Q0P5H7

PR
Gene name
RARS2 (RARSL)
Protein name
Probable arginine--tRNA ligase, mitochondrial
Names
Arginyl-tRNA synthetase, ArgRS
Species
Bos taurus (Bovine)
KEGG Pathway
bta:525894
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)

1-84 (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 Q0P5H7

Entry ID Method Resolution Chain Position Source
AF-Q0P5H7-F1 Predicted AlphaFoldDB

68 variants for Q0P5H7

Variant ID(s) Position Change Description Diseaes Association Provenance
rs480734689 39 V>G No EVA
rs449473968 41 D>H No EVA
rs461763773 43 Q>H No EVA
rs481835679 45 S>F No EVA
rs464272263 51 E>K No EVA
rs477877678 54 N>K No EVA
rs446697890 55 D>A No EVA
rs466735619 58 R>S No EVA
rs455508909 62 Q>* No EVA
rs438032655 63 I>M No EVA
rs469294603 63 I>N No EVA
rs451656196 64 Q>K No EVA
rs471738942 66 M>L No EVA
rs462666394 66 M>T No EVA
rs440428181 71 K>T No EVA
rs476305596 75 D>V No EVA
rs462694389 75 D>Y No EVA
rs458563585 79 S>G No EVA
rs478729856 81 I>S No EVA
rs441040005 88 V>G No EVA
rs481503940 94 R>K No EVA
rs449999522 95 E>K No EVA
rs470326767 97 L>V No EVA
rs459287796 207 V>G No EVA
rs473074521 211 K>E No EVA
rs441636331 234 D>H No EVA
rs461869176 244 F>V No EVA
rs524360311 245 R>Q No EVA
rs481900470 246 D>V No EVA
rs457917166 252 Y>C No EVA
rs450735332 252 Y>N No EVA
rs478158586 254 R>L No EVA
rs478158586 254 R>Q No EVA
rs466821072 257 Q>H No EVA
rs453751496 291 K>N No EVA
rs442236157 336 K>N No EVA
rs458082729 346 T>A No EVA
rs478513889 352 K>E No EVA
rs434156741 373 Q>H No EVA
rs465488905 373 Q>L No EVA
rs448014038 374 H>Y No EVA
rs468065187 375 V>M No EVA
rs719505425 401 R>Q No EVA
rs436170371 423 T>P No EVA
rs476534808 449 W>C No EVA
rs438791651 458 D>G No EVA
rs443885161 461 V>I No EVA
rs876039800 465 Y>S No EVA
rs876103907 466 T>P No EVA
rs876043158 467 H>P No EVA
rs452430222 472 S>T No EVA
rs448790959 480 G>D No EVA
rs459509035 510 Y>H No EVA
rs446788123 530 H>P No EVA
rs460485548 536 H>P No EVA
rs480726088 543 N>S No EVA
rs434850542 549 A>S No EVA
rs449485133 550 G>R No EVA
rs480311416 553 L>I No EVA
rs448824388 554 H>N No EVA
rs469054208 555 L>I No EVA
rs437627273 561 S>A No EVA
rs451285002 563 L>I No EVA
rs453923524 567 M>I No EVA
rs465027406 567 M>L No EVA
rs433752877 567 M>T No EVA
rs442797892 577 R>S No EVA
rs456491911 578 M>I No EVA

No associated diseases with Q0P5H7

3 regional properties for Q0P5H7

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 123 - 449 IPR035684

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

2 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.
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.

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.

2 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.
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.

5 homologous proteins in AiPD

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
Q5T160 RARS2 Probable arginine--tRNA ligase, mitochondrial Homo sapiens (Human) PR
Q3U186 Rars2 Probable arginine--tRNA ligase, mitochondrial Mus musculus (Mouse) 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
10 20 30 40 50 60
MACGFRRSIA SQLSRVLDLP PENLIKSISA VPISRKEEVA DFQLSVDSLL ENNNDHSRPD
70 80 90 100 110 120
IQIQAMRLAE KLKCDTVVSE ISTGQGTVNF KINRELLTKT VLQQVIEDGS KYGLKSELFS
130 140 150 160 170 180
GLPKKRIVVE FSSPNVAKKF HVGHLRSTII GNFIANLKEA LGHQVTRINY LGDWGMQFGL
190 200 210 220 230 240
LGTGFQLFGY EEKLQSSPLQ HLFEVYVQVN KEAADDKNVA KSAHEFFQRL ELGDMQALAL
250 260 270 280 290 300
WQKFRDLSID EYMRIYQRLG VHFDEYSGES FYREKSQEVL KLLDSKGLLQ KTLKGTAVVD
310 320 330 340 350 360
LSGNGDPSSV CTVMRSDGTS LYATRDLAAA IDRMEKYNFD KMIYVTDKGQ KKHFQQVFQI
370 380 390 400 410 420
LQIMGYDWAE RCQHVPFGVV QGMKTRRGDV TFLEDVLNEI RLRMLQNMAS IKTTKELENP
430 440 450 460 470 480
EETAEQVGLA ALIIQDFRGF LLSDYQFSWD RVFQSRGDTG VFLQYTHARL HSLEETFGCG
490 500 510 520 530 540
YLNDFNTACL QEPQSVSILQ HLLRFDEVLY RSSQDLQPRH IVSYLLTLSH LAAVAHRTLH
550 560 570
VRNSPPEVAG ARLHLFRAVR SVLANGMKLL GITPVCRM