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Q07527 (TRM3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA (guanosine(18)-2'-O)-methyltransferase

EC=2.1.1.34
Alternative name(s):
tRNA [Gm18] methyltransferase
tRNA methylase 3
Gene names
Name:TRM3
Ordered Locus Names:YDL112W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1436 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically methylates guanosine-18 in various tRNAs. Ref.4

Catalytic activity

S-adenosyl-L-methionine + guanosine18 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA.

Subcellular location

Cytoplasm Ref.5.

Miscellaneous

Present with 861 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the RNA methyltransferase TrmH family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA methylation

Inferred from direct assay Ref.4. Source: SGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

tRNA (guanine) methyltransferase activity

Inferred from direct assay Ref.4. Source: SGD

tRNA (guanosine-2'-O-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14361436tRNA (guanosine(18)-2'-O)-methyltransferase
PRO_0000270921

Regions

Compositional bias1013 – 10197Poly-Leu

Sites

Binding site13891S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site14091S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q07527 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4B14823AF6E858F1

FASTA1,436165,048
        10         20         30         40         50         60 
MVGGALICKY LPREEQLKLI SDLIQNDSLE EVLELIETSP LDITTDSNIE TPIFEKITEQ 

        70         80         90        100        110        120 
VIAYASIDGE AREMFRSSRA EMNKALRTSA QLLCCLPSVW HKFQVWMSYR LNDIISENYK 

       130        140        150        160        170        180 
HLFNDNFGKK IVQPFFDSFA EEQNANIKHE NLHLDILSLL HYLEVVYLFD ECKNGISSKC 

       190        200        210        220        230        240 
LDFIIVPLLG CNSEEIADSC SKLMRWHIKY LSKCCNTDSN FDKLIWTFIK QLYAEGSQQA 

       250        260        270        280        290        300 
WKQKNSLSFL LRFLLAAELS PELITYIKTD AYWRHIQTEL DNDVHEHRKL ALSILKLTIQ 

       310        320        330        340        350        360 
KLSSHGITLQ TTFYKCNDLA NIEMLGSWKK FTTLYEMIAL DTSLNQIQAA KQDIIKIFDN 

       370        380        390        400        410        420 
EHLHHSWGLI LLSTGLKSSM ESVRKYMMTL MFSITNMSAF SSNLPLLTKT LLPAAMSAHY 

       430        440        450        460        470        480 
FDVKGVSCPH GEKLSLFVNN LLSQTTEGIS DILFEILKLL VEKGTSFDPS RIYLSYGILV 

       490        500        510        520        530        540 
FFQNNKQKTI NSDHLSLIRK LYDFAAEEEV LETTIQTIYL KFLLYIDPSV SASELLFTLV 

       550        560        570        580        590        600 
SHIKLKGGTY KYVEPLFEDY RDLAVSHFDD LQAKENLTTN IGKDTIFDLL ASIIFDFKDI 

       610        620        630        640        650        660 
DITPDFLIEV AKSKQDIPVY TSKAVTFLTQ LLSGEPSNGY TYENATALLS YPNFTISTWK 

       670        680        690        700        710        720 
SINVNNLFKS VMEKFSLDKF KFFAEIYQKT YECRFDTIEL NFNDLLSLYE MVKKSANQCS 

       730        740        750        760        770        780 
RESFKVKDSA YSSYFELLNT FLKTYALNRD SSEGNDDELH ILLRLVDENI NKDNGNYLGN 

       790        800        810        820        830        840 
LAVCKLLYFI IDSYIHCSTS VSDDDIFIVK FIFEKFSFIW ECINSERLVL KERDLHLMLI 

       850        860        870        880        890        900 
KGLFHPVILY FGSNQYIDTL TSKLEEHAQT IISLSYSRRS LLPLLGSQLR VFMKFYGKLL 

       910        920        930        940        950        960 
REDVNYWWLI NIIVGVFKQP QMDVNLYKLK PVISSLFDHK LNNYYIKGDE LYEKVYGPDE 

       970        980        990       1000       1010       1020 
ILARVSIIDS ILYANDQLKI RLIEKVTEKT NALYAIKRTD GAEALQRLLQ WQLLLLSLLT 

      1030       1040       1050       1060       1070       1080 
TNEKKLSETS MIRILKSIED ESSPLVRVYK EWFISSKVVD YYKTGNPKFA EDYLFSLLED 

      1090       1100       1110       1120       1130       1140 
HSKPVFVVSA EKICFMVLKD LRNDEKKYGF TQLLDRFICT LVPNAASNKP LVRHFSNSLI 

      1150       1160       1170       1180       1190       1200 
ISLWPTFKAY LSDHTLRNII ENLYSNAKKT QIFGQYRAGD ANIWDLKGDR KLTNMFGGVL 

      1210       1220       1230       1240       1250       1260 
KKVTDHDCPY ISESVFEKYL QEKDIVPIGT DERSLWLDKR DTNTESVNNA NISCDTSPLQ 

      1270       1280       1290       1300       1310       1320 
TKSGAWETVL DLDNKKSNDV VTRSELIVVS SLVDKPPNLG GICRLCDVLG VGLLTVQDIK 

      1330       1340       1350       1360       1370       1380 
VKNHPQFKNV AVTADRWMPM EEVALDEIAS FMKEKKKEGY TLIGLEQTDK SVKLDNNFQF 

      1390       1400       1410       1420       1430 
PKKSLILLGT EAFGIPGTLL SELDLCLEIQ QFGVIRSMNI QTATAVIVHS YTVQHM 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames."
Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G., Jimenez A., Remacha M.A.
Yeast 12:1377-1384(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 955-1436.
Strain: ATCC 96604 / S288c / FY1679.
[4]"The yeast Saccharomyces cerevisiae YDL112w ORF encodes the putative 2'-O-ribose methyltransferase catalyzing the formation of Gm18 in tRNAs."
Cavaille J., Chetouani F., Bachellerie J.-P.
RNA 5:66-81(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z74160 Genomic DNA. Translation: CAA98680.1.
X95644 Genomic DNA. Translation: CAA64900.1.
Z74159 Genomic DNA. Translation: CAA98679.1.
BK006938 Genomic DNA. Translation: DAA11748.1.
PIRS67655.
RefSeqNP_010171.1. NM_001180171.1.

3D structure databases

ProteinModelPortalQ07527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31950. 52 interactions.
DIPDIP-2598N.
IntActQ07527. 5 interactions.
MINTMINT-657104.

Proteomic databases

PaxDbQ07527.
PeptideAtlasQ07527.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL112W; YDL112W; YDL112W.
GeneID851446.
KEGGsce:YDL112W.

Organism-specific databases

CYGDYDL112w.
SGDS000002270. TRM3.

Phylogenomic databases

eggNOGCOG0566.
GeneTreeENSGT00390000003939.
HOGENOMHOG000141850.
KOK15333.
OMAVTADRWM.
OrthoDBEOG7GFBDR.

Enzyme and pathway databases

BioCycYEAST:YDL112W-MONOMER.

Gene expression databases

GenevestigatorQ07527.

Family and domain databases

InterProIPR001537. SpoU_MeTrfase.
IPR025759. tRNA_mtfrase_TRM3.
[Graphical view]
PfamPF00588. SpoU_methylase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968696.

Entry information

Entry nameTRM3_YEAST
AccessionPrimary (citable) accession number: Q07527
Secondary accession number(s): D6VRN8 expand/collapse secondary AC list , P89896, Q05336, Q7LGS3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: April 16, 2014
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 chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families