Reviewed, UniProtKB/Swiss-Prot O67463 (TRMD_AQUAE)

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:	aq_1489

Organism

Aquifex aeolicus [Complete proteome] [HAMAP]

Taxonomic identifier

63363 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	257 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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. Ref.2
Subcellular location	Cytoplasm Potential.
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	3D-structure 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 – 257

257

tRNA (guanine-N(1)-)-methyltransferase HAMAP MF_00605

PRO_0000060317

Regions

Region

134 – 139

6

S-adenosyl-L-methionine binding By similarity

Sites

Binding site

115

1

S-adenosyl-L-methionine; via amide nitrogen By similarity

Secondary structure

1

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257

Helix Strand Turn

Details...

Beta strand

6 – 13

8

Helix

15 – 21

7

Helix

25 – 32

8

Beta strand

35 – 42

8

Helix

43 – 46

4

Beta strand

56 – 58

3

Helix

67 – 81

15

Beta strand

85 – 89

5

Helix

98 – 105

8

Beta strand

108 – 114

7

Helix

122 – 127

6

Beta strand

140 – 142

3

Helix

143 – 155

13

Turn

158 – 160

3

Beta strand

186 – 188

3

Helix

195 – 197

3

Beta strand

201 – 203

3

Turn

204 – 206

3

Helix

207 – 213

7

Turn

214 – 216

3

Helix

217 – 219

3

Helix

228 – 230

3

Turn

231 – 234

4

Sequences

	Sequence		Length	Mass (Da)
	O67463-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: F03ACF8EE2D7EBD5	FASTA	257	29,652
	10 20 30 40 50 60 MSSNPLRFFV LTIFPHIISC YSEYGIVKQA IKKGKVEVYP IDLREFAPKG QVDDVPYGGL 70 80 90 100 110 120 PGMVLKPEPI YEAYDYVVEN YGKPFVLITE PWGEKLNQKL VNELSKKERI MIICGRYEGV 130 140 150 160 170 180 DERVKKIVDM EISLGDFILS GGEIVALAVI DAVSRVLPGV LSEPQSIQED SFQNRWLGYP 190 200 210 220 230 240 VYTRPREYRG MKVPEELLSG HHKLIELWKL WHRIENTVKK RPDLIPKDLT ELEKDILNSI 250 LSGKSFKEWL KEHKHLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
[2]	"Crystal structure of tRNA (m1G37) methyltransferase from Aquifex aeolicus at 2.6 A resolution: a novel methyltransferase fold." Liu J., Wang W., Shin D.H., Yokota H., Kim R., Kim S.-H. Proteins 53:326-328(2003) [PubMed: 14517984] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE000657 Genomic DNA. Translation: AAC07418.1.

PIR

E70429.

RefSeq

NP_214028.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OY5	X-ray	2.60	A/B/C	1-257	[»]

ModBase

Search...

Genome annotation databases

GeneID

1192994.

GenomeReviews

Gene locus aq_1489 in contig AE000657_GR.

KEGG

aae:aq_1489.

NMPDR

fig|224324.1.peg.1043.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

O67463.

OMA

HRSVDDT.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_1489-MON.

BRENDA

2.1.1.31. 189781.

Family and domain databases

HAMAP

MF_00605.
[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.

ProDom

PD004978. tRNA_m1G_mtfrase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00088. trmD. 1 hit.

ProtoNet

Search...

Entry information

Entry name

TRMD_AQUAE

Accession

Primary (citable) accession number: O67463

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 1, 1998
Last modified:	November 3, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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