CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007010
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 tRNA (guanine(37)-N1)-methyltransferase 
Protein Synonyms/Alias
 M1G-methyltransferase; tRNA [GM37] methyltransferase; tRNA methyltransferase 5 
Gene Name
 TRM5 
Gene Synonyms/Alias
 YHR070W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
64KNISVFSKNFKNCILacetylation[1]
236PMKVIAGKSDSLVVEubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 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. 
Sequence Annotation
 REGION 307 308 S-adenosyl-L-methionine binding (By
 REGION 335 336 S-adenosyl-L-methionine binding (By
 BINDING 268 268 S-adenosyl-L-methionine (By similarity).
 BINDING 399 399 S-adenosyl-L-methionine (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Methyltransferase; Mitochondrion; Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 499 AA 
Protein Sequence
MKIALPVFQK FNRLISSCKM SGVFPYNPPV NRQMRELDRS FFITKIPMCA VKFPEPKNIS 60
VFSKNFKNCI LRVPRIPHVV KLNSSKPKDE LTSVQNKKLK TADGNNTPVT KGVLLHESIH 120
SVEDAYGKLP EDALAFLKEN SAEIVPHEYV LDYDFWKAEE ILRAVLPEQF LEEVPTGFTI 180
TGHIAHLNLR TEFKPFDSLI GQVILDKNNK IECVVDKVSS IATQFRTFPM KVIAGKSDSL 240
VVEQKESNCT FKFDFSKVYW NSRLHTEHER LVKQYFQPGQ VVCDVFAGVG PFAVPAGKKD 300
VIVLANDLNP ESYKYLKENI ALNKVAKTVK SFNMDGADFI RQSPQLLQQW IQDEEGGKIT 360
IPLPLKKRHR SQQHNDQQPP QPRTKELIIP SHISHYVMNL PDSAISFLGN FRGIFAAHTK 420
GATDTIQMPW VHVHCFEKYP PGDQVTEDEL HARVHARIIA ALKVTADDLP LNAVSLHLVR 480
KVAPTKPMYC ASFQLPANV 499 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:EC.
 GO:0016423; F:tRNA (guanine) methyltransferase activity; IGI:SGD. 
Interpro
 IPR025792; tRNA_Gua_MeTrfase_euk.
 IPR003402; tRNA_Trfase_Trm5/Tyw2. 
Pfam
 PF02475; Met_10 
SMART
  
PROSITE
  
PRINTS