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 Q72E47

Entry ID Method Resolution Chain Position Source
AF-Q72E47-F1 Predicted AlphaFoldDB

No variants for Q72E47

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q72E47

No associated diseases with Q72E47

5 regional properties for Q72E47

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 47 - 58 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 19 - 565 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 609 - 752 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 814 - 872 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 564 - 698 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
MAENALPKGY EPRDVEERWR RHWEDNRTFT PDMDAPGEPY SIVIPPPNVT GALHIGHALN
70 80 90 100 110 120
HVLIDVLCRN ARQQGKKVLW LPGTDHAGIA TQNVVERALA KEGLSRHDLG REAFIERVWQ
130 140 150 160 170 180
WKEEYGNRIL NQIRMLGDSV DWTRERFTMD EGLSKAVRKV FVDLYNGGYI YRGNYIINWC
190 200 210 220 230 240
NRCHTALADD EVDHMPEQGH LYHVRYDFED GSGSVVIATT RPETIMADTG VCVHPEDERY
250 260 270 280 290 300
AGLIGKKILV PVIGRAVPLF ADTYVDREFG TGALKVTPCH DPNDWTLGER HGLAFIQCID
310 320 330 340 350 360
EDGNMTAEAG PYAGLTKEEC RKRIVADLEA SGQLVRVEEL NHSVGHCYRC KTVVEPHMSE
370 380 390 400 410 420
QWFVASTKLA PRARAAVPQM TQIFPESWMK TYFNWLDNIR DWCISRQIWW GHRIPAWTCG
430 440 450 460 470 480
KCGKLIVSEQ DPTACPDCGC TDLTQDPDVL DTWFSSALWP FSTMGWPDKT KDLATFYPTS
490 500 510 520 530 540
VLVTGFDILF FWVARMMMLG MHFMDEVPFK HVYLHALVRD GEGRKMSKST GNVIDPLAMI
550 560 570 580 590 600
DKYGTDSLRF TLAAFAAMGR DIKLSEDRIE GYRHFVNKVW NAARFSLMNL PEEAPAALDL
610 620 630 640 650 660
DNVKGMHHKW ILHRLEELKA SQAAGIDGYR FNEVAQGLYR FWWNEFCDWY LELIKPDMQA
670 680 690 700 710 720
GGERQATAQY VLWTVLREAL LLLHPFMPFV TAEVWQALPG HAGDDIATKL YPAARPGCRD
730 740 750 760 770 780
VKDAEHMELV QATISAVRTI RAELNIAPSY RLTTLVRPAS AEDAATLEEG REMLMTLARL
790 800 810 820 830 840
DGLTVAVDVE APKASASSVV AGNEVIVPLT GAVDFEAELA RLDKELGKIE KDFVQVNKKL
850 860 870 880
ANESFVSKAP ADVVAKERAR AEELSDAKAK LEALQQRFRD AIGK