Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q43963 (TRMD_ACIAD)

Last modified November 3, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    tRNA (guanine-N(1)-)-methyltransferase
    EC=2.1.1.31
Alternative name(s):
    M1G-methyltransferase
    tRNA [GM37] methyltransferase
Gene names
Name: trmD
Ordered Locus Names: ACIAD3311
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Specifically methylates guanosine-37 in various tRNAs By similarity.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Potential.

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)
   Biological processtRNA modification

Inferred from electronic annotation. Source: HAMAP

   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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249tRNA (guanine-N(1)-)-methyltransferase HAMAP MF_00605
PRO_0000060313

Regions

Region137 – 1426S-adenosyl-L-methionine binding By similarity

Sites

Binding site1171S-adenosyl-L-methionine; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q43963-1 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: 215139F2B65A195C

FASTA24928,287
        10         20         30         40         50         60 
MFFAVITLFP EMFEAITAYG ISGRATKRQI ATVSCINPRD FAEGNYKRVD ERPFGGGPGM 

        70         80         90        100        110        120 
VMMAEPLAKA IIHAKQLAEQ AGCVHAPVVY MSPQGKTLNE HAVQQFVDYD GLIVLCGRYE 

       130        140        150        160        170        180 
GVDERLIQHY VDQEWSIGDY VLSGGELPAM VLLDSIIRRL PDAMSDEQSH IQDSFVDGLL 

       190        200        210        220        230        240 
DCPQYTKPDH FEGLDVPEVL KSGHHANIEK WRFLQRYQRT LDRRPELVEK VTLTKQQRKW 


LTFLDDSKN 

« Hide

References

« Hide 'large scale' references
[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Characterization of lipase-deficient mutants of Acinetobacter calcoaceticus BD413: identification of a periplasmic lipase chaperone essential for the production of extracellular lipase."
Kok R.G., Thor J.J., Nugteren-Roodzant I.M., Vosman B., Hellingwerf K.J.
J. Bacteriol. 177:3295-3307(1995) [PubMed: 7768830] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-249.

Cross-references

Sequence databases

CR543861 Genomic DNA. Translation: CAG69984.1.
X80800 Genomic DNA. Translation: CAA56781.1.
PIRS61928.
RefSeqYP_047806.1.

3D structure databases

HSSPHSSP built from PDB template 1UAJ based on UniProtKB P43912.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ43963.

Genome annotation databases

GeneID2880730.
GenomeReviewsGene locus ACIAD3311 in contig CR543861_GR.
KEGGaci:ACIAD3311.
NMPDRfig|62977.3.peg.2999.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ43963.
OMAHRSVDDT.

Enzyme and pathway databases

BioCycASP62977:ACIAD3311-MON.

Family and domain databases

HAMAPMF_00605.
[Tree]
InterProIPR016009. tRNA_m1G_MeTrfase.
IPR002649. tRNA_m1G_MeTrfase_bac.
[Graphical view]
PfamPF01746. tRNA_m1G_MT. 1 hit.
[Graphical view]
PIRSFPIRSF000386. tRNA_mtase. 1 hit.
ProDomPD004978. tRNA_m1G_mtfrase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00088. trmD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRMD_ACIAD
AccessionPrimary (citable) accession number: Q43963
Secondary accession number(s): Q6F7I1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 31, 2004
Last modified: November 3, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents