Primary Information |
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BoMiProt ID | Bomi10083 |
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Protein Name | tRNA methyltransferase 10 homolog C/Mitochondrial ribonuclease P protein 1/Mitochondrial RNase P protein 1/RNA (guanine-9-)-methyltransferase domain-containing protein 1/mRNA methyladenosine-N(1)-methyltransferase/tRNA (adenine(9)-N(1))-methyltransferase/tRNA (guanine(9)-N(1))-methyltransferase |
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Organism | Bos taurus |
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Uniprot ID | Q2KI45 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001039788.1 |
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Aminoacid Length | 426 |
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Molecular Weight | 49785 |
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FASTA Sequence |
Download |
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Gene Name | TRMT10C/MRPP1/RG9MTD1 |
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Gene ID | 532418 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | a subunit of the mitochondrial RNase P complex. Subunits TRMT10C and SDR5C1 form a subcomplex that binds conserved mitochondrial tRNA elements, including the anticodon loop, and positions the tRNA for methylation during RNA processing in mitochondria. |
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Biochemical Properties | consists of an N-terminal domain (NTD) and a dual-specificity C-terminal methyltransferase domain, which are both required for establishing a conserved m1G/A methylation at position 9 of mitochondrial tRNAs.methyltransferase domain recognizes the substrate and binds to it.N-terminal of the adapter helix, residues 175–182 of TRMT10C form an ‘adapter loop’, which is stabilized by hydrophobic interactions with SDR5C1. |
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PTMs | phosphorylation on Ser-86 |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q2KI45|TM10C_BOVIN tRNA methyltransferase 10 homolog C OS=Bos taurus OX=9913 GN=TRMT10C PE=2 SV=2
MPVLLKMSVSITFLRPFARVLVPFTLHRKRRVLYSTIMQRYMSSKIPAASYPNKESTPPS
EELELDRWKITMKSSVQEEDVSTATS*86SEDEDPLAATRELVEMWRLLGKEVPEHFSEEELK
TLMECVSKSSKRKYLKYLYIKEKMKKARQIKKEMKKAEKEEPKKDQLPETIKEDKQQNFL
FLRLWDRNMDIAMGWKGAQAMQFGQPLVFDMAYDDHMKPKELQNAVSQLLESEGCNRRNV
DPFHIYFCNLKTGGAYYKELVKRYGEKWNKLLLTATEKSHVDLFPKDSIIYLTADSPNVM
TTFKHDKIYIVGSFVDKNMQPGTSLAKAKRLKLATECLPLDKYLQWDTGTKNLTLDQMMR
ILLCLKNTGSWEEALKFVPSRKHAGYLEISQHSQEFLNRMKKSKTFNSFPRGSINRHRKS
SLKENI
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Predicted Disorder Regions | 48-94, 142-171, 403-426 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Additional Comments | mutation of the conserved active site residues D314 or Q226, to asparagine or alanine, respectively, leads to impaired methyltransferase activity |
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Bibliography | Bhatta A, Dienemann C, Cramer P, Hillen HS. Structural basis of RNA processing by human mitochondrial RNase P. Nat Struct Mol Biol. 2021 Sep;28(9):713-723. doi: 10.1038/s41594-021-00637-y. Epub 2021 Sep 6. PMID: 34489609; PMCID: PMC8437803. |