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Protein

tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial

Gene

TRM1

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

Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. Required for the modification of both mitochondrial and cytoplasmic tRNAs.

Catalytic activityi

2 S-adenosyl-L-methionine + guanine(26) in tRNA = 2 S-adenosyl-L-homocysteine + N(2)-dimethylguanine(26) in tRNA.PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  • tRNA (guanine-N2-)-methyltransferase activity Source: SGD
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

  • tRNA methylation Source: SGD
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

BioCyciYEAST:G3O-29720-MONOMER.
BRENDAi2.1.1.216. 5243.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial (EC:2.1.1.216)
Alternative name(s):
tRNA 2,2-dimethylguanosine-26 methyltransferase
tRNA(guanine-26,N(2)-N(2)) methyltransferase
tRNA(m(2,2)G26)dimethyltransferase
Gene namesi
Name:TRM1
Ordered Locus Names:YDR120C
ORF Names:YD9727.15C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR120C.
SGDiS000002527. TRM1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
  • nuclear envelope Source: SGD
  • nuclear inner membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi290 – 2901K → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 570tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrialPRO_0000035779
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 2 (identifier: P15565-2)
Modified residuei1 – 11N-acetylmethionine

Post-translational modificationi

Isoform 2 is N-acetylated by NatC at position 1. N-acetylation is necessary for targeting of the protein to the inner nuclear membrane.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP15565.
PeptideAtlasiP15565.

PTM databases

iPTMnetiP15565.

Interactioni

Protein-protein interaction databases

BioGridi32176. 95 interactions.
DIPiDIP-5202N.
IntActiP15565. 8 interactions.
MINTiMINT-475232.

Structurei

3D structure databases

ProteinModelPortaliP15565.
SMRiP15565. Positions 45-483.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 489447Trm1 methyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 15523Required and sufficient for inner nuclear membrane localizationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi95 – 1017Nuclear localization signal

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.PROSITE-ProRule annotation
Contains 1 Trm1 methyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000063646.
HOGENOMiHOG000177995.
InParanoidiP15565.
KOiK00555.
OMAiESHANRH.
OrthoDBiEOG78D7VT.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR002905. Trm1.
[Graphical view]
PANTHERiPTHR10631. PTHR10631. 1 hit.
PfamiPF02005. TRM. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 3 hits.
TIGRFAMsiTIGR00308. TRM1. 1 hit.
PROSITEiPS51626. SAM_MT_TRM1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P15565-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEGFFRIPLK RANLHGMLKA AISKIKANFT AYGAPRINIE DFNIVKEGKA
60 70 80 90 100
EILFPKKETV FYNPIQQFNR DLSVTCIKAW DNLYGEECGQ KRNNKKSKKK
110 120 130 140 150
RCAETNDDSS KRQKMGNGSP KEAVGNSNRN EPYINILEAL SATGLRAIRY
160 170 180 190 200
AHEIPHVREV IANDLLPEAV ESIKRNVEYN SVENIVKPNL DDANVLMYRN
210 220 230 240 250
KATNNKFHVI DLDPYGTVTP FVDAAIQSIE EGGLMLVTCT DLSVLAGNGY
260 270 280 290 300
PEKCFALYGG ANMVSHESTH ESALRLVLNL LKQTAAKYKK TVEPLLSLSI
310 320 330 340 350
DFYVRVFVKV KTSPIEVKNV MSSTMTTYHC SRCGSYHNQP LGRISQREGR
360 370 380 390 400
NNKTFTKYSV AQGPPVDTKC KFCEGTYHLA GPMYAGPLHN KEFIEEVLRI
410 420 430 440 450
NKEEHRDQDD TYGTRKRIEG MLSLAKNELS DSPFYFSPNH IASVIKLQVP
460 470 480 490 500
PLKKVVAGLG SLGFECSLTH AQPSSLKTNA PWDAIWYVMQ KCDDEKKDLS
510 520 530 540 550
KMNPNTTGYK ILSAMPGWLS GTVKSEYDSK LSFAPNEQSG NIEKLRKLKI
560 570
VRYQENPTKN WGPKARPNTS
Length:570
Mass (Da):64,052
Last modified:April 1, 1990 - v1
Checksum:i0AD935838BD90673
GO
Isoform 2 (identifier: P15565-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.

