ID TM10C_XENTR Reviewed; 448 AA.
AC A4IHS0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=tRNA methyltransferase 10 homolog C {ECO:0000305};
DE AltName: Full=Mitochondrial ribonuclease P protein 1 {ECO:0000250|UniProtKB:Q7L0Y3};
DE Short=Mitochondrial RNase P protein 1 {ECO:0000250|UniProtKB:Q7L0Y3};
DE AltName: Full=RNA (guanine-9-)-methyltransferase domain-containing protein 1 {ECO:0000250|UniProtKB:Q7L0Y3};
DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase {ECO:0000250|UniProtKB:Q7L0Y3};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q7L0Y3};
DE AltName: Full=tRNA (adenine(9)-N(1))-methyltransferase {ECO:0000250|UniProtKB:Q7L0Y3};
DE EC=2.1.1.218 {ECO:0000250|UniProtKB:Q7L0Y3};
DE AltName: Full=tRNA (guanine(9)-N(1))-methyltransferase {ECO:0000250|UniProtKB:Q7L0Y3};
DE EC=2.1.1.221 {ECO:0000250|UniProtKB:Q7L0Y3};
DE Flags: Precursor;
GN Name=trmt10c {ECO:0000250|UniProtKB:Q7L0Y3};
GN Synonyms=mrpp1 {ECO:0000250|UniProtKB:Q7L0Y3},
GN rg9mtd1 {ECO:0000250|UniProtKB:Q7L0Y3};
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial tRNA N(1)-methyltransferase involved in
CC mitochondrial tRNA maturation. Component of mitochondrial ribonuclease
CC P, which cleaves tRNA molecules in their 5'-ends. Together with
CC hsd17b10/mrpp2, forms a subcomplex of the mitochondrial ribonuclease P,
CC named MRPP1-MRPP2 subcomplex, which displays functions that are
CC independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex
CC catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at
CC position 9 (m1G9 and m1A9, respectively) in tRNAs; trmt10c/mrpp1 acting
CC as the catalytic N(1)-methyltransferase subunit. The MRPP1-MRPP2
CC subcomplex also acts as a tRNA maturation platform: following 5'-end
CC cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2
CC subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2,
CC retains the tRNA product after elac2 processing and presents the
CC nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1
CC enzyme. In addition to tRNA N(1)-methyltransferase activity,
CC trmt10c/mrpp1 also acts as a mRNA N(1)-methyltransferase by mediating
CC methylation of adenosine residues at the N(1) position of MT-ND5 mRNA.
CC {ECO:0000250|UniProtKB:Q7L0Y3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43148, Rhea:RHEA-COMP:10363, Rhea:RHEA-COMP:10364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.218;
CC Evidence={ECO:0000250|UniProtKB:Q7L0Y3};
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:Q7L0Y3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(1)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55392, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12415,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491;
CC Evidence={ECO:0000250|UniProtKB:Q7L0Y3};
CC -!- SUBUNIT: Component of mitochondrial ribonuclease P. Interacts with
CC HSD17B10/MRPP2. {ECO:0000250|UniProtKB:Q7L0Y3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000250|UniProtKB:Q7L0Y3}.
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; BC135659; AAI35660.1; -; mRNA.
DR RefSeq; NP_001096307.1; NM_001102837.1.
DR AlphaFoldDB; A4IHS0; -.
DR SMR; A4IHS0; -.
DR STRING; 8364.ENSXETP00000038566; -.
DR PaxDb; 8364-ENSXETP00000062534; -.
DR DNASU; 100124885; -.
DR GeneID; 100124885; -.
DR KEGG; xtr:100124885; -.
DR AGR; Xenbase:XB-GENE-877279; -.
DR CTD; 54931; -.
DR Xenbase; XB-GENE-877279; trmt10c.
DR eggNOG; KOG2967; Eukaryota.
DR InParanoid; A4IHS0; -.
DR OMA; IDPFHIY; -.
DR OrthoDB; 2998902at2759; -.
DR Proteomes; UP000008143; Chromosome 2.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0160106; F:tRNA (adenine(9)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052905; F:tRNA (guanosine(9)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; ISS:UniProtKB.
DR GO; GO:0090646; P:mitochondrial tRNA processing; ISS:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR CDD; cd18102; Trm10_MRRP1; 1.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR025812; Trm10_C_MTase_dom.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; TRNA (GUANINE-9-) METHYLTRANSFERASE; 1.
DR PANTHER; PTHR13563:SF5; TRNA METHYLTRANSFERASE 10 HOMOLOG C; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Methyltransferase; Mitochondrion; Mitochondrion nucleoid;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transit peptide;
KW tRNA processing.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..448
FT /note="tRNA methyltransferase 10 homolog C"
FT /id="PRO_0000311312"
FT DOMAIN 190..382
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT REGION 144..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 137..165
FT /evidence="ECO:0000255"
SQ SEQUENCE 448 AA; 52300 MW; 0553A28DC8B82B3F CRC64;
MAFVNTLLRT IRCSAVHTLV QEGRSLSLLK ASHQLTQSRK IMLSNHVRKE EAKSEPNETL
DLEEWKSILK SDIGNAEMVK TETQEDSSLN EMQELVEMWR LAGRAVPQSI TTEQLQVLME
LPTKTARKKY LKYLSVREVM KTNRKEKKKE LKESKSKIES LDQLETKEDT PEKKNTFLLH
VWDKSIDTMQ RWKCVQAMKF GQPLVFDMVY EKNMSRYELE NTVCQLMESE GWNRRSTDPF
HIYFCSLQPY SMYHKELVKR YIGAWDNVFV TATDKSHVEM FPKEQLVYLT ADSPNELKHF
DHTKIYIIGS LVDRCQQTGL SLANAKRLNL ATARLPLDRY LKWDVGAKNL TLDQMIRILL
CLKDTGDWKK ALSFVPNRKH DGFAEPAASK KRNIKNDGGM EYAASTKRNL QKNSKMYKFG
ASKSFIKPER TDDTSIRSTR KRWWEEEN
//
