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TRMB_MAIZE
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   03-AUG-2022, entry version 81.
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}.
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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.GRMZM2G019597_P03; -.
DR   PaxDb; B6SHG7; -.
DR   PRIDE; B6SHG7; -.
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   OMA; DLHNWMV; -.
DR   OrthoDB; 1417652at2759; -.
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-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   Gene3D; 3.40.50.150; -; 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   PANTHER; PTHR23417; PTHR23417; 1.
DR   PANTHER; PTHR23417:SF16; PTHR23417:SF16; 1.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00091; TIGR00091; 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
 
 
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