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TRMB_MYCGI
ID   TRMB_MYCGI              Reviewed;         263 AA.
AC   A4T3S4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Mflv_0454;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000656; ABP42948.1; -; Genomic_DNA.
DR   RefSeq; WP_011891455.1; NC_009338.1.
DR   AlphaFoldDB; A4T3S4; -.
DR   SMR; A4T3S4; -.
DR   STRING; 350054.Mflv_0454; -.
DR   EnsemblBacteria; ABP42948; ABP42948; Mflv_0454.
DR   KEGG; mgi:Mflv_0454; -.
DR   eggNOG; COG0220; Bacteria.
DR   HOGENOM; CLU_050910_0_2_11; -.
DR   OMA; PDPWHKS; -.
DR   OrthoDB; 1025521at2; -.
DR   UniPathway; UPA00989; -.
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; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..263
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_1000084445"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         146
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         169
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         242..245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   263 AA;  28766 MW;  001B73924B864736 CRC64;
     MSDHGRMHST GSEVAAPVAP DPDTEGVHPH FNRRVTSFRA RRSTISDGQQ ATWDRLWPQL
     GRQARDGDEP PGPLDTDAWF GRHAPVVLEI GCGTGTSTLA MAQAEPGIDV VAVEVYRRGL
     AQLLSAIDRT AATEHPVSNI RLIRGDGVDV LTHMFGSASL TGVRVFFPDP WPKARHHKRR
     LLQPDTMALI ADRLRPGGVL HAATDHQGYA AHIAEVGDAE PRLRRVAMDS ADLPMSVTRP
     VTKYERKALA GPVVTELLWE RTP
 
 
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