ProRule PRU01355
General rule information
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Accession | PRU01355 |
Dates | 5-DEC-2022 (Created)
-- (Last updated, Version 1) |
Data class | Domain; |
Predictors |
PROSITE; PS52011; PEPTIDASE_M2 |
Name | Peptidase family M2 domain |
Function | Members of the M2 family of peptidases, related to mammalian angiotensin converting enzyme (EC 3.4.15.1, ACE, peptidyl-dipeptidase A), play important roles in regulating a number of physiological processes. |
Scope(s) |
Eukaryota Metazoa |
Example(s) | Q56NL1 (ACE2_PAGLA); |
Propagated annotation
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Comments
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case <FTGroup:2> | |
COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; |
end case | |
SIMILARITY | Belongs to the peptidase M2 family. |
Keywords
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Carboxypeptidase | |
Hydrolase | |
Protease | |
end case | |
case (<FTGroup:1>) and (<FTGroup:2> or <FTGroup:3> or <FTGroup:4>) | |
Metalloprotease | |
end case | |
case (<FTGroup:2> or <FTGroup:3> or <FTGroup:4>) | |
Metal-binding | |
end case | |
case <FTGroup:2> | |
Zinc | |
end case | |
case <FTTag:disulf> | |
Disulfide bond | |
end case |
Gene Ontology
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case (<FTGroup:1>) and (<FTGroup:2> or <FTGroup:3> or <FTGroup:4>) | |
GO:0008237; Molecular function:metallopeptidase activity | |
end case | |
case (<FTGroup:1>) | |
GO:0008241; Molecular function:peptidyl-dipeptidase activity | |
GO:0004180; Molecular function:carboxypeptidase activity |
Features
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From: PS52011 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DOMAIN | from | to | /note="Peptidase M2 #" | |||||||||
ACT_SITE | 350 | 350 | /note="Proton acceptor #1" | E | 1 | |||||||
ACT_SITE | 479 | 479 | /note="Proton donor #1" | H | 1 | |||||||
BINDING | 349 | 349 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic" |
H | 2 | |||||||
BINDING | 353 | 353 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic" |
H | 2 | |||||||
BINDING | 377 | 377 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="#1" /ligand_note="catalytic" |
E | 2 | |||||||
BINDING | 152 | 152 | /ligand="chloride" /ligand_id="ChEBI:CHEBI:17996" /ligand_label="#1" |
R | 3 | |||||||
BINDING | 451 | 451 | /ligand="chloride" /ligand_id="ChEBI:CHEBI:17996" /ligand_label="#1" |
W | 3 | |||||||
BINDING | 455 | 455 | /ligand="chloride" /ligand_id="ChEBI:CHEBI:17996" /ligand_label="#1" |
[RK] | 3 | |||||||
case <Feature:PS52011:373=[P]> and <Feature:PS52011:485=[P]> | ||||||||||||
BINDING | 190 | 190 | /ligand="chloride" /ligand_id="ChEBI:CHEBI:17996" /ligand_label="#2" |
Y | 4 | |||||||
BINDING | 488 | 488 | /ligand="chloride" /ligand_id="ChEBI:CHEBI:17996" /ligand_label="#2" |
R | 4 | |||||||
end case | ||||||||||||
DISULFID | 115 | 123 | disulf | C-x*-C | ||||||||
DISULFID | 318 | 336 | disulf | C-x*-C | ||||||||
DISULFID | 504 | 522 | disulf | C-x*-C |
Additional information
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Size range | 580-591 amino acids |
Related rules |
None |
Fusion | None |
Repeats | 1-2 |
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
Eukaryota [22] All [ 22 ]
- Retrieve set of proteins with 3D structure for this domain