ID   TM10A_XENTR             Reviewed;         334 AA.
AC   Q66JJ4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=tRNA methyltransferase 10 homolog A;
DE            EC=2.1.1.221 {ECO:0000250|UniProtKB:Q8TBZ6};
DE   AltName: Full=RNA (guanine-9-)-methyltransferase domain-containing protein 2;
DE   AltName: Full=tRNA (guanine(9)-N(1))-methyltransferase TRMT10A;
GN   Name=trmt10a; Synonyms=rg9mtd2; ORFNames=TEgg011a17.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 tRNAs. Probably not able to catalyze formation of
CC       N(1)-methyladenine at position 9 (m1A9) in tRNAs.
CC       {ECO:0000250|UniProtKB:Q8TBZ6}.
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:Q8TBZ6};
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; CR762095; CAJ81400.1; -; mRNA.
DR   EMBL; BC080890; AAH80890.1; -; mRNA.
DR   RefSeq; NP_001008012.1; NM_001008011.1.
DR   AlphaFoldDB; Q66JJ4; -.
DR   SMR; Q66JJ4; -.
DR   STRING; 8364.ENSXETP00000048013; -.
DR   PaxDb; Q66JJ4; -.
DR   DNASU; 493374; -.
DR   GeneID; 493374; -.
DR   KEGG; xtr:493374; -.
DR   CTD; 93587; -.
DR   Xenbase; XB-GENE-942310; trmt10a.
DR   eggNOG; KOG2967; Eukaryota.
DR   HOGENOM; CLU_034384_7_0_1; -.
DR   InParanoid; Q66JJ4; -.
DR   OMA; RLPIKEH; -.
DR   OrthoDB; 1396299at2759; -.
DR   PhylomeDB; Q66JJ4; -.
DR   TreeFam; TF330972; -.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000012132; Expressed in ovary and 12 other tissues.
DR   ExpressionAtlas; Q66JJ4; differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Coiled coil; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..334
FT                   /note="tRNA methyltransferase 10 homolog A"
FT                   /id="PRO_0000311318"
FT   DOMAIN          98..289
FT                   /note="SAM-dependent MTase TRM10-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          62..94
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        18..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  38514 MW;  07EB3A5841E5CEF6 CRC64;
     MSLEAVTEPG KCSIDPNTKD LLASQHAGNN TPLQENSSAP RSECKAQDAM SKRQMKKFLK
     QKQWEDQREL RKQKRKEKRQ KRKLERQAQA EHNIDANSRK RFRHEVQPSA LRLIIDCSFD
     DLMALRDVKK LNKQIRRCYA ENRRAVHPVQ LYLTSHGGQL KSNMDEYDKG WINWKDIHIK
     PEHYKDLIKK EDLVYLTSDS PEVLSELDET KAYIIGGLVD HNHHKGITYK KALELGISHA
     QLPLGNFVKM NTRKVLAVNH VFEIILAFLE KKEWKEAFFS VLPQRKGAIP LTETGEQPEC
     RASEQEDGED SDSDSSIDES ATIQPSVRCE EQNS