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 Q83ME2

Entry ID Method Resolution Chain Position Source
AF-Q83ME2-F1 Predicted AlphaFoldDB

No variants for Q83ME2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q83ME2

No associated diseases with Q83ME2

1 regional properties for Q83ME2

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

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
aminoacyl-tRNA ligase activity Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
zinc ion binding Binding to a zinc ion (Zn).

2 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.
tRNA modification The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLPPYFLFKE MTDTQYIGRF APSPSGELHF GSLIAALGSY LQARARQGRW LVRIEDIDPP
70 80 90 100 110 120
REVPGAAETI LRQLEHYGLH WDGDVLWQSQ RHDAYREALA WLHEQGLSYY CTCTRARIQS
130 140 150 160 170 180
IGGIYDGHCR VLHHGPDNAA VRIRQQHPVT QFTDLLRGII HADEKLARED FIIHRRDGLF
190 200 210 220 230 240
AYNLAVVVDD HFQGVTEIVR GADLIEPTVR QIPLYQLFGW KVPDYIHLPL ALNPQGAKLS
250 260 270 280 290 300
KQNHAPALPK GDPRPVLIAA LQFLGQQAEA HWQDFSVEQI LQSAVKNWML TAVPESAIVN
STFSNASC