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B2TJ31 (TRMD_CLOBB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
tRNA (guanine-N(1)-)-methyltransferase
EC=2.1.1.228
Alternative name(s):
M1G-methyltransferase
tRNA [GM37] methyltransferase
Gene names
Name:trmD
Ordered Locus Names:CLL_A1249
OrganismClostridium botulinum (strain Eklund 17B / Type B) [Complete proteome] [HAMAP]
Taxonomic identifier508765 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Specifically methylates guanosine-37 in various tRNAs By similarity. HAMAP-Rule MF_00605

Catalytic activity

S-adenosyl-L-methionine + guanine37 in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine37 in tRNA. HAMAP-Rule MF_00605

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00605.

Sequence similarities

Belongs to the RNA methyltransferase TrmD family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

tRNA (guanine(37)-N(1))-methyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 238238tRNA (guanine-N(1)-)-methyltransferase HAMAP-Rule MF_00605
PRO_1000130151

Regions

Region129 – 1346S-adenosyl-L-methionine binding By similarity

Sites

Binding site1101S-adenosyl-L-methionine; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B2TJ31 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 5ACDDB01CEE101B9

FASTA23827,431
        10         20         30         40         50         60 
MKISILTLFP EMFSIFNHSI IGRAQENNIV ELELLNIRDN TLDKHKKVDD YPYGGGAGMV 

        70         80         90        100        110        120 
MAPQPIIDTI RKAKENNKGK VIFLGPRGKT FNQKMAMDLS KEENLIFLCG HYEGIDERVY 

       130        140        150        160        170        180 
KHIDMEVSLG DFILTGGEMA AIPVIDSILR LIPGVLGKEE SFVDESFSED LLEYPQYTRP 

       190        200        210        220        230 
YEFEGEHVPE ILLSGHHENI RKWRRLQSLD LTRKRRPDLY KNVILTKEDK KLLGRKNK

« Hide

References

[1]"Complete sequence of Clostridium botulinum strain Eklund."
Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Eklund 17B / Type B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001056 Genomic DNA. Translation: ACD23339.1.
RefSeqYP_001885447.1. NC_010674.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING508765.CLL_A1249.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD23339; ACD23339; CLL_A1249.
GeneID6293082.
KEGGcbk:CLL_A1249.
PATRIC19395340. VBICloBot123574_1180.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0336.
HOGENOMHOG000016242.
KOK00554.
OMANRYDLYL.
ProtClustDBPRK00026.

Enzyme and pathway databases

BioCycCBOT508765:GJ4H-1243-MONOMER.

Family and domain databases

Gene3D1.10.1270.20. 1 hit.
HAMAPMF_00605. TrmD.
InterProIPR016009. tRNA_m1G_MeTrfase.
IPR002649. tRNA_m1G_MeTrfase_bac.
IPR023148. tRNA_m1G_MeTrfase_C.
[Graphical view]
PfamPF01746. tRNA_m1G_MT. 1 hit.
[Graphical view]
PIRSFPIRSF000386. tRNA_mtase. 1 hit.
TIGRFAMsTIGR00088. trmD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRMD_CLOBB
AccessionPrimary (citable) accession number: B2TJ31
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: May 1, 2013
This is version 36 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

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