TRM10_CANAL
ID TRM10_CANAL Reviewed; 323 AA.
AC Q59Q39; A0A1D8PHS2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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};
GN OrderedLocusNames=CAALFM_C206480WA; ORFNames=CaO19.25, CaO19.7696;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017624; AOW27652.1; -; Genomic_DNA.
DR RefSeq; XP_711832.1; XM_706740.1.
DR AlphaFoldDB; Q59Q39; -.
DR SMR; Q59Q39; -.
DR STRING; 237561.Q59Q39; -.
DR PRIDE; Q59Q39; -.
DR GeneID; 3646568; -.
DR KEGG; cal:CAALFM_C206480WA; -.
DR CGD; CAL0000179584; orf19.7696.
DR VEuPathDB; FungiDB:C2_06480W_A; -.
DR eggNOG; KOG2967; Eukaryota.
DR HOGENOM; CLU_034384_1_0_1; -.
DR InParanoid; Q59Q39; -.
DR OMA; FKKNDGW; -.
DR OrthoDB; 1396299at2759; -.
DR PRO; PR:Q59Q39; -.
DR Proteomes; UP000000559; Chromosome 2.
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..323
FT /note="tRNA (guanine(9)-N1)-methyltransferase"
FT /id="PRO_0000060511"
FT DOMAIN 99..319
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14214"
FT BINDING 225..226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 245
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 249..253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 257
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 271
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 283..285
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
SQ SEQUENCE 323 AA; 37760 MW; FFBC5E16F5B11B6A CRC64;
MTEQTSEATV VNNSPAPTIP KIKREKPTPE EIEERRKLKQ LEVVPEGFSR KQWKRELKKQ
RWQDTKQEYL EVQREKKRLA RQRKRERLKD LDENDELRKA QPIPSRQIST NNVSVIIDCD
FDELMHEKEI VSLSNQIKAC YSAMRHCTYK LPIQITSFNK RLKQRFEAQL HDYHLWQGNI
SFTDRSLTEY VTGAPNSESK DNDGNSNSNT TNSTDTINTE NLVYLTADTD EEITKLEPNH
TYIIGGIVDK NRHKQLCYNK AKELGIKVAR LPIGKYIEMN GRHVLVTSHV YELLCKWFEN
DGDWETAFNK VLPPRKIKSK SPS
