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 Q92QQ2

Entry ID Method Resolution Chain Position Source
AF-Q92QQ2-F1 Predicted AlphaFoldDB

No variants for Q92QQ2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q92QQ2

No associated diseases with Q92QQ2

1 regional properties for Q92QQ2

Type Name Position InterPro Accession
domain Adaptor protein ClpS, core 20 - 98 IPR003769

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

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
protein dimerization activity The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
unfolded protein binding Binding to an unfolded protein.
zinc ion binding Binding to a zinc ion (Zn).

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSKVSGSNGG DSKNTLYCSF CGKSQHEVRK LIAGPTVFIC DECVELCMDI IREENKTSMV
70 80 90 100 110 120
KSRDGVPTPQ EIIKVLDEYV IGQQQAKRIL SVAVHNHYKR LAHAAKSSDV ELAKSNIMLV
130 140 150 160 170 180
GPTGCGKTYL AQTLARIIDV PFTMADATTL TEAGYVGEDV ENIILKLLQA ADYNVERAQR
190 200 210 220 230 240
GIVYIDEVDK ISRKSDNPSI TRDVSGEGVQ QALLKIMEGT VASVPPQGGR KHPQQEFLQV
250 260 270 280 290 300
DTTNILFICG GAFAGLDKII SARGEKTSIG FGATVRAPED RRVGEVLREL EPEDLVKFGL
310 320 330 340 350 360
IPEFIGRLPV LATLEDLDED ALIQILSEPK NALVKQYQRL FEMEDVELNF HEDALREIAR
370 380 390 400 410 420
RAIVRKTGAR GLRSIMEKIL LDTMFELPTL EGVREVVISD EVVKGTARPL YIYSERSEEK
TNVSA