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Protein

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

Gene

trmB

Organism
Bacillus cereus (strain B4264)
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

Pathway:iN(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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441S-adenosyl-L-methionineUniRule annotation
Binding sitei69 – 691S-adenosyl-L-methionineUniRule annotation
Binding sitei96 – 961S-adenosyl-L-methionineUniRule annotation
Active sitei118 – 1181By similarity
Binding sitei118 – 1181S-adenosyl-L-methionineUniRule annotation
Binding sitei122 – 1221SubstrateUniRule annotation
Binding sitei154 – 1541SubstrateUniRule annotation

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

BioCyciBCER405532:GI1K-4767-MONOMER.
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:BCB4264_A4811
OrganismiBacillus cereus (strain B4264)
Taxonomic identifieri405532 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000007096 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217tRNA (guanine-N(7)-)-methyltransferasePRO_1000136340Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB7H758.
SMRiB7H758. Positions 11-213.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0220.
HOGENOMiHOG000251689.
KOiK03439.
OMAiAHPEINY.
OrthoDBiEOG6K6VBC.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01057. tRNA_methyltr_TrmB.
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.

B7H758-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLRHKPYAM DRINEYSHIV IGNPEERAGS WKEVFGNEQP IHIEVGTGRG
60 70 80 90 100
RFMYDMAKAN PHINYIGIEK FTSVVVDALD KLIEEELPNL KLINKDAEDL
110 120 130 140 150
TVFFAKGEID RVYLNFSDPW PKKRHTKRRL TYKTFLRNYE EVLVEGGEIH
160 170 180 190 200
FKTDNQGLFE YSLMSMAEYG MLLTYLSLDL HNSDFEGNIM TEYEEKFSSK
210
GHRIYRVEAK YRTEPMQ
Length:217
Mass (Da):25,573
Last modified:February 10, 2009 - v1
Checksum:iBAD77596E615D77A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001176 Genomic DNA. Translation: ACK61400.1.
RefSeqiWP_001239385.1. NC_011725.1.

Genome annotation databases

EnsemblBacteriaiACK61400; ACK61400; BCB4264_A4811.
KEGGibcb:BCB4264_A4811.
PATRICi18881519. VBIBacCer117876_4663.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001176 Genomic DNA. Translation: ACK61400.1.
RefSeqiWP_001239385.1. NC_011725.1.

3D structure databases

ProteinModelPortaliB7H758.
SMRiB7H758. Positions 11-213.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACK61400; ACK61400; BCB4264_A4811.
KEGGibcb:BCB4264_A4811.
PATRICi18881519. VBIBacCer117876_4663.

Phylogenomic databases

eggNOGiCOG0220.
HOGENOMiHOG000251689.
KOiK03439.
OMAiAHPEINY.
OrthoDBiEOG6K6VBC.

Enzyme and pathway databases

UniPathwayiUPA00989.
BioCyciBCER405532:GI1K-4767-MONOMER.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01057. tRNA_methyltr_TrmB.
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...

Publicationsi

  1. "Genome sequence of Bacillus cereus B4264."
    Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B4264.

Entry informationi

Entry nameiTRMB_BACC4
AccessioniPrimary (citable) accession number: B7H758
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: July 22, 2015
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

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

External Data

Dasty 3

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 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.