Q22398
Gene name |
nas-22 (T11F9.6) |
Protein name |
Zinc metalloproteinase nas-22 |
Names |
Nematode astacin 22 |
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_T11F9.6 |
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 Q22398
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q22398-F1 | Predicted | AlphaFoldDB |
No variants for Q22398
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for Q22398 |
No associated diseases with Q22398
1 GO annotations of cellular component
Name | Definition |
---|---|
extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
2 GO annotations of molecular function
Name | Definition |
---|---|
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. |
zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
Name | Definition |
---|---|
molting cycle, collagen and cuticulin-based cuticle | The periodic shedding of part or all of a collagen and cuticulin-based cuticle, which is then replaced by a new collagen and cuticulin-based cuticle. An example of this is found in the Nematode worm, Caenorhabditis elegans. |
proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
10 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
Q6HA09 | Astl | Astacin-like metalloendopeptidase | Mus musculus (Mouse) | PR |
Q18439 | nas-8 | Zinc metalloproteinase nas-8 | Caenorhabditis elegans | PR |
P55112 | nas-4 | Zinc metalloproteinase nas-4 | Caenorhabditis elegans | PR |
P55113 | nas-7 | Zinc metalloproteinase nas-7 | Caenorhabditis elegans | PR |
Q9U3S9 | nas-6 | Zinc metalloproteinase nas-6 | Caenorhabditis elegans | PR |
Q21252 | nas-3 | Zinc metalloproteinase nas-3 | Caenorhabditis elegans | PR |
O62243 | nas-1 | Zinc metalloproteinase nas-1 | Caenorhabditis elegans | PR |
Q20942 | nas-38 | Zinc metalloproteinase nas-38 | Caenorhabditis elegans | PR |
P55115 | nas-15 | Zinc metalloproteinase nas-15 | Caenorhabditis elegans | PR |
Q20176 | nas-39 | Zinc metalloproteinase nas-39 | Caenorhabditis elegans | PR |
10 | 20 | 30 | 40 | 50 | 60 |
MKSFFILLSI | LQECYGKDIV | ARIGGRNVAE | KIGGARHRRQ | VLIRGSDEER | RHKWFNNTVH |
70 | 80 | 90 | 100 | 110 | 120 |
YYFYEENFDF | TVKESILRAM | ELISNHTCIK | FSTEPSEKSI | RMESDSTTIA | CYAEIGQVRE |
130 | 140 | 150 | 160 | 170 | 180 |
NQLFSFNSDC | YSAGVAVHEL | IHSLGFIHAH | QRSDRDQYLE | FKKNLDELNQ | TYQEQYKIWE |
190 | 200 | 210 | 220 | 230 | 240 |
YQEILVPYDV | GSVMQYPNEE | DEEYYPVRKY | RTMANTMGSA | IVAFYDYLMI | NKYYECSCAN |
250 | 260 | 270 | 280 | 290 | 300 |
NLSCKNHGYP | NPSNCSQCNC | PYGFGGADCS | QRAEPGATFQ | ATETWQNVTI | SLDAGYRYLE |
310 | 320 | 330 | 340 | 350 | 360 |
NNQKLPQVDF | IYQFLWIMAP | ANKTTQIRVE | KFVEGKCLPG | CIRGGVEIKT | NEDPRLTSPR |
LCCEETS |