Q1RJ70
Gene name |
hscA (RBE_0513) |
Protein name |
Chaperone protein HscA homolog |
Names |
|
Species |
Rickettsia bellii (strain RML369-C) |
KEGG Pathway |
rbe:RBE_0513 |
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 Q1RJ70
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q1RJ70-F1 | Predicted | AlphaFoldDB |
No variants for Q1RJ70
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q1RJ70 | |||||
No associated diseases with Q1RJ70
1 regional properties for Q1RJ70
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Heat shock protein 70, conserved site | 197 - 210 | IPR018181 |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQIIEIREPG | QAESKQEVKI | AVGIDFGTTN | SLIAISVGRK | VKIIQTEDNK | ELIPTTIEFT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NNNITVGSNK | GLRSIKRLFG | KTLNEILNTP | ALFSLVKDYI | DLQSQEVKLN | FANKQMRIAE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IAAEVFIYLK | QQAEKELTTE | VTQAVITVPA | HFNDAARGQV | MLAARLAGLE | VLRLIAEPTA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AAYAYGLNKN | QTGCYLVYDL | GGGTFDVSIL | NITEGVFQVI | ATSGDNMLGG | DDIDKIIADY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FCNKFSLLDN | LDTLRLAKKA | KEALLNQDNF | EFNNISLDKQ | TFEQLITPII | GRTINIAKEC |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LEIAGNPNID | GIILVGGVTH | ITLIKEELYK | AFKVNILSDI | DPDKAIVYGA | ALQAENLTTP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NIDSLLIDVV | PLSLGMELYG | GIVEKIIMRN | TPIPISVVKE | FTTYADNQTG | IQFHILQGER |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EMVADCRTLA | RFELKGLPPM | KAGSIRAEVT | FSIDADGILS | VSAYEKISNT | SHIVEVKPDY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GIDTSEVDKV | LENAYKNAKL | DHAARLLQET | VIEAESLIFN | IEHAIKELVD | LLSENEKHII |
| 550 | 560 | 570 | 580 | 590 | |
| SSLLNNIKHA | IDARDRALIN | NAVKDFKSKT | KKSLNTKINI | VISDLLKGKN | INQIK |