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A5HZ44 (TRMB_CLOBH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA (guanine-N(7)-)-methyltransferase

EC=2.1.1.33
Alternative name(s):
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase
Gene names
Name:trmB
Ordered Locus Names:CBO0499, CLC_0573
OrganismClostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) [Reference proteome] [HAMAP]
Taxonomic identifier441771 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA By similarity. HAMAP-Rule MF_01057

Catalytic activity

S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. HAMAP-Rule MF_01057

Pathway

tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_01057

Sequence similarities

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

Ontologies

Keywords
   Biological processtRNA processing
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functiontRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_1000136346

Regions

Region129 – 1346Interaction with RNA Potential
Region196 – 1994Substrate binding By similarity

Sites

Binding site431S-adenosyl-L-methionine By similarity
Binding site681S-adenosyl-L-methionine By similarity
Binding site1011S-adenosyl-L-methionine By similarity
Binding site1231S-adenosyl-L-methionine By similarity
Binding site1271Substrate By similarity
Binding site1591Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A5HZ44 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: C9CEDFA575906AD2

FASTA21726,259
        10         20         30         40         50         60 
MRLRKKWWAR PEIEASDKFA EEPKELRGKW NKEFNNNNDI HLELGCGRGG FISQLVEKNK 

        70         80         90        100        110        120 
DINYVGIDLK DEVIVYAIRK VKEKEEEVKR EFKNIKFVTM NIMGIAEVFD KNEISKIYIN 

       130        140        150        160        170        180 
FCNPWPKERH NKRRLTHTKL LTEYKKFLKP NTEIWFKTDD KELFEDSQEY FKESGFNIEY 

       190        200        210 
ITYDLHNSDF KENIKTEYET KFETMGMKIM FLKARLL 

« Hide

References

[1]"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes."
Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. expand/collapse author list , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J.
Genome Res. 17:1082-1092(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.
[2]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000727 Genomic DNA. Translation: ABS38078.1.
AM412317 Genomic DNA. Translation: CAL82053.1.
RefSeqYP_001253043.1. NC_009495.1.
YP_001386456.1. NC_009698.1.

3D structure databases

ProteinModelPortalA5HZ44.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413999.CBO0499.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS38078; ABS38078; CLC_0573.
GeneID5184754.
5399680.
KEGGcbh:CLC_0573.
cbo:CBO0499.
PATRIC19363117. VBICloBot22612_0502.

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000251689.
KOK03439.
OMADNVMTEY.
OrthoDBEOG6K6VBC.

Enzyme and pathway databases

BioCycCBOT413999:GJ72-562-MONOMER.
CBOT441771:GIWX-545-MONOMER.
UniPathwayUPA00989.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
HAMAPMF_01057. tRNA_methyltr_TrmB.
InterProIPR029063. SAM-dependent_MTases-like.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
PROSITEPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRMB_CLOBH
AccessionPrimary (citable) accession number: A5HZ44
Secondary accession number(s): A7G137
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 26, 2007
Last modified: June 11, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways