AC   PRU01355;
DC   Domain;
TR   PROSITE; PS52011; PEPTIDASE_M2; 1; level=0
XX
Names: 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.
XX
case <FTGroup:2>
CC   -!- COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
end case
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
XX
case (<FTGroup:1>) and (<FTGroup:2> or <FTGroup:3> or <FTGroup:4>)
GO   GO:0008237; F:metallopeptidase activity
end case
case (<FTGroup:1>)
GO   GO:0008241; F:peptidyl-dipeptidase activity
GO   GO:0004180; F:carboxypeptidase activity
XX
KW   Carboxypeptidase
KW   Hydrolase
KW   Protease
end case
case (<FTGroup:1>) and (<FTGroup:2> or <FTGroup:3> or <FTGroup:4>)
KW   Metalloprotease
end case
case (<FTGroup:2> or <FTGroup:3> or <FTGroup:4>)
KW   Metal-binding
end case
case <FTGroup:2>
KW   Zinc
end case
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: PS52011
FT   DOMAIN          from..to
FT                   /note="Peptidase M2 #"
FT   ACT_SITE        350
FT                   /note="Proton acceptor #1"
FT   Group: 1; Condition: E
FT   ACT_SITE        479
FT                   /note="Proton donor #1"
FT   Group: 1; Condition: H
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 2; Condition: H
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 2; Condition: H
FT   BINDING         377
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="#1"
FT                   /ligand_note="catalytic"
FT   Group: 2; Condition: E
FT   BINDING         152
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="#1"
FT   Group: 3; Condition: R
FT   BINDING         451
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="#1"
FT   Group: 3; Condition: W
FT   BINDING         455
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="#1"
FT   Group: 3; Condition: [RK]
case <Feature:PS52011:373=[P]> and <Feature:PS52011:485=[P]>
FT   BINDING         190
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="#2"
FT   Group: 4; Condition: Y
FT   BINDING         488
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="#2"
FT   Group: 4; Condition: R
end case
FT   DISULFID        115..123
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID        318..336
FT   Tag: disulf; Condition: C-x*-C
FT   DISULFID        504..522
FT   Tag: disulf; Condition: C-x*-C
XX
Chop: Nter=0; Cter=0;
Size: 580-591;
Related: None;
Repeats: 1-2;
Topology: Undefined;
Example: Q56NL1;
Scope:
 Eukaryota; Metazoa
Comments: None;
XX
# Revision 1.1 2022/12/05
//