ID   TRMB_DROSE              Reviewed;         256 AA.
AC   B4I9N7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 64.
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};
GN   ORFNames=GM18921;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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; CH480825; EDW43918.1; -; Genomic_DNA.
DR   RefSeq; XP_002040447.1; XM_002040411.1.
DR   AlphaFoldDB; B4I9N7; -.
DR   SMR; B4I9N7; -.
DR   STRING; 7238.B4I9N7; -.
DR   EnsemblMetazoa; FBtr0201906; FBpp0200398; FBgn0173824.
DR   GeneID; 6616081; -.
DR   KEGG; dse:6616081; -.
DR   HOGENOM; CLU_050910_3_1_1; -.
DR   OMA; LPNYFAK; -.
DR   OrthoDB; 116813at2759; -.
DR   PhylomeDB; B4I9N7; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
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..256
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_0000370574"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        160
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         79
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         102..103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         137..138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
FT   BINDING         235..237
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03055"
SQ   SEQUENCE   256 AA;  29416 MW;  928DC69DC546222D CRC64;
     MVATGGQAQD QSQNQEPDVL NPTSAVTGLP QKRYYRQRAH SNPIADHSFD YPARPEDVDW
     RSMYPSIQQG QQVSFADVGC GYGGFLVTLG EMFPEKLSIG MEIRVKVSDY VVDRVAALRR
     RCADTGAYQN IACLRTNAMK YLPNYFSKGQ LEKMFFLYPD PHFKRAKHKW RIINQALLSE
     YAYVLRKGGL VYTMTDVEDL HKWIVTHMEE HPLYERLTEE EANADPITPK LYQSSEEGAK
     VVRNKGDHFL AIFRRL
//