Q5BBF1
Gene name |
rri1 (csn5, csnE, AN2129) |
Protein name |
COP9 signalosome complex subunit 5 |
Names |
|
Species |
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
KEGG Pathway |
ani:AN2129.2 |
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 Q5BBF1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5BBF1-F1 | Predicted | AlphaFoldDB |
No variants for Q5BBF1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5BBF1 | |||||
No associated diseases with Q5BBF1
No regional properties for Q5BBF1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q5BBF1 | |||
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| COP9 signalosome | A protein complex that catalyzes the deneddylation of proteins, including the cullin component of SCF ubiquitin E3 ligase; deneddylation increases the activity of cullin family ubiquitin ligases. The signalosome is involved in many regulatory process, including some which control development, in many species; also regulates photomorphogenesis in plants; in many species its subunits are highly similar to those of the proteasome. |
| 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 |
|---|---|
| deNEDDylase activity | An isopeptidase activity that cleaves NEDD8 from a target protein to which it is conjugated. |
| 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. |
| 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. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cleistothecium development | The process whose specific outcome is the progression of the cleistothecium over time, from its formation to the mature structure. The cleistothecium is a closed sexual fruiting body that contains ascospores in linear asci, characteristic of some filamentous Ascomycete fungi such as members of the genera Aspergillus and Emericella. |
| hyphal growth | Growth of fungi as threadlike, tubular structures that may contain multiple nuclei and may or may not be divided internally by septa, or cross-walls. |
| protein deneddylation | The removal of a ubiquitin-like protein of the NEDD8 type from a protein. |
| protein neddylation | Covalent attachment of the ubiquitin-like protein NEDD8 (RUB1) to another protein. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQAAQLSWEL | ENAVTLIDPQ | RDSLYRYDEE | THKYLSDTRP | WTKDPHYFKS | VRISAVALLK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MVMHARSGGS | LEVMGLMQGY | ILPNTFVVTD | AFRLPVEGTE | TRVNAQDEAN | EYMVSYLQSC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| REAGRMENAV | GWYHSHPGYG | CWLSGIDVST | QDMQQMSGPF | VAVVIDPERT | ISAGKVDIGA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FRTFPKDYTP | PKEEQEEDEY | QTVPLNKAED | FGAHASHYYS | LEVSLFKSAL | DTEILSLLWN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KYWVATLSQS | PLFTTRDYGS | KQMLDLSQKT | RRVARGIESN | PPRGGAPTQV | RDQQLERVVK |
| 310 | 320 | 330 | |||
| DGQRIVSEEV | KGLLAAEVKM | QLFQGIGGKQ | TVEST |