P38793 (TRM5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
tRNA (guanine(37)-N1)-methyltransferase
EC=2.1.1.228

Alternative name(s):
M1G-methyltransferase
tRNA [GM37] methyltransferase
tRNA methyltransferase 5

Gene names

Name:	TRM5
Ordered Locus Names:	YHR070W

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	499 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	Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding. Postspliced cytoplasmic tRNAs are imported into the nucleus, where this first step seems to take place, after which they are reexported to the cytoplasm, where the yW sythesis is completed by cytoplasmic enzymes. Ref.3 Ref.6 Ref.7 Ref.8
Catalytic activity	S-adenosyl-L-methionine + guanine(37) in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion matrix. Nucleus. Cytoplasm. Note: Predominantly in the mitochondria and in the nucleus. Ref.4 Ref.6 Ref.8
Miscellaneous	Present with 4120 molecules/cell in log phase SD medium. Ref.5 It is unsure how the mitochondrial and cytoplasmic forms of this protein are produced. The cytoplasmic form may be produced by alternative initiation at a downstream in-frame AUG codon at position 34, lacking a mitochondrial transit peptide.
Sequence similarities	Belongs to the TRM5 / TYW2 family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Cytoplasm Mitochondrion Nucleus
Domain	Transit peptide
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	mitochondrial matrix Inferred from direct assay Ref.6. Source: SGD nucleus Inferred from direct assay Ref.4. Source: SGD
Molecular function	tRNA (guanine) methyltransferase activity Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-24581,EBI-24581

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 44	44	Mitochondrion Potential
	Chain	45 – 499	455	tRNA (guanine(37)-N1)-methyltransferase		PRO_0000202899
Regions
	Region	307 – 308	2	S-adenosyl-L-methionine binding By similarity
	Region	335 – 336	2	S-adenosyl-L-methionine binding By similarity
Sites
	Binding site	268	1	S-adenosyl-L-methionine By similarity
	Binding site	399	1	S-adenosyl-L-methionine By similarity
Experimental info
	Mutagenesis	1 – 33	33	Missing: Abolishes mitochondrial localization and activity, but not cytoplasmic activity of the enzyme. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P38793 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 4ADFE01440FF2188	FASTA	499	56,514
	10 20 30 40 50 60 MKIALPVFQK FNRLISSCKM SGVFPYNPPV NRQMRELDRS FFITKIPMCA VKFPEPKNIS 70 80 90 100 110 120 VFSKNFKNCI LRVPRIPHVV KLNSSKPKDE LTSVQNKKLK TADGNNTPVT KGVLLHESIH 130 140 150 160 170 180 SVEDAYGKLP EDALAFLKEN SAEIVPHEYV LDYDFWKAEE ILRAVLPEQF LEEVPTGFTI 190 200 210 220 230 240 TGHIAHLNLR TEFKPFDSLI GQVILDKNNK IECVVDKVSS IATQFRTFPM KVIAGKSDSL 250 260 270 280 290 300 VVEQKESNCT FKFDFSKVYW NSRLHTEHER LVKQYFQPGQ VVCDVFAGVG PFAVPAGKKD 310 320 330 340 350 360 VIVLANDLNP ESYKYLKENI ALNKVAKTVK SFNMDGADFI RQSPQLLQQW IQDEEGGKIT 370 380 390 400 410 420 IPLPLKKRHR SQQHNDQQPP QPRTKELIIP SHISHYVMNL PDSAISFLGN FRGIFAAHTK 430 440 450 460 470 480 GATDTIQMPW VHVHCFEKYP PGDQVTEDEL HARVHARIIA ALKVTADDLP LNAVSLHLVR 490 KVAPTKPMYC ASFQLPANV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"A primordial tRNA modification required for the evolution of life?" Bjork G.R., Jacobsson K., Nilsson K., Johansson M.J., Bystroem A.S., Persson O.P. EMBO J. 20:231-239(2001) [PubMed: 11226173] [Abstract] Cited for: FUNCTION.
[4]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"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].
[6]	"Yeast mitochondrial initiator tRNA is methylated at guanosine 37 by the Trm5-encoded tRNA (guanine-N1-)-methyltransferase." Lee C., Kramer G., Graham D.E., Appling D.R. J. Biol. Chem. 282:27744-27753(2007) [PubMed: 17652090] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 1-MET--GLN-33.
[7]	"The use of Saccharomyces cerevisiae proteomic libraries to identify RNA-modifying proteins." Jackman J.E., Grayhack E.J., Phizicky E.M. Methods Mol. Biol. 488:383-393(2008) [PubMed: 18982304] [Abstract] Cited for: FUNCTION.
[8]	"Retrograde nuclear import of tRNA precursors is required for modified base biogenesis in yeast." Ohira T., Suzuki T. Proc. Natl. Acad. Sci. U.S.A. 108:10502-10507(2011) [PubMed: 21670254] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00061 Genomic DNA. Translation: AAB68376.1. BK006934 Genomic DNA. Translation: DAA06763.1.
PIR	S46697.
RefSeq	NP_011937.1. NM_001179200.1.
3D structure databases
ProteinModelPortal	P38793.
SMR	P38793. Positions 179-343.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2950N.
IntAct	P38793. 4 interactions.
MINT	MINT-582793.
STRING	P38793.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR070W; YHR070W; YHR070W.
GeneID	856467.
KEGG	sce:YHR070W.
NMPDR	fig|4932.3.peg.3092.
Organism-specific databases
CYGD	YHR070w.
SGD	S000001112. TRM5.
Phylogenomic databases
eggNOG	fuNOG04366.
GeneTree	EFGT00050000006070.
HOGENOM	HBG592917.
OMA	YVMNLPD.
OrthoDB	EOG4PVS7B.
Gene expression databases
ArrayExpress	P38793.
Genevestigator	P38793.
GermOnline	YHR070W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003402. tRNA_Trfase_Trm5/Tyw2. [Graphical view]
KO	K15429.
Pfam	PF02475. Met_10. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982126.

Entry information

Entry name

TRM5_YEAST

Accession

Primary (citable) accession number: P38793
Secondary accession number(s): D3DL19

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program