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Q12009 (TRMB_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA (guanine-N(7)-)-methyltransferase
EC=2.1.1.33
Alternative name(s):
Transfer RNA methyltransferase 8
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase
Gene names
Name:TRM8
Ordered Locus Names:YDL201W
ORF Names:D1075
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.7 Ref.8

Catalytic activity

S-adenosyl-L-methionine + guanine(46) in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA. Ref.6

Pathway

tRNA modification; N(7)-methylguanine-tRNA biosynthesis.

Subunit structure

Forms a complex with TRM82. Ref.12

Subcellular location

Nucleus Ref.4.

Miscellaneous

Present with 2630 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the methyltransferase superfamily. TrmB family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRM82Q037742EBI-19552,EBI-19486

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286tRNA (guanine-N(7)-)-methyltransferase
PRO_0000171437

Regions

Region126 – 1272S-adenosyl-L-methionine binding
Region161 – 1622S-adenosyl-L-methionine binding
Region259 – 2613S-adenosyl-L-methionine binding

Sites

Active site1841 Probable
Binding site1031S-adenosyl-L-methionine; via carbonyl oxygen
Binding site1811S-adenosyl-L-methionine; via carbonyl oxygen

Amino acid modifications

Modified residue71Phosphoserine; by ATM or ATR Ref.10 Ref.11
Modified residue371Phosphoserine Ref.11
Modified residue591Phosphoserine Ref.9

Secondary structure

1 ................................... 286
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12009 [UniParc].

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

FASTA28633,391
        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

References

« Hide '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. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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.
[4]"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].
[5]"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].
[6]"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.
[7]"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.
[8]"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.
[9]"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.
Strain: ADR376.
[10]"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.
[11]"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.
[12]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X99000 Genomic DNA. Translation: CAA67468.1.
Z74249 Genomic DNA. Translation: CAA98779.1.
BK006938 Genomic DNA. Translation: DAA11663.1.
PIRS67760.
RefSeqNP_010080.1. NM_001180261.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VDUX-ray2.40E/F39-286[»]
2VDVX-ray2.30E/F47-286[»]
ProteinModelPortalQ12009.
SMRQ12009. Positions 60-286.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-8614N.
IntActQ12009. 1 interaction.
MINTMINT-2782058.
STRINGQ12009.

Proteomic databases

PeptideAtlasQ12009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL201W; YDL201W; YDL201W.
GeneID851326.
KEGGsce:YDL201W.
NMPDRfig|4932.3.peg.813.

Organism-specific databases

CYGDYDL201w.
SGDS000002360. TRM8.

Phylogenomic databases

eggNOGfuNOG04894.
GeneTreeEFGT00050000004745.
HOGENOMHBG324627.
OMAIGMEIRV.
OrthoDBEOG4M3DJF.

Gene expression databases

ArrayExpressQ12009.
GenevestigatorQ12009.
GermOnlineYDL201W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
KOK03439.
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
ProtoNetSearch...

Other

NextBio968378.

Entry information

Entry nameTRMB_YEAST
AccessionPrimary (citable) accession number: Q12009
Secondary accession number(s): D6VRF3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

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

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents