Q1E910
Gene name |
ATP23 (CIMG_00953) |
Protein name |
Mitochondrial inner membrane protease ATP23 |
Names |
|
Species |
Coccidioides immitis (strain RS) (Valley fever fungus) |
KEGG Pathway |
cim:CIMG_00953 |
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 Q1E910
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q1E910-F1 | Predicted | AlphaFoldDB |
No variants for Q1E910
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q1E910 | |||||
No associated diseases with Q1E910
No regional properties for Q1E910
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q1E910 | |||
1 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. |
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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAEAASSGSN | STSPPKDNGY | IPGDDAWTIC | RNLWRGLTGK | MTQEGMEQFR | VARDVRNEKE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DCKRCEDQRD | YLLQYSPLIR | FLQDNIQQLG | GNISKHNIFC | RRCKNRQAGG | FDPDYGIQIC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ANEMRNQGHL | EDTLAHEMIH | AYDHMRFKVD | WDDNLRHAAC | AEIRASNLSG | ECRWMREFFS |
| 190 | 200 | 210 | 220 | 230 | |
| RGQWKFAQHH | QECVRRRAIL | SVQARPACKD | EQHATQVVNE | VWDSCFRDTR | PFDEIYR |