Reviewed, UniProtKB/Swiss-Prot P43912 (TRMD_HAEIN)

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:	HI0202

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	246 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 – 246

246

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

PRO_0000060385

Regions

Region

133 – 138

6

S-adenosyl-L-methionine binding HAMAP MF_00605

Sites

Active site

169

1

Proton acceptor Potential

Binding site

86

1

S-adenosyl-L-methionine HAMAP MF_00605

Binding site

113

1

S-adenosyl-L-methionine; via amide nitrogen HAMAP MF_00605

Secondary structure

1

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246

Helix Strand Turn

Details...

Beta strand

1 – 6

6

Helix

10 – 13

4

Helix

14 – 17

4

Helix

20 – 27

8

Beta strand

30 – 36

7

Helix

38 – 41

4

Helix

64 – 78

15

Beta strand

83 – 87

5

Beta strand

91 – 93

3

Helix

96 – 102

7

Beta strand

106 – 111

6

Helix

120 – 125

6

Beta strand

128 – 133

6

Helix

142 – 153

12

Beta strand

185 – 187

3

Helix

194 – 197

4

Helix

201 – 219

19

Helix

221 – 223

3

Turn

224 – 226

3

Helix

231 – 245

15

Sequences

	Sequence		Length	Mass (Da)
	P43912-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: DEEF238159B1003D	FASTA	246	27,543
	10 20 30 40 50 60 MWIGVISLFP EMFKAITEFG VTGRAVKHNL LKVECWNPRD FTFDKHKTVD DRPYGGGPGM 70 80 90 100 110 120 LMMVQPLRDA IHTAKAAAGE GAKVIYLSPQ GRKLDQGGVT ELAQNQKLIL VCGRYEGIDE 130 140 150 160 170 180 RLIQTEIDEE WSIGDYVLTG GELPAMTLID AVARFIPGVL GKQASAEEDS FADGLLDCPH 190 200 210 220 230 240 YTRPEVLEGL TVPPVLMSGH HEEIRKWRLK QSLQRTWLRR PELLEGLALT DEQRKLLKEA QAEHNS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition." Ahn H.J., Kim H.-W., Yoon H.-J., Lee B.I., Suh S.W., Yang J.K. EMBO J. 22:2593-2603(2003) [PubMed: 12773376] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L42023 Genomic DNA. Translation: AAC21871.1.

PIR

C64054.

RefSeq

NP_438371.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UAJ	X-ray	1.85	A	1-246	[»]
1UAK	X-ray	2.05	A	1-246	[»]
1UAL	X-ray	1.80	A	1-246	[»]
1UAM	X-ray	2.20	A	1-246	[»]

ModBase

Search...

Genome annotation databases

GeneID

951111.

GenomeReviews

Gene locus HI0202 in contig L42023_GR.

KEGG

hin:HI0202.

TIGR

HI0202.

Phylogenomic databases

HOGENOM

P43912.

OMA

P43912. HRSVDDT.

Enzyme and pathway databases

BioCyc

HINF71421:HI_0202-MON.

BRENDA

2.1.1.31. 109.

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_HAEIN

Accession

Primary (citable) accession number: P43912

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 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)