Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

3 structures for O59147

Entry ID Method Resolution Chain Position Source
2ZUE X-ray 200 A A 1-629 PDB
2ZUF X-ray 230 A A 1-629 PDB
AF-O59147-F1 Predicted AlphaFoldDB

No variants for O59147

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O59147

No associated diseases with O59147

4 regional properties for O59147

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 130 - 139 IPR001412
domain Arginyl tRNA synthetase N-terminal domain 7 - 90 IPR005148
domain DALR anticodon binding 507 - 629 IPR008909
domain Arginyl-tRNA synthetase, catalytic core domain 100 - 493 IPR035684

Functions

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

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

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
MLMEIRESVK ERIEEIIKEI APQWEGEIEL KETPDPKLGD FGTPIAFKLA KLLKRPPIEI
70 80 90 100 110 120
AEKIVEKLKL NLPEGIKDVK AVNGYINVFI DYPHFARILI NDILAKGDRF GSSEIGKGKK
130 140 150 160 170 180
VIVEHTSVNP TKPLHMGHAR NAILGDVMAR ILRFLGYEVE VQNYIDDLGI QFAQVYWGYL
190 200 210 220 230 240
RLKEEFERIM NELRERGLKD NPIDHALGLL YVEVNRRLED NPELENEIRD IMKKLESGEL
250 260 270 280 290 300
YGRKLAEEVV RAQMVTTYKL GVKYDLLVWE SDIVRRKLFE IALELLSKNE NFYIPSDGKY
310 320 330 340 350 360
RGAFVMDLRK LFPDMKNPIL VLRRSDGTAT YTGKDIAYHL WKFGKIDVDL LYKEWDSTTW
370 380 390 400 410 420
TTAPDGKSMP NKFGNANIVI NVIGAEQKHP QLAIKYALQL LGFEDAAANL YHLAYEHVER
430 440 450 460 470 480
PEGKFSGRKG TWVGFTVDEV IQEAVKRARE LIEEKNPALS DEEKAEVAEK VGIGAIRYNL
490 500 510 520 530 540
IKYSPDKKII FRWEDVLNFE GESAPYIQYA HARCSSILRK AEEEGIKVDP ETLFKNADFT
550 560 570 580 590 600
KLSERERELV IMLSKFPRIV EQAGKDVKPH LIAWFANELA SLFNKFYMDH PVLKAEEGVR
610 620
EARLLLVMAV EQVLKNALYL MGIEAPERM