EUCGR 
ID   A0A059BRE6_EUCGR        Unreviewed;       773 AA.
AC   A0A059BRE6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KCW68687.1};
DE   Flags: Fragment;
GN   ORFNames=EUGRSUZ_F02284 {ECO:0000313|EMBL:KCW68687.1};
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:KCW68687.1};
RN   [1] {ECO:0000313|EMBL:KCW68687.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW68687.1};
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; KK198758; KCW68687.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059BRE6; -.
DR   EnsemblPlants; KCW68687; KCW68687; EUGRSUZ_F02284.
DR   Gramene; KCW68687; KCW68687; EUGRSUZ_F02284.
DR   InParanoid; A0A059BRE6; -.
DR   OMA; NILIWCA; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR   CDD; cd00028; B_lectin; 1.
DR   CDD; cd00053; EGF; 1.
DR   CDD; cd01098; PAN_AP_plant; 1.
DR   CDD; cd14066; STKc_IRAK; 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; IPR000742; EGF-like_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR024171; SRK-like_kinase.
DR   PANTHER; PTHR47974; OS07G0415500 PROTEIN; 1.
DR   PANTHER; PTHR47974:SF3; RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00954; S_locus_glycop; 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; PS50026; EGF_3; 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   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..773
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001568544"
FT   DOMAIN          20..154
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          285..320
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          499..773
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         527
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         773
FT                   /evidence="ECO:0000313|EMBL:KCW68687.1"
SQ   SEQUENCE   773 AA;  87315 MW;  8D4F33E56331D712 CRC64;
     MNAIRNSHLF LALSLFLSFS FTSSTRLTLH QGSSLSIGNA DNILTSNDGA FSAGFFPIGP
     NAYCFTIWFS KPSCSIPNCT TVWMANRDEP VNGRFSKLSL RENGDLELID AGGTVVWSTD
     TGSSSRSSTN LQLLNTGNLV LRDDKHATLW QSFDSPTDTL LPEQKLTSNT PLVSSRSKSN
     FSSGYYKLYF DNDNLLHLLF SGQTTSVYWP NPWLNSWQAG RSSYNDSRVA MLDHYGNFIS
     SDNLTFLTAD YGAKIQRRLT VDPDGNLRVY SQADGGKWMV SWQAKSDPCT VHGICGPNSL
     CTYHPSEGRS CICVPGYEWE NLYDWTKGCK PKFNSFCDSK VETEFVELPH SDFYGYDKGF
     FPGYTLEMCK KICLDLCDCL GFQYKFSNCY PKLLLLNGHY APKVNGSIHF KLPKLNVSYD
     IPKIEHATLQ CTAKEIMLPR TYLKRRECGT GVEAIVVLMV WCFLYRTRPE KGGAHIDGYH
     AGLTGFQRFT YDELKKATRN FSEEIGRGSG GVVYKAVLSD CRVTAVKRLN EANQGENEFL
     AEVSTIGNLH HMNLIDMWGY CAEGKHRLLI YEFMEHGSLA ENLFSPTELD WPRRFEIAVG
     SARGLAYLHE ECLEWVLHCD VKPQNILLDS TYQPKVADFG LSKILKREGL NYSSFSKIRG
     TRGYMAPEWI YNFPITSKVD VYSYGIVLLE MVTGRSPSGE HEKIEGSDAQ EIKKFTSWVR
     EKKGLGVPAH TWIEEIVDPR VRGEYDIRKI EILVAVALKC VEEDRDARPT MRQ
//
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