ID   TRMB_YARLI              Reviewed;         292 AA.
AC   Q6CE12;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 114.
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=Transfer RNA methyltransferase 8 {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};
GN   Name=TRM8 {ECO:0000255|HAMAP-Rule:MF_03055};
GN   OrderedLocusNames=YALI0B19558g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- SUBUNIT: Forms a complex with TRM82. {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; CR382128; CAG83353.1; -; Genomic_DNA.
DR   RefSeq; XP_501100.1; XM_501100.1.
DR   AlphaFoldDB; Q6CE12; -.
DR   SMR; Q6CE12; -.
DR   STRING; 284591.Q6CE12; -.
DR   EnsemblFungi; CAG83353; CAG83353; YALI0_B19558g.
DR   GeneID; 2907246; -.
DR   KEGG; yli:YALI0B19558g; -.
DR   VEuPathDB; FungiDB:YALI0_B19558g; -.
DR   HOGENOM; CLU_050910_3_1_1; -.
DR   InParanoid; Q6CE12; -.
DR   OMA; LPNYFAK; -.
DR   OrthoDB; 116813at2759; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000001300; Chromosome B.
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   3: Inferred from homology;
KW   Methyltransferase; Nucleus; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..292
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_0000370606"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         133..134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         168..169
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         188
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         266..268
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
SQ   SEQUENCE   292 AA;  33982 MW;  EB71F2EF1F73C1D5 CRC64;
     MLKRDQSEMD IEAETANMGK EEKESFVHKR QKYRQEQEEK RLAAKKGVSF EQPEDGEIKL
     PKKRYYRQRA HSNPFSDHQL EYPESPADMD WDVLYPNRKE GQKVEVADIG CGFGGLLVAL
     SPQLPNQLIL GMEIRVQVTN YVEDRIVALR HQNKETDGYQ NISVLRGNAM KFLPNFFEKG
     QLSKIFFCFP DPHFKQRKHK ARIVTTTLCS EYAYVVRPGG IVYTITDVKD LHEWMVKHLA
     AHPLFERLTK EEEDADPCVA TMLVETEEGK KVARNEGDKF VACFRRKENP EW
//