tRNA (guanine-N(7)-)-methyltransferase - Escherichia coli (strain K12)

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P0A8I5 (TRMB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
tRNA (guanine-N(7)-)-methyltransferase
EC=2.1.1.33

Alternative name(s):
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase

Gene names

Name:	trmB
Synonyms:	trmI, yggH
Ordered Locus Names:	b2960, JW2927

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	239 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. HAMAP-Rule MF_01057
Catalytic activity	S-adenosyl-L-methionine + guanine₄₆ in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine₄₆ in tRNA. Ref.4
Pathway	tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_01057
Subunit structure	Monomer. Ref.4
Sequence similarities	Belongs to the methyltransferase superfamily. TrmB family.
Sequence caution	The sequence AAA72956.1 differs from that shown. Reason: Frameshift at position 29.

Ontologies

Keywords
Biological process	tRNA processing
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA (guanine-N7)-methylation Inferred from electronic annotation. Source: GOC
Molecular_function	tRNA (guanine-N7-)-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 – 239

239

tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057

PRO_0000171326

Regions

Region

150 – 155

Interaction with RNA Potential

Region

217 – 220

Substrate binding Potential

Sites

Binding site

S-adenosyl-L-methionine By similarity

Binding site

S-adenosyl-L-methionine By similarity

Binding site

121

S-adenosyl-L-methionine By similarity

Binding site

144

S-adenosyl-L-methionine By similarity

Binding site

148

Substrate By similarity

Binding site

180

Substrate Potential

Experimental info

Mutagenesis

R → A: Reduces catalytic activity over 10-fold. Ref.5

Mutagenesis

144

D → A: Loss of activity. Ref.5

Mutagenesis

150

R → A: Reduces catalytic activity about 3-fold. Ref.5

Mutagenesis

151

H → A: Reduces catalytic activity over 10-fold. Ref.5

Mutagenesis

152

N → A: No effect. Ref.5

Mutagenesis

154

R → A: Loss of activity. Ref.5

Mutagenesis

155

R → A: Loss of activity. Ref.5

Mutagenesis

180

D → A: Reduces catalytic activity over 10-fold. Ref.5

Mutagenesis

217

T → A: Reduces catalytic activity over 10-fold. Ref.5

Mutagenesis

220

E → A: Reduces catalytic activity 10-fold. Ref.5

Secondary structure

239

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A8I5 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: B4C8AF9A1EF85FEB
Show »

FASTA

239

27,307

        10         20         30         40         50         60 
MKNDVISPEF DENGRPLRRI RSFVRRQGRL TKGQEHALEN YWPVMGVEFS EDMLDFPALF 

        70         80         90        100        110        120 
GREAPVTLEI GFGMGASLVA MAKDRPEQDF LGIEVHSPGV GACLASAHEE GLSNLRVMCH 

       130        140        150        160        170        180 
DAVEVLHKMI PDNSLRMVQL FFPDPWHKAR HNKRRIVQVP FAELVKSKLQ LGGVFHMATD 

       190        200        210        220        230 
WEPYAEHMLE VMSSIDGYKN LSESNDYVPR PASRPVTKFE QRGHRLGHGV WDLMFERVK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the Escherichia coli micA gene required for A/G-specific mismatch repair: identity of micA and mutY." Tsai-Wu J.-J., Radicella J.P., Lu A.-L. J. Bacteriol. 173:1902-1910(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The yggH gene of Escherichia coli encodes a tRNA (m7G46) methyltransferase." De Bie L.G.S., Roovers M., Oudjama Y., Wattiez R., Tricot C., Stalon V., Droogmans L., Bujnicki J.M. J. Bacteriol. 185:3238-3243(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBUNIT. Strain: K12 / XL1-Blue.
[5]	"Sequence-structure-function relationships of a tRNA (m7G46) methyltransferase studied by homology modeling and site-directed mutagenesis." Purta E., van Vliet F., Tricot C., De Bie L.G., Feder M., Skowronek K., Droogmans L., Bujnicki J.M. Proteins 59:482-488(2005) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ARG-26; ASP-144; ARG-150; HIS-151; ASN-152; ARG-154; ARG-155; ASP-180; THR-217 AND GLU-220.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M59471 Genomic DNA. Translation: AAA72956.1. Frameshift.
U28377 Genomic DNA. Translation: AAA69127.1.
U00096 Genomic DNA. Translation: AAC75997.1.
AP009048 Genomic DNA. Translation: BAE77023.1.

PIR

G65081.

RefSeq

NP_417435.1. NC_000913.2.
YP_491159.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DXX	X-ray	2.05	A	33-239	[»]
3DXY	X-ray	1.50	A	33-239	[»]
3DXZ	X-ray	1.58	A	33-239	[»]

ProteinModelPortal

P0A8I5.

SMR

P0A8I5. Positions 36-239.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36015N.

IntAct

P0A8I5. 45 interactions.

STRING

511145.b2960.

Proteomic databases

PaxDb

P0A8I5.

PRIDE

P0A8I5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75997; AAC75997; b2960.
BAE77023; BAE77023; BAE77023.

GeneID

12933364.
947448.

KEGG

ecj:Y75_p2890.
eco:b2960.

PATRIC

32121334. VBIEscCol129921_3055.

Organism-specific databases

EchoBASE

EB1727.

EcoGene

EG11779. trmI.

Phylogenomic databases

eggNOG

COG0220.

HOGENOM

HOG000073968.

K03439.

OMA

CEVHEPG.

ProtClustDB

PRK00121.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11779-MONOMER.
ECOL316407:JW2927-MONOMER.
MetaCyc:EG11779-MONOMER.

UniPathway

UPA00989.

Gene expression databases

Genevestigator

P0A8I5.

Family and domain databases

HAMAP

MF_01057. tRNA_methyltr_TrmB.

InterPro

IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]

Pfam

PF02390. Methyltransf_4. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00091. TIGR00091. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A8I5.

Entry information

Entry name

TRMB_ECOLI

Accession

Primary (citable) accession number: P0A8I5
Secondary accession number(s): P32049, P58089, Q2M9N3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents