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 O83998

Entry ID Method Resolution Chain Position Source
AF-O83998-F1 Predicted AlphaFoldDB

No variants for O83998

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O83998

No associated diseases with O83998

5 regional properties for O83998

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 60 - 71 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 31 - 579 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 623 - 769 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 831 - 895 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 578 - 714 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
MTQKLQKIVL PPVYGPADFE ARVYACWEQR QAFSPRARGS GTSDSEGCDG HSRQIEGGAR
70 80 90 100 110 120
TFVIAIPPPN ITGVLHMGHC LNTVLQDIVI RYQRMAGACT LWIPGTDHAG IATQHVVERA
130 140 150 160 170 180
LRKEGIHKRE VTREQFVART QQIKDSHQDT IRMQLRKMGA SCDWTCERFT LDAGMSASVR
190 200 210 220 230 240
EAFVTLYERG LLYRSMYLVN WCPRCGTALS DDEVFHQEKD GALYYVRYPL LPRTEEEGNG
250 260 270 280 290 300
VPPPLGTAQV GETIIIATTR PETILADVAV AVHPDDARYQ SLIGRKVCVP MVNRIVPIIA
310 320 330 340 350 360
DSYVAQDFGT GMVKITPAHD PNDWDIGTRH SLEAINMLNP DGSLNDQVPA AYRGLSCAQA
370 380 390 400 410 420
RIQIVADLQA HGLLSREERI VHSVGVCYRC EAVIEPYLSL QWFVKMKPLA SQALAAWKRA
430 440 450 460 470 480
DVQFHPKKWE NTYVRWLEHI RDWCISRQLW WGHRIPVWYC AQCAQQTVSR VDVQRCAHCG
490 500 510 520 530 540
SADITQDPDV LDTWFSSWLW PFSTLGWPQE TQKLRAFYPT SAVITAYDII FFWVARMIMA
550 560 570 580 590 600
GLEFTQTVPF RDVYLHGLVR DKQGRKMSKS LNNGVDPLHI IRTYGADALR FTLAFMCAQG
610 620 630 640 650 660
QDVLIEMDSF KMGSRFANKV WNASRYILGN LEGRRVYAIA HVSLTELDRW IFHTFNETVQ
670 680 690 700 710 720
QVRTALEAYR FNDAAQAVYE FFWNSFCDWY VEASKCSFQK PDEQEKDRAA SVLCTLLEET
730 740 750 760 770 780
LRLLHPFLPF VTEEIYRSLS PSVHDTTQAI PSGAHALLMC APYPVYVPSR VDARACAHIG
790 800 810 820 830 840
AVQEIVRAVR TLRAACGIDP QKAVSVRLRP SSPAQDANAA AQVSCVHDPG AVARTYEELI
850 860 870 880 890 900
CVLAGISSLV YLESDAPKPQ VAVATAGTGF ELFLVTTEGI DRTMLCARLQ KAWQKARQKV
910 920 930 940 950
QQVERKLADA QFCTHAPEEV VTAERKKLAE ARATCHTLAG YLADMNGKPG PLSDSD