Q9VXN4

PR
Gene name
ArgRS
Protein name
Probable arginine--tRNA ligase, cytoplasmic
Names
Arginyl-tRNA synthetase
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG9020
EC number
6.1.1.19: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-113 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9VXN4

Entry ID Method Resolution Chain Position Source
AF-Q9VXN4-F1 Predicted AlphaFoldDB

No variants for Q9VXN4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VXN4

No associated diseases with Q9VXN4

4 regional properties for Q9VXN4

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 205 - 216 IPR001412
domain Arginyl tRNA synthetase N-terminal domain 81 - 171 IPR005148
domain DALR anticodon binding 540 - 665 IPR008909
domain Arginyl-tRNA synthetase, catalytic core domain 182 - 526 IPR035684

Functions

Description
EC Number 6.1.1.19 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, cytosol
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
aminoacyl-tRNA synthetase multienzyme complex A multienzyme complex found in all multicellular eukaryotes composed of eight proteins with aminoacyl-tRNA synthetase activities (abbreviated as: ArgRS, AspRS, GluProRS, GlnRS, IleRS, LeuRS, LysRS, MetRS where RS is the enzyme, preceded by the amino acid it uses as a substrate) as well as three non-synthetase proteins (p43, p38, and p18) with diverse functions. Several of these subunits are known dimers, so the total polypeptide count in the multisynthetase complex is at least fifteen. All of the enzymes in this assembly catalyze the same reaction, the covalent attachment of an amino acid to either the 2'- or 3'-hydroxyl of the 3'-terminal adenosine of tRNA, but using different substrates.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

2 GO annotations of molecular function

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.

1 GO annotations of biological process

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.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O23247 EMB1027 Arginine--tRNA ligase, chloroplastic/mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
Q9C713 At1g66530 Arginine--tRNA ligase, cytoplasmic Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSELNMELKK LRELELKTQG LAARIQTAKS GEQLDVDLVQ LQIENKKLKN RLFILKKSIA
70 80 90 100 110 120
EESTAAGGDV SKPKESSSIT EHLESVFRQA IASAFPEFRD TPVIIAPVNS TSAKFGDYQC
130 140 150 160 170 180
NNAMGLSKKL KEKGINKAPR DIATELKGHC PASPIIEKLE IAGAGFVNVF LSKDYASLAL
190 200 210 220 230 240
SNLLRNGVKP PEVIKKRVLV DFSSPNIAKQ MHVGHLRSTI IGESLCRLLE FLQHDVIRIN
250 260 270 280 290 300
HLGDWGTQFG MLIAHLEDRF PNYLNESPPI SDLQLFYKES KKRFDEDEEF KKRAYSRVVS
310 320 330 340 350 360
LQKGVPNSIK AWELICNVSR KEFQTIYERL DISVKERGES FYQSRMLSVV EYLRGKGLLE
370 380 390 400 410 420
VDEGREIMWP DDTKTGIPLT IVKSDGGFTY DTSDMAAIRH RLEEELCDWI IYVVDSGQST
430 440 450 460 470 480
HFNTIFKAAE RSAILNPLSH RVDHVQFGVV LGEDGKKFKT RSGDTVKLSD LLDEGMKRSL
490 500 510 520 530 540
QQLESRGRDK VLTPQELKDA QESLAYGCIK YSDLCHNRIS DYIFSFDKML EDRGNTAVYL
550 560 570 580 590 600
LYTYTRICSI ARNSGEDFTN LPEILKKTNI VLDHEKEWKL AKTLLKLHDI LIKCSKELFL
610 620 630 640 650 660
HFLCEFCFEV CTVFTEFYDS CYCIEKNKQG DIIGVNHSRI LLCEATAAVL RQCFYILGLK
PVSKM