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B7GP38 (TRMB_BIFLS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 39. 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:Blon_0537, BLIJ_0540
OrganismBifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) [Complete proteome] [HAMAP]
Taxonomic identifier391904 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length286 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.

Sequence caution

The sequence BAJ68134.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processtRNA processing
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete 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 – 286286tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_1000149646

Regions

Region262 – 2654Substrate binding By similarity

Sites

Active site1651 By similarity
Binding site911S-adenosyl-L-methionine By similarity
Binding site1161S-adenosyl-L-methionine By similarity
Binding site1431S-adenosyl-L-methionine By similarity
Binding site1651S-adenosyl-L-methionine By similarity
Binding site1691Substrate By similarity
Binding site2011Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B7GP38 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 8ED56510E51E2CEE

FASTA28631,140
        10         20         30         40         50         60 
MTDPESTAID SVAAMATDHT EAPAHPLHKV LSFVRRSGRL DDRLQRAWDN YAGTYLLDIA 

        70         80         90        100        110        120 
AGNLLDVREG VTLDRALVES AWGNDNPLIV EIGTGQGENV VAAAAAHPET NFLALEVYDP 

       130        140        150        160        170        180 
GVAHTLLLAG KQGLTNIRVA QVNAPELFKV TAPGTAAEVW TFFPDPWPKK KHHKRRIVQE 

       190        200        210        220        230        240 
AMAGDIHRAL AADGVWRIAT DIEDYALHVH EVMDGLDGWK NLGSVTVSLP LEHVGKGNAD 

       250        260        270        280 
LAADMPHADF TESERFEGRV LTNFEKKGLA AGRVIHDFTY QAVALH 

« Hide

References

[1]"The genome sequence of Bifidobacterium longum subsp. infantis reveals adaptations for milk utilization within the infant microbiome."
Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R., Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P., Richardson P.M., Mills D.A.
Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12.
[2]"Bifidobacteria can protect from enteropathogenic infection through production of acetate."
Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T., Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J., Morita H., Hattori M., Ohno H.
Nature 469:543-547(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001095 Genomic DNA. Translation: ACJ51650.1.
AP010889 Genomic DNA. Translation: BAJ68134.1. Different initiation.
RefSeqYP_002322028.1. NC_011593.1.
YP_005584304.1. NC_017219.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391904.Blon_0537.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ51650; ACJ51650; Blon_0537.
BAJ68134; BAJ68134; BLIJ_0540.
GeneID12166110.
7053197.
KEGGbln:Blon_0537.
blon:BLIJ_0540.
PATRIC21121984. VBIBifLon71229_0522.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000073968.
KOK03439.
OrthoDBEOG6K6VBC.

Enzyme and pathway databases

BioCycBLON391904:GCDR-553-MONOMER.
UniPathwayUPA00989.

Family and domain databases

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_BIFLS
AccessionPrimary (citable) accession number: B7GP38
Secondary accession number(s): E8MQ59
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: June 11, 2014
This is version 39 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