Q7S7C0
Gene name |
cym-1 (B13M13.120, NCU01272) |
Protein name |
Mitochondrial presequence protease |
Names |
|
Species |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
KEGG Pathway |
ncr:NCU01272 |
EC number |
|
Protein Class |
|
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 Q7S7C0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7S7C0-F1 | Predicted | AlphaFoldDB |
No variants for Q7S7C0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7S7C0 | |||||
No associated diseases with Q7S7C0
4 regional properties for Q7S7C0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M16, C-terminal | 232 - 419 | IPR007863-1 |
| domain | Peptidase M16, C-terminal | 834 - 923 | IPR007863-2 |
| domain | Peptidase M16, N-terminal | 72 - 160 | IPR011765 |
| domain | Peptidase M16C associated | 489 - 747 | IPR013578 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial intermembrane space | The region between the inner and outer lipid bilayers of the mitochondrial envelope. |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
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. |
| proteolysis involved in protein catabolic process | The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLRNATKGAA | RRAVTELSQY | PKPGEKLHGF | TLLRSKHVPE | LELTALHLQH | DKTGAEHLHI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ARDDSNNVFS | IGFKTNPPDD | TGVPHILEHT | TLCGSQKYPI | RDPFFKMLPR | TLSNFMNAFT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ASDHTFYPFA | TTNAQDFKNL | MSVYLDATLH | PLLKETDFTQ | EGWRIGPENP | QALVAAEGNA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KPEDRKLVFK | GVVYNEMKGQ | MSDAAYLFWI | RFQDHIFPDI | HNSGGDPQKI | TDLTYQQLKK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FHADHYHPSN | AKVFTYGDMP | LADHLKEIGA | QLDVFEKIRA | DVAHHSPIDL | SSGPREVKLY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GPIDPLVDAN | KQFKTSVSWV | LGETNNVVES | FSLALISALL | MDGYGSPLYK | GLIESGLGTD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| WSPNTGYDSS | GKLGIFSIGL | SGVQEEDVPK | VKAKVQEILR | SMRDKGFERS | KIDGYLHQLE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LGLKHKTANF | GMSLLHRLKP | KWFVGVDPFD | SLAWNDTIAA | FETELAKGGY | LEGLIDKYLI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NDNTLSFTMA | PSPTFSQELA | QEEETRLSTK | ISEVVKAAGS | EEEARAALEA | RELKLLAEQS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KTNTEDLGCL | PSVHVKDIPR | QKDSVILRHD | NTARVKTQWH | EAPTNGLTYF | RAINQLENLP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DELRSLIPLF | TDSIMRLGTK | DMTMEQLEDL | IKLKTGGVSV | GYHSASHPTD | FTRATEGLMF |
| 670 | 680 | 690 | 700 | 710 | 720 |
| SGMALDRHVP | TMFDLLRKLV | VETDFDSPQA | AQQIRQLLQA | SADGVVNDIA | SSGHAYARRA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| AESGLTWDSF | LKEQVSGLSQ | VKLVTSLASR | PESDPLEDVI | AKLKQIQQFA | LAGNLRTAIT |
| 790 | 800 | 810 | 820 | 830 | 840 |
| CDSGSVSDNA | KALLNFVNSL | PSEAVTFPSR | GPPNFTRDIK | TFYPLPYQVY | YGALALPTAS |
| 850 | 860 | 870 | 880 | 890 | 900 |
| YTASVNAPLQ | ILSQLLTHKH | LHHEIREKGG | AYGGGSYARP | LDGIFGFYSY | RDPNPVNTLK |
| 910 | 920 | 930 | 940 | 950 | 960 |
| IMRNAGQWAV | DKEWTDRDLE | DAKISVFQGV | DAPKAVNEEG | MAQFLYGITD | EMKQKRREEL |
| 970 | 980 | 990 | 1000 | 1010 | |
| LDVTKDQVRE | VAQEYVVKAL | NNGSERVVFL | GEKRDWVDKS | WAVKEMDING | ST |