ID K2NB24_9BACI Unreviewed; 213 AA.
AC K2NB24;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057};
DE EC=2.1.1.33 {ECO:0000256|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057};
GN Name=trmB {ECO:0000256|HAMAP-Rule:MF_01057,
GN ECO:0000313|EMBL:EKF36540.1};
GN ORFNames=BA1_05077 {ECO:0000313|EMBL:EKF36540.1};
OS Bacillus xiamenensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1178537 {ECO:0000313|EMBL:EKF36540.1, ECO:0000313|Proteomes:UP000010122};
RN [1] {ECO:0000313|EMBL:EKF36540.1, ECO:0000313|Proteomes:UP000010122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYC-10 {ECO:0000313|EMBL:EKF36540.1,
RC ECO:0000313|Proteomes:UP000010122};
RX PubMed=23209239; DOI=10.1128/JB.01920-12;
RA Lai Q., Liu Y., Shao Z.;
RT "Genome Sequence of Bacillus sp. Strain HYC-10, Isolated from Intestinal
RT Tract Contents from a Marine Fish (Mugil cephalus).";
RL J. Bacteriol. 194:6991-6991(2012).
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01057};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01057}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000256|HAMAP-Rule:MF_01057}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKF36540.1}.
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DR EMBL; AMSH01000008; EKF36540.1; -; Genomic_DNA.
DR RefSeq; WP_008356399.1; NZ_LDHZ01000013.1.
DR AlphaFoldDB; K2NB24; -.
DR KEGG; bxi:BK049_13840; -.
DR PATRIC; fig|1178537.3.peg.1046; -.
DR eggNOG; COG0220; Bacteria.
DR OrthoDB; 9802090at2; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000010122; Unassembled WGS sequence.
DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 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:SF14; PPR_LONG DOMAIN-CONTAINING PROTEIN; 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 {ECO:0000256|HAMAP-Rule:MF_01057,
KW ECO:0000313|EMBL:EKF36540.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01057};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01057, ECO:0000313|EMBL:EKF36540.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01057}.
FT REGION 124..129
FT /note="Interaction with RNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 44
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 191..194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
SQ SEQUENCE 213 AA; 24714 MW; 39E18905249B0AFC CRC64;
MRMRHKPWAD DYLAENAHIA LANPEQYKGK WHELFGNDHP IHIEVGTGKG SFIAGMGKLH
PDINYIGIEL FKSVIVTAVD KIKETDVENV KLLNINAETL TDVFEENEID RVYLNFSDPW
PKSRHEKRRL TFKAFLERYE QILRPGGELH FKTDNRGLFE YSLKSFSAYG LLLTYVSLDL
HEDGLEGNVM TEYEEKFSSM GQPIYRSEVK FPE
//
