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Protein

tRNA methyltransferase 10 homolog C

Gene

Trmt10c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Mitochondrial tRNA N1-methyltransferase involved in mitochondrial tRNA maturation. Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP3, which cleaves tRNA molecules in their 5'-ends. Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N1-methylguanine and N1-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting as the catalytic N1-methyltransferase subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. In addition to tRNA N1-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNA N1-methyltransferase by mediating methylation of adenosine residues at the N1 position of MT-ND5 mRNA.By similarity

Catalytic activityi

S-adenosyl-L-methionine + adenine9 in tRNA = S-adenosyl-L-homocysteine + N1-methyladenine9 in tRNA.By similarity
S-adenosyl-L-methionine + guanine9 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA.By similarity
S-adenosyl-L-methionine + adenine in mRNA = S-adenosyl-L-homocysteine + N1-methyladenine in mRNA.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processtRNA processing
LigandS-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA methyltransferase 10 homolog CCurated
Alternative name(s):
Mitochondrial ribonuclease P protein 1By similarity
Short name:
Mitochondrial RNase P protein 1By similarity
RNA (guanine-9-)-methyltransferase domain-containing protein 1By similarity
mRNA methyladenosine-N(1)-methyltransferaseBy similarity (EC:2.1.1.-By similarity)
tRNA (adenine(9)-N(1))-methyltransferaseBy similarity (EC:2.1.1.218By similarity)
tRNA (guanine(9)-N(1))-methyltransferaseBy similarity (EC:2.1.1.221By similarity)
Gene namesi
Name:Trmt10cImported
Synonyms:Mrpp1, Rg9mtd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1196261 Trmt10c

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion, Mitochondrion nucleoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 35MitochondrionSequence analysisAdd BLAST35
ChainiPRO_000031131036 – 414tRNA methyltransferase 10 homolog CAdd BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei79PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3UFY8
MaxQBiQ3UFY8
PaxDbiQ3UFY8
PeptideAtlasiQ3UFY8
PRIDEiQ3UFY8

PTM databases

iPTMnetiQ3UFY8
PhosphoSitePlusiQ3UFY8

Expressioni

Gene expression databases

BgeeiENSMUSG00000044763
GenevisibleiQ3UFY8 MM

Interactioni

Subunit structurei

Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31. Interacts with HSD17B10/MRPP2; forming the MRPP1-MRPP2 subcomplex of the mitochondrial ribonuclease P complex. Interacts with GRSF1.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000058954

Structurei

3D structure databases

ProteinModelPortaliQ3UFY8
SMRiQ3UFY8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini186 – 378SAM-dependent MTase TRM10-typePROSITE-ProRule annotationAdd BLAST193

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili133 – 171Sequence analysisAdd BLAST39

Sequence similaritiesi

Belongs to the class IV-like SAM-binding methyltransferase superfamily. TRM10 family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

eggNOGiKOG2967 Eukaryota
ENOG4111JE4 LUCA
GeneTreeiENSGT00530000063169
HOGENOMiHOG000088648
HOVERGENiHBG108146
InParanoidiQ3UFY8
KOiK17654
OMAiKTLMECV
OrthoDBiEOG091G09AL
PhylomeDBiQ3UFY8
TreeFamiTF319795

Family and domain databases

Gene3Di3.40.1280.30, 1 hit
InterProiView protein in InterPro
IPR028564 MT_TRM10-typ
IPR038459 MT_TRM10-typ_sf
IPR025812 TRM10C
IPR007356 tRNA_m1G_MeTrfase_euk
IPR016009 tRNA_MeTrfase_TRMD/TRM10
PANTHERiPTHR13563 PTHR13563, 1 hit
PTHR13563:SF5 PTHR13563:SF5, 1 hit
PfamiView protein in Pfam
PF01746 tRNA_m1G_MT, 1 hit
PROSITEiView protein in PROSITE
PS51675 SAM_MT_TRM10, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3UFY8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVTVRFLRP FARCLVPYTF HRKRSHLYSG VLQRYMSSKA PSLSCHNKDS
60 70 80 90 100
ASPPEQLELD GWKATMKSSI QEDGVSEVSD KDEDSLASTR ELIEMWRLLG
110 120 130 140 150
KEVPEHITEE DLKTLMECAS KSAKKKYLRY LYGKEKAKKA KQVKKEMKAE
160 170 180 190 200
AREEAKRARL LETTAEEQQQ DFMFLRLWDR QINIALGWKG VQAMQFGQPL
210 220 230 240 250
VFDMAYDNYM KPSELQNTVS QLLESEGWNR RNVDPFHIYF CNLKIDSAYH
260 270 280 290 300
RELVKRYREK WDKLLLTATE KSPVDLFPKD SIIYLTADSP NVMTTFKHDK
310 320 330 340 350
IYIIGSFVDK NTQTGTSLAK AKRLNIATEC LPLDKYLQWE IGNKNLTLDQ
360 370 380 390 400
MIRILLCLKN TGNWEEALKF VPRRKHTGYL EVSEQSQELV RKLKKTKTLN
410
SFRKGSLNVR TWKR
Length:414
Mass (Da):48,386
Last modified:November 13, 2007 - v2
Checksum:iA48979421D1E7038
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti40A → T in BAE28421 (PubMed:16141072).Curated1
Sequence conflicti111D → E in BAE28421 (PubMed:16141072).Curated1
Sequence conflicti137A → V in BAE28421 (PubMed:16141072).Curated1
Sequence conflicti226E → G in BAE28421 (PubMed:16141072).Curated1
Sequence conflicti326I → L in BAE28421 (PubMed:16141072).Curated1
Sequence conflicti363N → S in AAI06132 (PubMed:15489334).Curated1
Sequence conflicti363N → S in AAH23147 (PubMed:15489334).Curated1
Sequence conflicti408N → S in BAE28421 (PubMed:16141072).Curated1
Sequence conflicti409V → A in BAE28421 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005047 mRNA Translation: BAB23773.1
AK087991 mRNA Translation: BAC40080.1
AK135426 mRNA Translation: BAE22529.1
AK148219 mRNA Translation: BAE28421.1
AK166781 mRNA Translation: BAE39015.1
BC023147 mRNA Translation: AAH23147.1
BC106131 mRNA Translation: AAI06132.1
CCDSiCCDS28220.1
RefSeqiNP_083368.1, NM_029092.3
UniGeneiMm.288742

Genome annotation databases

EnsembliENSMUST00000059052; ENSMUSP00000058954; ENSMUSG00000044763
GeneIDi52575
KEGGimmu:52575
UCSCiuc007zmd.1 mouse

Similar proteinsi

Entry informationi

Entry nameiTM10C_MOUSE
AccessioniPrimary (citable) accession number: Q3UFY8
Secondary accession number(s): Q8R588, Q9DBC1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: March 28, 2018
This is version 93 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health