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 B3CL71

Entry ID Method Resolution Chain Position Source
AF-B3CL71-F1 Predicted AlphaFoldDB

No variants for B3CL71

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B3CL71

No associated diseases with B3CL71

1 regional properties for B3CL71

Type Name Position InterPro Accession
conserved_site Chaperonin Cpn60, conserved site 410 - 421 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
MANIVVSGEQ LQEAFREVAA MVDSTVGATA GPRGNTIGIS KPYGGPEVTK DGYKVMKGIK
70 80 90 100 110 120
PEKPLHSAIV STIAQSASQC NDKVGDGTTT CSILTSNMIM EASKSIAAGN DRICIKNGIQ
130 140 150 160 170 180
KAKDVILKEI TSMSRTISLE KMDEVAQVAI ISANGDKDIG NSIADAVKKV GKEGVITVEE
190 200 210 220 230 240
SKGSKELEVE LTTGMQFDRG YLSPYFVTNN EKMSVELDDP YLLITEKKLN IIQPLLPILE
250 260 270 280 290 300
AIFKSGKPLF IIAEDVEGEA LSTLVINKLR GLKVAAVKAP GFGDRRKEML EDIAALTGAK
310 320 330 340 350 360
YVIKDELGIK MEDLTLEDLG TAKNVKITKD NTTIVSEDSD CDKQNRVNAR INQIKSQIET
370 380 390 400 410 420
STSDYDKEKL RERLAKLSGG VAVLKVGGAT EVEVKERRDR VEDALHATRA AIEEGIVPGG
430 440 450 460 470 480
GVALLYAASA LDKLKASSDE EQIGINIVKK VLSAPIKRLV KNAGLESAVI IDYLIKQNDK
490 500 510 520 530 540
ELIYNVEAMN YANASTAGVI DPAKVVRIAF ETAVSVASAL ITTESMIVDL PNKEENASSP
550
MGAGAMGGMG GF