TRM5_YEAST
ID TRM5_YEAST Reviewed; 499 AA.
AC P38793; D3DL19;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=tRNA (guanine(37)-N1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA methyltransferase 5 {ECO:0000255|HAMAP-Rule:MF_03152};
DE Flags: Precursor;
GN Name=TRM5 {ECO:0000255|HAMAP-Rule:MF_03152}; OrderedLocusNames=YHR070W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=11226173; DOI=10.1093/emboj/20.1.231;
RA Bjork G.R., Jacobsson K., Nilsson K., Johansson M.J., Bystroem A.S.,
RA Persson O.P.;
RT "A primordial tRNA modification required for the evolution of life?";
RL EMBO J. 20:231-239(2001).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1-MET--GLN-33.
RX PubMed=17652090; DOI=10.1074/jbc.m704572200;
RA Lee C., Kramer G., Graham D.E., Appling D.R.;
RT "Yeast mitochondrial initiator tRNA is methylated at guanosine 37 by the
RT Trm5-encoded tRNA (guanine-N1-)-methyltransferase.";
RL J. Biol. Chem. 282:27744-27753(2007).
RN [7]
RP FUNCTION.
RX PubMed=18982304; DOI=10.1007/978-1-60327-475-3_25;
RA Jackman J.E., Grayhack E.J., Phizicky E.M.;
RT "The use of Saccharomyces cerevisiae proteomic libraries to identify RNA-
RT modifying proteins.";
RL Methods Mol. Biol. 488:383-393(2008).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21670254; DOI=10.1073/pnas.1105645108;
RA Ohira T., Suzuki T.;
RT "Retrograde nuclear import of tRNA precursors is required for modified base
RT biogenesis in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10502-10507(2011).
CC -!- FUNCTION: Specifically methylates the N1 position of guanosine-37 in
CC various cytoplasmic and mitochondrial tRNAs. Methylation is not
CC dependent on the nature of the nucleoside 5' of the target nucleoside.
CC This is the first step in the biosynthesis of wybutosine (yW), a
CC modified base adjacent to the anticodon of tRNAs and required for
CC accurate decoding. Postspliced cytoplasmic tRNAs are imported into the
CC nucleus, where this first step seems to take place, after which they
CC are reexported to the cytoplasm, where the yW sythesis is completed by
CC cytoplasmic enzymes. {ECO:0000255|HAMAP-Rule:MF_03152,
CC ECO:0000269|PubMed:11226173, ECO:0000269|PubMed:17652090,
CC ECO:0000269|PubMed:18982304, ECO:0000269|PubMed:21670254}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03152};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Nucleus. Cytoplasm.
CC Note=Predominantly in the mitochondria and in the nucleus.
CC -!- MISCELLANEOUS: Present with 4120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: It is unsure how the mitochondrial and cytoplasmic forms
CC of this protein are produced. The cytoplasmic form may be produced by
CC alternative initiation at a downstream in-frame AUG codon at position
CC 34, lacking a mitochondrial transit peptide.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000305}.
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DR EMBL; U00061; AAB68376.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06763.1; -; Genomic_DNA.
DR PIR; S46697; S46697.
DR RefSeq; NP_011937.1; NM_001179200.1.
DR AlphaFoldDB; P38793; -.
DR BioGRID; 36502; 17.
DR DIP; DIP-2950N; -.
DR IntAct; P38793; 6.
DR MINT; P38793; -.
DR STRING; 4932.YHR070W; -.
DR iPTMnet; P38793; -.
DR MaxQB; P38793; -.
DR PaxDb; P38793; -.
DR PRIDE; P38793; -.
DR EnsemblFungi; YHR070W_mRNA; YHR070W; YHR070W.
DR GeneID; 856467; -.
DR KEGG; sce:YHR070W; -.
DR SGD; S000001112; TRM5.
DR VEuPathDB; FungiDB:YHR070W; -.
DR eggNOG; KOG2078; Eukaryota.
DR GeneTree; ENSGT00940000153304; -.
DR HOGENOM; CLU_022610_2_2_1; -.
DR InParanoid; P38793; -.
DR OMA; PKKQMFC; -.
DR BioCyc; MetaCyc:G3O-31120-MON; -.
DR BioCyc; YEAST:G3O-31120-MON; -.
DR BRENDA; 2.1.1.228; 984.
DR PRO; PR:P38793; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38793; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IDA:SGD.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070901; P:mitochondrial tRNA methylation; IDA:SGD.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; TAS:Reactome.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IDA:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03152; TRM5; 1.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025792; tRNA_Gua_MeTrfase_euk.
DR Pfam; PF02475; Met_10; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Mitochondrion; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT CHAIN 45..499
FT /note="tRNA (guanine(37)-N1)-methyltransferase"
FT /id="PRO_0000202899"
FT BINDING 268
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 307..308
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 335..336
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 399
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT MUTAGEN 1..33
FT /note="Missing: Abolishes mitochondrial localization and
FT activity, but not cytoplasmic activity of the enzyme."
FT /evidence="ECO:0000269|PubMed:17652090"
SQ SEQUENCE 499 AA; 56514 MW; 4ADFE01440FF2188 CRC64;
MKIALPVFQK FNRLISSCKM SGVFPYNPPV NRQMRELDRS FFITKIPMCA VKFPEPKNIS
VFSKNFKNCI LRVPRIPHVV KLNSSKPKDE LTSVQNKKLK TADGNNTPVT KGVLLHESIH
SVEDAYGKLP EDALAFLKEN SAEIVPHEYV LDYDFWKAEE ILRAVLPEQF LEEVPTGFTI
TGHIAHLNLR TEFKPFDSLI GQVILDKNNK IECVVDKVSS IATQFRTFPM KVIAGKSDSL
VVEQKESNCT FKFDFSKVYW NSRLHTEHER LVKQYFQPGQ VVCDVFAGVG PFAVPAGKKD
VIVLANDLNP ESYKYLKENI ALNKVAKTVK SFNMDGADFI RQSPQLLQQW IQDEEGGKIT
IPLPLKKRHR SQQHNDQQPP QPRTKELIIP SHISHYVMNL PDSAISFLGN FRGIFAAHTK
GATDTIQMPW VHVHCFEKYP PGDQVTEDEL HARVHARIIA ALKVTADDLP LNAVSLHLVR
KVAPTKPMYC ASFQLPANV
