ProRule PRU10073
General rule information
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Accession | PRU10073 |
Dates | 16-OCT-2006 (Created)
19-NOV-2022 (Last updated, Version 13) |
Data class | Domain; |
Predictors |
PROSITE; PS00869; RENAL_DIPEPTIDASE_1 PROSITE; PS51365; RENAL_DIPEPTIDASE_2 |
Name | Renal dipeptidase family |
Function | Renal dipeptidase (rDP) (EC 3.4.13.19) and related enzymes are zinc-dependent metalloenzymes which hydrolyze a wide range of dipeptides. |
Scope(s) |
Eukaryota Bacteria Archaea |
Example(s) | Q3SZM7 (DPEP1_BOVIN); |
Propagated annotation
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Identifier, protein and gene names
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case <FTGroup:1> or <FTGroup:2> or not <AnyFeature:PS51365> | |
Protein name | + AltName: Full=dipeptidase; EC=3.4.13.19; |
Comments
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CATALYTIC ACTIVITY | Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid; Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:77460; EC=3.4.13.19; |
COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; |
end case | |
case <Feature:PS51365:365=C> and <FTGroup:3> and <FTGroup:4> | |
SUBUNIT | Homodimer; disulfide-linked. |
end case | |
SIMILARITY | Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family. |
Keywords
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Dipeptidase | |
Hydrolase | |
Metal-binding | |
Metalloprotease | |
Protease | |
Zinc | |
end case | |
case <FTTag:disulf> | |
Disulfide bond | |
end case |
Gene Ontology
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case <FTGroup:1> or <FTGroup:2> | |
GO:0016805; Molecular function:dipeptidase activity | |
GO:0016787; Molecular function:hydrolase activity | |
GO:0046872; Molecular function:metal ion binding | |
GO:0008237; Molecular function:metallopeptidase activity | |
GO:0008233; Molecular function:peptidase activity | |
GO:0008270; Molecular function:zinc ion binding |
Features
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From: PS51365 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 20 | 20 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic" |
H | 1 | |||||||
BINDING | 22 | 22 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic" |
D | 1 | |||||||
BINDING | 125 | 125 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic" |
E | 1 | |||||||
BINDING | 125 | 125 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /ligand_note="catalytic" |
E | 2 | |||||||
BINDING | 198 | 198 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /ligand_note="catalytic" |
Y | 2 | |||||||
BINDING | 219 | 219 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#2" /ligand_note="catalytic" |
H | 2 | |||||||
BINDING | 152 | 152 | /ligand="substrate" | H | ||||||||
BINDING | 230 | 230 | /ligand="substrate" | R | ||||||||
BINDING | 290 | 290 | /ligand="substrate" | D | ||||||||
DISULFID | 71 | 154 | disulf | C-x*-C | 3 | |||||||
DISULFID | 226 | 258 | disulf | C-x*-C | 4 | |||||||
DISULFID | 365 | 365 | /note="Interchain" | disulf | C-x*-C | |||||||
From: PS00869 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
case not <AnyFeature:PS51365> | ||||||||||||
BINDING | 2 | 2 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic" |
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end case |
Additional information
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Size range | 260-380 amino acids |
Related rules |
None |
Fusion | None |
Repeats | 1 |
Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Bacteria [2] Eukaryota [30] All [ 32 ]
- Retrieve set of proteins with 3D structure for this domain