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Database: UniProt
Entry: A0A059BVV1_EUCGR
LinkDB: A0A059BVV1_EUCGR
Original site: A0A059BVV1_EUCGR 
ID   A0A059BVV1_EUCGR        Unreviewed;       826 AA.
AC   A0A059BVV1;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-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_F03370 {ECO:0000313|EMBL:KCW70066.1};
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:KCW70066.1, ECO:0000313|Proteomes:UP000030711};
RN   [1] {ECO:0000313|Proteomes:UP000030711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BRASUZ1 {ECO:0000313|Proteomes:UP000030711};
RX   PubMed=24919147; DOI=10.1038/nature13308;
RA   Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA   Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA   Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA   van der Merwe K., Singh P., van Jaarsveld I., Silva-Junior O.B.,
RA   Togawa R.C., Pappas M.R., Faria D.A., Sansaloni C.P., Petroli C.D.,
RA   Yang X., Ranjan P., Tschaplinski T.J., Ye C.Y., Li T., Sterck L.,
RA   Vanneste K., Murat F., Soler M., Clemente H.S., Saidi N., Cassan-Wang H.,
RA   Dunand C., Hefer C.A., Bornberg-Bauer E., Kersting A.R., Vining K.,
RA   Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.E., Liston A.,
RA   Spatafora J.W., Dharmwardhana P., Raja R., Sullivan C., Romanel E.,
RA   Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA   Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA   Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA   Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA   Grima-Pettenati J., Salse J., Van de Peer Y., Rokhsar D.S., Schmutz J.;
RT   "The genome of Eucalyptus grandis.";
RL   Nature 510:356-362(2014).
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}.
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; KCW70066.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059BVV1; -.
DR   EnsemblPlants; KCW70066; KCW70066; EUGRSUZ_F03370.
DR   Gramene; KCW70066; KCW70066; EUGRSUZ_F03370.
DR   Proteomes; UP000030711; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR   Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 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; IPR000742; EGF-like_dom.
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:SF183; S-LOCUS LECTIN KINASE FAMILY PROTEIN; 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; PS50026; EGF_3; 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   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000641}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000641};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030711};
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|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000641};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..826
FT                   /note="Receptor-like serine/threonine-protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001573880"
FT   TRANSMEM        451..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        482..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..148
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          287..323
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          342..422
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          551..826
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   826 AA;  92959 MW;  821DABA8F4E616BF CRC64;
     MRTVLSFFMI FLFYASSPYV AQVSEALDSI TANQSIQDGG SLVSAGGTFE LGFFSTGLPS
     RRYLGIWYKK VATMTVVWVA NRVTPLADSV GTLKVTGSGS LVLLNANGSE IWSSNSSTDA
     RNPVAQLLDS GNLVVKDVDG TGSGFLLWQS FDYPTDTLLA GMKMGRNRTT GFERYLTSWK
     SIDDPSPGNF TYKIDPNGFP QSLLRQGSVV KFRSGPWNGV RYSGMPNLDP NPYYSYEFVL
     DDDEIYYHFE LLDSSFISRL VLSSNGIVQR FTWIDRTQGW TLYLTVPIDN CDTYALCGAY
     SSCKIDESPV CRCLTGFTPR YSQEWDILDW SHGCVRKTPL DCGKDIFVKY PGVKLPDTGN
     SWFNKTMDLQ ECKEICKKNC SCMAYSTLDI RGGGTGCLQW FGELIDIREL NQNGQDLYIR
     MAASESEYRQ EFAEIQREKW SRDFDKSLKE VLYLYYLVLT LDLYAVLLVL DLLQSKQTKQ
     KLFISLAVSF GVVSLCLVLT FCILQNKRKK MKHLKGEDGI FESGDNSECQ KEDLELPVFD
     LGTVAIATNN FSEENKLGEG GFGPVYKGVL EDGQEIAVKK LSRYSRQGLH EFKNEVLFIS
     KLQHRNLVKL LGCCIQEEVL LIYEFMPNNS LDSCLFDQNQ RKLLEWSTRF GIISGIARGL
     LYLHQDSRLR IIHRDLKAGN ILLDNEMNPK ISDFGSAKCF VGNETEANTL RVVGTYGYMS
     PEYAIDGVFS IKSDVFSYGV LVLETVSGKR NRGFCHPDHC HNLVGHQCPE DRPSMSALIL
     MLGSDNELPL PKEPGFYNER KLLPENTFGH LVHSPNEVTM TSLSPR
//
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