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 Q8G0Y3

Entry ID Method Resolution Chain Position Source
AF-Q8G0Y3-F1 Predicted AlphaFoldDB

No variants for Q8G0Y3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8G0Y3

No associated diseases with Q8G0Y3

5 regional properties for Q8G0Y3

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 45 - 56 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 15 - 594 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 636 - 780 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 842 - 902 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 593 - 725 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
MLEKTYDAAA TEPKIAERWE EAGAFKAGAG AKPGADPFAV VIPPPNVTGS LHMGHALNNT
70 80 90 100 110 120
IQDIMVRFER MRGKNVLWQP GIDHAGIATQ MVVERQLAER KEPNRHAMGR EKFIERIWQW
130 140 150 160 170 180
KAESGGMISN QLRRLGASCD WSRERFTMDE GLSRAVLEVF VTLYKQGLIY RDKRLVNWDP
190 200 210 220 230 240
KLLTAISDIE VESREIKGHL WHFRYPLENV PFDPENPHTY IIVATTRPET MLGDTGVAVN
250 260 270 280 290 300
PKDERYHALV GNDVILPLVG RHIPIVADDY ADPEAGSGAV KITPAHDFND FEVGKRNNLR
310 320 330 340 350 360
AINILTPEAA ITLKDNVDFL EDLELTAELK ALIVELDGMD RFAARKRIVE LMDERGYLEK
370 380 390 400 410 420
IDDHTHAVPH GDRGGVPIEP YLTDQWYVNA GELAKPAMAA VRDGRTQIVP KNWEKTYFDW
430 440 450 460 470 480
MENIQPWCVS RQLWWGHQIP AWYGPDGHCF VEKSEAEAKA AARAHYGEDV ALERDTDVLD
490 500 510 520 530 540
TWFSSALWPF STLGWPDKTP ELATYYPTSV LVTGFDILFF WVARMMMMGL HFMEEIPFHT
550 560 570 580 590 600
VYLHALVRDK HGAKMSKSKG NVIDPLELMD EYGADALRFT LAIMAAQGRD VKLDPARIAG
610 620 630 640 650 660
YRNFGTKLWN ATRFAQMNGV KLAPDFRPEN AKLAVNRWIL TELTRATRAV TEGIATYRFN
670 680 690 700 710 720
EAAGAAYRFV WNQFCDWYLE FLKPIFMGDD EAAKAEAQAT AAYCLDQVYK LLHPFMPFMT
730 740 750 760 770 780
EELWSLTASE GKKRDTVLAL AEWPELSFED EDAAADINWL VDLVTGIRSV RAEMNVPAGA
790 800 810 820 830 840
IAPVVVLDAN KVTVDRFARH DAAIKRLARV ERISFEQQAP KGAAQMLLGE ATICIPLGSL
850 860 870 880 890 900
IDLQAEAARL AKEAGKIAAE MDRIEKKLAN EKFVANAREE VVEAERERLV ELKEAAQRVA
TAESRIRDAS