Reviewed, UniProtKB/Swiss-Prot A3M9G5 (TRMD_ACIBT)

Names and origin

Protein names

Recommended 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:	A1S_3162

Organism

Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]

Taxonomic identifier

400667 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Specifically methylates guanosine-37 in various tRNAs By similarity. HAMAP MF_00605
Catalytic activity	S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N(1)-methylguanine. 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.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	tRNA modification Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 246	246	tRNA (guanine-N(1)-)-methyltransferase HAMAP MF_00605		PRO_1000130122
Regions
	Region	137 – 142	6	S-adenosyl-L-methionine binding By similarity
Sites
	Binding site	117	1	S-adenosyl-L-methionine; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3M9G5-1 [UniParc]. Last modified September 2, 2008. Version 2. Checksum: 46A5E4D5112A3331	FASTA	246	27,851
	10 20 30 40 50 60 MFFAVITLFP EMFEAITAYG ISGRAAKRDI VQVTCINPRD FAEGNYRRVD ERPFGGGPGM 70 80 90 100 110 120 VMMAEPLAKA INHAKQLASQ AGCVHVPVVY MSPQGKTLNE QAVQQFVDYD GLIVLCGRYE 130 140 150 160 170 180 GVDERLIQHY VDQEWSIGDY VLSGGELPAM VLLDSIIRRL PNVMSDEQSA IQDSFVDGLL 190 200 210 220 230 240 DCPQYTKPDQ FEGLDVPEIL KSGHHANIEK WRFLQRYQRT LERRPELIEK VALTKQQKKW LSDEQG

References

[1]

"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis." Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M. Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000521 Genomic DNA. Translation: ABO13559.2.
RefSeq	YP_001086161.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A3M9G5.
Genome annotation databases
GeneID	4919390.
GenomeReviews	Gene locus A1S_3162 in contig CP000521_GR.
KEGG	acb:A1S_3162.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0336.
HOGENOM	HBG285805.
Family and domain databases
HAMAP	MF_00605. TrmD. [Tree]
InterPro	IPR016009. tRNA_m1G_MeTrfase. IPR002649. tRNA_m1G_MeTrfase_bac. [Graphical view]
Pfam	PF01746. tRNA_m1G_MT. 1 hit. [Graphical view]
PIRSF	PIRSF000386. tRNA_mtase. 1 hit.
TIGRFAMs	TIGR00088. trmD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

TRMD_ACIBT

Accession

Primary (citable) accession number: A3M9G5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	September 2, 2008
Last modified:	February 9, 2010
This is version 30 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)