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 O88967

Entry ID Method Resolution Chain Position Source
AF-O88967-F1 Predicted AlphaFoldDB

28 variants for O88967

Variant ID(s) Position Change Description Diseaes Association Provenance
rs215141265 29 I>T No EVA
rs240457152 30 S>C No EVA
rs222174932 36 P>S No EVA
rs241853508 39 Q>P No EVA
rs247964847 40 K>N No EVA
rs3388531008 76 M>K No EVA
rs3388529791 129 K>I No EVA
rs3388533267 145 I>K No EVA
rs3388527451 157 T>I No EVA
rs3388533280 158 R>G No EVA
rs3388533712 193 L>M No EVA
rs3388530955 195 K>Q No EVA
rs3388529803 320 V>I No EVA
rs3388530251 374 P>L No EVA
rs3388533632 386 G>C No EVA
rs3388526481 397 Y>F No EVA
rs3388533291 399 R>G No EVA
rs3391333631 403 N>I No EVA
rs3391352009 406 L>I No EVA
rs3388530978 423 A>T No EVA
rs3388533331 460 W>R No EVA
rs3388529961 491 L>F No EVA
rs3388529885 496 A>T No EVA
rs3388534220 519 I>V No EVA
rs3388533717 521 M>K No EVA
rs3388532783 538 T>R No EVA
rs3388527423 545 H>Y No EVA
rs3388529947 713 E>G No EVA

No associated diseases with O88967

5 regional properties for O88967

Type Name Position InterPro Accession
domain Peptidase M41 530 - 704 IPR000642
domain AAA+ ATPase domain 313 - 450 IPR003593
domain ATPase, AAA-type, core 317 - 448 IPR003959
conserved_site ATPase, AAA-type, conserved site 418 - 436 IPR003960
domain AAA ATPase, AAA+ lid domain 470 - 513 IPR041569

Functions

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

4 GO annotations of cellular component

Name Definition
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
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.
nuclear body Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.

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.
metal ion binding Binding to a metal ion.
metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

8 GO annotations of biological process

Name Definition
cell population proliferation The multiplication or reproduction of cells, resulting in the expansion of a cell population.
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.
mitochondrial protein processing The peptide cleavage of mitochondrial proteins, including cleavage contributing to their import.
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.
negative regulation of apoptotic process Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
protein hexamerization The formation of a protein hexamer, a macromolecular structure consisting of six noncovalently associated identical or nonidentical subunits.
protein quality control for misfolded or incompletely synthesized proteins The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8LQJ8 FTSH5 ATP-dependent zinc metalloprotease FTSH 5, mitochondrial Oryza sativa subsp japonica (Rice) PR
A2ZVG7 FTSH9 ATP-dependent zinc metalloprotease FTSH 9, chloroplastic/mitochondrial Oryza sativa subsp japonica (Rice) PR
O80983 FTSH4 ATP-dependent zinc metalloprotease FTSH 4, mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
Q9FGM0 FTSH11 ATP-dependent zinc metalloprotease FTSH 11, chloroplastic/mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
Q8W585 FTSH8 ATP-dependent zinc metalloprotease FTSH 8, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MFSLSSTVQP QVTIPLSHLI NAFHSPKNIS VSVNTPVSQK QHRDTVPEHE APSSEPVLNL
70 80 90 100 110 120
RDLGLSELKI GQIDKMVENL LPGFYKDKRV SSCWHTSHIS AQSFFENKYG HLDMFSTLRS
130 140 150 160 170 180
SSLYRQHPKT LRSICSDLQY FPVFIQSRGF KTLKSRTRRL QSTSERLVEA QNIAPSFVKG
190 200 210 220 230 240
FLLRDRGTDL ESLDKLMKTK NIPEAHQDAF KTGFAEGFLK AQALTQKTND SLRRTRLILF
250 260 270 280 290 300
VLLLFGIYGL LKNPFLSVRF RTTTGLDSAV DPVQMKNVTF EHVKGVEEAK QELQEVVEFL
310 320 330 340 350 360
KNPQKFTVLG GKLPKGILLV GPPGTGKTLL ARAVAGEADV PFYYASGSEF DEMFVGVGAS
370 380 390 400 410 420
RIRNLFREAK ANAPCVIFID ELDSVGGKRI ESPMHPYSRQ TINQLLAEMD GFKPNEGVII
430 440 450 460 470 480
IGATNFPEAL DNALIRPGRF DMQVTVPRPD VKGRTEILKW YLNKIKFDKS VDPEIIARGT
490 500 510 520 530 540
VGFSGAELEN LVNQAALKAA VDGKEMVTMK ELEFSKDKIL MGPERRSVEI DNKNKTITAY
550 560 570 580 590 600
HESGHAIIAY YTKDAMPINK ATIMPRGPTL GHVSLLPEND RWNETRAQLL AQMDVSMGGR
610 620 630 640 650 660
VAEELIFGTD HITTGASSDF DNATKIAKRM VTKFGMSEKL GVMTYSDTGK LSPETQSAIE
670 680 690 700 710
QEIRILLRES YERAKHILKT HAKEHKNLAE ALLTYETLDA KEIQIVLEGK KLEVR