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 Q8D375

Entry ID Method Resolution Chain Position Source
AF-Q8D375-F1 Predicted AlphaFoldDB

No variants for Q8D375

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8D375

No associated diseases with Q8D375

1 regional properties for Q8D375

Type Name Position InterPro Accession
domain Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain 19 - 284 IPR020058

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
MTVRTRFAPS PTGELHLGSI RTALYSWLFA RKNNGEFILR IEDTDEERIK KISINNIIET
70 80 90 100 110 120
MKLLGLNWDH GPYFQTKKLE KYNIIAKEMI YSGIAYKCYC SKNRINNLRI MQINKGEKPK
130 140 150 160 170 180
YDGFCRNIEE KNIKNKRFVV RFSNPKNGYV IFNDLIRGTL KFKNSELDDL IILRSNKIPT
190 200 210 220 230 240
YNFCSVIDDH DMNISHVIRG EDHINNTPRQ INIFKALKIK CPKYAHISMI LDKDRKKLSK
250 260 270 280 290 300
KNQSTDVMKY IKNGFLPEAL LNYLVRLGWS YGNQEIFNID EMKKLFNLKS VGKSSCIFDI
310 320 330 340 350 360
NKLLWINQYY IQKLSDYDIS SQIKKFFNKK EIDFNQGPKI ENLIKIFKKK SRTLKEIFNQ
370 380 390 400 410 420
ILFFYEDFSK VNFDLIKKYF TIDTNVHLKI FCKKLEKTSL WSVEEIKNTF FCTIKELNFN
430 440 450 460 470
IKKIAMPIRI ILSGSEHSPS IYSIIYSCGK LQTIKKIKIA IKFINDNKKK LNL