TRM51_VITVI
ID TRM51_VITVI Reviewed; 608 AA.
AC F6H2F8;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=tRNA (guanine(37)-N1)-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03152};
DE EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=M1G-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA [GM37] methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA methyltransferase 5 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03152};
GN OrderedLocusNames=VIT_19s0014g03930;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024;
RX PubMed=17721507; DOI=10.1038/nature06148;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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. {ECO:0000255|HAMAP-Rule:MF_03152}.
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 {ECO:0000255|HAMAP-
CC Rule:MF_03152}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the
CC mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000305}.
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DR EMBL; FN595229; CCB46402.1; -; Genomic_DNA.
DR EMBL; FN597046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002284299.1; XM_002284263.3.
DR AlphaFoldDB; F6H2F8; -.
DR SMR; F6H2F8; -.
DR STRING; 29760.VIT_19s0014g03930.t01; -.
DR EnsemblPlants; Vitvi19g00319_t001; Vitvi19g00319_P001; Vitvi19g00319.
DR GeneID; 100241770; -.
DR Gramene; Vitvi19g00319_t001; Vitvi19g00319_P001; Vitvi19g00319.
DR KEGG; vvi:100241770; -.
DR eggNOG; KOG2078; Eukaryota.
DR HOGENOM; CLU_034422_1_0_1; -.
DR InParanoid; F6H2F8; -.
DR OrthoDB; 788980at2759; -.
DR Proteomes; UP000009183; Chromosome 19.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Mitochondrion; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..608
FT /note="tRNA (guanine(37)-N1)-methyltransferase 1"
FT /id="PRO_0000414140"
FT REGION 207..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 463..464
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 491..492
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 514
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ SEQUENCE 608 AA; 69213 MW; E1B11A88B9DE8B04 CRC64;
MVTKLFLRPH SLSFTLLSGI HLFPKTSLSK PITLCLLSTT ATTPILTLTQ TLDPNLSYGP
SLHKGTKPLN HQNHQLIAAT PGEEECVFDK EAFTRVFNLT AIRVPSKDCF ALENRLRGHL
LNWPRIRNVA RVPGDEVEDG LVKLLGEKRN SSDGSESEGD FDSLNRRIYG KAEGDGEILS
PVLYRDTLAK TFDSQGFANF RNLAKLSRPK KKKRRKEEER SEGKKRTGKN EFAMVEVVED
GEEGEDLRGL LGEEFKRKRW RGSTRLLLLD ERYADKGVEE LPEAIKAVLK EDTGQSMTST
FELVKCKLTL FYNYWQMNEI LEALLPEGMI VPSAFEMVGH IAHLNLRDEH LPYKKLIAKV
VLDKNKPKIQ TVVNKTDAIH NDYRTMQLEV LAGNRSLVTT VIENGMRFQV DLATVYWNSR
LATERQRLLN CFTRNDVVCD VFSGVGPIAI SAAKKVKRVY ANDLNPYAIE YLESNSVLNK
LERKIKVFNM DGRRFINAMF TSDKAESITQ VVMNLPNDAA EFLDAFRGIF RKKSRDKQLK
LPMIHVYGFS KAQDPEFDFH QRIRIALSEV AVDVEMHRVR LVAPGKWMLR ASFILPKSVV
FAKAVLYM
