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Q65G12 (TRMB_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. 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:BLi03141, BL00042
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length213 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
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 – 213213tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000229154

Regions

Region124 – 1296Interaction with RNA Potential
Region191 – 1944Substrate binding By similarity

Sites

Active site1181 By similarity
Binding site441S-adenosyl-L-methionine By similarity
Binding site691S-adenosyl-L-methionine By similarity
Binding site961S-adenosyl-L-methionine By similarity
Binding site1181S-adenosyl-L-methionine By similarity
Binding site1221Substrate By similarity
Binding site1541Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65G12 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: DABC74446D43BA28

FASTA21324,431
        10         20         30         40         50         60 
MRMRHKPWAD DYLAENSHIV ISEPSQYKGK WHSVFGNDNP IHIEVGTGKG QFISGMALQN 

        70         80         90        100        110        120 
PDVNYIGIEL FKSVIVTAVD KVKQTEAPNV KLLNINANML SDVFADGEVD RVYLNFSDPW 

       130        140        150        160        170        180 
PKKRHEKRRL TNHAFLKKYE QVLGGKGAIH FKTDNRGLFE YSLTSFSEYG LVLTFVSLDL 

       190        200        210 
HQSDFEGNVM TEYEEKFAAK GQPIYRVEAE WRT 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU42002.1.
CP000002 Genomic DNA. Translation: AAU24643.1.
RefSeqYP_006714473.1. NC_006322.1.
YP_080281.1. NC_006270.3.

3D structure databases

ProteinModelPortalQ65G12.
SMRQ65G12. Positions 10-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL00042.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU24643; AAU24643; BL00042.
AAU42002; AAU42002; BLi03141.
GeneID3027940.
3098881.
KEGGbld:BLi03141.
bli:BL00042.
PATRIC18952020. VBIBacLic203714_3210.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000251689.
KOK03439.
OMAKTDDDEL.
OrthoDBEOG6K6VBC.
ProtClustDBPRK00121.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-3113-MONOMER.
UniPathwayUPA00989.

Family and domain databases

HAMAPMF_01057. tRNA_methyltr_TrmB.
InterProIPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
PROSITEPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRMB_BACLD
AccessionPrimary (citable) accession number: Q65G12
Secondary accession number(s): Q62RG7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2004
Last modified: April 16, 2014
This is version 73 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