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 Q824C7

Entry ID Method Resolution Chain Position Source
AF-Q824C7-F1 Predicted AlphaFoldDB

No variants for Q824C7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q824C7

No associated diseases with Q824C7

1 regional properties for Q824C7

Type Name Position InterPro Accession
active_site ClpP, histidine active site 105 - 118 IPR033135

Functions

Description
EC Number 3.4.21.92 Serine endopeptidases
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-dependent peptidase activity Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPDGEVNKLR DVIDKKILDA RRVFFSEPVT DKSAADAIKK LWYLELSHPG QPIVFVINSP
70 80 90 100 110 120
GGSVDAGFAV WDQIKMMTSP VTTVVTGLAA SMGSVLSLCA APGRRFATPH SRIMIHQPSI
130 140 150 160 170 180
GGPITGQATD LDIHAREILK TKKRIVDVYL EATGQPREVI EKAIDRDMWM TADEAKDFGL
190
LDGILFSFDD L