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 A6UW15

Entry ID Method Resolution Chain Position Source
AF-A6UW15-F1 Predicted AlphaFoldDB

No variants for A6UW15

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6UW15

No associated diseases with A6UW15

1 regional properties for A6UW15

Type Name Position InterPro Accession
domain FAD-dependent oxidoreductase 2, FAD binding domain 5 - 410 IPR003953

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.

2 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).

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
MSDIRDTILK YVLQNSIKFK GAPNPKAIMG KILGENPDLR KKAGEVSKII AEIIKEIENM
70 80 90 100 110 120
PLNEQQAKLE SLAPELLNSK PAERKKKELQ LKNVKEGAPV VMRFAPNPSG PLHLGHARAA
130 140 150 160 170 180
VLNDYFAKKY NGKLILRLED TDPKRVMPEA YEMIKEDLEW LGVKIDDVIV QSDRLPIYYE
190 200 210 220 230 240
YGTKLIEMGH AYVCDCEAEE FRELRANGKP CVCRDLGVEK NLELWNKMLN NEIDGVAVRL
250 260 270 280 290 300
KTDIEHKNPS IRDFPIFRIE NTPHPKTGTK YRVYPLMNLS VSVDDHLLGM THVLRGKDHI
310 320 330 340 350 360
VNTEKQKYIF DYFGWEMPEY IHYGILKIDG PILSTSKMSE GIKNNEFTGW DDPRFGTLRA
370 380 390 400 410 420
LKRRGIKPEA IYKSMVDIGV KQADVKYSWE NLHAVNKDII DKDARRFFFV ENPKTLIIEG
430 440 450 460 470 480
AKITTINLRA HPSREEFGTR ELIFDGNIYI SDDLEVNKMY RLMELHNIVV EKIENNTIYA
490 500 510 520 530 540
KYHSDDFKIA KENKAKIIHW IPVKDAIPTT VINTEGEKIK GFAEKDFKIV NIDDFVQFER
550 560
FGFVRIDEKK DDEIICYYTH N