TRM10_ASHGO
ID TRM10_ASHGO Reviewed; 296 AA.
AC Q75A17;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=tRNA (guanine(9)-N1)-methyltransferase {ECO:0000250|UniProtKB:Q12400};
DE EC=2.1.1.221 {ECO:0000250|UniProtKB:Q12400};
DE AltName: Full=tRNA methyltransferase 10 {ECO:0000250|UniProtKB:Q12400};
DE AltName: Full=tRNA(m1G9)-methyltransferase {ECO:0000250|UniProtKB:Q12400};
DE Short=tRNA(m1G9)MTase {ECO:0000250|UniProtKB:Q12400};
GN Name=TRM10 {ECO:0000250|UniProtKB:Q12400}; OrderedLocusNames=ADR110C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent guanine N(1)-
CC methyltransferase that catalyzes the formation of N(1)-methylguanine at
CC position 9 (m1G9) in cytoplasmic tRNA. {ECO:0000250|UniProtKB:Q12400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC Evidence={ECO:0000250|UniProtKB:Q12400};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O14214}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12400}. Nucleus
CC {ECO:0000250|UniProtKB:Q12400}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
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DR EMBL; AE016817; AAS52030.1; -; Genomic_DNA.
DR RefSeq; NP_984206.1; NM_209559.1.
DR AlphaFoldDB; Q75A17; -.
DR SMR; Q75A17; -.
DR STRING; 33169.AAS52030; -.
DR EnsemblFungi; AAS52030; AAS52030; AGOS_ADR110C.
DR GeneID; 4620377; -.
DR KEGG; ago:AGOS_ADR110C; -.
DR eggNOG; KOG2967; Eukaryota.
DR HOGENOM; CLU_034384_1_0_1; -.
DR InParanoid; Q75A17; -.
DR OMA; FKKNDGW; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR016653; TRM10/TRM10A.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; PTHR13563; 1.
DR PANTHER; PTHR13563:SF13; PTHR13563:SF13; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PIRSF; PIRSF016323; tRNA_m1G_mtfrase_met; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..296
FT /note="tRNA (guanine(9)-N1)-methyltransferase"
FT /id="PRO_0000060509"
FT DOMAIN 85..274
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14214"
FT BINDING 181..182
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 205..209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 239..241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
SQ SEQUENCE 296 AA; 34049 MW; 3C2C10CDBEDE032F CRC64;
MTPETNNDET LSRPKPRAAL PPVPEGMSKS QWKKQWKKEQ FELNKPLYAK IRKEKKQKAR
EQRRERLQKA LEENGGEIPE ELRRTPRVNV NQKDSGIKVI IDCAFDELMN EKEIVSLSTQ
ITRAYSANKR ENHFADVKVT SFNKRLKERF DCGLKGANYD AWKHFEFTDE SALPTTNAVY
LTADTDETLE TLEPGTTYIV GGIVDKNRHK ALCYNKAKEL GIPTRRLPIG EYIKLCGRKV
LTTTHVIQIM LRYFDNHDWK EAFESVLPAR KLAELADHAQ ESNSSSPAEE QDAQDI
