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 Q6CNR9

Entry ID Method Resolution Chain Position Source
AF-Q6CNR9-F1 Predicted AlphaFoldDB

No variants for Q6CNR9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6CNR9

No associated diseases with Q6CNR9

5 regional properties for Q6CNR9

Type Name Position InterPro Accession
domain Lon protease, N-terminal domain 184 - 448 IPR003111
domain AAA+ ATPase domain 594 - 740 IPR003593
domain ATPase, AAA-type, core 598 - 736 IPR003959
active_site Peptidase S16, active site 988 - 996 IPR008268
domain Peptidase S16, Lon proteolytic domain 877 - 1085 IPR008269

Functions

Description
EC Number 3.4.21.53 Serine endopeptidases
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrial chromosome A chromosome found in the mitochondrion of a eukaryotic cell.

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.
ATP-dependent peptidase activity Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
sequence-specific DNA binding Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

6 GO annotations of biological process

Name Definition
cellular response to oxidative stress 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 oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
chaperone-mediated protein complex assembly The aggregation, arrangement and bonding together of a set of components to form a protein complex, mediated by chaperone molecules that do not form part of the finished complex.
mitochondrial protein catabolic process The chemical reactions and pathways resulting in the breakdown of a mitochondrial protein. This process is necessary to maintain the healthy state of mitochondria and is thought to occur via the induction of an intramitochondrial lysosome-like organelle that acts to eliminate the damaged oxidised mitochondrial proteins without destroying the mitochondrial structure.
oxidation-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the oxidation of one or more amino acid residues in the protein.
protein quality control for misfolded or incompletely synthesized proteins The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
regulation of mitochondrial DNA metabolic process Any process that modulates the frequency, rate or extent of mitochondrial DNA metabolic process.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLRSSRSRLV TRNILLRQFK NGNNVRLMNA TRFQHNGIVG NEKLASDSQK FVDESYHWMQ
70 80 90 100 110 120
YRKQMNDPVS RQRLEQLESQ WVKSIQLKQD DKGKDIDQPE SENRKKEEEQ VPTEEKDNDT
130 140 150 160 170 180
AKESETSQQR DSVAETQGPA STSGGASGNG ESSGNGSGDD GNNGSGNGKP SKNAKQPFPE
190 200 210 220 230 240
VYPQVMALPI SRRPLFPGFY KAVVISDERV MKAIKDMSDR QQPYIGAFLL KDSTVDTDVI
250 260 270 280 290 300
HKADEVYNVG VFAQVTSAFP SKDEKTGAET MTALLYPHRR IKLDELIPPT SEQNLKDESD
310 320 330 340 350 360
VSKSEGVENN EQEVVKASLQ KMENMKDVEE DDDENLTGFL KDYDVSLVNV SNLADKEFNP
370 380 390 400 410 420
NSPVINALTS EILKVFKEIS QLNTMFREQI ATFSASIQSA TTNIFEEPAR LADFAAAVSA
430 440 450 460 470 480
GEEEELQEIL ESLDIEQRLE KALTVLKKEL MNAELQNKIS KDVETKIQKR QREYYLMEQL
490 500 510 520 530 540
KGIKRELGID DGRDKLIESF KDRVSKLQLP ETVQKVFDDE ITKLATLETS QSEFGVIRNY
550 560 570 580 590 600
LDWITSLPWG IISKEQYSIP KAKKILDEDH YGMKDVKDRI LEFIAVGKLL GKVDGKIICF
610 620 630 640 650 660
VGPPGVGKTS IGKSIARSLN RQFFRFSVGG MTDVAEIKGH RRTYIGALPG RVIQALKKCQ
670 680 690 700 710 720
TQNPLILIDE IDKIGHGGIH GDPAAALLEL LDPEQNNSFL DNYMDIPIDL SKVLFVCTAN
730 740 750 760 770 780
SLETIPRPLL DRMEVIELTG YVAEEKVKIA ENYLSPSAKK SAGLDNANVN ITENAIVSLM
790 800 810 820 830 840
KHYCRESGVR SLKKHIEKIY RKAALNVVKQ LSIDDKPMEN EEVKDQKDIK VKQSENKSSA
850 860 870 880 890 900
EASTVESTTE ENELIKTQKS HDNKGSLEVP ETVSVTVDEN NLKDYVGPPI FTTDRLYEST
910 920 930 940 950 960
PPGVVMGLAW TSMGGCAMYV ESVLEQPLTH STQPTLERTG QLGDVMKESS RLAYSFSKMY
970 980 990 1000 1010 1020
LAKKFPENRF FEVAKIHLHC PEGATPKDGP SAGVTMASSF LSLALNKGLD PTVAMTGELT
1030 1040 1050 1060 1070 1080
LTGKVLRIGG LREKAVAAKR SGAKTIIFPK DNLSDWAELP ENVKEGLEPL AADWYEDVFQ
1090 1100 1110
RLFGDVDTNK GNTVWSEDFK KIDEKRNKET K