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 Q8FAD1

Entry ID Method Resolution Chain Position Source
AF-Q8FAD1-F1 Predicted AlphaFoldDB

No variants for Q8FAD1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8FAD1

No associated diseases with Q8FAD1

5 regional properties for Q8FAD1

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 53 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 14 - 631 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 674 - 824 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 886 - 944 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 630 - 764 IPR033705

Functions

Description
EC Number 6.1.1.9 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.

3 GO annotations of molecular function

Name Definition
aminoacyl-tRNA editing activity The hydrolysis of an incorrectly aminoacylated tRNA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
valine-tRNA ligase activity Catalysis of the reaction: L-valine + ATP + tRNA(Val) = L-valyl-tRNA(Val) + AMP + diphosphate + 2 H(+).

1 GO annotations of biological process

Name Definition
valyl-tRNA aminoacylation The process of coupling valine to valyl-tRNA, catalyzed by valyl-tRNA synthetase. The valyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a valine-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
MEKTYNPQDI EQPLYEHWEK QGYFKPNGDE SQESFCIMIP PPNVTGSLHM GHAFQQTIMD
70 80 90 100 110 120
TMIRYQRMQG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TRHDYGREAF IDKIWEWKAE
130 140 150 160 170 180
SGGTITRQMR RLGNSVDWER ERFTMDEGLS NAVKEVFVRL YKEDLIYRGK RLVNWDPKLR
190 200 210 220 230 240
TAISDLEVEN RESKGSMWHI RYPLADGAKT ADGKDYLVVA TTRPETLLGD TGVAVNPEDP
250 260 270 280 290 300
RYKDLIGKYV ILPLVNRRIP IVGDEHADME KGTGCVKITP AHDFNDYEVG KRHALPMINI
310 320 330 340 350 360
LTFDGDIRES AQVFDTKGNE SDIYSSEIPA EFQKLERFAA RKAVVAAVDA LGLLEEIKPH
370 380 390 400 410 420
DLTVPYGDRG GVVIEPMLTD QWYVRADVLA KPAVEAVENG DIQFVPKQYE NMYFSWMRDI
430 440 450 460 470 480
QDWCISRQLW WGHRIPAWYD EAGNVYVGRN EDEVRKENNL GADVALRQDE DVLDTWFSSA
490 500 510 520 530 540
LWTFSTLGWP ENTDALRQFH PTSVMVSGFD IIFFWIARMI MMTMHFIKDE NGKPQVPFHT
550 560 570 580 590 600
VYMTGLIRDD EGQKMSKSKG NVIDPLDMVD GISLPELLEK RTGNMMQPQL ADKIRKRTEK
610 620 630 640 650 660
QFPNGIEPHG TDALRFTLAA LASTGRDINW DMKRLEGYRN FCNKLWNASR FVLMNTEGQD
670 680 690 700 710 720
CGFNGGEMTL SLADRWILAE FNQTIKAYRE ALDSFRFDIA AGILYEFTWN QFCDWYLELT
730 740 750 760 770 780
KPVMNGGTEA ELRGTRHTLV TVLEGLLRLA HPIIPFITET IWQRVKVLCG ITADTIMLQP
790 800 810 820 830 840
FPQYDASQVD EAALADTEWL KQAIVAVRNI RAEMNIAPGK PLELLLRGCS ADAERRVNEN
850 860 870 880 890 900
RGFLQTLARL ESITVLPADD KGPVSVTKIV DGAELLIPMA GLINKEDELA RLAKEVAKIE
910 920 930 940 950
GEISRIENKL ANEGFVARAP EAVIAKEREK LEGYAEAKAK LIEQQAVIAA L