ID   TRMB_METPP              Reviewed;         469 AA.
AC   A2SJR5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase;
DE            EC=2.1.1.33;
DE   AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase;
DE   AltName: Full=tRNA(m7G46)-methyltransferase;
GN   Name=trmB; OrderedLocusNames=Mpe_A2850;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
CC   -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC       (m7G46) in tRNA. {ECO:0000250}.
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;
CC   -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TrmB family. {ECO:0000305}.
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DR   EMBL; CP000555; ABM95804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2SJR5; -.
DR   SMR; A2SJR5; -.
DR   STRING; 420662.Mpe_A2850; -.
DR   EnsemblBacteria; ABM95804; ABM95804; Mpe_A2850.
DR   KEGG; mpt:Mpe_A2850; -.
DR   eggNOG; COG0220; Bacteria.
DR   HOGENOM; CLU_582419_0_0_4; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000000366; Chromosome.
DR   GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01057; tRNA_methyltr_TrmB; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR   PANTHER; PTHR23417; PTHR23417; 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   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..469
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_0000288178"
FT   REGION          1..221
FT                   /note="Unknown"
FT   REGION          1..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..469
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT   COMPBIAS        7..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..83
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         362
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         398
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         433..436
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  50968 MW;  E173CAD6CD3C08D3 CRC64;
     MRGGAHGPGD RAGRCREHRQ DHAGPCAGAG APFARPAGHA GGRVPARVLR RARPHAAARG
     TGRHRRRAMA SHRGRRAGRS HRAGRHHAAD DRGLQRVRVR RPQSLPPGAR APAPLRPHAA
     DRPRPGLAAR RPAARRRPGA RPGRPLGPRR AGLCRAALFG GLWRRLGAHG SRCGCAAPAA
     APARPGGPRA RRPAAAWPLP RMPAARMRTS VVRVRGEAPI AMSEPDSSSP PAHPPRPIRS
     FVLRAGRMGS GQTRALAELG PRFVLPFQRE PLDPQTVFGR RAPRVFEIGF GMGDATAQIA
     AARPDTDFIG CEVHTPGVGA LLKQIGEREL TNLRIVQHDA VEVLDHMIEP GSLAGIHLFF
     PDPWHKKKHH KRRLVQPAFV ERLVTRLAPG GYLHCATDWQ PYAEQMLEVL GAEPALRNSA
     DGYAPRPEYR PLTKFEQRGL RLGHGVWDLV FTKHQGRSAS KQCTATSSP