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 Q96UX5

Entry ID Method Resolution Chain Position Source
AF-Q96UX5-F1 Predicted AlphaFoldDB

No variants for Q96UX5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q96UX5

No associated diseases with Q96UX5

8 regional properties for Q96UX5

Type Name Position InterPro Accession
domain AAA+ ATPase domain 125 - 271 IPR003593-1
domain AAA+ ATPase domain 526 - 672 IPR003593-2
domain ATPase, AAA-type, core 130 - 235 IPR003959-1
domain ATPase, AAA-type, core 525 - 693 IPR003959-2
conserved_site ClpA/B, conserved site 1 221 - 233 IPR018368
domain Clp ATPase, C-terminal 699 - 788 IPR019489
conserved_site ClpA/B, conserved site 2 560 - 578 IPR028299
domain ClpA/ClpB, AAA lid domain 269 - 370 IPR041546

Functions

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

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.

5 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.
chaperone binding Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
misfolded protein binding Binding to a misfolded protein.
unfolded protein binding Binding to an unfolded protein.

7 GO annotations of biological process

Name Definition
cellular heat acclimation Any process that increases heat tolerance of a cell in response to high temperatures.
cellular response to heat 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 a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
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.
mitochondrial genome maintenance The maintenance of the structure and integrity of the mitochondrial genome; includes replication and segregation of the mitochondrial chromosome.
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.
protein stabilization Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
protein unfolding The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLSSRIPKGK LLKQTSATSY LNLAKSMPIT TARYRPNQYY ANELAKLNVF TIHNIPSPCF
70 80 90 100 110 120
SQVRNFHSSF PRKLQMQQTE QGDNRPALEK FGSDLTQLAK EGKLDPVIGR DHEIRRTIQI
130 140 150 160 170 180
LSRRTKNNPV LIGNAGTGKT AVMEGLAQRI IRGEVPDSMK DKQIITLDLA GIISGAKYRG
190 200 210 220 230 240
DFESKLKSIL KEVEEKNGKV ILFIDEFHLL MGLGKAEGSI DASNLLKPAL ARGKLSMCGA
250 260 270 280 290 300
TTIEEYRKYV EKDAALARRF SPVTVNEPTV EDTISILRGL KERYEVHHGV RIMDSALVTA
310 320 330 340 350 360
ALYSNRYITD RFLPDKAIDL VDEASSTLRL QHESRPDAIA TLDRQIMTIE IELESLRKEE
370 380 390 400 410 420
DQLSIDRKHK LEKELEVKKS ELKELTDQWE SEKRAIDAVK NAKSELEKAK YELEQATREG
430 440 450 460 470 480
DYARASRIQY ASIPELQDKI QELSKNELAA KSSNLLHDSV TSEDIAGVIS KMTGIPVNNL
490 500 510 520 530 540
LKGEKDKLLD MNILLRQSVV GQDEAIDAVS DAVRLQRAGL TSENRPIASF MFLGPTGTGK
550 560 570 580 590 600
TEGGKSLAQF LFNDKNAVVR FDMSEFQEKH TISRLIGSPP GYVGYEESGE LTEAVRRKPY
610 620 630 640 650 660
SVVLFDEFEK AHPDLSKLLL QVLDEGSLTD SHGKKIDFKN TIIVMTSNIG QEILLADKNT
670 680 690 700 710 720
YEDGHINSEV KSQVLENLRH HYAPEFLNRI DDIVVFNRLS KTALKEILDI RLREIGDRLV
730 740 750 760 770 780
DKRIILQLTD EAKTLLCDMG YDPTYGARPL NRVLRKKLLD PLAMRLIKGQ VQENETVKVE
790 800 810
VKDHKIYVVP NHSEGTVIEK EEDYFKEDKD DN