Q3M1B1
Gene name |
groEL3 |
Protein name |
Chaperonin GroEL 3 |
Names |
60 kDa chaperonin 3, Chaperonin-60 3, Cpn60 3 |
Species |
Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis) |
KEGG Pathway |
ava:Ava_C0144 |
EC number |
5.6.1.7: Enzymes altering polypeptide conformation or assembly |
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 Q3M1B1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3M1B1-F1 | Predicted | AlphaFoldDB |
No variants for Q3M1B1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q3M1B1 | |||||
No associated diseases with Q3M1B1
1 regional properties for Q3M1B1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Chaperonin Cpn60, conserved site | 403 - 414 | IPR018370 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.6.1.7 | Enzymes altering polypeptide conformation or assembly |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
4 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. |
| isomerase activity | Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5. |
| unfolded protein binding | Binding to an unfolded protein. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protein refolding | The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVKTILYKDT | ARWTLEKGFD | ALTEAVAVTL | GPKGRNIVLE | KKFGAPQIVN | DGVTIAKEIE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LEDPAENTGI | SLLRQAASKT | NDVAGDGTTT | AIVLAHAMLK | EGLRNVTAGA | DPLTVKRGID |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KATEFVIEKI | QEHARPIKDS | RDIEQVATIS | AGNDPEVGRI | VAEAMERVGK | EGVISLEEGR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| STTTELEVTE | GMRFDRGYVS | PYFVTDPERM | EAVLEEPHIL | ITDRKITMVQ | DLVPILEQIA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RTGKPLLIIA | DDIEKEALAT | LVVNHLRGVL | RVAAVKAPGF | GAQRKAVLED | IAALTGGQVI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SEDTGLKLEN | VRLEMLGKAR | RAIVTKDDTT | IVAEGNEEAV | KARIEQIRRQ | IQEVESSYDK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EKLQQRLAKL | AGGVAVIKVG | AATETELKDR | KLRLEDAINA | TKAAVEEGIV | PGGGTTIAHI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| APQLEEWAKS | QMKDEELTGT | MIVARALYAP | LRRIADNAGA | NGAVIVERVR | ELPFDEGYDA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VANKFVNMFE | AGIVDPAKVT | RSALQNAASI | GGMVLTTEGV | VVEKPDKQAK | APAGVGPGPG |
| EGFDY |