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 Q9M9L8

Entry ID Method Resolution Chain Position Source
AF-Q9M9L8-F1 Predicted AlphaFoldDB

103 variants for Q9M9L8

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_3_1719428_G_A 16 R>C No 1000Genomes
ENSVATH10512671 24 L>W No 1000Genomes
ENSVATH02116676 29 S>N No 1000Genomes
tmp_3_1719382_G_A 31 T>I No 1000Genomes
ENSVATH10512669 32 L>P No 1000Genomes
tmp_3_1719360_G_C 38 Y>* No 1000Genomes
tmp_3_1719362_A_C 38 Y>D No 1000Genomes
tmp_3_1719356_C_G 40 A>P No 1000Genomes
tmp_3_1719341_G_A 45 P>S No 1000Genomes
ENSVATH00308072 50 I>V No 1000Genomes
ENSVATH05778604 59 L>Q No 1000Genomes
ENSVATH13875445 64 P>R No 1000Genomes
ENSVATH05778603 71 N>S No 1000Genomes
ENSVATH10512667 79 G>S No 1000Genomes
ENSVATH05778602 80 R>L No 1000Genomes
ENSVATH00308071 81 R>P No 1000Genomes
ENSVATH13875384 87 R>L No 1000Genomes
tmp_3_1719176_G_A 100 L>F No 1000Genomes
tmp_3_1718977_G_T 119 H>Q No 1000Genomes
ENSVATH00308070 128 M>I No 1000Genomes
ENSVATH00308069 131 H>Q No 1000Genomes
ENSVATH02116665 147 Q>K No 1000Genomes
ENSVATH13875382 151 Y>H No 1000Genomes
ENSVATH02116664 160 C>G No 1000Genomes
tmp_3_1718734_T_G 172 E>D No 1000Genomes
ENSVATH05778597 223 I>T No 1000Genomes
ENSVATH02116656 225 E>K No 1000Genomes
ENSVATH02116653 236 R>K No 1000Genomes
ENSVATH00308068 248 D>E No 1000Genomes
ENSVATH05778591 250 A>T No 1000Genomes
ENSVATH05778590 253 K>T No 1000Genomes
ENSVATH02116645 265 E>D No 1000Genomes
ENSVATH05778589 273 W>R No 1000Genomes
ENSVATH02116644 275 D>G No 1000Genomes
ENSVATH05778588 292 G>R No 1000Genomes
ENSVATH02116643 299 H>D No 1000Genomes
ENSVATH02116642 315 E>A No 1000Genomes
ENSVATH05778586 331 K>E No 1000Genomes
ENSVATH05778586 331 K>Q No 1000Genomes
tmp_3_1717415_C_T 345 V>I No 1000Genomes
tmp_3_1717392_G_C 352 D>E No 1000Genomes
ENSVATH02116633 359 I>L No 1000Genomes
ENSVATH02116632 387 H>D No 1000Genomes
ENSVATH10512573 392 L>P No 1000Genomes
ENSVATH05778584 394 W>* No 1000Genomes
tmp_3_1717133_T_G 401 N>H No 1000Genomes
ENSVATH05778579 408 K>E No 1000Genomes
tmp_3_1717081_A_C 418 L>* No 1000Genomes
ENSVATH05778578 418 L>F No 1000Genomes
tmp_3_1717061_T_A 425 I>L No 1000Genomes
ENSVATH10512569 426 L>S No 1000Genomes
tmp_3_1717021_G_A 438 S>L No 1000Genomes
ENSVATH05778573 475 G>V No 1000Genomes
ENSVATH00308064 489 Y>C No 1000Genomes
tmp_3_1716624_T_A 511 I>F No 1000Genomes
ENSVATH13875378 515 E>Q No 1000Genomes
tmp_3_1716604_A_T 517 D>E No 1000Genomes
ENSVATH05778567 527 P>S No 1000Genomes
tmp_3_1716462_G_A 530 A>V No 1000Genomes
ENSVATH02116621 542 K>N No 1000Genomes
ENSVATH02116620 548 L>I No 1000Genomes
tmp_3_1716226_T_A 562 T>S No 1000Genomes
tmp_3_1716213_A_G 566 I>T No 1000Genomes
tmp_3_1716126_C_T 595 R>K No 1000Genomes
ENSVATH05778566 603 C>Y No 1000Genomes
ENSVATH02116617 604 R>* No 1000Genomes
ENSVATH05778565 612 H>Q No 1000Genomes
ENSVATH05778564 618 A>S No 1000Genomes
ENSVATH10512566 621 L>F No 1000Genomes
ENSVATH05778562 629 R>T No 1000Genomes
ENSVATH05778561 634 R>S No 1000Genomes
ENSVATH10512565 645 R>C No 1000Genomes
ENSVATH05778558 648 A>S No 1000Genomes
ENSVATH02116616 650 E>G No 1000Genomes
ENSVATH05778557 660 D>E No 1000Genomes
ENSVATH05778556 661 V>G No 1000Genomes
ENSVATH02116615 661 V>I No 1000Genomes
ENSVATH10512534 679 R>K No 1000Genomes
tmp_3_1715703_C_G 704 S>T No 1000Genomes
ENSVATH05778554 710 T>I No 1000Genomes
ENSVATH05778554 710 T>N No 1000Genomes
ENSVATH05778553 713 K>R No 1000Genomes
tmp_3_1715616_T_C 733 E>G No 1000Genomes
tmp_3_1715554_C_G 754 G>R No 1000Genomes
ENSVATH10512532 761 T>I No 1000Genomes
ENSVATH02116613 768 L>* No 1000Genomes
ENSVATH02116614 768 L>V No 1000Genomes
tmp_3_1715475_C_G 780 G>A No 1000Genomes
ENSVATH05778551 788 Q>E No 1000Genomes
ENSVATH00308061 792 T>I No 1000Genomes
ENSVATH00308061 792 T>K No 1000Genomes
tmp_3_1715420_C_T 798 M>I No 1000Genomes
tmp_3_1715407_G_A 803 P>S No 1000Genomes
ENSVATH05778549 808 F>S No 1000Genomes
tmp_3_1715370_A_C 815 L>* No 1000Genomes
tmp_3_1715356_C_T 820 G>R No 1000Genomes
tmp_3_1715341_C_A 825 D>Y No 1000Genomes
tmp_3_1715338_C_G 826 G>R No 1000Genomes
tmp_3_1715334_G_A 827 P>L No 1000Genomes
tmp_3_1715289_A_T 842 M>K No 1000Genomes
ENSVATH05778547 861 R>S No 1000Genomes
ENSVATH00308059 910 D>A No 1000Genomes
ENSVATH05778544 923 D>G No 1000Genomes

