Primary Information |
|---|
| BoMiProt ID | Bomi5023 |
|---|
| Protein Name | D-aminoacyl-tRNA deacylase 1/DNA-unwinding element-binding protein B/Gly-tRNA(Ala) deacylase |
|---|
| Organism | Bos taurus |
|---|
| Uniprot ID | Q2T9V8 |
|---|
| Milk Fraction | Exosomes,MFGM |
|---|
| Ref Sequence ID | NP_001033193.1 |
|---|
| Aminoacid Length | 209 |
|---|
| Molecular Weight | 23232 |
|---|
| FASTA Sequence |
Download |
|---|
| Gene Name | DTD1 |
|---|
| Gene ID | 514493 |
|---|
| Protein Existence Status | Reviewed |
|---|
Secondary Information |
|---|
| Presence in other biological fluids/tissue/cells | granulosa cell |
|---|
| Protein Function | d-aminoacyl-tRNA-deacylase (DTD) prevents the incorporation of d-amino acids into proteins during translation by hydrolyzing the ester bond between mistakenly attached amino acids and tRNAs. |
|---|
| Biochemical Properties | The Gly137-Pro138 motif is conserved in DTDs, being crucial for providing enantioselectivity to the enzyme. |
|---|
| PTMs | Phosphorylation at Ser |
|---|
Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q2T9V8|DTD1_BOVIN D-aminoacyl-tRNA deacylase 1 OS=Bos taurus OX=9913 GN=DTD1 PE=2 SV=1
MKAVVQRVTRASVTVGGEQISAIGRGICVLLGISLEDTQKELEHMVRKILNLRVFEDESG
KHWSKSVMDKQYEVLCVSQFTLQCVLKGNKPDFHLAMPAEQAESFYKGFLEQLRKAYRPE
LVKDGKFGAYMQVHIQNDGPVTIELESPAPGAAASDPKQLSKLEKQQQRKEKTRAKGPSE
SSKERSAPRKEDRSASS*197GAEGDVS*204S*205EREP
|
|---|
| Predicted Disorder Regions | 149-209 |
|---|
| DisProt Annotation | |
|---|
| TM Helix Prediction | No TM helices |
|---|
| Significance of PTMs | Phosphorylation in the C-terminus weakens the interaction with CDC45 |
|---|
| Bibliography | 1.Ilchenko MM, Rybak MY, Rayevsky AV, Kovalenko OP, Dubey IY, Tukalo MA. Substrate-assisted mechanism of catalytic hydrolysis of misaminoacylated tRNA required for protein synthesis fidelity. Biochem J. 2019 Feb 28;476(4):719-732. doi: 10.1042/BCJ20180910. PMID: 30718305. 2.Pawar KI, Suma K, Seenivasan A, Kuncha SK, Routh SB, Kruparani SP, et al. Role of Daminoacyl-tRNA deacylase beyond chiral proofreading as a cellular defense against glycine mischarging by AlaRS. eLife. 2017;6. |
|---|
