Q9K8H4
Gene name |
BH3032 |
Protein name |
UPF0758 protein BH3032 |
Names |
|
Species |
Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) (Bacillus halodurans) |
KEGG Pathway |
bha:BH3032 |
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 Q9K8H4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9K8H4-F1 | Predicted | AlphaFoldDB |
No variants for Q9K8H4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9K8H4 | |||||
No associated diseases with Q9K8H4
No regional properties for Q9K8H4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9K8H4 | |||
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| 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. |
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 |
| MSNMSMTLRD | VPNRERPRER | LLHEGAHALS | NQEIVAIMLR | TGTKNESVLQ | LAQHVLCHFD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GLRLLREATV | EELTSIHGIG | EAKAIEFCAA | IELGRRIHTM | QEMDRYVIRT | PEDVSRFVME |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EMRFLSQENF | VCLYLNTKNQ | VLHKQTVFIG | SLNASIVHPR | EVFKEALRRS | AASLICLHNH |
| 190 | 200 | 210 | 220 | 230 | |
| PSGDPTPSRE | DIEVTHRLAQ | VGKLIGIELL | DHVIIGDRTF | VSLKEKGHLP | FS |