No associated diseases with Q9M9L8

5 regional properties for Q9M9L8

Type Name Position InterPro Accession
domain Lon protease, N-terminal domain 111 - 323 IPR003111
domain AAA+ ATPase domain 439 - 584 IPR003593
domain ATPase, AAA-type, core 443 - 579 IPR003959
active_site Peptidase S16, active site 825 - 833 IPR008268
domain Peptidase S16, Lon proteolytic domain 716 - 922 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
P93655 SYP22 Lon protease homolog 1, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
Q9M9L7 LON4 Lon protease homolog 4, chloroplastic/mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MMPKRFNTSG FDTTLRLPSY YGFLHLTQSL TLNSRVFYGA RHVTPPAIRI GSNPVQSLLL
70 80 90 100 110 120
FRAPTQLTGW NRSSRDLLGR RVSFSDRSDG VDLLSSSPIL STNPNLDDSL TVIALPLPHK
130 140 150 160 170 180
PLIPGFYMPI HVKDPKVLAA LQESTRQQSP YVGAFLLKDC ASTDSSSRSE TEDNVVEKFK
190 200 210 220 230 240
VKGKPKKKRR KELLNRIHQV GTLAQISSIQ GEQVILVGRR RLIIEEMVSE DPLTVRVDHL
250 260 270 280 290 300
KDKPYDKDNA VIKASYVEVI STLREVLKTN SLWRDQDIGD FSYQHLADFG AGISGANKHK
310 320 330 340 350 360
NQGVLTELDV HKRLELTLEL VKKQVEINKI KETDDGSSLS AKIRVRIDTK RDKIPKHVIK
370 380 390 400 410 420
VMEEEFTKLE MLEENYSDFD LTYNYLHWLT VLPWGNFSYE NFDVLRAKKI LDEDHYGLSD
430 440 450 460 470 480
VKERILEFIA VGRLRGTSQG KIICLSGPPG VGKTSIGRSI ARALDRKFFR FSVGGLSDVA
490 500 510 520 530 540
EIKGHCQTYV GAMPGKMVQC LKSVGTANPL ILFDEIDKLG RCHTGDPASA LLEVMDPEQN
550 560 570 580 590 600
AKFLDHFLNV TIDLSKVLFV CTANVIEMIP GPLLDRMEVI DLSGYVTDEK MHIARDYLVK
610 620 630 640 650 660
KTCRDCGIKP EHVDLSDAAL LSLIENYCRE AGVRNLQKQI EKIYRKVALE LVRQGAVSFD
670 680 690 700 710 720
VTDTKDTKSL AKTDSEVKRM KVADIMKILE SATGDSTESK TKQSGLVAKT FEKVMIDESN
730 740 750 760 770 780
LADYVGKPVF QEEKIYEQTP VGVVMGLAWT SMGGSTLYIE TTFVEEGLGK GGLHITGQLG
790 800 810 820 830 840
DVMKESAQIA HTVARRIMFE KEPENLFFAN SKLHLHVPEG ATPKDGPSAG CTMITSFLSL
850 860 870 880 890 900
AMKKLVRKDL AMTGEVTLTG RILPIGGVKE KTIAARRSQI KTIIFPEANR RDFEELAENM
910 920
KEGLDVHFVD EYEKIFDLAF NYDH