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 Q9A8N3

Entry ID Method Resolution Chain Position Source
AF-Q9A8N3-F1 Predicted AlphaFoldDB

No variants for Q9A8N3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9A8N3

No associated diseases with Q9A8N3

5 regional properties for Q9A8N3

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 54 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 15 - 588 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 630 - 778 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 838 - 902 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 587 - 720 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
MLEKTFDPQS VEPRLYAAWE ASGAFKPAED PNAEPFVIVI PPPNVTGSLH IGHALNNTLQ
70 80 90 100 110 120
DVLTRFHRMR GKAALWLPGT DHAGIATQMV VERQLAAAGN IGRRDMGREA FVDKVWEWKA
130 140 150 160 170 180
ESGGAITNQL RRLGASCDWS RERFTLDEGL SAAVRKVFVQ LYKQNLLYRD KRLVNWDPQF
190 200 210 220 230 240
QTAISDLEVE QKEVDGAYWH FAYPLADGVT YQHPIAFDED GKATEFETRD YIVVATTRPE
250 260 270 280 290 300
TMLGDTGVAV HPDDERYKGL VGKFVTLPIV GRRIPIVADD YADPTKGSGA VKITPAHDFN
310 320 330 340 350 360
DFGVGKRAGL EAINILTVEA KLNDSVPAEY VGMDRFVARK AIVARAEEEG WLKEIEKTKH
370 380 390 400 410 420
MVPHGDRSGV VIEPFLTDQW YVDAKTLAQP ALKAVETGET IFEPKHWEKT YFEWLRNIEP
430 440 450 460 470 480
WCVSRQLWWG HRIPAWFGPE GSIFVEESEE AAYAAARAQF GADVQLTQDE DVLDTWFSSA
490 500 510 520 530 540
LWPFSTLGWP EKTSDLERFY PTSTLVTGFD IIFFWVARMM MMGIHFMGEA PFKQVFINAL
550 560 570 580 590 600
VRDEKGAKMS KSKGNVMDPL ILIDELGCDA VRFTLTAMSG QARDIKLSKQ RIEGYRNFGT
610 620 630 640 650 660
KLWNASRFAQ MNECVRVEGF DPSTVQQPIN KWIRGETVKT VAEVTKALEA PSFDEAAGAL
670 680 690 700 710 720
YRFVWNVFCD WYLELAKPIL NGDDAAAKAE TRATAAWALD VILKLLHPVM PFITEELWEK
730 740 750 760 770 780
TAEFGPARET MLISAKWPEL PADWIDAEAE AEIGWLVETV GEIRSIRAEM NVPPSAKPGL
790 800 810 820 830 840
TIVGAGPETK ARLARHRDLL LTLARLDAVR EADAAPAGSA PVVMGEATGA LGVAEFIDVA
850 860 870 880 890 900
AEKARLTKDI AGHAGEIEKV NKKLGNPDFL ARAKEEVVEE NRERLAEAEA AKAKLEAALS
RLASVG