A0AAD9RLE6 · A0AAD9RLE6_9HYME
- ProteinPeptidase metallopeptidase domain-containing protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids627 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Cofactor
Protein has several cofactor binding sites:
Note: Can bind about 5 Ca2+ ions per subunit.
Note: Binds 2 Zn2+ ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 88 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 163 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 173 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 175 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 180 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 181 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 188 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 197 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 199 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 201 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 203 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 206 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 206 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 227 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 228 | |||||
Sequence: E | ||||||
Binding site | 231 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 237 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 245 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: M | ||||||
Binding site | 393 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 395 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 440 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 489 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 536 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 538 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular matrix | |
Cellular Component | membrane | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended namePeptidase metallopeptidase domain-containing protein
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Vespoidea > Vespidae > Eumeninae > Odynerus
Accessions
- Primary accessionA0AAD9RLE6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 607-626 | Helical | ||||
Sequence: LVSRFSMGAIVIIVAFVSVF |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MIFHVMLVLYFSVLVAG | ||||||
Chain | PRO_5041916066 | 18-627 | Peptidase metallopeptidase domain-containing protein | |||
Sequence: APRSSMIYADDKVQNYLMKFGYLPQSNLETGNLMTEDQLRDAIKNLQRFSGIPETGEIDDTTRKLMKARRCGLPDKPNPRYSRTRRKRFTIHGQQWPYRNLTWSLRTKQPSGLETGGVRLELSKALDLWARNSKLTFQEVNSDRADILVYFHRGSHGDGYPFDGRGQILAHAFFPGKDRGGDAHFDEEEIWYLQDNSNEDGTSLFAVAAHEFGHSLGLAHSSVQGALMYPWYQGLSPNYELPEDDRHGIQQMYGAPEERLWGNIPGGPPPPERPTPATTTTTVATTYRPSRTRPTRPNHYPDYGRPRRPDRYPSKPDYRTERPDYRPQRPHKPHRHHTTTLATTTTTVRPTFQRPRFRWTPPPRHDVPDKCNTSYDAISIIRREVFIFKGRYLWRIGDQGLYEGYPAEITRLFNLPEDIDHVDAVYERPDKKIVFFIGKKYYVFNANNLEPGYPRPLTILGLPASLEKIDGAMVWGHNSRTYFFSGSMYWRFDESVNHVELDYPRDISSNFVGVGNDIDAVFQWKDGKTYFFKGKGFWLFDDLRMKVAHEKQKLSAPFWMGCPRTLETNDVENNIPKKAKITSSAADSVLVSRFSMGAIVIIVAFVSVFA | ||||||
Modified residue | 470 | Phosphotyrosine; by PKDCC | ||||
Sequence: Y |
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 109-272 | Peptidase metallopeptidase | ||||
Sequence: HGQQWPYRNLTWSLRTKQPSGLETGGVRLELSKALDLWARNSKLTFQEVNSDRADILVYFHRGSHGDGYPFDGRGQILAHAFFPGKDRGGDAHFDEEEIWYLQDNSNEDGTSLFAVAAHEFGHSLGLAHSSVQGALMYPWYQGLSPNYELPEDDRHGIQQMYGA | ||||||
Region | 276-362 | Disordered | ||||
Sequence: RLWGNIPGGPPPPERPTPATTTTTVATTYRPSRTRPTRPNHYPDYGRPRRPDRYPSKPDYRTERPDYRPQRPHKPHRHHTTTLATTT | ||||||
Compositional bias | 294-310 | Polar residues | ||||
Sequence: ATTTTTVATTYRPSRTR | ||||||
Compositional bias | 315-345 | Basic and acidic residues | ||||
Sequence: NHYPDYGRPRRPDRYPSKPDYRTERPDYRPQ | ||||||
Repeat | 385-433 | Hemopexin | ||||
Sequence: PDKCNTSYDAISIIRREVFIFKGRYLWRIGDQGLYEGYPAEITRLFNLP | ||||||
Repeat | 436-481 | Hemopexin | ||||
Sequence: IDHVDAVYERPDKKIVFFIGKKYYVFNANNLEPGYPRPLTILGLPA | ||||||
Repeat | 483-531 | Hemopexin | ||||
Sequence: LEKIDGAMVWGHNSRTYFFSGSMYWRFDESVNHVELDYPRDISSNFVGV | ||||||
Repeat | 532-579 | Hemopexin | ||||
Sequence: GNDIDAVFQWKDGKTYFFKGKGFWLFDDLRMKVAHEKQKLSAPFWMGC |
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length627
- Mass (Da)72,171
- Last updated2024-05-29 v1
- Checksum08A15D06B8320BA5
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 294-310 | Polar residues | ||||
Sequence: ATTTTTVATTYRPSRTR | ||||||
Compositional bias | 315-345 | Basic and acidic residues | ||||
Sequence: NHYPDYGRPRRPDRYPSKPDYRTERPDYRPQ |
Keywords
- Technical term