TRMB_METH1
ID TRMB_METH1 Reviewed; 202 AA.
AC Q9F411; D1J8L3;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=MHO_4250;
OS Metamycoplasma hominis (strain ATCC 23114 / DSM 25592 / NBRC 14850 / NCTC
OS 10111 / PG21) (Mycoplasma hominis).
OC Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC Metamycoplasma.
OX NCBI_TaxID=347256;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10991851; DOI=10.1128/aac.44.10.2719-2727.2000;
RA Bebear C.M., Grau O., Charron A., Renaudin H., Gruson D., Bebear C.;
RT "Cloning and nucleotide sequence of the DNA gyrase (gyrA) gene from
RT Mycoplasma hominis and characterization of quinolone-resistant mutants
RT selected In vitro with trovafloxacin.";
RL Antimicrob. Agents Chemother. 44:2719-2727(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23114 / DSM 25592 / NBRC 14850 / NCTC 10111 / PG21;
RX PubMed=19816563; DOI=10.1371/journal.pgen.1000677;
RA Pereyre S., Sirand-Pugnet P., Beven L., Charron A., Renaudin H., Barre A.,
RA Avenaud P., Jacob D., Couloux A., Barbe V., de Daruvar A., Blanchard A.,
RA Bebear C.;
RT "Life on arginine for Mycoplasma hominis: clues from its minimal genome and
RT comparison with other human urogenital mycoplasmas.";
RL PLoS Genet. 5:E1000677-E1000677(2009).
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; U59880; AAG28841.1; -; Genomic_DNA.
DR EMBL; FP236530; CAX37560.1; -; Genomic_DNA.
DR RefSeq; WP_012855699.1; NC_013511.1.
DR AlphaFoldDB; Q9F411; -.
DR SMR; Q9F411; -.
DR STRING; 347256.MHO_4250; -.
DR EnsemblBacteria; CAX37560; CAX37560; MHO_4250.
DR KEGG; mho:MHO_4250; -.
DR eggNOG; COG0220; Bacteria.
DR HOGENOM; CLU_050910_2_1_14; -.
DR OMA; WRGAKTA; -.
DR OrthoDB; 1025521at2; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000002631; 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..202
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000171352"
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 202 AA; 23951 MW; D8993C44B381BB0B CRC64;
MRLRFNKNAE TSLMASPMTF KDFPIDNKKN TILEIGMGRG TMLTKLALMH PDIEYIGLEK
YSTPAYSALK KAIDLNLENF HIIIGDAINL STYFKNKIKT IWLTFSDPWP KKRHYKRRLV
YRDFLKIYQN VLDKDGVVYF KTDNDMLYQF AIDELKEINA KIIYQTSDLH HCNFKIENVF
TDYEEKFNKL NKNINFIAFT FN
