ID A0A3B6NQN0_WHEAT Unreviewed; 462 AA.
AC A0A3B6NQN0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=tRNA (guanine(37)-N1)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
DE EC=2.1.1.228 {ECO:0000256|HAMAP-Rule:MF_03152};
DE AltName: Full=M1G-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA methyltransferase 5 homolog {ECO:0000256|HAMAP-Rule:MF_03152};
GN ORFNames=CFC21_083595 {ECO:0000313|EMBL:KAF7079352.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS6A02G216600.2};
RN [1] {ECO:0000313|EMBL:KAF7079352.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7079352.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS6A02G216600.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS6A02G216600.2};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS6A02G216600.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7079352.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7079352.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_03152};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03152}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-
CC Rule:MF_03152}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03152}. Cytoplasm
CC {ECO:0000256|HAMAP-Rule:MF_03152}. Note=Predominantly in the
CC mitochondria and in the nucleus. {ECO:0000256|HAMAP-Rule:MF_03152}.
CC -!- SIMILARITY: Belongs to the TRM5 / TYW2 family. {ECO:0000256|HAMAP-
CC Rule:MF_03152}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000256|ARBA:ARBA00009775}.
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DR EMBL; CM022226; KAF7079352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6NQN0; -.
DR EnsemblPlants; TraesCS6A02G216600.2; TraesCS6A02G216600.2; TraesCS6A02G216600.
DR Gramene; TraesCS6A02G216600.2; TraesCS6A02G216600.2; TraesCS6A02G216600.
DR Gramene; TraesCS6A03G0594700.1; TraesCS6A03G0594700.1.CDS; TraesCS6A03G0594700.
DR Gramene; TraesKAR6A01G0244990.1; cds.TraesKAR6A01G0244990.1; TraesKAR6A01G0244990.
DR Gramene; TraesRN6A0100568900.1; TraesRN6A0100568900.1; TraesRN6A0100568900.
DR Proteomes; UP000019116; Chromosome 6A.
DR Proteomes; UP000815260; Chromosome 6A.
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)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.30.300.110; Met-10+ protein-like domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 PANTHER; PTHR23245:SF36; TRNA (GUANINE(37)-N1)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23245; TRNA METHYLTRANSFERASE; 1.
DR Pfam; PF02475; Met_10; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03152};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03152};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03152};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03152};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03152};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03152};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03152}.
FT DOMAIN 99..451
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
FT REGION 288..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT BINDING 227..228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT BINDING 255..256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT BINDING 370
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
SQ SEQUENCE 462 AA; 52329 MW; B4BD56946BFFFB04 CRC64;
MEKLDESKFE QQLQLWALRI PRELASAVTR LLRSGSLLDM PRVKPVVEDP GSDKNRLVVL
SEKIQNPDLS DIPEQVHNSL KQLCSVDVVP YMLTLGYSYF SAGHVAHLNI PDDLLAYKDV
IAKVIYDKNY PRIQTVVNKV GAISNEFRVP KFEILAGKKD MVTEVKQYGA TFRLDYGLVY
WNSRLEHEHI RLVSLFKKGD VICDMFAGIG PFSIPARQKG CVVYANDLNP DSIHYLKTNA
KINKVEDYIF TYNMDARVFM QSLMAVPDPE TKSECQFAAA NRCSEEIVSG NEHPTPNGNH
NDVQETWQGS LDGSSMVSTS AKRRQETSSE GDVAGQEDAS QTKKRNNKKV KSSGPLPVKP
WEHIDHVLMN LPASALQFLD CFSGLIQKRY WKGSLPWIHC YCFIRSSETE ESILCEAQNK
LNAKIAEPIF HRVRDVAPNK AMFCLSFRLP VECLKEETED HI
//
