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Protein

eRF1 methyltransferase catalytic subunit MTQ2

Gene

MTQ2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Methylates eRF1 on 'Gln-182' using S-adenosyl L-methionine as methyl donor. eRF1 needs to be complexed to eRF3 in its GTP-bound form to be efficiently methylated.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei77 – 771S-adenosyl-L-methionineBy similarity
Binding sitei122 – 1221S-adenosyl-L-methionineBy similarity

GO - Molecular functioni

  • nucleic acid binding Source: InterPro
  • protein methyltransferase activity Source: SGD
  • S-adenosylmethionine-dependent methyltransferase activity Source: SGD

GO - Biological processi

  • peptidyl-glutamine methylation Source: SGD
  • regulation of translation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-29737-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
eRF1 methyltransferase catalytic subunit MTQ2 (EC:2.1.1.-)
Short name:
eRF1 MTase catalytic subunit MTQ2
Alternative name(s):
N(5)-glutamine methyltransferase MTQ2
Gene namesi
Name:MTQ2
Synonyms:MTC6
Ordered Locus Names:YDR140W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR140W.
SGDiS000002547. MTQ2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • eRF1 methyltransferase complex Source: SGD
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 221221eRF1 methyltransferase catalytic subunit MTQ2PRO_0000245840Add
BLAST

Proteomic databases

MaxQBiQ03920.
PeptideAtlasiQ03920.

Interactioni

Subunit structurei

Heterodimer of MTQ2-TRM112. MTQ2 is the catalytic subunit carrying the catalytic and the S-adenosyl L-methionine binding sites.

Binary interactionsi

WithEntry#Exp.IntActNotes
TRM112P537384EBI-31378,EBI-28520

Protein-protein interaction databases

BioGridi32194. 16 interactions.
DIPiDIP-1755N.
IntActiQ03920. 5 interactions.
MINTiMINT-405233.

Structurei

3D structure databases

ProteinModelPortaliQ03920.
SMRiQ03920. Positions 15-208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 545S-adenosyl-L-methionine bindingBy similarity
Regioni122 – 1254Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000013073.
HOGENOMiHOG000219949.
InParanoidiQ03920.
KOiK19589.
OMAiVICLEIG.
OrthoDBiEOG7KM64K.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR002052. DNA_methylase_N6_adenine_CS.
IPR004557. PrmC-related.
IPR029063. SAM-dependent_MTases.
IPR007848. Small_mtfrase_dom.
[Graphical view]
PfamiPF05175. MTS. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00537. hemK_rel_arch. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03920-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPTPYVKCD YDKVYEPAED SFLILDCLEK EHDFLKQKFG NRLAIVCEIG
60 70 80 90 100
SGSGIVTTFL MQNKIIPQEN SIHLAVDINP WALEATLDTA KLNSCKSSFL
110 120 130 140 150
EVIQADLNSS IRNNQVDVLI FNPPYVPAEC VPDVPGSREE ADQWLDLALL
160 170 180 190 200
GGKDGMAITD KLLRQLEQIL SPDGVAYILF CARNKPKEVI KRFVDTYKWN
210 220
VKLIETRKAG WEVLSVYSFT R
Length:221
Mass (Da):24,973
Last modified:November 1, 1996 - v1
Checksum:iC3CF6BF6A05E862D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48179 Genomic DNA. Translation: CAA88222.1.
AY557676 Genomic DNA. Translation: AAS56002.1.
BK006938 Genomic DNA. Translation: DAA11983.1.
PIRiS51868.
RefSeqiNP_010424.3. NM_001180447.3.

Genome annotation databases

EnsemblFungiiYDR140W; YDR140W; YDR140W.
GeneIDi851718.
KEGGisce:YDR140W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48179 Genomic DNA. Translation: CAA88222.1.
AY557676 Genomic DNA. Translation: AAS56002.1.
BK006938 Genomic DNA. Translation: DAA11983.1.
PIRiS51868.
RefSeqiNP_010424.3. NM_001180447.3.

3D structure databases

ProteinModelPortaliQ03920.
SMRiQ03920. Positions 15-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32194. 16 interactions.
DIPiDIP-1755N.
IntActiQ03920. 5 interactions.
MINTiMINT-405233.

Proteomic databases

MaxQBiQ03920.
PeptideAtlasiQ03920.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR140W; YDR140W; YDR140W.
GeneIDi851718.
KEGGisce:YDR140W.

Organism-specific databases

EuPathDBiFungiDB:YDR140W.
SGDiS000002547. MTQ2.

Phylogenomic databases

GeneTreeiENSGT00390000013073.
HOGENOMiHOG000219949.
InParanoidiQ03920.
KOiK19589.
OMAiVICLEIG.
OrthoDBiEOG7KM64K.

Enzyme and pathway databases

BioCyciYEAST:G3O-29737-MONOMER.

Miscellaneous databases

NextBioi969418.
PROiQ03920.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR002052. DNA_methylase_N6_adenine_CS.
IPR004557. PrmC-related.
IPR029063. SAM-dependent_MTases.
IPR007848. Small_mtfrase_dom.
[Graphical view]
PfamiPF05175. MTS. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00537. hemK_rel_arch. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "The glutamine residue of the conserved GGQ motif in Saccharomyces cerevisiae release factor eRF1 is methylated by the product of the YDR140w gene."
    Heurgue-Hamard V., Champ S., Mora L., Merkulova-Rainon T., Kisselev L.L., Buckingham R.H.
    J. Biol. Chem. 280:2439-2445(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Trm11p and Trm112p are both required for the formation of 2-methylguanosine at position 10 in yeast tRNA."
    Purushothaman S.K., Bujnicki J.M., Grosjean H., Lapeyre B.
    Mol. Cell. Biol. 25:4359-4370(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRM112.
  8. "The yeast translation release factors Mrf1p and Sup45p (eRF1) are methylated, respectively, by the methyltransferases Mtq1p and Mtq2p."
    Polevoda B., Span L., Sherman F.
    J. Biol. Chem. 281:2562-2571(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "The zinc finger protein Ynr046w is plurifunctional and a component of the eRF1 methyltransferase in yeast."
    Heurgue-Hamard V., Graille M., Scrima N., Ulryck N., Champ S., van Tilbeurgh H., Buckingham R.H.
    J. Biol. Chem. 281:36140-36148(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRM112.

Entry informationi

Entry nameiMTQ2_YEAST
AccessioniPrimary (citable) accession number: Q03920
Secondary accession number(s): D6VSC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3390 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.