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Protein

tRNA (guanine-N(7)-)-methyltransferase

Gene

trmB

Organism
Francisella tularensis subsp. holarctica (strain OSU18)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + guanine(46) in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA.UniRule annotation

Pathwayi: N(7)-methylguanine-tRNA biosynthesis

This protein is involved in the pathway N(7)-methylguanine-tRNA biosynthesis, which is part of tRNA modification.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway N(7)-methylguanine-tRNA biosynthesis and in tRNA modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei62S-adenosyl-L-methionineUniRule annotation1
Binding sitei87S-adenosyl-L-methionineUniRule annotation1
Binding sitei114S-adenosyl-L-methionineUniRule annotation1
Active sitei137By similarity1
Binding sitei137S-adenosyl-L-methionineUniRule annotation1
Binding sitei141SubstrateUniRule annotation1
Binding sitei173SubstrateUniRule annotation1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00989.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine-N(7)-)-methyltransferaseUniRule annotation (EC:2.1.1.33UniRule annotation)
Alternative name(s):
tRNA (guanine(46)-N(7))-methyltransferaseUniRule annotation
tRNA(m7G46)-methyltransferaseUniRule annotation
Gene namesi
Name:trmBUniRule annotation
Ordered Locus Names:FTH_0631
OrganismiFrancisella tularensis subsp. holarctica (strain OSU18)
Taxonomic identifieri393011 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002881501 – 229tRNA (guanine-N(7)-)-methyltransferaseAdd BLAST229

Structurei

3D structure databases

ProteinModelPortaliQ0BMU5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni143 – 148Interaction with RNAUniRule annotation6
Regioni208 – 211Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000073968.
KOiK03439.
OMAiGNLRVMC.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01057. tRNA_methyltr_TrmB. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR003358. tRNA_(Gua-N-7)_MeTrfase_Trmb.
[Graphical view]
PfamiPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00091. TIGR00091. 1 hit.
PROSITEiPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0BMU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDKSKENLR QIKSYVQRAG RVTKKQQQAL DNYAAKYLIE YAKDRKLDFT
60 70 80 90 100
EIFANTNDVV LEIGFGMGGS LVEMALANPA KNYLGIEVHK AGVGNILYEI
110 120 130 140 150
EHQNIANLLV MSHDAVEILE NMIADQSLAS IQVYFPDPWH KKKHNKRRLV
160 170 180 190 200
NQTNIDLFAK KLKVGGVFHY ASDWLPYAEE VLELLENDSK YRNLYSGFAP
210 220
RPEWRPLTKF EKRGQNLDHP ISDILFEKI
Length:229
Mass (Da):26,385
Last modified:October 17, 2006 - v1
Checksum:i9B52D52645F6474F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000437 Genomic DNA. Translation: ABI82589.1.
RefSeqiWP_003015034.1. NC_017463.1.

Genome annotation databases

EnsemblBacteriaiABI82589; ABI82589; FTH_0631.
KEGGifth:FTH_0631.
PATRICi17951108. VBIFraTul3936_0704.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000437 Genomic DNA. Translation: ABI82589.1.
RefSeqiWP_003015034.1. NC_017463.1.

3D structure databases

ProteinModelPortaliQ0BMU5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI82589; ABI82589; FTH_0631.
KEGGifth:FTH_0631.
PATRICi17951108. VBIFraTul3936_0704.

Phylogenomic databases

HOGENOMiHOG000073968.
KOiK03439.
OMAiGNLRVMC.

Enzyme and pathway databases

UniPathwayiUPA00989.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01057. tRNA_methyltr_TrmB. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR003358. tRNA_(Gua-N-7)_MeTrfase_Trmb.
[Graphical view]
PfamiPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00091. TIGR00091. 1 hit.
PROSITEiPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRMB_FRATO
AccessioniPrimary (citable) accession number: Q0BMU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 17, 2006
Last modified: November 2, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.