TM10C_RAT
ID TM10C_RAT Reviewed; 414 AA.
AC Q5U2R4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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:0000312|RGD:1306333};
GN Synonyms=Mrpp1 {ECO:0000250|UniProtKB:Q7L0Y3},
GN Rg9mtd1 {ECO:0000250|UniProtKB:Q7L0Y3};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Mitochondrial tRNA N(1)-methyltransferase involved in
CC mitochondrial tRNA maturation. Component of mitochondrial ribonuclease
CC P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3,
CC 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 Associates with mitochondrial DNA complexes at the nucleoids to
CC initiate RNA processing and ribosome assembly.
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, a complex composed
CC of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3. Interacts with
CC HSD17B10/MRPP2; forming the MRPP1-MRPP2 subcomplex of the mitochondrial
CC ribonuclease P complex. Interacts with GRSF1.
CC {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; BC085895; AAH85895.1; -; mRNA.
DR RefSeq; NP_001008338.1; NM_001008337.1.
DR AlphaFoldDB; Q5U2R4; -.
DR SMR; Q5U2R4; -.
DR BioGRID; 257741; 1.
DR STRING; 10116.ENSRNOP00000002198; -.
DR PaxDb; Q5U2R4; -.
DR PRIDE; Q5U2R4; -.
DR Ensembl; ENSRNOT00000002198; ENSRNOP00000002198; ENSRNOG00000039567.
DR GeneID; 304012; -.
DR KEGG; rno:304012; -.
DR UCSC; RGD:1306333; rat.
DR CTD; 54931; -.
DR RGD; 1306333; Trmt10c.
DR eggNOG; KOG2967; Eukaryota.
DR GeneTree; ENSGT00530000063169; -.
DR HOGENOM; CLU_034384_3_1_1; -.
DR InParanoid; Q5U2R4; -.
DR OMA; IDPFHIY; -.
DR OrthoDB; 1569668at2759; -.
DR PhylomeDB; Q5U2R4; -.
DR TreeFam; TF319795; -.
DR PRO; PR:Q5U2R4; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000039567; Expressed in thymus and 19 other tissues.
DR Genevisible; Q5U2R4; RN.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0030678; C:mitochondrial ribonuclease P complex; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043527; C:tRNA methyltransferase complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0061953; F:mRNA (adenine-N1-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0000964; P:mitochondrial RNA 5'-end processing; ISS:UniProtKB.
DR GO; GO:1990180; P:mitochondrial tRNA 3'-end processing; ISO:RGD.
DR GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; ISS:UniProtKB.
DR GO; GO:0070901; P:mitochondrial tRNA methylation; ISO:RGD.
DR GO; GO:0090646; P:mitochondrial tRNA processing; ISS:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR025812; TRM10C.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; PTHR13563; 1.
DR PANTHER; PTHR13563:SF5; PTHR13563:SF5; 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 Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW Transit peptide; tRNA processing.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..414
FT /note="tRNA methyltransferase 10 homolog C"
FT /id="PRO_0000311311"
FT DOMAIN 186..378
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT COILED 133..162
FT /evidence="ECO:0000255"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UFY8"
SQ SEQUENCE 414 AA; 48293 MW; E43A3D273A43A469 CRC64;
MNVTVRFLRP FARYLVPYTF HRTRSNSYSR VLQRYVSSKV PSLPCHNKDS TSPPEQLELD
GWKTTMKSSI QENGVSVVSD KDEDSLAATR ELIEMWRLLG KEVPEHITEE ELKTLMECAS
KSAKKKYLRY LYGKEMMKKA KQMKKEMKAA AREEAKRARS LEPSTGEEQR DFMFLRLWDR
QTNIALGWKG VQAMQFGQPL VFDMAYDNYM KPSELQNTVS QLLESEGWNR RNVDPFHIYF
CNLEVDGAYH RELVKRYGEK WDKLLLTATE KSPVDLFPKD SIIYLTADSP NVMTTFKHDK
IYIIGSFVDK NTQTGTSLAK AKRQNLATEC LPLDKYLQWD VGNKNLTLDQ MIRILLCLKN
TGNWEEALKF VPRRKHTGYL EVPEHSQAAF RKLKKTKTLN SFRKGSLNVH MWKR
