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 Q8I0H7

Entry ID Method Resolution Chain Position Source
AF-Q8I0H7-F1 Predicted AlphaFoldDB

No variants for Q8I0H7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8I0H7

No associated diseases with Q8I0H7

3 regional properties for Q8I0H7

Type Name Position InterPro Accession
conserved_site Heat shock protein 70, conserved site 35 - 42 IPR018181-1
conserved_site Heat shock protein 70, conserved site 219 - 232 IPR018181-2
conserved_site Heat shock protein 70, conserved site 360 - 374 IPR018181-3

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
extracellular matrix A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

7 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.
heat shock protein binding Binding to a heat shock protein, a protein synthesized or activated in response to heat shock.
misfolded protein binding Binding to a misfolded protein.
protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process.
unfolded protein binding Binding to an unfolded protein.

3 GO annotations of biological process

Name Definition
cellular response to unfolded protein Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.
chaperone cofactor-dependent protein refolding The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release.
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
MLRSLKALKL NSLNAQKGIR QFCSDSKISG QVIGIDLGTT NSCVAVMQGA EARVLENAEG
70 80 90 100 110 120
GRTTPSVVAF TEDNQKIVGL PAKRQMVTNA ENTLFATKRL IGRRFDDPMT KKDMTMVPYK
130 140 150 160 170 180
IVKGPNGDAW FEVKGKMISP SEAGAMVLQK MKETAETNLG GPVTDAVITV PAYFDDSQRQ
190 200 210 220 230 240
ATRDAGTIAG LKVQRIINEP TAAALAYGFK KDEPKTVAVY DLGGGTFDIS ILEIVGGVFE
250 260 270 280 290 300
VRATNGDTFL GGEDFDNALL EHFVAEFKKE KGIDLTKDTM ATQRLREAAE KAKCELSSTL
310 320 330 340 350 360
TTEINLPYIS AGPSGPVHFN MKLTRSKFEQ LVADLIQRTI GPCNICLKDA GLSTSEINEV
370 380 390 400 410 420
ILVGGMTRMP KVQELAKSTF NKEPFKGVNP DEAVAVGAAI QGGVLKGDTK GIVLVDVTPL
430 440 450 460 470 480
SLGIETLGGV FTRLIKKNTN IPASKTDTFS TAADGQSEVE IKVFQGEREM AVDNKLLAKF
490 500 510 520 530 540
TLFGLPPLPK GVPQIEVTFD IDVNGMLQVI AKDKATGKAQ QVRIQTSGGL SKDDIARILK
550 560 570 580 590 600
ESEANAEVDR KRKELVEARN NGESVVYQVE KDLVEFKDYL SQPQTEEIKK AVQAVRDVLA
610 620 630 640 650
KEDGSAIEAE IKKLHDLTRS SFETAYKAKL DSSASKSSST ENKENKDNTT EAEFTEKK