Show »
Length:554
Mass (Da):62,184
Checksum:i08FFBE80B74C1CEF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti203 – 2031T → S in strain: D4 and YF+.
Natural varianti467 – 4671S → L in strain: D4; loss of activity.
Natural varianti517 – 5171G → R in strain: D4 and YF+.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1616Missing in isoform 2. CuratedVSP_018902Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17193 Genomic DNA. Translation: AAA35150.1.
AF086825 Genomic DNA. Translation: AAD29858.1.
AF086826 Genomic DNA. Translation: AAD29859.1.
Z48758 Genomic DNA. Translation: CAA88673.1.
BK006938 Genomic DNA. Translation: DAA11966.1.
PIRiA28323.
RefSeqiNP_010405.3. NM_001180428.3. [P15565-1]

Genome annotation databases

EnsemblFungiiYDR120C; YDR120C; YDR120C. [P15565-1]
GeneIDi851698.
KEGGisce:YDR120C.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17193 Genomic DNA. Translation: AAA35150.1.
AF086825 Genomic DNA. Translation: AAD29858.1.
AF086826 Genomic DNA. Translation: AAD29859.1.
Z48758 Genomic DNA. Translation: CAA88673.1.
BK006938 Genomic DNA. Translation: DAA11966.1.
PIRiA28323.
RefSeqiNP_010405.3. NM_001180428.3. [P15565-1]

3D structure databases

ProteinModelPortaliP15565.
SMRiP15565. Positions 45-483.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32176. 95 interactions.
DIPiDIP-5202N.
IntActiP15565. 8 interactions.
MINTiMINT-475232.

PTM databases

iPTMnetiP15565.

Proteomic databases

MaxQBiP15565.
PeptideAtlasiP15565.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR120C; YDR120C; YDR120C. [P15565-1]
GeneIDi851698.
KEGGisce:YDR120C.

Organism-specific databases

EuPathDBiFungiDB:YDR120C.
SGDiS000002527. TRM1.

Phylogenomic databases

GeneTreeiENSGT00530000063646.
HOGENOMiHOG000177995.
InParanoidiP15565.
KOiK00555.
OMAiESHANRH.
OrthoDBiEOG78D7VT.

Enzyme and pathway databases

BioCyciYEAST:G3O-29720-MONOMER.
BRENDAi2.1.1.216. 5243.

Miscellaneous databases

NextBioi969365.
PROiP15565.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR002905. Trm1.
[Graphical view]
PANTHERiPTHR10631. PTHR10631. 1 hit.
PfamiPF02005. TRM. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 3 hits.
TIGRFAMsiTIGR00308. TRM1. 1 hit.
PROSITEiPS51626. SAM_MT_TRM1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amino-terminal extension generated from an upstream AUG codon is not required for mitochondrial import of yeast N2,N2-dimethylguanosine-specific tRNA methyltransferase."
    Ellis S.R., Hopper A.K., Martin N.C.
    Proc. Natl. Acad. Sci. U.S.A. 84:5172-5176(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE INITIATION.
  2. "Point and deletion mutations eliminate one or both methyl group transfers catalysed by the yeast TRM1 encoded tRNA (m22G26)dimethyltransferase."
    Liu J., Liu J., Straby K.B.
    Nucleic Acids Res. 26:5102-5108(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY.
    Strain: D4 and YF+.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Location of N2,N2-dimethylguanosine-specific tRNA methyltransferase."
    Rose A.M., Belford H.G., Shen W.C., Greer C.L., Hopper A.K., Martin N.C.
    Biochimie 77:45-53(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Caenorhabditis elegans ZC376.5 encodes a tRNA (m2/2G(26))dimethyltransferance in which (246)arginine is important for the enzyme activity."
    Liu J.M., Zhou G.Q., Straby K.B.
    Gene 226:73-81(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-290.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Genome-wide screen for inner nuclear membrane protein targeting in Saccharomyces cerevisiae: roles for N-acetylation and an integral membrane protein."
    Murthi A., Hopper A.K.
    Genetics 170:1553-1560(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT MET-1 (ISOFORM 2), SUBCELLULAR LOCATION.
  9. "Mechanism and a peptide motif for targeting peripheral proteins to the yeast inner nuclear membrane."
    Lai T.P., Stauffer K.A., Murthi A., Shaheen H.H., Peng G., Martin N.C., Hopper A.K.
    Traffic 10:1243-1256(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiTRM1_YEAST
AccessioniPrimary (citable) accession number: P15565
Secondary accession number(s): D6VSA6, Q9URQ7, Q9URQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 11, 2016
This is version 158 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 15500 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.