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 A5US83

Entry ID Method Resolution Chain Position Source
AF-A5US83-F1 Predicted AlphaFoldDB

No variants for A5US83

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A5US83

No associated diseases with A5US83

1 regional properties for A5US83

Type Name Position InterPro Accession
conserved_site Chaperonin Cpn60, conserved site 404 - 415 IPR018370

Functions

Description
EC Number 5.6.1.7 Enzymes altering polypeptide conformation or assembly
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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
isomerase activity Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
unfolded protein binding Binding to an unfolded protein.

1 GO annotations of biological process

Name Definition
protein refolding The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAKQVIFNEQ ARAALKHGVD TLALAVKTTL GPRGRNVAMG KKWGAPSVTH DGVTVAKEVE
70 80 90 100 110 120
LKDPFQNMGA QLLKEAASKT NDVAGDGTTT ATVLAQAMID EGLKLVAAGA NPMIFKRGLD
130 140 150 160 170 180
KGREALVARI KEQSITLKSR DEIRQVATIS AQDPEIGELL ATIMDKIGHD GVVTIEEGKG
190 200 210 220 230 240
TTLEYELVEG MQFDRGYISP YFVTDSSRME AVIDEPYILI TDKKISAVND LLPILEAVLA
250 260 270 280 290 300
TGKKDLVIIA EDVDGEALAT LVVNKMRGTL NALAVKAPGF GDRRKAMLQD IAILTGGTVI
310 320 330 340 350 360
SEEVGRKLDS AKVQDLGRAR RVKSDKDNTV IVEGFGDKQA IQARIRQLKQ QIETTTSDYD
370 380 390 400 410 420
REKLQERVAK LSGGVAVIKV GAPTEPALKE RKARVEDALN ATRAAVEEGI VPGGGIALLN
430 440 450 460 470 480
AIPALDNVQT QFEEERMALN ILRRALEEPL RQLAINAGED GSVVVNQVRT LQREHNNPNY
490 500 510 520 530 540
GFDVMTGKYV DLMQAGIIDP AKVVRTALEN AVSVAGIVLT TDALITDAPE PKKNGARTPS
MPEEEF