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Q8NNX7 (TRMD_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. 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:Cgl2050, cg2249
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

S-adenosyl-L-methionine + guanine(37) in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA. HAMAP MF_00605

Subunit structure

Homodimer By similarity. HAMAP MF_00605

Subcellular location

Cytoplasm Potential HAMAP MF_00605.

Sequence similarities

Belongs to the RNA methyltransferase TrmD family.

Sequence caution

The sequence BAB99443.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionRNA binding

Inferred from electronic annotation. Source: InterPro

tRNA (guanine-N1-)-methyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289tRNA (guanine-N(1)-)-methyltransferase HAMAP MF_00605
PRO_0000060365

Regions

Region90 – 12334Insert HAMAP MF_00605
Region181 – 1866S-adenosyl-L-methionine binding By similarity

Sites

Binding site1571S-adenosyl-L-methionine; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NNX7 [UniParc].

Last modified December 6, 2002. Version 2.
Checksum: 816A508AD7E6E4A8

FASTA28931,791
        10         20         30         40         50         60 
MTSSENLDSH RLRLDVVTIF PEYLDPLRHA LLGKAIEDGI LEVGVHDLRN WATGGHKAVD 

        70         80         90        100        110        120 
DTPYGGGPGM VMKPEVWGPA LDDVAAGRVS GAELDSASLH LKNVRHDELG GVEKRAYVVE 

       130        140        150        160        170        180 
EDRDLPLLLV PTPAGKPFTQ ADAQAWSNEE HIVFACGRYE GIDQRVIDDA ANRYRVREVS 

       190        200        210        220        230        240 
IGDYVLIGGE VAVLVIAEAV VRLIPGVLGN RRSHEEDSFS DGLLEGPSYT KPRTWRGLDV 

       250        260        270        280 
PEVLFSGNHA KVDRWRRDQA LLRTQAIRPE LIDASLLDST DLKVLGLDK 

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB99443.1. Different initiation.
BX927154 Genomic DNA. Translation: CAF20388.1.
RefSeqNP_601253.1. NC_003450.3.
YP_226289.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NNX7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1020004.
3343898.
GenomeReviewsGene locus Cgl2050 in contig BA000036_GR.
Gene locus cg2249 in contig BX927147_GR.
KEGGcgb:cg2249.
cgl:NCgl1972.
PATRIC21496102. VBICorGlu203724_1987.

Phylogenomic databases

HOGENOMHBG285805.
OMAVCGRFEG.
PhylomeDBQ8NNX7.
ProtClustDBPRK00026.

Enzyme and pathway databases

BioCycCGLU196627:CG2249-MONOMER.

Family and domain databases

HAMAPMF_00605. TrmD. Divergent sequence.
[Tree]
InterProIPR016009. tRNA_m1G_MeTrfase.
IPR002649. tRNA_m1G_MeTrfase_bac.
IPR023148. tRNA_m1G_MeTrfase_C.
[Graphical view]
Gene3DG3DSA:1.10.1270.20. tRNA_m1G_MeTrfase_C. 1 hit.
KOK00554.
PANTHERPTHR10056. PTHR10056. 1 hit.
PfamPF01746. tRNA_m1G_MT. 2 hits.
[Graphical view]
PIRSFPIRSF000386. tRNA_mtase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRMD_CORGL
AccessionPrimary (citable) accession number: Q8NNX7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: December 6, 2002
Last modified: January 25, 2012
This is version 60 of the entry and version 2 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