ID TRMB_MAIZE Reviewed; 255 AA. AC B6SHG7; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 24-JAN-2024, entry version 89. DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055}; DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_03055}; DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055}; DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03055}; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4; RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V., RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.; RT "Insights into corn genes derived from large-scale cDNA sequencing."; RL Plant Mol. Biol. 69:179-194(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. B73; RA Yu Y., Currie J., Lomeli R., Angelova A., Collura K., Wissotski M., RA Campos D., Kudrna D., Golser W., Ashely E., Haller K., Descour A., RA Fernandes J., Zuccolo A., Soderlund C., Walbot V.; RT "Maize full-length cDNA project."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46 CC (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_03055}. CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)- CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03055}; CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_03055}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03055}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_03055}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU952182; ACG24300.1; -; mRNA. DR EMBL; BT066355; ACN33252.1; -; mRNA. DR RefSeq; NP_001146900.1; NM_001153428.1. DR RefSeq; XP_008677164.1; XM_008678942.1. DR RefSeq; XP_008677165.1; XM_008678943.1. DR RefSeq; XP_008677166.1; XM_008678944.1. DR AlphaFoldDB; B6SHG7; -. DR SMR; B6SHG7; -. DR STRING; 4577.B6SHG7; -. DR PaxDb; 4577-GRMZM2G019597_P03; -. DR EnsemblPlants; Zm00001eb208790_T001; Zm00001eb208790_P001; Zm00001eb208790. DR EnsemblPlants; Zm00001eb208790_T002; Zm00001eb208790_P002; Zm00001eb208790. DR EnsemblPlants; Zm00001eb208790_T003; Zm00001eb208790_P003; Zm00001eb208790. DR GeneID; 100280508; -. DR Gramene; Zm00001eb208790_T001; Zm00001eb208790_P001; Zm00001eb208790. DR Gramene; Zm00001eb208790_T002; Zm00001eb208790_P002; Zm00001eb208790. DR Gramene; Zm00001eb208790_T003; Zm00001eb208790_P003; Zm00001eb208790. DR KEGG; zma:100280508; -. DR eggNOG; KOG3115; Eukaryota. DR HOGENOM; CLU_050910_3_0_1; -. DR InParanoid; B6SHG7; -. DR OMA; LPNYFAK; -. DR OrthoDB; 116813at2759; -. DR UniPathway; UPA00989; -. DR Proteomes; UP000007305; Chromosome 4. DR ExpressionAtlas; B6SHG7; baseline and differential. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central. DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central. DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR025763; Trm8_euk. DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb. DR NCBIfam; TIGR00091; tRNA (guanosine(46)-N7)-methyltransferase TrmB; 1. DR PANTHER; PTHR23417; 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE; 1. DR PANTHER; PTHR23417:SF16; TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE; 1. DR Pfam; PF02390; Methyltransf_4; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51625; SAM_MT_TRMB; 1. PE 2: Evidence at transcript level; KW Methyltransferase; Nucleus; Reference proteome; RNA-binding; KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding. FT CHAIN 1..255 FT /note="tRNA (guanine-N(7)-)-methyltransferase" FT /id="PRO_0000370580" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 154 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 75 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 98..99 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 131..132 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 151 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" FT BINDING 229..231 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03055" SQ SEQUENCE 255 AA; 29119 MW; 292FD6EE2F697E22 CRC64; MTRTNDASGG GKLPRKRFYR ARAHSNPLSD SHFPVPISPE EVDLSQHYPR YFPADKGSDG EEAAAPQQIR FADVGCGFGG LLVGLSPLFP DTLMIGMELR DKVTEYVKER ILALRGANPG QYDNISVVRT NSMKYIPNYF RKAQLTKMFF LFPDPHFKEK NHRRRVISMQ LLDEYAYVME VGGIIYTITD VEELGEWMRS CLEKHPLFET VPEEEIKADP VFKLLSTATE ESQKVARNGG QTFYAIFRRI SLQEE //