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Database: UniProt
Entry: A0A059AGT2_EUCGR
LinkDB: A0A059AGT2_EUCGR
Original site: A0A059AGT2_EUCGR 
ID   A0A059AGT2_EUCGR        Unreviewed;       407 AA.
AC   A0A059AGT2;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Methyltransferase small domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EUGRSUZ_J02331 {ECO:0000313|EMBL:KCW53038.1};
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:KCW53038.1};
RN   [1] {ECO:0000313|EMBL:KCW53038.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW53038.1};
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   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01024}.
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DR   EMBL; KK198762; KCW53038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059AGT2; -.
DR   EnsemblPlants; KCW53038; KCW53038; EUGRSUZ_J02331.
DR   Gramene; KCW53038; KCW53038; EUGRSUZ_J02331.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR47548; BNAA06G32370D PROTEIN; 1.
DR   PANTHER; PTHR47548:SF1; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF03602; Cons_hypoth95; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}.
FT   BINDING         279
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         306
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         329
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         377
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   407 AA;  44507 MW;  597D2928C5B6750D CRC64;
     MSLCLLSARS LCPTASCRLS PAASAPPSPP PPPPAPATLR LSPASTSPAC ALQCSHFQSC
     SGCTHELNLH RPSVVDDAAD FFKSLGVSDF TFDSCKLWGW RCRAKLAVRG SSVDPLIGLY
     QEGTHSVVDI PNCKAHHPNI NAAMELLKQG IKELGIEPHD EDQGTGDLRY VQMAVTTYNT
     SIPASERYQH GQVQVALVWN SRNENSPNSD KLNALAHFLW QNGGSKCKVP FIHSVWANFQ
     TSTSNVIFGN RWRHLLGDRD FWEHLGGIDV SLAPSSFGQA NTRAFNSLLR KLQKYVPYGA
     SVTDLYAGSG VIGLSLAATR KCRSVRCVEI NKESKLSFEK TVERLPKYVD SSISWHQADT
     SVEPTSWLVG SDVIVVDPPR KGLEASLVGA LQTLPEWELK TRSSPER
//
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