tRNA (guanine-N(7)-)-methyltransferase - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot Q12009 (TRMB_YEAST)

Last modified June 16, 2009. Version 69. History...

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

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Names and origin

Protein names

Recommended name:
    tRNA (guanine-N(7)-)-methyltransferase
    EC=2.1.1.33
Alternative name(s):
    tRNA(m7G46)-methyltransferase
    Transfer RNA methyltransferase 8

Gene names

Name:	TRM8
Ordered Locus Names:	YDL201W
ORF Names:	D1075

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Methyltransferase that catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity. Ref.6 Ref.7
Catalytic activity	S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N(7)-methylguanine. Ref.5
Pathway	tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subunit structure	Forms a complex with TRM82. Ref.11
Subcellular location	Nucleus. Ref.3
Miscellaneous	Present with 2630 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the methyltransferase superfamily. TrmB family.

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Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Ligand	RNA-binding S-adenosyl-L-methionine tRNA-binding
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	tRNA methylation Ref.2 Ref.7 Inferred from direct assay. Source: SGD
Cellular component	nucleus Ref.3 Inferred from direct assay. Source: SGD
Molecular function	protein binding Ref.2 Inferred from physical interaction. Source: IntAct tRNA (guanine-N7-)-methyltransferase activity Ref.2 Ref.7 Inferred from electronic annotation. Source: EC tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRM82	Q03774	1	EBI-19552,EBI-19486

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 286

286

tRNA (guanine-N(7)-)-methyltransferase

PRO_0000171437

Regions

Region

126 – 127

S-adenosyl-L-methionine binding

Region

161 – 162

S-adenosyl-L-methionine binding

Region

259 – 261

S-adenosyl-L-methionine binding

Sites

Active site

184

Probable

Binding site

103

S-adenosyl-L-methionine; via carbonyl oxygen

Binding site

181

S-adenosyl-L-methionine; via carbonyl oxygen

Amino acid modifications

Modified residue

Phosphoserine; by ATM or ATR Ref.9 Ref.10

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphoserine Ref.8

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Sequences

Sequence

Length

Mass (Da)

Tools

Q12009-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0280B9A7B02C85B7
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FASTA

286

33,391

        10         20         30         40         50         60 
MKAKPLSQDP GSKRYAYRIN KEENRKELKH VKINESSLVQ EGQKIDLPKK RYYRQRAHSN 

        70         80         90        100        110        120 
PFSDHQLEYP VSPQDMDWSK LYPYYKNAEN GQMTKKVTIA DIGCGFGGLM IDLSPAFPED 

       130        140        150        160        170        180 
LILGMEIRVQ VTNYVEDRII ALRNNTASKH GFQNINVLRG NAMKFLPNFF EKGQLSKMFF 

       190        200        210        220        230        240 
CFPDPHFKQR KHKARIITNT LLSEYAYVLK EGGVVYTITD VKDLHEWMVK HLEEHPLFER 

       250        260        270        280 
LSKEWEENDE CVKIMRNATE EGKKVERKKG DKFVACFTRL PTPAIL

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"Two proteins that form a complex are required for 7-methylguanosine modification of yeast tRNA." Alexandrov A., Martzen M.R., Phizicky E.M. RNA 8:1253-1266(2002) [PubMed: 12403464] [Abstract] Cited for: CHARACTERIZATION, INTERACTION WITH TRM82.
[3]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"tRNA m7G methyltransferase Trm8p/Trm82p: evidence linking activity to a growth phenotype and implicating Trm82p in maintaining levels of active Trm8p." Alexandrov A., Grayhack E.J., Phizicky E.M. RNA 11:821-830(2005) [PubMed: 15811913] [Abstract] Cited for: CATALYTIC ACTIVITY, TRNA-BINDING, INTERACTION WITH TRM82.
[6]	"Rapid tRNA decay can result from lack of nonessential modifications." Alexandrov A., Chernyakov I., Gu W., Hiley S.L., Hughes T.R., Grayhack E.J., Phizicky E.M. Mol. Cell 21:87-96(2006) [PubMed: 16387656] [Abstract] Cited for: FUNCTION.
[7]	"RNA recognition mechanism of eukaryote tRNA (m7G46) methyltransferase (Trm8-Trm82 complex)." Matsumoto K., Toyooka T., Tomikawa C., Ochi A., Takano Y., Takayanagi N., Endo Y., Hori H. FEBS Lett. 581:1599-1604(2007) [PubMed: 17382321] [Abstract] Cited for: FUNCTION.
[8]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, MASS SPECTROMETRY.
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, MASS SPECTROMETRY.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-37, MASS SPECTROMETRY.
[11]	"Structure of the yeast tRNA m7G methylation complex." Leulliot N., Chaillet M., Durand D., Ulryck N., Blondeau K., van Tilbeurgh H. Structure 16:52-61(2008) [PubMed: 18184583] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 29-286 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND TRM82, SUBUNIT, PROBABLE ACTIVE SITE.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X99000 Genomic DNA. Translation: CAA67468.1.
Z74249 Genomic DNA. Translation: CAA98779.1.

PIR

S67760.

RefSeq

NP_010080.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VDU	X-ray	2.40	E/F	39-286	[»]
2VDV	X-ray	2.30	E/F	47-286	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:8614N.

IntAct

Q12009. 1 interaction.

Proteomic databases

PeptideAtlas

Q12009.

Genome annotation databases

Ensembl

YDL201W. Saccharomyces cerevisiae. [Contig view]

GeneID

851326.

GenomeReviews

Gene locus YDL201W in contig Z71256_GR.

KEGG

sce:YDL201W.

NMPDR

fig|4932.3.peg.813.

Organism-specific databases

CYGD

YDL201w.

SGD

S000002360. TRM8.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q12009.

OMA

Q12009. PDPHFKQ.

Enzyme and pathway databases

BRENDA

2.1.1.33. 250.

Gene expression databases

GermOnline

YDL201W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

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

PANTHER

PTHR23417:SF1. Methyltransf_4. 1 hit.

Pfam

PF02390. Methyltransf_4. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00091. CHP91. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

968378.

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Entry information

Entry name

TRMB_YEAST

Accession

Primary (citable) accession number: Q12009

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents