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 Q6N6N1

Entry ID Method Resolution Chain Position Source
AF-Q6N6N1-F1 Predicted AlphaFoldDB

No variants for Q6N6N1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6N6N1

No associated diseases with Q6N6N1

5 regional properties for Q6N6N1

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 45 - 56 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 17 - 610 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 653 - 827 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 889 - 954 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 610 - 741 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
MIEKTYQPAD IEARISRAWE DAEAFKAGRP ERRDAVPYSI VIPPPNVTGS LHMGHALNNT
70 80 90 100 110 120
LQDILCRFER MRGRDVLWQP GTDHAGIATQ MVVERQLMER QEPSRRDMGR AKFLERVWQW
130 140 150 160 170 180
KAESGGVIVN QLKRLGASCD WSRERFTMDE GLSRAVAKVF VELHRQGLIY KDKRLVNWDP
190 200 210 220 230 240
KLLTAISDLE VQQIEVKGNL WHLRYPIEGK TFDPADPSSF IVVATTRPET MLGDSAVAVN
250 260 270 280 290 300
PEDERYTHLV GKHVILPLVG RRIPIVADEY SDPEKGSGAV KITPAHDFND FEVGKRHHLP
310 320 330 340 350 360
QINVLDIEGK ISVADNSAYL EGLPEGAREF AGEIDGTDRF VARKIIVARL DDFGFLEKIE
370 380 390 400 410 420
PNVHMVPHGD RSGVVIEPFL TDQWYVDAKT LAQPAIAAVR SGETTFVPKN WEKTYFEWME
430 440 450 460 470 480
NIQPWCISRQ LWWGHQIPAW YGPDGKVFVA ETEEEAVGNA LGYYVEQEVI TPAQAHDMAE
490 500 510 520 530 540
DPAKREGFIT RDEDVLDTWF SSALWPFSTL GWPDETPELD RYYPTNVLVT GFDIIFFWVA
550 560 570 580 590 600
RMMMMGLHFM DDVPFPTVYI HALVRDEKGA KMSKSKGNVI DPLNLIDEYG ADALRFTLAA
610 620 630 640 650 660
MAAQGRDIKL ATSRVEGYRN FATKLWNACR FAEMNGCVAP AGFDYTAAKE TLNRWIAHET
670 680 690 700 710 720
VRAVREVTEA IESYRFNDAA EAAYRFVWNV YCDWYLELAK PVLMGEEGAA KTETRAMVAW
730 740 750 760 770 780
ARDEILKILH PFMPFITEEL WAVTAPRDGL LALAPWSRKG GISDEEVSVL AASAATDPMA
790 800 810 820 830 840
GPAMLAIPEP QEPDFTDDAA EAEIGWVVDL VTAIRSVRAE MNIVPSTLTP LVLAGASADT
850 860 870 880 890 900
NARASRWSDV IKRLARVGEI SFADAAPQGA VQLLVRGEVA ALPLKGVVDF AAEQARLEKE
910 920 930 940 950
LGKAEADIKR AEAKLANEKF VANAAEEVVE EEREKREAAV ARKVKILEAL LRLKNAS