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 Q9DC61

Entry ID Method Resolution Chain Position Source
AF-Q9DC61-F1 Predicted AlphaFoldDB

15 variants for Q9DC61

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3391360316 31 R>G No EVA
rs3388539064 43 L>P No EVA
rs218719524 164 D>G No EVA
rs3388537684 186 A>S No EVA
rs3391389558 299 V>L No EVA
rs3391398468 300 E>* No EVA
rs3391302249 302 D>H No EVA
rs1133297829 383 Y>* No EVA
rs1134260645 385 D>H No EVA
rs1134827924 394 S>R No EVA
rs3388536557 439 E>K No EVA
rs27202002 513 N>D No EVA
rs3388536931 515 H>Y No EVA
rs3388535104 519 S>T No EVA
rs3388536916 522 L>M No EVA

No associated diseases with Q9DC61

3 regional properties for Q9DC61

Type Name Position InterPro Accession
binding_site Peptidase M16, zinc-binding site 96 - 119 IPR001431
domain Peptidase M16, C-terminal 231 - 430 IPR007863
domain Peptidase M16, N-terminal 76 - 225 IPR011765

Functions

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

3 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
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.

4 GO annotations of molecular function

Name Definition
endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
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.
metallopeptidase activity Catalysis of the hydrolysis of peptide bonds 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.

2 GO annotations of biological process

Name Definition
protein processing Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
protein processing involved in protein targeting to mitochondrion The cleavage of peptide bonds in proteins, usually near the N terminus, contributing to the process of import into the mitochondrion. Several different peptidases mediate cleavage of proteins destined for different mitochondrial compartments.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P20069 Pmpca Mitochondrial-processing peptidase subunit alpha Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MATAVWAAAR LLRGSAVLCA RPRFGSPAHR RFSSGATYPN IPLSSPLPGV PKPIFATVDG
70 80 90 100 110 120
QEKFETKVTT LDNGLRVASQ NKFGQFCTVG ILINSGSRYE AKYLSGIAHF LEKLAFSSTA
130 140 150 160 170 180
RFDSKDEILL TLEKHGGICD CQTSRDTTMY AVSADSKGLD TVVDLLADVV LHPRLTDEEI
190 200 210 220 230 240
EMTRMAVQFE LEDLNMRPDP EPLLTEMIHE AAFRENTVGL HRFCPVENIA KIDREVLHSY
250 260 270 280 290 300
LKNYYTPDRM VLAGVGVEHE HLVECARKYL VGAEPAWGAP GTVDVDRSVA QYTGGIIKVE
310 320 330 340 350 360
RDMSNVSLGP TPIPELTHIM VGLESCSFLE DDFIPFAVLN MMMGGGGSFS AGGPGKGMFS
370 380 390 400 410 420
RLYLNVLNRH HWMYNATSYH HSYEDTGLLC IHASADPRQV REMVEIITKE FILMGRTVDL
430 440 450 460 470 480
VELERAKTQL MSMLMMNLES RPVIFEDVGR QVLATHSRKL PHELCTLIRN VKPEDIKRVA
490 500 510 520
SKMLRGKPAV AALGDLTDLP TYEHIQAALS SRNGHLPRSY RLFR