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 Q7VNS3

Entry ID Method Resolution Chain Position Source
AF-Q7VNS3-F1 Predicted AlphaFoldDB

No variants for Q7VNS3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7VNS3

No associated diseases with Q7VNS3

1 regional properties for Q7VNS3

Type Name Position InterPro Accession
domain Threonylcarbamoyl-AMP synthase-like domain 1 - 184 IPR006070

Functions

Description
EC Number 2.7.7.87 Nucleotidyltransferases
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.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
double-stranded RNA binding Binding to double-stranded RNA.
L-threonylcarbamoyladenylate synthase Catalysis of the reaction: L-threonine + ATP + bicarbonate = L-threonylcarbamoyladenylate + diphosphate + H(2)O.

1 GO annotations of biological process

Name Definition
tRNA threonylcarbamoyladenosine modification The attachment of a carbonyl group and a threonine to the amino group of the adenine residue immediately 3' of the anticodon, in tRNAs that decode ANN codons (where N is any base).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNNLLAVIEL LKQNQVVAYP TESVFGLGCN PNNEEAIRQL LQLKNRPIEK GLILVAPTKE
70 80 90 100 110 120
LLLPYIDESQ LTEKHWQRFD TITEQAVTWI MPVHKNVSHY LTGKFNTIAV RLCRVPAVVK
130 140 150 160 170 180
LCESLGFALT STSANFTGLP PCRTALEVKQ QFGDHFPVLE AETGNRMNPS EIRDIFTQHI
FRQG