AiPD: Autoinhibited Protein Database

Gene name	Dars2
Protein name	Aspartate--tRNA ligase, mitochondrial
Names	Aspartyl-tRNA synthetase, AspRS
Species	Mus musculus (Mouse)
KEGG Pathway	mmu:226539
EC number	6.1.1.12: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

1-72 (Predicted disordered autoinhibitory region) PR

1-72 (Predicted disordered autoinhibitory region)

cis-regPred

No accessory elements

Entry ID	Method	Resolution	Chain	Position	Source
AF-Q8BIP0-F1	Predicted				AlphaFoldDB

Variant ID(s)	Position	Change	Diseaes Association	Provenance
rs246378572	5	F>S	No	EVA
rs51557988	9	R>S	No	EVA
rs3388512970	38	Q>L	No	EVA
rs3390872287	81	V>G	No	EVA
rs3388510407	108	E>G	No	EVA
rs3388509327	109	A>G	No	EVA
rs3388509401	110	P>S	No	EVA
rs3388507075	111	V>G	No	EVA
rs3388506071	115	V>G	No	EVA
rs3388511401	116	R>S	No	EVA
rs3388509788	117	V>L	No	EVA
rs3388509841	118	S>Y	No	EVA
rs3388509777	134	P>*	No	EVA
rs3388511337	134	P>R	No	EVA
rs3388509392	141	K>N	No	EVA
rs3388508371	143	K>*	No	EVA
rs3388509844	167	A>*	No	EVA
rs3388510848	167	A>E	No	EVA
rs3412833541	189	R>G	No	EVA
rs233525171	196	M>I	No	EVA
rs3388508403	252	G>R	No	EVA
rs3388510901	266	D>G	No	EVA
rs3388511430	304	W>*	No	EVA
rs3388508395	310	P>S	No	EVA
rs3388511222	323	A>T	No	EVA
rs229942736	326	T>N	No	EVA
rs3388509816	338	M>V	No	EVA
rs3388509825	346	V>M	No	EVA
rs232005332	352	L>I	No	EVA
rs3388509304	367	K>R	No	EVA
rs33754544	370	C>R	No	EVA
rs31573477	429	M>L	No	EVA
rs254984776	436	I>M	No	EVA
rs3388507052	469	L>F	No	EVA
rs3390884397	492	S>C	No	EVA
rs3388510906	500	H>N	No	EVA
rs3388510460	500	H>R	No	EVA
rs3388512982	507	N>Y	No	EVA
rs3388508566	529	V>F	No	EVA
rs3388510895	532	G>D	No	EVA
rs229027610	620	V>M	No	EVA
rs3388509361	630	I>T	No	EVA
rs246962275	640	E>D	No	EVA

Type	Name	Position	InterPro Accession
domain	Aminoacyl-tRNA synthetase, class II (D/K/N)	166 - 605	IPR004364
domain	OB-fold nucleic acid binding domain, AA-tRNA synthetase-type	65 - 148	IPR004365
domain	Aminoacyl-tRNA synthetase, class II	186 - 604	IPR006195
domain	GAD domain	356 - 451	IPR029351
domain	Aspartate-tRNA ligase, type 1, anticodon recognition domain	49 - 182	IPR047089
domain	Aspartate-tRNA ligase, type 1, core domain	186 - 606	IPR047090

		Description
EC Number	6.1.1.12	Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization	Mitochondrion matrix Mitochondrion membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category	No pathway information available

Name	Definition
mitochondrial matrix	The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrion	A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
nucleoplasm	That part of the nuclear content other than the chromosomes or the nucleolus.

Name	Definition
aspartate-tRNA ligase activity	Catalysis of the reaction: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).
aspartate-tRNA(Asn) ligase activity	Catalysis of the reaction: tRNA(Asx) + L-aspartate + ATP = aspartyl-tRNA(Asx) + diphosphate + AMP.
ATP binding	Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
nucleic acid binding	Binding to a nucleic acid.
protein homodimerization activity	Binding to an identical protein to form a homodimer.

Name	Definition
aspartyl-tRNA aminoacylation	The process of coupling aspartate to aspartyl-tRNA, catalyzed by aspartyl-tRNA synthetase. The aspartyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of an aspartic acid accetping tRNA.
mitochondrial asparaginyl-tRNA aminoacylation	The process of coupling asparagine to asparaginyl-tRNA in a mitochondrion, catalyzed by asparaginyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA.
tRNA aminoacylation	The chemical reactions and pathways by which the various amino acids become bonded to their corresponding tRNAs. The most common route for synthesis of aminoacyl tRNA is by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, usually catalyzed by the cognate aminoacyl-tRNA ligase. A given aminoacyl-tRNA ligase aminoacylates all species of an isoaccepting group of tRNA molecules.

UniProt AC	Gene Name	Protein Name	Species	Evidence Code
A6QPU5	DARS2	Aspartate--tRNA ligase, mitochondrial	Bos taurus (Bovine)	PR
P21889	aspS	Aspartate--tRNA ligase	Escherichia coli (strain K12)	PR
Q8BGV0	Nars2	Probable asparagine--tRNA ligase, mitochondrial	Mus musculus (Mouse)	PR