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 B5YL60

Entry ID Method Resolution Chain Position Source
AF-B5YL60-F1 Predicted AlphaFoldDB

No variants for B5YL60

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B5YL60

No associated diseases with B5YL60

4 regional properties for B5YL60

Type Name Position InterPro Accession
domain Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal 198 - 443 IPR006096
domain Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, dimerisation domain 53 - 181 IPR006097
active_site Leu/Phe/Val dehydrogenases active site 118 - 131 IPR033524
domain NAD(P) binding domain of glutamate dehydrogenase 191 - 444 IPR033922

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
asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: L-glutamine + aspartyl-tRNA(Asn) + ATP = L-glutamate + asparaginyl-tRNA(Asn) + phosphate + ADP.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP.

2 GO annotations of biological process

Name Definition
glutaminyl-tRNAGln biosynthesis via transamidation A tRNA aminoacylation process in which glutaminyl-tRNAGln is formed by a tRNA-dependent two-step pathway. In the first step a non-discriminating glutamyl-tRNAGlx synthetase generates the misacylated L-glutamyl-tRNAGln species, and in the second step it is amidated to the correctly charged L-glutaminyl-tRNAGln by a glutamyl-tRNAGln amidotransferase.
translation The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MQYEAVIGLE VHAQLLTESK IFCGCSTQFG AEPNTQVCPV CLGMPGVLPV LNKKAVEYTV
70 80 90 100 110 120
KTGLAMNCKI APYSRFARKN YFYPDLPKGY QISQYELPLC EDGYLEIMLN GTKRKIRIKR
130 140 150 160 170 180
IHLEEDAGKN IHDPSGYSFV DFNRTGVPLM EIVSEPDIRS PKEAALYMKK LRAILRYLGV
190 200 210 220 230 240
CDGNLEQGSL RCDANVSVRP VGSTEFGVKT EIKNINSFRF VEKALEYEIK RQIKLIENGE
250 260 270 280 290 300
KIIQETRLWD SQTGTTQSMR SKEEAHDYRY FPEPDLVPVV VSEDWIEKIK KDMPELPDQK
310 320 330 340 350 360
IERFIKEYGL PQYDSEILTE EKALSEWFEE AVKLGGKPKE VANWIMVELL RLLNEEGKDI
370 380 390 400 410 420
NECSLKPIQL VELIELINKG TINRNTAKEV FEEMYKTGKT AEAIVREKGL TQISDDSVII
430 440 450 460 470
EAIKEVMNKN PKEVERFRNG EEKLIGFFVG QVMKITKGKA NPKLVNELIF KILKE