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Q4A9M3 (TRMB_MYCHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. 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:MHJ_0462
OrganismMycoplasma hyopneumoniae (strain J / ATCC 25934 / NCTC 10110) [Complete proteome] [HAMAP]
Taxonomic identifier262719 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length201 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 – 201201tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
PRO_0000229175

Regions

Region180 – 1834Substrate binding Potential

Sites

Active site1061 By similarity
Binding site331S-adenosyl-L-methionine By similarity
Binding site581S-adenosyl-L-methionine By similarity
Binding site851S-adenosyl-L-methionine By similarity
Binding site1061S-adenosyl-L-methionine By similarity
Binding site1101Substrate By similarity
Binding site1421Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4A9M3 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 2328CAE53945D5FB

FASTA20123,713
        10         20         30         40         50         60 
MRLRNIPDAL ERIQNQNLLV KTPWNIDDSW IIEIGMGKGK MISQLAFDNP NKNFLGVEKY 

        70         80         90        100        110        120 
PSAAVKAIKY VKKYNLSNFF ILISDAKDLL DRIKGKASTI WLTFPDPWPK NRHYKRRLTY 

       130        140        150        160        170        180 
KDFLEIYANL LVKDGILKLK TDNLKFFEFS IESLKENGWK ITYQTNDLHN SLVNSSNIKT 

       190        200 
TYEEKWVNLN YKIHYLEAIF I 

« Hide

References

[1]"Swine and poultry pathogens: the complete genome sequences of two strains of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae."
Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L., Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R., Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M., Brocchi M., Burity H.A., Camargo A.A., Camargo S.S. expand/collapse author list , Carepo M.S., Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G., Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P., Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S., Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B., Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A., Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B., Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C., Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L., Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R., Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N., Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C., Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P., Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.
J. Bacteriol. 187:5568-5577(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J / ATCC 25934 / NCTC 10110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017243 Genomic DNA. Translation: AAZ44548.1.
RefSeqYP_279259.1. NC_007295.1.

3D structure databases

ProteinModelPortalQ4A9M3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262719.MHJ_0462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ44548; AAZ44548; MHJ_0462.
GeneID3563571.
KEGGmhj:MHJ_0462.
PATRIC20014794. VBIMycHyo90918_0520.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMHYO262719:GJ59-483-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_MYCHJ
AccessionPrimary (citable) accession number: Q4A9M3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: September 13, 2005
Last modified: April 16, 2014
This is version 60 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