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

1 structures for A5N8F9

Entry ID Method Resolution Chain Position Source
AF-A5N8F9-F1 Predicted AlphaFoldDB

No variants for A5N8F9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5N8F9

No associated diseases with A5N8F9

3 regional properties for A5N8F9

Type Name Position InterPro Accession
conserved_site Fumarate lyase, conserved site 281 - 290 IPR020557
domain Fumarate lyase, N-terminal 12 - 306 IPR022761
domain Argininosuccinate lyase, C-terminal 369 - 437 IPR029419

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
MDFKKLAAEE IKKNIDLELN FIEGLIEVPP KPEMGDYAFP CFQLAKVLKK APNIISKELK
70 80 90 100 110 120
DKLHSKYFEK IENLGPYVNF FVDKKIFTEY TLKEILLKGD SYGSSDMGEG KNVVVEYSSP
130 140 150 160 170 180
NIAKPFHVGH LFSTSIGNAL YKMINFQGYN CTRINHLGDW GTQFGKLIAA YNRWCNAEEL
190 200 210 220 230 240
NRDPIKELLR IYVKFHEEAE KDPSLNEEGR MYFKKLEDGS EEEIKLWKKF KDLSLREFKK
250 260 270 280 290 300
VYDLLKVDFD SYAGESFYTD KMDAVVEEID KKGLLVESNG AKVVLLDEYN IPPCIVKKSD
310 320 330 340 350 360
GTTIYATRDL AAAIYRKKTY DFYKSIYVVG LDQSLHFKQV FTTLKLMGKD WADSCKHVGF
370 380 390 400 410 420
GLVRFANKKL STRKGDVIFL EELLNKSVER TLEIINEKNP KLENKEEAAK KIGIGAVIFT
430 440 450 460 470 480
YLKNNREKDI VFDWNEMLSF EGETGPYVQY SYARGKSILR KSEEASYDEN QIDYSKLGSK
490 500 510 520 530 540
EEFELVKILE NFNKSIINAI NRLEPFIVTR YVIDVAKAFN KFYNAHSIMN AADENIKKAR
550 560
LYLVKCTCQV LKNGLNLMGI EVVEKM