P0CQ16

PR
Gene name
PIM1
Protein name
Lon protease homolog, mitochondrial
Names
Species
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
KEGG Pathway
cne:CND03865
EC number
3.4.21.53: Serine endopeptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

42-158 (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 P0CQ16

Entry ID Method Resolution Chain Position Source
AF-P0CQ16-F1 Predicted AlphaFoldDB

No variants for P0CQ16

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0CQ16

No associated diseases with P0CQ16

4 regional properties for P0CQ16

Type Name Position InterPro Accession
domain Lon protease, N-terminal domain 154 - 442 IPR003111
domain AAA+ ATPase domain 589 - 734 IPR003593
domain ATPase, AAA-type, core 593 - 729 IPR003959
domain Peptidase S16, Lon proteolytic domain 871 - 1082 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 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.

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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLPLRAFARL AQRPRLSRPT QLARSSLPRP SPSRPAAHYL ALAPAPSTRF LHSSPPVLKE
70 80 90 100 110 120
KRWLNNTPPE DDGEDGQNPK QDDQVEKPLP DAESSKSAEE RAKSQSSKPD IKASSSDSVS
130 140 150 160 170 180
SSAPAPGSAD GGSPPGAGGP KEVAKPVIPE IYPQVLAIPI THRPLFPGFY KAVTVRSPPV
190 200 210 220 230 240
IKAIRELQAH GQPYVGAFLL KDSTVDSDVV TDINQVQPVG VFCQITSCFT SQEGEGKPEA
250 260 270 280 290 300
LTAVLFPHRR IKINELVKSS GTKGDGTVGV GGLVEGSQDS AKGEGEVKSF ESEVPGVEEV
310 320 330 340 350 360
REELGTVSID SEQPDVHKEN RDLETKEVTQ IDFLHSLLPQ VSLTNVSNLS IEPYEKDSQV
370 380 390 400 410 420
IRAIMSELIS VFKEIAQLQP MFREQVTSFA ISNTSSQVFD EPDKLADLAA VVSTADVSDL
430 440 450 460 470 480
QAVLSSTSIE DRLQRALVLL KKELINAQLQ FKISRDVDTK IQKRQREYYL MEQLKGIKKE
490 500 510 520 530 540
LGMESDGKDK LVEGFKEKAS KLAMPEGVRK VFDEELNKLV HLEPAASEFN VTRNYIDWLT
550 560 570 580 590 600
QVPWGVHTPE NYNISHAIKI LDEDHYGLKD VKDRILEFMA IGKLRGSVEG KILCLVGPPG
610 620 630 640 650 660
VGKTSIGKSI AKALGRQFFR FSVGGLTDVA EIKGHRRTYI GAMPGKPIQA LKKVATENPL
670 680 690 700 710 720
ILIDEVDKIS KAYNGDPASA LLEMLDPEQN KSFLDHYLDV PIDLSKVLFV CTANVLETIP
730 740 750 760 770 780
GPLLDRMEVL EVSGYVSAEK MNIAERYLSP QAKVAAGLED VNIELEPGAI EALIRYYCRE
790 800 810 820 830 840
SGVRNLKKHI DKIYRKAAFK IVTDLGESGL PEPATPPAEN QVEAQYPDIK PASELTYNVI
850 860 870 880 890 900
PGTEVSGVDT KTDVTTVPRE PMKVPAGIHV KVTQENLKDY VGPPLYHKDR LYTHSPPAGV
910 920 930 940 950 960
STGLGYLGNG SGAVMPVEIN SMPGKGNLQL TGKLGEVIRE SAQIAMSWVK SNAYLLGITK
970 980 990 1000 1010 1020
SEAEATLNDR DVHLHMPEGG IGKEGPSAGT AILTAFVSLF TKTRVDPDIA MTGEISLLGQ
1030 1040 1050 1060 1070 1080
VLPVGGLKEK ILAAHRAGIK KLIVPAGCKP DIDENVPESV KGGIEFVFVE DVRQVLHEAF
1090 1100
RGTEVEKRWQ ETLPMEEEPQ RERH