Q4WZP2
Gene name |
csn5 (AFUA_2G16250) |
Protein name |
COP9 signalosome complex subunit 5 |
Names |
|
Species |
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
KEGG Pathway |
afm:AFUA_2G16250 |
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 Q4WZP2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q4WZP2-F1 | Predicted | AlphaFoldDB |
No variants for Q4WZP2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q4WZP2 | |||||
No associated diseases with Q4WZP2
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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protein deneddylation | The removal of a ubiquitin-like protein of the NEDD8 type from a protein. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQAAQQSWEL | ENTISLIDPQ | RDALYRYDEE | THKALSAARP | WAKDPHYFKS | IRISAVALIK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MTMHARSGGS | LEVMGLMQGY | ILPETFVVTD | AFRLPVEGTE | TRVNAQEEAN | EYMVSYLQSC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RDAGRMENAV | GWYHSHPGYG | CWLSGIDVTT | QDMQQLGGPF | VAVVIDPERT | ISAGKVDIGA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FRTFPKDYTP | PKEGNEDEDY | QTIPLSKAED | FGAYAHQYYS | LEVSFFKSSL | DTELLSQLWN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KYWVATLSQS | PLFTTRDYGS | RQMMDLSQKV | RRAARGIESS | GSRGGATTPK | DQQLEKIVRD |
| 310 | 320 | 330 | |||
| GQRIVSEEVK | GLLAAEVKMK | LFQGIGEGTQ | TGAS |