TRM1/YDR120C Protein Information

Standard Name	Trm1p
Systematic Name	Ydr120cp
ORF Classification	Verified
Description	tRNA methyltransferase; two forms of the protein are made by alternative translation starts; localizes to both the nucleus and mitochondrion to produce the modified base N2,N2-dimethylguanosine in tRNAs in both compartments (1, 2, 3)
Name Description	Transfer RNA Methyltransferase

Experimental Data
Molecules/cell	15500 4

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	570
Molecular Weight (Da)	64,052
Isoelectric Point (pI)	9.79

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Trm1p (InterPro)
Physical Interactions	There are 21 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI00001373EC \| P15565 MIPS: YDR120C NCBI: 136242 \| 172940 \| 398365717 \| 4808559 \| 4808561 \| 747894 \| NP_010405.3 GenBank/EMBL/DDBJ: DAA11966.1 \| AF086825 \| AF086826 \| M17193 \| Z48758
External Classifications	EC: 2.1.1.216 [tRNA (guanine(26)-N(2))-dimethyltransferase]

Amino Acid Sequence (or in FASTA format)
1 MEGFFRIPLK RANLHGMLKA AISKIKANFT AYGAPRINIE DFNIVKEGKA 51 EILFPKKETV FYNPIQQFNR DLSVTCIKAW DNLYGEECGQ KRNNKKSKKK 101 RCAETNDDSS KRQKMGNGSP KEAVGNSNRN EPYINILEAL SATGLRAIRY 151 AHEIPHVREV IANDLLPEAV ESIKRNVEYN SVENIVKPNL DDANVLMYRN 201 KATNNKFHVI DLDPYGTVTP FVDAAIQSIE EGGLMLVTCT DLSVLAGNGY 251 PEKCFALYGG ANMVSHESTH ESALRLVLNL LKQTAAKYKK TVEPLLSLSI 301 DFYVRVFVKV KTSPIEVKNV MSSTMTTYHC SRCGSYHNQP LGRISQREGR 351 NNKTFTKYSV AQGPPVDTKC KFCEGTYHLA GPMYAGPLHN KEFIEEVLRI 401 NKEEHRDQDD TYGTRKRIEG MLSLAKNELS DSPFYFSPNH IASVIKLQVP 451 PLKKVVAGLG SLGFECSLTH AQPSSLKTNA PWDAIWYVMQ KCDDEKKDLS 501 KMNPNTTGYK ILSAMPGWLS GTVKSEYDSK LSFAPNEQSG NIEKLRKLKI 551 VRYQENPTKN WGPKARPNTS *

Amino Acid Sequence (or in FASTA format)

       1  MEGFFRIPLK RANLHGMLKA AISKIKANFT AYGAPRINIE DFNIVKEGKA
      51  EILFPKKETV FYNPIQQFNR DLSVTCIKAW DNLYGEECGQ KRNNKKSKKK
     101  RCAETNDDSS KRQKMGNGSP KEAVGNSNRN EPYINILEAL SATGLRAIRY
     151  AHEIPHVREV IANDLLPEAV ESIKRNVEYN SVENIVKPNL DDANVLMYRN
     201  KATNNKFHVI DLDPYGTVTP FVDAAIQSIE EGGLMLVTCT DLSVLAGNGY
     251  PEKCFALYGG ANMVSHESTH ESALRLVLNL LKQTAAKYKK TVEPLLSLSI
     301  DFYVRVFVKV KTSPIEVKNV MSSTMTTYHC SRCGSYHNQP LGRISQREGR
     351  NNKTFTKYSV AQGPPVDTKC KFCEGTYHLA GPMYAGPLHN KEFIEEVLRI
     401  NKEEHRDQDD TYGTRKRIEG MLSLAKNELS DSPFYFSPNH IASVIKLQVP
     451  PLKKVVAGLG SLGFECSLTH AQPSSLKTNA PWDAIWYVMQ KCDDEKKDLS
     501  KMNPNTTGYK ILSAMPGWLS GTVKSEYDSK LSFAPNEQSG NIEKLRKLKI
     551  VRYQENPTKN WGPKARPNTS *

external links for Trm1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Candida (CGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA

References cited on this page View Complete Literature Guide for Trm1p

1)	Ellis SR, et al. (1989) Amino-terminal extension generated from an upstream AUG codon increases the efficiency of mitochondrial import of yeast N2,N2-dimethylguanosine-specific tRNA methyltransferases. Mol Cell Biol 9(4):1611-20
2)	Ellis SR, et al. (1986) Isolation and characterization of the TRM1 locus, a gene essential for the N2,N2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNA in Saccharomyces cerevisiae. J Biol Chem 261(21):9703-9
3)	Rose AM, et al. (1992) Separate information required for nuclear and subnuclear localization: additional complexity in localizing an enzyme shared by mitochondria and nuclei. Mol Cell Biol 12(12):5652-8
4)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41