P15565 (TRM1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TRM1
Ordered Locus Names:	YDR120C
ORF Names:	YD9727.15C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	2 S-adenosyl-L-methionine + guanine(26) in tRNA = 2 S-adenosyl-L-homocysteine + N(2)-dimethylguanine(26) in tRNA. Ref.2
Subcellular location	Isoform 1: Mitochondrion Ref.5 Ref.8 Ref.9. Isoform 2: Mitochondrion. Nucleus inner membrane; Peripheral membrane protein; Nucleoplasmic side. Note: Predominantly targeted to the nucleus. Ref.5 Ref.8 Ref.9
Post-translational modification	Isoform 2 is N-acetylated by NatC at position 1. N-acetylation is necessary for targeting of the protein to the inner nuclear membrane.
Miscellaneous	Present with 15500 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the TRM1 family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative initiation
Domain	Transit peptide
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	mitochondrion Inferred from direct assay Ref.5. Source: SGD nuclear inner membrane Inferred from direct assay Ref.5. Source: SGD
Molecular function	RNA binding Inferred from electronic annotation. Source: InterPro tRNA (guanine-N2-)-methyltransferase activity Inferred from direct assay Ref.2. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHO1	P08456	1	EBI-19543,EBI-14055
PMP2	P40975	1	EBI-19543,EBI-2043041

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform 1 (identifier: P15565-1)

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.

Isoform 2 (identifier: P15565-2)

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

Note: N-acetylated at position 1.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion
	Chain	? – 570		tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial		PRO_0000035779
Regions
	Region	133 – 155	23	Required and sufficient for inner nuclear membrane localization
	Motif	95 – 101	7	Nuclear localization signal
Amino acid modifications
	Modified residue	17	1	N-acetylmethionine; in isoform 2
Natural variations
	Alternative sequence	1 – 16	16	Missing in isoform 2.		VSP_018902
	Natural variant	203	1	T → S in strain: D4 and YF+.
	Natural variant	467	1	S → L in strain: D4; loss of activity.
	Natural variant	517	1	G → R in strain: D4 and YF+.
Experimental info
	Mutagenesis	290	1	K → A: Loss of activity. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 0AD935838BD90673	FASTA	570	64,052
	10 20 30 40 50 60 MEGFFRIPLK RANLHGMLKA AISKIKANFT AYGAPRINIE DFNIVKEGKA EILFPKKETV 70 80 90 100 110 120 FYNPIQQFNR DLSVTCIKAW DNLYGEECGQ KRNNKKSKKK RCAETNDDSS KRQKMGNGSP 130 140 150 160 170 180 KEAVGNSNRN EPYINILEAL SATGLRAIRY AHEIPHVREV IANDLLPEAV ESIKRNVEYN 190 200 210 220 230 240 SVENIVKPNL DDANVLMYRN KATNNKFHVI DLDPYGTVTP FVDAAIQSIE EGGLMLVTCT 250 260 270 280 290 300 DLSVLAGNGY PEKCFALYGG ANMVSHESTH ESALRLVLNL LKQTAAKYKK TVEPLLSLSI 310 320 330 340 350 360 DFYVRVFVKV KTSPIEVKNV MSSTMTTYHC SRCGSYHNQP LGRISQREGR NNKTFTKYSV 370 380 390 400 410 420 AQGPPVDTKC KFCEGTYHLA GPMYAGPLHN KEFIEEVLRI NKEEHRDQDD TYGTRKRIEG 430 440 450 460 470 480 MLSLAKNELS DSPFYFSPNH IASVIKLQVP PLKKVVAGLG SLGFECSLTH AQPSSLKTNA 490 500 510 520 530 540 PWDAIWYVMQ KCDDEKKDLS KMNPNTTGYK ILSAMPGWLS GTVKSEYDSK LSFAPNEQSG 550 560 570 NIEKLRKLKI VRYQENPTKN WGPKARPNTS
	Isoform 2 [UniParc]. Checksum: 08FFBE80B74C1CEF	FASTA	554	62,184
	10 20 30 40 50 60 MLKAAISKIK ANFTAYGAPR INIEDFNIVK EGKAEILFPK KETVFYNPIQ QFNRDLSVTC 70 80 90 100 110 120 IKAWDNLYGE ECGQKRNNKK SKKKRCAETN DDSSKRQKMG NGSPKEAVGN SNRNEPYINI 130 140 150 160 170 180 LEALSATGLR AIRYAHEIPH VREVIANDLL PEAVESIKRN VEYNSVENIV KPNLDDANVL 190 200 210 220 230 240 MYRNKATNNK FHVIDLDPYG TVTPFVDAAI QSIEEGGLML VTCTDLSVLA GNGYPEKCFA 250 260 270 280 290 300 LYGGANMVSH ESTHESALRL VLNLLKQTAA KYKKTVEPLL SLSIDFYVRV FVKVKTSPIE 310 320 330 340 350 360 VKNVMSSTMT TYHCSRCGSY HNQPLGRISQ REGRNNKTFT KYSVAQGPPV DTKCKFCEGT 370 380 390 400 410 420 YHLAGPMYAG PLHNKEFIEE VLRINKEEHR DQDDTYGTRK RIEGMLSLAK NELSDSPFYF 430 440 450 460 470 480 SPNHIASVIK LQVPPLKKVV AGLGSLGFEC SLTHAQPSSL KTNAPWDAIW YVMQKCDDEK 490 500 510 520 530 540 KDLSKMNPNT TGYKILSAMP GWLSGTVKSE YDSKLSFAPN EQSGNIEKLR KLKIVRYQEN 550 PTKNWGPKAR PNTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3299379] [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: 9801306] [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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 7599275] [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: 10048958] [Abstract] Cited for: MUTAGENESIS OF LYS-290.
[7]	"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].
[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: 15911569] [Abstract] Cited for: ACETYLATION, 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: 19602197] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	A28323.
RefSeq	NP_010405.1. NM_001180428.1.
3D structure databases
ProteinModelPortal	P15565.
SMR	P15565. Positions 42-491.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5202N.
IntAct	P15565. 10 interactions.
MINT	MINT-475232.
STRING	P15565.
Proteomic databases
PeptideAtlas	P15565.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR120C; YDR120C; YDR120C.
GeneID	851698.
KEGG	sce:YDR120C.
NMPDR	fig|4932.3.peg.1154.
Organism-specific databases
CYGD	YDR120c.
SGD	S000002527. TRM1.
Phylogenomic databases
eggNOG	fuNOG07744.
HOGENOM	HBG386594.
OMA	LGGPMWA.
OrthoDB	EOG425925.
Gene expression databases
ArrayExpress	P15565.
Genevestigator	P15565.
GermOnline	YDR120C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002905. TRM_MeTrfase. [Graphical view]
KO	K00555.
PANTHER	PTHR10631. TRM_mtfrase. 1 hit.
Pfam	PF02005. TRM. 1 hit. [Graphical view]
TIGRFAMs	TIGR00308. TRM1. 1 hit.
ProtoNet	Search...
Other
NextBio	969365.

Entry information

Entry name

TRM1_YEAST

Accession

Primary (citable) accession number: P15565
Secondary accession number(s): D6VSA6, Q9URQ7, Q9URQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	December 14, 2011
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program