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Protein

tRNA (guanine(10)-N2)-methyltransferase

Gene

TRM11

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

Catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + guanine(10) in tRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(10) in tRNA.1 Publication

GO - Molecular functioni

  • RNA binding Source: SGD
  • S-adenosylmethionine-dependent methyltransferase activity Source: SGD
  • tRNA (guanine-N2-)-methyltransferase activity Source: SGD
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

  • tRNA methylation Source: SGD
  • tRNA modification Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine, tRNA-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16616.
YEAST:G3O-33520-MONOMER.
BRENDAi2.1.1.214. 984.
ReactomeiR-SCE-6782315. tRNA modification in the nucleus and cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine(10)-N2)-methyltransferase (EC:2.1.1.214)
Alternative name(s):
tRNA [Gm10] methyltransferase
tRNA guanosine-2'-O-methyltransferase TRM11
tRNA methylase 11
Gene namesi
Name:TRM11
Ordered Locus Names:YOL124C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL124C.
SGDiS000005484. TRM11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: Reactome
  • tRNA (m2G10) methyltransferase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi215 – 2151D → A: Abolishes activity. 1 Publication
Mutagenesisi291 – 2911D → A: Abolishes activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433tRNA (guanine(10)-N2)-methyltransferasePRO_0000270922Add
BLAST

Proteomic databases

MaxQBiQ12463.

Interactioni

Subunit structurei

Interacts with TRM112.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TRM112P537384EBI-30471,EBI-28520

Protein-protein interaction databases

BioGridi34251. 54 interactions.
DIPiDIP-6751N.
IntActiQ12463. 1 interaction.
MINTiMINT-641577.

Structurei

3D structure databases

ProteinModelPortaliQ12463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM11 methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000018131.
HOGENOMiHOG000191866.
InParanoidiQ12463.
KOiK15430.
OMAiIDYNTIH.
OrthoDBiEOG7966SK.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR002052. DNA_methylase_N6_adenine_CS.
IPR000241. RNA_methylase_dom.
IPR029063. SAM-dependent_MTases.
IPR016691. tRNA_mtfrase_TRM11.
[Graphical view]
PfamiPF01170. UPF0020. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
PS51627. SAM_MT_TRM11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12463-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKYLLYMVQ VHLNFRRAEL ESLADLYNLS IDFSQYDANS PFFIVELEND
60 70 80 90 100
QQAKDWIKRS ILTRGIYEYW GQGTTLDELH KDIQRQSNFE QDLQLKFKHS
110 120 130 140 150
TFKFEFECYK GNSKAKRVEQ IETFRYLGFE GKIDMKHPQE VFTVIEEYTP
160 170 180 190 200
ISENVGGKTP TRIYFGRQVQ MSNRSAMEKY DLKKRPYKGT TSFEAELSLV
210 220 230 240 250
SANIAQVKPG TIMYDPFAGT GSFLVAGGHF GSLVIGSDID GRMIRGKGAQ
260 270 280 290 300
VNISANFKKY GESSQFLDVL TMDFTNNALR NNLVIDTILC DPPYGIRESI
310 320 330 340 350
KVLGAKDPER FLGKEDMEID GEKAYLRRDY IPTKKPYALD SLLDDLLQYS
360 370 380 390 400
SERLPIGGRL AFWMPTANDA NIETIVPMHE NLELKYNCVQ EFNKWSRRLL
410 420 430
VYINRGSTFN GSSNHGIKRS KDNFRERYFN NFN
Length:433
Mass (Da):50,073
Last modified:November 1, 1996 - v1
Checksum:i61B291029D55263D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41293 Genomic DNA. Translation: AAC49469.1.
Z74866 Genomic DNA. Translation: CAA99143.1.
BK006948 Genomic DNA. Translation: DAA10660.1.
PIRiS63447.
RefSeqiNP_014517.1. NM_001183378.1.

Genome annotation databases

EnsemblFungiiYOL124C; YOL124C; YOL124C.
GeneIDi853996.
KEGGisce:YOL124C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41293 Genomic DNA. Translation: AAC49469.1.
Z74866 Genomic DNA. Translation: CAA99143.1.
BK006948 Genomic DNA. Translation: DAA10660.1.
PIRiS63447.
RefSeqiNP_014517.1. NM_001183378.1.

3D structure databases

ProteinModelPortaliQ12463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34251. 54 interactions.
DIPiDIP-6751N.
IntActiQ12463. 1 interaction.
MINTiMINT-641577.

Proteomic databases

MaxQBiQ12463.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL124C; YOL124C; YOL124C.
GeneIDi853996.
KEGGisce:YOL124C.

Organism-specific databases

EuPathDBiFungiDB:YOL124C.
SGDiS000005484. TRM11.

Phylogenomic databases

GeneTreeiENSGT00390000018131.
HOGENOMiHOG000191866.
InParanoidiQ12463.
KOiK15430.
OMAiIDYNTIH.
OrthoDBiEOG7966SK.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16616.
YEAST:G3O-33520-MONOMER.
BRENDAi2.1.1.214. 984.
ReactomeiR-SCE-6782315. tRNA modification in the nucleus and cytosol.

Miscellaneous databases

PROiQ12463.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR002052. DNA_methylase_N6_adenine_CS.
IPR000241. RNA_methylase_dom.
IPR029063. SAM-dependent_MTases.
IPR016691. tRNA_mtfrase_TRM11.
[Graphical view]
PfamiPF01170. UPF0020. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
PS51627. SAM_MT_TRM11. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 13.4 kbp fragment from the left arm of chromosome XV reveals a malate dehydrogenase gene, a putative Ser/Thr protein kinase, the ribosomal L25 gene and four new open reading frames."
    Casamayor A., Khalid H., Balcells L., Aldea M., Casas C., Herrero E., Arino J.
    Yeast 12:1013-1020(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TRM112, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-215 AND ASP-291.

Entry informationi

Entry nameiTRM11_YEAST
AccessioniPrimary (citable) accession number: Q12463
Secondary accession number(s): D6W1U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 126 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 2020 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.