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 A6SUQ8

Entry ID Method Resolution Chain Position Source
AF-A6SUQ8-F1 Predicted AlphaFoldDB

No variants for A6SUQ8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6SUQ8

No associated diseases with A6SUQ8

5 regional properties for A6SUQ8

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 44 - 55 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 18 - 636 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 690 - 842 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 901 - 965 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 635 - 779 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
MELAKSFDPA DIEAFWRTEW EKRGYYTATT DADKPAFSIQ LPPPNVTGTL HLGHGFNQTI
70 80 90 100 110 120
MDGLTRYHRM RGFNTAWIPG TDHAGIATQI VVERQLDAQK ITRHDLGREK FVEKVWEWKE
130 140 150 160 170 180
KSGSTITGQI RRLGASPDWS REYFTMDEPR SKTVTEVFVR LVEQGLIYRG KRLVNWDPVL
190 200 210 220 230 240
GTAVSDLEVV SEEEDGQMWN IRYPLADGSS YKFPIAFDEA GNATEWEERN FIVVATTRPE
250 260 270 280 290 300
TMLGDVAVAV DPTDTRYQHL VGKLLTLPLC ERTIPIIADD YVDKEFGTGC VKITPAHDFN
310 320 330 340 350 360
DYAVGQRHNL DKISILTLDA KINENAPAAY QGLDRFAARK QIVADLDAQG LLELVKPHKL
370 380 390 400 410 420
MVPRGDRTNT VIEPMLTDQW FVAMSKPAPE GTYFPGKSIT EVALEKVANG EIKMLPENWT
430 440 450 460 470 480
NTYNQWLNNI QDWCISRQLW WGHQIPAWYD SEGKVYVARN EDEAKAKATA AGYNGPLTRD
490 500 510 520 530 540
EDVLDTWFSS ALVPFSTLGW PEETPDFKTF LPSSVLVTGF DIIFFWVARM VMMTTHFTGK
550 560 570 580 590 600
VPFKTVYVHG LIRDSSGQKM SKSKGNTLDP IDLIDGINVD ELVAKRTVGL MNPKQAASIE
610 620 630 640 650 660
KSTRKEFPAG ISAYGTDALR FTMASYASLG RNINFDLSRC EGYRNFCNKL WNATRFVLMN
670 680 690 700 710 720
CEGHDCGFRD APCAAGDCDP GGYTDFSQAD RWIVSKLQRT EADIAKGFAD YRFDNIAASL
730 740 750 760 770 780
YQFIWDEYCD WYLEVAKVQI QTGTEAQQRA TRRTLLRVLE TILRLAHPVI PFITEALWQT
790 800 810 820 830 840
VAPLTGYKPN PAGDSIMLQP YPEAQAGKID EQAENWMAEL KAMTDACRNL RGEMQLSPAL
850 860 870 880 890 900
RVPLIMEASD PTQAARLQSF APYLQALAKL SEVNVADKLP ESPAPVSIVG TAKLMLKVEI
910 920 930 940 950 960
DVAAERERLS KEIARLDGEI TKANSKLGNE SFVARAPAQV VAQEKERVAN FSATLNKLRE
QFAKL