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 Q8P040

Entry ID Method Resolution Chain Position Source
AF-Q8P040-F1 Predicted AlphaFoldDB

No variants for Q8P040

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8P040

No associated diseases with Q8P040

6 regional properties for Q8P040

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 45 - 56 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 17 - 429 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 435 - 559 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 609 - 753 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 813 - 877 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 558 - 697 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
MTELSPKYNP AEVEAGRYQK WLDADVFKPS GDQKAKPYSI VIPPPNVTGK LHLGHAWDTT
70 80 90 100 110 120
LQDIIIRQKR MQGFDTLWLP GMDHAGIATQ AKVEERLREQ GISRYDLGRD KFLDKVWEWK
130 140 150 160 170 180
DEYATTIKEQ WGKMGLSVDY SRERFTLDEG LSKAVRKVFV DLYKKGWIYR GEFIINWDPA
190 200 210 220 230 240
ARTALSDIEV IHKDVEGAFY HMNYMLEDDS RALQVATTRP ETMFGDVAVA VNPEDPRYKD
250 260 270 280 290 300
LIGKHVILPI VNKLIPIVGD EHADPEFGTG VVKITPAHDP NDFEVGQRHN LPQVNVMNDD
310 320 330 340 350 360
GTMNELAGDF AGMDRFEARQ ATVAKLEELG ALVNIEKRVH SVGHSERSGA VVEPRLSTQW
370 380 390 400 410 420
FVKMDELAKQ AMDNQETDDR VDFYPPRFND TFLQWMENVH DWVISRQLWW GHQIPAWYNA
430 440 450 460 470 480
EGEIYVGEEA PEGDGWTQDE DVLDTWFSSA LWPFSTMGWP DTDVEDFKRY FPTSTLVTGY
490 500 510 520 530 540
DIIFFWVSRM IFQSLEFTGR QPFQNVLIHG LIRDEEGRKM SKSLGNGIDP MDVIEKYGAD
550 560 570 580 590 600
SLRWFLSNGS APGQDVRFSY EKMDASWNFI NKIWNISRYI LMNNEGLSLE EAESNVAKVA
610 620 630 640 650 660
ASEAGNVTDQ WILHNLNETI AKVTENFDKF EFGVAGHILY NFIWEEFANW YVELTKEVLY
670 680 690 700 710 720
SDNEAEKVIT RSVLLYTLDK ILRLLHPIMP FVTEEIYAQY AQGSIVTVDY PTVTPAFENE
730 740 750 760 770 780
AAHKGVESLK DLIRAVRNAR AEVNVAPSKP ITILVKTADS ELEDFFTSNV NYIKRFTNPE
790 800 810 820 830 840
KLEISSAIAA PELAMTSIIT GAEIYLPLAD LLNVEEELAR LDKELAKWQK ELDMVGKKLG
850 860 870 880
NERFVANAKP EVVQKEKDKQ ADYQAKYDAT QERIAEMHKL VK