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 Q6LUW1

Entry ID Method Resolution Chain Position Source
AF-Q6LUW1-F1 Predicted AlphaFoldDB

No variants for Q6LUW1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6LUW1

No associated diseases with Q6LUW1

5 regional properties for Q6LUW1

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 53 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 14 - 631 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 675 - 828 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 888 - 946 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 630 - 764 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
MEKTYNPQSI EQALYQRWEE AGYFKPHGDT SKDAYSIMIP PPNVTGSLHM GHAFQDTIMD
70 80 90 100 110 120
TLIRAERMKG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TKHDYGRDAF IDKIWEWKAE
130 140 150 160 170 180
SGGTITKQLR RLGASVDWDR ERFTMDDGLS AATQEVFVRL FEEDLIYRGK RLVNWDPKLH
190 200 210 220 230 240
TAISDLEVES KDKKGFMWHF RYPLADGVKT ADGKDYIVVA TTRPETMLGD TGVAVNPEDP
250 260 270 280 290 300
RYKDLIGKQI KLPIVGRLIP IVGDEHADMD KGTGCVKITP AHDFNDYEVG KRHSLPMINI
310 320 330 340 350 360
LTFNADIRDA AEVFDTNGEA NDAYNSELPA KYHGMERFAA RKAIVAEFDE LGLLEEVKDH
370 380 390 400 410 420
DLTVPYGDRG GVAIEPMLTD QWYVRTAPLA APAVKAVEDG QIQFVPKQYE NMYFAWMRDV
430 440 450 460 470 480
QDWCISRQLW WGHRIPAWYD NYGKVYVGRT EDEVREKNNL ASVVVLRQDD DVLDTWFSSA
490 500 510 520 530 540
LWTFGTQGWP ENTDALKTFH PSEVLVSGFD IIFFWVARMI MMTMHFVKDE EGNAQVPFKT
550 560 570 580 590 600
VYMTGLIRDE NGDKMSKSKG NVLDPIDMID GIGLEELVEK RCGNMMQPKL AAKIEKQTRK
610 620 630 640 650 660
AFEGGIEPYG TDALRFTLAA MASTGRDINW DMKRLEGYRN FCNKLWNASR YVLMNTEEHD
670 680 690 700 710 720
CGMAEGAELE FSLADQWITS QFEVAAKEFN AHLDNYRLDM AANTLYEFIW NQFCDWYLEL
730 740 750 760 770 780
TKPVLWKGTE AQQRATRYTL ITVLEKTLRL AHPILPYITE SIWQSVKPLV DGVEGETIMT
790 800 810 820 830 840
QALPQFNEDN FNADVVADLE WVKAFITSIR NLRAEYDIAP SKGLDVMIKV ADEKDAARIQ
850 860 870 880 890 900
ANEIVLTSLA KLDSIKVLAK NEETQACATS LVGKSELMIP MAGLIDKDAE LARLDKEVAK
910 920 930 940 950
TQGEIKRIEG KLNNQGFVAK APEVVITKER EKLEGYQETL VKLEAQKETI AAL