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Q9PN20 (TRMB_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 78. 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:Cj1278c
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length392 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 – 392392tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000171312

Sites

Binding site1231S-adenosyl-L-methionine By similarity
Binding site1481S-adenosyl-L-methionine By similarity
Binding site1751S-adenosyl-L-methionine By similarity
Binding site2011Substrate By similarity
Binding site2311Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PN20 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1EA67D8B6EA4A190

FASTA39246,184
        10         20         30         40         50         60 
MPNFKSKKIK EINLPYSKDD VEFLWLAKND NVSLIYTKVQ EESFFLQIKK AQNGFVIKGD 

        70         80         90        100        110        120 
KHTKPSKIGY LQKALKIFKE GFCEDIINEA FGLKNNALIE KTPFIVDNFD ELLSRLQGKI 

       130        140        150        160        170        180 
YIEIGFGSGR HLLYQAKENP NVLILGVEIY NPALTQVAKL AKAQNVNNIL LIQSDARLLL 

       190        200        210        220        230        240 
SVLKSKSVEK IFLHFPVPWD KKPHRRVIGK DFCKECARVL VQNGRFELRT DSFEYFNFTL 

       250        260        270        280        290        300 
EQFLTFPAPK FSLRKNENLE ISSKYEDRWK KQEKNIYDLW VWNFNQECKN YELNEFNLSS 

       310        320        330        340        350        360 
VEFSKEDLKK IEQNFKNITI KKDDFFLHFE SIYKQDENLL LKVAFGAFNK PEHCYLHLDK 

       370        380        390 
TIDFAFKEPF KIQENIKAIN ELKEILKVQF KI 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL35393.1.
PIRH81335.
RefSeqYP_002344669.1. NC_002163.1.

3D structure databases

ProteinModelPortalQ9PN20.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING192222.Cj1278c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL35393; CAL35393; Cj1278c.
GeneID905569.
KEGGcje:Cj1278c.
PATRIC20059518. VBICamJej33762_1261.

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000252163.
KOK03439.
OMASKYEARW.
OrthoDBEOG6K6VBC.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-1250-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_CAMJE
AccessionPrimary (citable) accession number: Q9PN20
Secondary accession number(s): Q0P8X8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 78 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