TRMB_MYCPU
ID TRMB_MYCPU Reviewed; 203 AA.
AC Q98R44;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
GN Name=trmB {ECO:0000255|HAMAP-Rule:MF_01057}; OrderedLocusNames=MYPU_1660;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_01057}.
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_01057};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01057}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_01057}.
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DR EMBL; AL445563; CAC13339.1; -; Genomic_DNA.
DR PIR; F90532; F90532.
DR RefSeq; WP_010924970.1; NC_002771.1.
DR AlphaFoldDB; Q98R44; -.
DR SMR; Q98R44; -.
DR STRING; 272635.MYPU_1660; -.
DR EnsemblBacteria; CAC13339; CAC13339; CAC13339.
DR KEGG; mpu:MYPU_1660; -.
DR eggNOG; COG0220; Bacteria.
DR HOGENOM; CLU_050910_2_1_14; -.
DR OMA; WRGAKTA; -.
DR OrthoDB; 1025521at2; -.
DR BioCyc; MPUL272635:G1GT6-167-MON; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000000528; 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..203
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000171360"
FT ACT_SITE 107
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 181..184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ SEQUENCE 203 AA; 23782 MW; 2A28826B06FBBE29 CRC64;
MRLRNNKNAK LELESCENVI KNFPFKVEKN STLEIGMGKG QMLIELAQKN PQKIFVGIEK
YPTVALIAAK KAKKLELNNF FIIVDDVENA LDFFEGTFDL IWLTFSDPWP KKRHYKRRLT
YEKFLKIYSK ILSENGLIKL KTDNDDFFQW TLESLEKNGL NIINKTSDLE KSEFAKDNVK
TSYEQKFVSL GKNINFVEFS FKK
