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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

ProRule PRU00957


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00957
General rule information [?]

Accession PRU00957
Dates 14-DEC-2011 (Created)
13-OCT-2023 (Last updated, Version 13)
Data class Domain;
Predictors PROSITE; PS51625; SAM_MT_TRMB
Name tRNA (guanine-N(7)-)-methyltransferase
Function tRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.33) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to tRNA to form tRNA containing N(7)-methylguanine and S-adenosyl-L-homocysteine.
Scope(s) Bacteria
Eukaryota
Example(s) Q6NU94;

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name + RecName: EC=2.1.1.33;

Comments [?]

CATALYTIC ACTIVITY Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)- methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74480; EC=2.1.1.33;
SIMILARITYBelongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.

Keywords [?]

Methyltransferase
S-adenosyl-L-methionine
Transferase
tRNA processing
case <OC:Eukaryota>
tRNA-binding
end case

Gene Ontology [?]

GO:0000049; Molecular function:tRNA binding
GO:0008176; Molecular function:tRNA (guanine(46)-N7)-methyltransferase activity
GO:0008033; Biological process:tRNA processing
GO:0032259; Biological process:methylation
GO:0046500; Biological process:S-adenosylmethionine metabolic process

Features [?]

From: PS51625
Key From To Description Tag Condition FTGroup
case <OC:Eukaryota> and <Feature:PS51625:74-75=E-[IL]>
BINDING 74 75 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"
end case
case <OC:Eukaryota> and <Feature:PS51625:101-102=N-[AST]>
BINDING 101 102 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"
end case
case <OC:Eukaryota> and <Feature:PS51625:197=T>
BINDING 197 199 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"
end case
case <OC:Bacteria> and <Feature:PS51625:197-200=T-[AEKNRSY]-[FY]-E>
BINDING 197 200 /ligand="substrate"
end case
ACT_SITE 124 124 D
case <OC:Bacteria>
BINDING 49 49 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 [DE]
end case
case <OC:Eukaryota>
BINDING 51 51 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 G
end case
case <OC:Bacteria>
BINDING 74 74 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 [DE]
BINDING 101 101 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 [DEN]
end case
case <OC:Eukaryota>
BINDING 121 121 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 [CL]
end case
case <OC:Bacteria>
BINDING 124 124 /ligand="S-adenosyl-L-methionine"
/ligand_id="ChEBI:CHEBI:59789"		 D
BINDING 128 128 /ligand="substrate" K
BINDING 160 160 /ligand="substrate" D
end case

Additional information [?]

Size range unlimited amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

UniProtKB rule member sequences [?]