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 Q72LI9

Entry ID Method Resolution Chain Position Source
AF-Q72LI9-F1 Predicted AlphaFoldDB

No variants for Q72LI9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q72LI9

No associated diseases with Q72LI9

3 regional properties for Q72LI9

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 100 - 111 IPR001412
domain Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain 93 - 395 IPR020058
domain Glutamyl/glutaminyl-tRNA synthetase, class Ib, anti-codon binding domain 398 - 541 IPR020059

Functions

Description
EC Number 6.1.1.17 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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
glutamate-tRNA ligase activity Catalysis of the reaction: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).
tRNA binding Binding to a transfer RNA.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
glutamyl-tRNA aminoacylation The process of coupling glutamate to glutamyl-tRNA, catalyzed by glutamyl-tRNA synthetase. The glutamyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a glutamic acid-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
MVVTRIAPSP TGDPHVGTAY IALFNYAWAR RNGGRFIVRI EDTDRARYVP GAEERILAAL
70 80 90 100 110 120
KWLGLSYDEG PDVGGPHGPY RQSERLPLYQ KYAEELLKRG WAYRAFETPE ELEQIRKEKG
130 140 150 160 170 180
GYDGRARNIP PEEAEERARR GEPHVIRLKV PRPGTTEVKD ELRGVVVYDN QEIPDVVLLK
190 200 210 220 230 240
SDGYPTYHLA NVVDDHLMGV TDVIRAEEWL VSTPIHVLLY RAFGWEAPRF YHMPLLRNPD
250 260 270 280 290 300
KTKISKRKSH TSLDWYKAEG FLPEALRNYL CLMGFSMPDG REIFTLEEFI QAFTWERVSL
310 320 330 340 350 360
GGPVFDLEKL RWMNGKYIRE VLSLEEVAER VKPFLREAGL SWESEAYLRR AVELMRPRFD
370 380 390 400 410 420
TLKEFPEKAR YLFTEDYPVS EKAQRKLEEG LPLLKELYPR LRTQEEWTEA ALEALLRGFA
430 440 450 460
AEKGVKLGQV AQPLRAALTG SLETPGLFEI LALLGKERAL RRLERALA