Search by BoMiProt ID - Bomi10083


Primary Information

BoMiProt ID Bomi10083
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
Organism Bos taurus
Uniprot IdQ2KI45
Milk FractionWhey
Ref Sequence Id NP_001039788.1
Aminoacid Length 426
Molecular Weight 49785
Fasta Sequence https://www.uniprot.org/uniprot/Q2KI45.fasta
Gene Name TRMT10C/MRPP1/RG9MTD1
Gene Id 532418
Protein Existence Status reviewed

Secondary Information

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.
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.
PTMs phosphorylation on Ser-86
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
Predicted Disorder Regions 48-94, 142-171, 403-426
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments mutation of the conserved active site residues D314 or Q226, to asparagine or alanine, respectively, leads to impaired methyltransferase activity
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.