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 P93655

Entry ID Method Resolution Chain Position Source
AF-P93655-F1 Predicted AlphaFoldDB

No variants for P93655

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P93655

No associated diseases with P93655

5 regional properties for P93655

Type Name Position InterPro Accession
domain Lon protease, N-terminal domain 99 - 307 IPR003111
domain AAA+ ATPase domain 456 - 601 IPR003593
domain ATPase, AAA-type, core 460 - 597 IPR003959
active_site Peptidase S16, active site 838 - 846 IPR008268
domain Peptidase S16, Lon proteolytic domain 729 - 935 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

2 GO annotations of cellular component

Name Definition
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.
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.

6 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).
single-stranded DNA binding Binding to single-stranded DNA.

5 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.
mitochondrion organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
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.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9M9L7 LON4 Lon protease homolog 4, chloroplastic/mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
Q9M9L8 LON3 Lon protease homolog 3, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MLKLFTSSAS RVHHLTPVSR VVGSSPVESP LFKALSQITG WNRRSTSLGH RAFFCSEPTN
70 80 90 100 110 120
GEAAAEAETK AVESDSEVSD SKSSSAIVPT NPRPEDCLTV LALPVPHRPL FPGFYMPIYV
130 140 150 160 170 180
KDPKVLAALQ ESRRRQAPYA GAFLLKDDPS ADSSSSTDAE KNINELKGKE LLNRLHEVGT
190 200 210 220 230 240
LAQISSIQGD QVILVGHRRL RIKEMVSEEP LTVKVDHLKD NPFDMDDDVV KATSFEVIST
250 260 270 280 290 300
LRDVLKTSSL WRDHVQTYTQ HIGDFTYPRL ADFGAAICGA NRHQAQEVLE ELDVHKRLRL
310 320 330 340 350 360
TLELMKKEME ISKIQETIAK AIEEKISGEQ RRYLLNEQLK AIKKELGVET DDKSALSAKF
370 380 390 400 410 420
KERIEPNKEK IPAHVLQVIE EELTKLQLLE ASSSEFNVTR NYLDWLTILP WGNYSNENFD
430 440 450 460 470 480
VARAQTILDE DHYGLSDVKE RILEFIAVGR LRGTSQGKII CLSGPPGVGK TSIGRSIARA
490 500 510 520 530 540
LNRKFFRFSV GGLADVAEIK GHRRTYVGAM PGKMVQCLKS VGTANPLVLI DEIDKLGRGH
550 560 570 580 590 600
AGDPASALLE LLDPEQNANF LDHYLDVTID LSKVLFVCTA NVIDMIPNPL LDRMEVISIA
610 620 630 640 650 660
GYITDEKVHI ARDYLEKTAR GDCGVKPEQV EVSDAALLSL IENYCREAGV RNLQKQIEKI
670 680 690 700 710 720
YRKIALKLVR EGAVPEEPAV ASDPEEAEIV ADVGESIENH TVEENTVSSA EEPKEEAQTE
730 740 750 760 770 780
KIAIETVMID ESNLADYVGK PVFHAEKLYE QTPVGVVMGL AWTSMGGSTL YIETTVVEEG
790 800 810 820 830 840
EGKGGLNITG QLGDVMKESA QIAHTVARKI MLEKEPENQF FANSKLHLHV PAGATPKDGP
850 860 870 880 890 900
SAGCTMITSL LSLATKKPVR KDLAMTGEVT LTGRILPIGG VKEKTIAARR SQIKTIIFPE
910 920 930
ANRRDFDELA ENVKEGLNVH FVDDYGKIFE LAFGYDKQED