Q5REH3

PR
Gene name
RARS2 (RARSL)
Protein name
Probable arginine--tRNA ligase, mitochondrial
Names
Arginyl-tRNA synthetase, ArgRS
Species
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
KEGG Pathway
pon:100189650
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)

1-97 (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 Q5REH3

Entry ID Method Resolution Chain Position Source
AF-Q5REH3-F1 Predicted AlphaFoldDB

No variants for Q5REH3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5REH3

No associated diseases with Q5REH3

4 regional properties for Q5REH3

Type Name Position InterPro Accession
domain Ras-associating domain 198 - 292 IPR000159
domain Protein kinase C-like, phorbol ester/diacylglycerol-binding domain 50 - 105 IPR002219
domain SARAH domain 294 - 341 IPR011524
domain Ras association domain-containing protein 1, RA domain 134 - 290 IPR033600

Functions

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

1 GO annotations of cellular component

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.

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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MACGFRRAIA CQLSRVLNLP PENLITSISA VPISQKEEVA DFQLSVDSLL EKDNDHSRPD
70 80 90 100 110 120
IQVQAKRLAE KLRCDTVVSE ISTGQRTVNF KINRELLTKT VLQQVIEDGS KYGLKSELFS
130 140 150 160 170 180
GLPQKKIVVE FSSPNVAKKF HVGHLRSTII GNFIANLKEA LGHQVIRINY LGDWGMQFGL
190 200 210 220 230 240
LGTGFQLFGY EEKLQSNPLQ HLFEVYVQVN KEAADDKSVA KAAQEFFQRL ELGDVQALSL
250 260 270 280 290 300
WQKFRDLSIE EYIRVYKRLG VYFDEYSGES FYREKSQEVL KLLESKGLLL RTIKGTAVVD
310 320 330 340 350 360
LSGNGDPSSI CTVMRSDGTS LYATRDLAAA IDRMDKYNFD TMIYVTDKGQ KKHFQQVFQM
370 380 390 400 410 420
LKIMGYDWAE RCQHVPFGVV QGMKTRRGDV TFLEDVLNEI QLRMLQNMAS IKTTKELKNP
430 440 450 460 470 480
QETAERVGLA ALIIQDFKGL LLSDYKFSWD RVFQSRGDTG VFLQYTHARL HSLEETFGCG
490 500 510 520 530 540
YLNDFNTACL QEPQSVSILQ HLLRFDEVLY KSSQDFQPRH IVSYLLTLSH LAAVAHKTLQ
550 560 570
IKDSPPEVAG ARLHLFKAVR SVLANGMKLL GITPVCRM