A0A1V1G1G3 · A0A1V1G1G3_9NEOP
- ProteinPutative carboxypeptidase 7
- GeneCPase7
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids530 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
Catalytic activity
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-phenylalanine = H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-phenylalanineThis reaction proceeds in the forward and the backward directions.
- (9Z)-octadecenoate + L-phenylalanine = H2O + N-(9Z-octadecenoyl)-L-phenylalanineThis reaction proceeds in the forward and the backward directions.
- (9Z)-octadecenoate + glycine = H2O + N-(9Z-octadecenoyl)glycineThis reaction proceeds in the backward direction.
- H2O + N-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-L-phenylalanine = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + L-phenylalanineThis reaction proceeds in the forward direction.
- H2O + N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycineThis reaction proceeds in the forward and the backward directions.
- H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-serineThis reaction proceeds in the forward and the backward directions.
- H2O + N-(9Z-octadecenoyl)-L-asparagine = (9Z)-octadecenoate + L-asparagineThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-glutamine = (9Z)-octadecenoate + L-glutamineThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-leucine = (9Z)-octadecenoate + L-leucineThis reaction proceeds in the forward and the backward directions.
- H2O + N-(9Z-octadecenoyl)-L-lysine = (9Z)-octadecenoate + L-lysineThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-methionine = (9Z)-octadecenoate + L-methionineThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-serine = (9Z)-octadecenoate + L-serineThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-tryptophan = (9Z)-octadecenoate + L-tryptophanThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-tyrosine = (9Z)-octadecenoate + L-tyrosineThis reaction proceeds in the forward direction.
- H2O + N-hexadecanoyl-L-phenylalanine = hexadecanoate + L-phenylalanineThis reaction proceeds in the forward direction.
- H2O + N-octadecanoyl-L-phenylalanine = L-phenylalanine + octadecanoateThis reaction proceeds in the forward direction.
Pathway
Lipid metabolism; fatty acid metabolism.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 145 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 147 | |||||
Sequence: D | ||||||
Binding site | 178 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 178 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 212 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 213 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 240 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 486 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides | |
Molecular Function | metal ion binding | |
Molecular Function | metallocarboxypeptidase activity | |
Biological Process | amide biosynthetic process | |
Biological Process | amide catabolic process | |
Biological Process | amino acid metabolic process | |
Biological Process | cellular lipid metabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Polyneoptera > Dictyoptera > Blattodea > Blattoidea > Termitoidae > Rhinotermitidae > Reticulitermes > Frontotermes
Accessions
- Primary accessionA0A1V1G1G3
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 20-43 | Helical | ||||
Sequence: LALIGFPLAAGLLLVFVAIFRAVF |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 262-405 | Peptidase M20 dimerisation | ||||
Sequence: ISEKGTATLELSVSGNPGHSSFPPPESAIGILAAAVARLEENPQPSLLGKGPESATFKYLAPHVSFFYRLLYNNMWLFSGLMARQMERVPLTNAFVRTTTAITVFHGGIKDNVVPPSAKAVINHRVHPSQTVAEAIAYDRKIIS |
Sequence similarities
Belongs to the peptidase M20A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length530
- Mass (Da)59,418
- Last updated2017-06-07 v1
- Checksum0FCC704FFBEAA4E9