Q09769

PR
Gene name
pim1 (SPAC22F3.06c)
Protein name
Lon protease homolog, mitochondrial
Names
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPAC22F3.06c
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

35-154 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q09769

Entry ID Method Resolution Chain Position Source
AF-Q09769-F1 Predicted AlphaFoldDB

12 variants for Q09769

Variant ID(s) Position Change Description Diseaes Association Provenance
I_693862_G_A 11 R>K No Jeffares_SNPs
I_693906_C_T 26 H>Y No Jeffares_SNPs
I_693936_A_T 36 T>S No Jeffares_SNPs
I_694050_A_G 74 T>A No Jeffares_SNPs
I_694110_A_G 94 K>E No Jeffares_SNPs
I_694464_A_G 212 T>A No Jeffares_SNPs
I_694554_A_G 242 S>G No Jeffares_SNPs
I_694674_G_T 282 D>Y No Jeffares_SNPs
I_694704_G_C 292 E>Q No Jeffares_SNPs
I_696043_G_C 738 G>A No Jeffares_SNPs
I_696858_G_A 1010 D>N No Jeffares_SNPs
I_696996_T_C 1056 S>P No Jeffares_SNPs

No associated diseases with Q09769

5 regional properties for Q09769

Type Name Position InterPro Accession
domain Lon protease, N-terminal domain 161 - 423 IPR003111
domain AAA+ ATPase domain 570 - 715 IPR003593
domain ATPase, AAA-type, core 574 - 711 IPR003959
active_site Peptidase S16, active site 943 - 951 IPR008268
domain Peptidase S16, Lon proteolytic domain 832 - 1040 IPR008269

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
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.

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.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MITRLSGACL RRSGAKRNWP REHLVHRSLL ASFSTTQRVL KCSVGPFRTS NVVFKSKEPK
70 80 90 100 110 120
DNKPLDNKND PKKTHNEDES HTNESLPSTD KKKKKDNDDF KQNLKSSSNK TEEKYSATQA
130 140 150 160 170 180
SKSKNDEFEL GGEENEDEMP LNGEFNKNVP AKYSVPDVYP QLLALPIARR PLFPGFYKAI
190 200 210 220 230 240
VTKNPSVSEA IKELIKKRQP YIGAFLLKDE NTDTDVITNI DQVYPVGVFA QITSIFPAKS
250 260 270 280 290 300
GSEPALTAVL YPHRRIRITE LIPPKEDADS AASSDAAELE TDKSSNLSSN GEVKSDLKQD
310 320 330 340 350 360
NGKEEPEKEV ESTPSILQNF KVSLVNVENV PNEPFKRQDP VIKAVTSEIM NVFKDIANVS
370 380 390 400 410 420
PLFREQIANF SISQTSGNVF DEPAKLADFA AAVSAADHRE LQEVLEATNI GDRLQKALYV
430 440 450 460 470 480
LKKELLNAQL QHKINKEIEQ KITQRHKEYL LTEQLKQIKR ELGQELDSKE ALVTEFKKRT
490 500 510 520 530 540
ESLSMPDHVK KVFNDELSKF QHLEPMAAEF NITRNYLDWI TQLPWGKRSV ENFDLDHAKE
550 560 570 580 590 600
VLDRDHYGLK DVKDRVLELV AVGKLRGTMQ GKIMCLVGPP GVGKTSVGKS IASALNREFF
610 620 630 640 650 660
RFSVGGLTDV AEIKGHRRTY IGAMPGKIVQ ALKKVQTENP LILIDEIDKV GKSHQGDPAS
670 680 690 700 710 720
ALLELLDSEQ NSAFLDYYMD IPLDVSSVLF VCTANTIDTI PPPLLDRMEV IELSGYVSAE
730 740 750 760 770 780
KVNIAKGYLI PQAKAACGLK DANVNISDDA IKGLISYYAH ESGVRNLKKS IEKIFRKTSF
790 800 810 820 830 840
SIVKEIDDEL NSKEKSTGKS GKKTSPQSSE DAANKEASSV PLKVPDKVNI EIEEKDLTKY
850 860 870 880 890 900
LGPPIYTSQR LYDTTPPGVV MGLGWTPMGG VSMYVETIVK NILSSNSTPS LERTGQLGDV
910 920 930 940 950 960
MKESSEISYS FSKSFLSKHF PNNKFFEHAR LHMHCPEGSI SKDGPSAGIT MATSLLSLAL
970 980 990 1000 1010 1020
DTPVPATTAM TGELTLTGKI LRIGGLREKT VAAKLSGMKE ILFPKSNLAD WEQLPDYVKE
1030 1040 1050 1060
GLTGVPVAWY DDVFKRVFSN IDAEKCNNLW PNLIKSSSKQ HQISPSH