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Database: UniProt
Entry: A0A059AD12_EUCGR
LinkDB: A0A059AD12_EUCGR
Original site: A0A059AD12_EUCGR 
ID   A0A059AD12_EUCGR        Unreviewed;       908 AA.
AC   A0A059AD12;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=EUGRSUZ_J01389 {ECO:0000313|EMBL:KCW51942.1};
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:KCW51942.1};
RN   [1] {ECO:0000313|EMBL:KCW51942.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW51942.1};
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.
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DR   EMBL; KK198762; KCW51942.1; -; Genomic_DNA.
DR   RefSeq; XP_018719906.1; XM_018864361.1.
DR   AlphaFoldDB; A0A059AD12; -.
DR   EnsemblPlants; KCW51942; KCW51942; EUGRSUZ_J01389.
DR   Gramene; KCW51942; KCW51942; EUGRSUZ_J01389.
DR   eggNOG; KOG1187; Eukaryota.
DR   InParanoid; A0A059AD12; -.
DR   OMA; QASLATW; -.
DR   OrthoDB; 388268at2759; -.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045272; ANXUR1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024788; Malectin-like_Carb-bd_dom.
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   PANTHER; PTHR34590:SF15; CARBOHYDRATE-BINDING PROTEIN OF THE ER PROTEIN; 1.
DR   PANTHER; PTHR34590; OS03G0124300 PROTEIN-RELATED; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|SAM:Phobius};
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|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..908
FT                   /note="Protein kinase domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001567505"
FT   TRANSMEM        461..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          538..813
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          62..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..449
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         567
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   908 AA;  99465 MW;  6A9314220F92E8E7 CRC64;
     MKNMKPPLLL FIFISVSLEA LPISVTGDNV DAYRPTDDIA VDCGSSTSST VENRNWIGDA
     ADRSDYSPIE KTHSSIPTQA SSSSPRVPGT APYLTARLSR SEFAYTFHVT AGPKFVRLHF
     VPSDYPNFRR VDSFFSVGAA GYTLLRNFSA SLFADYPPSV SFFSKEFCLS VGEDQILNIT
     FTPTPGNSDA YAFVNGIEVV SMPESLYYNT VVDSEGVKLA GQLAPFTFRT TDALEAVKRL
     NIGGQFVSPA EDTGMDRTWE ADDEYVTSSG FGVLPVNTTI QLNYSEQVPN YTAPDRVYTT
     ARTMGTHKRI NLSYNLTWSV EVDTNFYYLV RLHFCEFQIE INKPLDRVFE IFIDSQLVED
     HADVISWSGK KGVPVYRDFA VALYDSQKKR TNLSIALGAL PNGSTLYSDA ILNGLEIFKI
     NNPDENLAGL NPDPVPNKRP PPPGPPQSSK APSSLSKAAK IAIIAGGTSG FTVLSLLAFF
     LYRRRNRAKD STSSDGTSWW GPFSYATTKS TKTQGSSLPS DLCRHFSLTE IRAATNNFDE
     VFIIGVGGFG NVYKGYVDGG ATQVAIKRLN PGSQQGHHEF MTEIEMLSHL RHLHLVSLIG
     FCNDAGEMIL VYDYMARGTL RDHLYNTDNP PLPWKQRLQI CTEAARGLHY LHTGAKQTII
     HRDMKTTNIL LDEKWVAKVS DFGLSKVGPT SVSKAHVSTV VKGTFGYLDP EYYRRQQLTD
     KSDVYSFGVV LFEVLCARPA VNRTAQKKQI SLAAWAQSCC KSGSIDKIVD PQLKGAIAPE
     CLNKFCEIAM SCLQDEGTKR PSMNDVVWGL EFALQLQVSS EKGVIDNVVA SVHNGDACDD
     DAAPIEGNLM GHSDEVFSTN NSGGGKSLGA AATTTGSDGV YDESTTSYDS DKLLSGAVFS
     EILNPKAR
//
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