AiPD: Autoinhibited Protein Database

Gene name	Rars2 (Rarsl)
Protein name	Probable arginine--tRNA ligase, mitochondrial
Names	Arginyl-tRNA synthetase, ArgRS
Species	Mus musculus (Mouse)
KEGG Pathway	mmu:109093
EC number	6.1.1.19: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

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

11-81 (Predicted disordered autoinhibitory region) PR

11-81 (Predicted disordered autoinhibitory region)

cis-regPred

No accessory elements

Entry ID	Method	Resolution	Chain	Position	Source
AF-Q3U186-F1	Predicted				AlphaFoldDB

Variant ID(s)	Position	Change	Diseaes Association	Provenance
rs263603148	29	S>A	No	EVA
rs231472125	53	N>S	No	EVA
rs3388674017	75	D>E	No	EVA
rs3388676739	80	A>S	No	EVA
rs3388673553	89	N>K	No	EVA
rs3388676712	93	N>Y	No	EVA
rs3388676098	168	I>L	No	EVA
rs3388679507	182	G>A	No	EVA
rs3393841601	192	E>D	No	EVA
rs3388672086	259	L>F	No	EVA
rs3388673583	288	L>I	No	EVA
rs226014584	294	E>K	No	EVA
rs245997775	297	V>F	No	EVA
rs3388679505	301	L>I	No	EVA
rs3388680060	304	T>S	No	EVA
rs27773149	306	D>G	No	EVA
rs3388672083	341	T>K	No	EVA
rs3388679554	360	M>K	No	EVA
rs3388668695	449	W>C	No	EVA
rs3388680058	466	T>N	No	EVA
rs3388674069	467	H>P	No	EVA
rs237846249	485	S>F	No	EVA
rs251404630	498	I>V	No	EVA
rs3388676703	535	A>T	No	EVA
rs27773099	540	Q>K	No	EVA
rs3388668704	544	S>I	No	EVA
rs3388673641	550	G>E	No	EVA
rs3388673609	573	T>I	No	EVA

Type	Name	Position	InterPro Accession
conserved_site	Aminoacyl-tRNA synthetase, class I, conserved site	134 - 145	IPR001412
domain	DALR anticodon binding	463 - 578	IPR008909
domain	Arginyl-tRNA synthetase, catalytic core domain	124 - 449	IPR035684

		Description
EC Number	6.1.1.19	Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization	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.

Name	Definition
arginine-tRNA ligase activity	Catalysis of the reaction: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).
ATP binding	Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

Name	Definition
arginyl-tRNA aminoacylation	The process of coupling arginine to arginyl-tRNA, catalyzed by arginyl-tRNA synthetase. The arginyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of an alanine accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
mitochondrial translation	The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.

UniProt AC	Gene Name	Protein Name	Species	Evidence Code
Q05506	YDR341C	Arginine--tRNA ligase, cytoplasmic	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)	PR
Q0P5H7	RARS2	Probable arginine--tRNA ligase, mitochondrial	Bos taurus (Bovine)	PR
Q5T160	RARS2	Probable arginine--tRNA ligase, mitochondrial	Homo sapiens (Human)	PR
Q9C713	At1g66530	Arginine--tRNA ligase, cytoplasmic	Arabidopsis thaliana (Mouse-ear cress)	PR
O23247	EMB1027	Arginine--tRNA ligase, chloroplastic/mitochondrial	Arabidopsis thaliana (Mouse-ear cress)	PR