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Q03774 (TRM82_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. 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 subunit TRM82
Alternative name(s):
Transfer RNA methyltransferase 82
Gene names
Name:TRM82
Ordered Locus Names:YDR165W
ORF Names:YD8358.19
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 length444 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for 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. In the complex, it is required to stabilize and induce conformational change of the catalytic subunit. Ref.6 Ref.7 Ref.8 Ref.11

Pathway

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

Subunit structure

Forms a complex with TRM8. Ref.11

Subcellular location

Nucleus Ref.4.

Miscellaneous

Present with 5910 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the WD repeat TRM82 family.

Contains 7 WD repeats.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentNucleus
   DomainRepeat
WD repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtRNA methylation

Inferred from direct assay Ref.8. Source: SGD

   Cellular componentnucleus

Inferred from direct assay Ref.4. Source: SGD

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRM8Q120092EBI-19486,EBI-19552

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444tRNA (guanine-N(7)-)-methyltransferase subunit TRM82
PRO_0000051295

Regions

Repeat1 – 4747WD 1
Repeat48 – 9952WD 2
Repeat100 – 14748WD 3
Repeat148 – 19245WD 4
Repeat193 – 23745WD 5
Repeat238 – 27942WD 6
Repeat308 – 35447WD 7

Amino acid modifications

Modified residue671Phosphoserine Ref.9
Modified residue931Phosphoserine Ref.9 Ref.10

Secondary structure

1 ................................................................... 444
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q03774 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F1E0847F44376969

FASTA44450,488
        10         20         30         40         50         60 
MSVIHPLQNL LTSRDGSLVF AIIKNCILSF KYQSPNHWEF AGKWSDDFDK IQESRNTTAK 

        70         80         90        100        110        120 
EQQGQSSENE NENKKLKSNK GDSIKRTAAK VPSPGLGAPP IYSYIRNLRL TSDESRLIAC 

       130        140        150        160        170        180 
ADSDKSLLVF DVDKTSKNVL KLRKRFCFSK RPNAISIAED DTTVIIADKF GDVYSIDINS 

       190        200        210        220        230        240 
IPEEKFTQEP ILGHVSMLTD VHLIKDSDGH QFIITSDRDE HIKISHYPQC FIVDKWLFGH 

       250        260        270        280        290        300 
KHFVSSICCG KDYLLLSAGG DDKIFAWDWK TGKNLSTFDY NSLIKPYLND QHLAPPRFQN 

       310        320        330        340        350        360 
ENNDIIEFAV SKIIKSKNLP FVAFFVEATK CIIILEMSEK QKGDLALKQI ITFPYNVISL 

       370        380        390        400        410        420 
SAHNDEFQVT LDNKESSGVQ KNFAKFIEYN LNENSFVVNN EKSNEFDSAI IQSVQGDSNL 

       430        440 
VTKKEEIYPL YNVSSLRKHG EHYS

« 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 204511 / S288c / AB972.
[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.
[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: FUNCTION, INTERACTION WITH TRM8.
[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]"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-67 AND SER-93, 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-93, 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) IN COMPLEX WITH TRM8, FUNCTION, SUBUNIT, DOMAINS WD REPEATS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z50046 Genomic DNA. Translation: CAA90385.1.
BK006938 Genomic DNA. Translation: DAA12005.1.
PIRS57989.
RefSeqNP_010449.1. NM_001180472.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VDUX-ray2.40B/D1-444[»]
ProteinModelPortalQ03774.
SMRQ03774. Positions 2-436.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-8795N.
IntActQ03774. 4 interactions.
MINTMINT-2782077.
STRINGQ03774.

Proteomic databases

PeptideAtlasQ03774.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR165W; YDR165W; YDR165W.
GeneID851743.
KEGGsce:YDR165W.
NMPDRfig|4932.3.peg.1198.

Organism-specific databases

CYGDYDR165w.
SGDS000002572. TRM82.

Phylogenomic databases

eggNOGfuNOG08053.
GeneTreeEFGT00050000005157.
HOGENOMHBG397716.
OMAMKHPFQI.
OrthoDBEOG4DNJDK.

Gene expression databases

ArrayExpressQ03774.
GenevestigatorQ03774.
GermOnlineYDR165W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KOK15443.
PfamPF00400. WD40. 1 hit.
[Graphical view]
SMARTSM00320. WD40. 3 hits.
[Graphical view]
SUPFAMSSF50978. WD40_like. 1 hit.
PROSITEPS00678. WD_REPEATS_1. False negative.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969484.

Entry information

Entry nameTRM82_YEAST
AccessionPrimary (citable) accession number: Q03774
Secondary accession number(s): D6VSE5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: November 1, 1996
Last modified: January 25, 2012
This is version 89 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