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 A9M5C1

Entry ID Method Resolution Chain Position Source
AF-A9M5C1-F1 Predicted AlphaFoldDB

No variants for A9M5C1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9M5C1

No associated diseases with A9M5C1

1 regional properties for A9M5C1

Type Name Position InterPro Accession
domain Adaptor protein ClpS, core 34 - 111 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
MSKVSNGGGD SKNTLYCSFC GKSQHEVRKL IAGPTVFICD ECVELCMDII REENKSSMVK
70 80 90 100 110 120
SREGVPTPQE IMAVLDDYVI GQKDAKRVLS VAVHNHYKRL AHQSKNSDIE LAKSNILLVG
130 140 150 160 170 180
PTGCGKTYLA QTLARIIDVP FIMADATTLT EAGYVGEDVE NIILKLLQAA DYNVERAQRG
190 200 210 220 230 240
IVYIDEVDKI SRKSDNPSIT RDVSGEGVQQ ALLKIMEGTV ASVPPQGGRK HPQQEFLQVD
250 260 270 280 290 300
TTNILFICGG AFASLDRIIS ARGEKTSIGF GATVKSVDER RIGEVFKELE PEDLLKFGLI
310 320 330 340 350 360
PEFVGRLPVI ATLEDLDVDA LVQILTEPKN ALVKQYQRLF DMENVELVFH DDALRAIANK
370 380 390 400 410 420
VVEHKTGARG LRSIMEKILL DTMFELPTLE GVREVVISGD VVDGSARPLY IYAERQDEKG
NVSA