Q57VB1
Gene name |
HslU1 (Tb927.5.1520) |
Protein name |
ATP-dependent protease ATPase subunit HslU1 |
Names |
Mitochondrial proteasome-like protease HslVU ATPase subunit 1 |
Species |
Trypanosoma brucei brucei (strain 927/4 GUTat101) |
KEGG Pathway |
tbr:Tb927.5.1520 |
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 Q57VB1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q57VB1-F1 | Predicted | AlphaFoldDB |
No variants for Q57VB1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q57VB1 | |||||
No associated diseases with Q57VB1
4 regional properties for Q57VB1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | AAA+ ATPase domain | 97 - 368 | IPR003593 |
| domain | ATPase, AAA-type, core | 101 - 155 | IPR003959-1 |
| domain | ATPase, AAA-type, core | 242 - 361 | IPR003959-2 |
| domain | Clp ATPase, C-terminal | 367 - 461 | IPR019489 |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| HslUV protease complex | A protein complex that possesses ATP-dependent protease activity; consists of an ATPase large subunit with homology to other ClpX family ATPases and a peptidase small subunit related to the proteasomal beta-subunits of eukaryotes. In the E. coli complex, a double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. |
| kinetoplast | A sub-structure within the large single mitochondrion of kinetoplastid parasites and which is closely associated with the flagellar pocket and basal body of the flagellum. |
| mitochondrial nucleoid | The region of a mitochondrion to which the DNA is confined. |
3 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. |
| peptidase activity | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| mitochondrial DNA replication | The process in which new strands of DNA are synthesized in the mitochondrion. |
| 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. |
| rolling circle DNA replication | A DNA-dependent DNA replication process in which a single-stranded DNA molecule is synthesized from a circular duplex template. Replication typically does not cease when one circumference has been replicated, but continues around the circumference several more times, producing a long single strand comprising multimers of the replicon. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MMRRVTSSLP | SALKLGRSLG | PNVRFSGGAA | AVEASPAIPP | NSSSGKTLVR | NMKPRELMQE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LDNYIIGQTE | AKKAVAVALR | NRWRRHQVDA | AIREEISPKN | ILMIGPTGVG | KTEIARRLAK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LVDAPFIKVE | ATKFTEVGFH | GRDVESIIED | LYKASLTQTK | QNIMRRHEET | ARQKAENRIL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KALAGVSDGF | REHLRSGALD | DIEVIVELQE | KKEKPKNSGT | NEGVFISLEI | PSSIGGQRPQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TVKKVMKIKD | AIPAVLQEEL | DKIVDTEDVS | AEALRACEED | GIVVIDEIDK | IVTASGGYKG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HQASAEGVQQ | DLLPLVEGTT | VSTKGNVQIK | TDKILFICSG | AFHSVKPSDM | LAELQGRLPI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RVELKPLTKE | DFHRIITEPR | YNLIKQHVMM | MKTEGVDLVF | TDDALWEIAS | IAAHINSTVQ |
| 430 | 440 | 450 | 460 | 470 | |
| NIGARRLITI | TEKVVEEVSF | DGPDRKGETF | VIDAAYVRNS | VESMMKKVDI | KKFIL |