Primary Information |
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| BoMiProt ID | Bomi4055 |
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| Protein Name | Aspartate--tRNA ligase, mitochondrial/Aspartyl-tRNA synthetase/AspRS |
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| Organism | Bos taurus |
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| Uniprot ID | A6QPU5 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001095692.1 |
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| Aminoacid Length | 651 |
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| Molecular Weight | 73688 |
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| FASTA Sequence |
Download |
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| Gene Name | DARS2 |
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| Gene ID | 538772 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | Recognition of Asp for protein synthesis. |
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| Biochemical Properties | Binds to Asp and ATP.DARS2 contains conserved residues involved in ATP binding, tRNA binding, and aspartic acid recognition, as well as catalytic site motifs characteristic of amino acid tRNA synthetases. arg263-to-ter (R263X) mutation in the DARS2 gene that was found in compound heterozygous state in a patient with leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation |
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| PTMs | Acetylation, Phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|A6QPU5|SYDM_BOVIN Aspartate--tRNA ligase, mitochondrial OS=Bos taurus OX=9913 GN=DARS2 PE=2 SV=1
MFCWLSRLCGELSTPTRRTTQLIWSSAARSMVLSSQRIPELSSFVARTNTCGELRSSHLG
QEVTLCGWIQFRRQNIFLVLRDFHGLVQVVIPQDESAASVKKILCEAPMESVVQVSGTVI
SRPPGQKNPKMPTGEIEIKVKTAKLLNSCKKLPFEIKDFMKKTETLRLQYRYLDLRSVQM
QYNLRLRSQMVMKMREYLCNLHGFVDVETPTLFKRT*216PGGAKEFVIPSREPGKFYSLPQS*239P
QQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGVQSLIEGLLQY
SWPSDKDPLVVPFPSMPFAEALASYGTDKPDTRFGMKIVDISDMFRNTEVGFLQDALSKP
QGTVKAICIRKGAKYLKRKDIESIRKFAADHFNEEVLPIFLKTNENWNSPVAKFIMEEQG
LGLVKLLETQEEDVVLLTAGEHKKACSLMGKLRLECADLLEARGVVLRDPALFSFLWVVD
FPLFLPKEENPQELESAHHPFTAPHPSDIHLLYTEPHKVRSQHYDLVLNGNEIGGGSIRI
HNSELQHCVLDTVLKEDVKLLSHLLQALDYGAPPHGGIALGLDRLMCLVTGAPSIRDVIA
FPKSFRGHDLMSNAPDSIPPEELKPYHIQVSWPMDAETEKSSSNHPCRSES
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| Predicted Disorder Regions | 634-651 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | Bonnefond L, Fender A, Rudinger-Thirion J, Giegé R, Florentz C, Sissler M. Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. doi: 10.1021/bi047527z. PMID: 15779907. |
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