General rule information
[?]
Accession |
PRU00680 |
Dates |
18-DEC-2007 (Created) 14-MAY-2022 (Last updated, Version 11) |
Predictors |
PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2
|
Name |
Glycosyl hydrolases family 22 (GH22) domain |
Function |
Alpha-lactalbumin, a regulatory protein in milk, and lysozyme (EC 3.2.1.17) C (chicken type), which acts as a bacteriolytic enzyme, belong to a family of proteins with eight conserved cysteines that form four disulfide bonds. Alpha-lactalbumin lacks the enzymatic activity and the corresponding Glu and Asp residues. Alpha-lactalbumin binds a calcium ion, while most lysozyme C do not bind calcium. |
Propagated annotation
[?]
case <FTGroup:1>
+ AltName: Full=lysozyme C;
EC 3.2.1.17;
AltName: Full=1,4-beta-N-acetylmuramidase C; |
Function |
Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. |
Catalytic activity |
Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; |
end case
Similarity |
Belongs to the glycosyl hydrolase 22 family. |
PROSITE |
PS00128; GLYCOSYL_HYDROL_F22_1; 1; |
case <FTGroup:1>
GO:0003824; Molecular function: catalytic activity.
GO:0019835; Biological process: cytolysis.
GO:0042742; Biological process: defense response to bacterium.
GO:0016798; Molecular function: hydrolase activity, acting on glycosyl bonds.
GO:0008152; Biological process: metabolic process.
GO:0016787; Molecular function: hydrolase activity.
end case
case <Feature:PS51348:85=D> and <Feature:PS51348:90-91=D-D>
GO:0005509; Molecular function: calcium ion binding.
end case
case <FTGroup:1>
end case
case <Feature:PS51348:85=D> and <Feature:PS51348:90-91=D-D>
end case
case <FTTag:disulf>
end case
From: PS51348 |
Key
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From
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To
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Description
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Tag
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Condition
|
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FTGroup
|
DOMAIN
|
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from
|
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to
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C-type lysozyme #
|
|
|
|
|
|
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ACT_SITE
|
|
35
|
|
35
|
|
|
|
|
|
E
|
|
1
|
ACT_SITE
|
|
52
|
|
52
|
|
|
|
|
|
D
|
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1
|
case <Feature:PS51348:85=D> and <Feature:PS51348:90-91=D-D>
BINDING
|
|
82
|
|
82
|
|
/ligand="Ca(2+)" /ligand_id="29108" /ligand_label="#1
|
|
binds
|
|
[HCUEDKQNMYWSTRX]
|
|
|
BINDING
|
|
85
|
|
85
|
|
/ligand="Ca(2+)" /ligand_id="29108" /ligand_label="#1
|
|
binds
|
|
[HCUEDKQNMYWSTRX]
|
|
|
BINDING
|
|
87
|
|
87
|
|
/ligand="Ca(2+)" /ligand_id="29108" /ligand_label="#1
|
|
binds
|
|
[HCUEDKQNMYWSTRX]
|
|
|
BINDING
|
|
90
|
|
90
|
|
/ligand="Ca(2+)" /ligand_id="29108" /ligand_label="#1
|
|
binds
|
|
[HCUEDKQNMYWSTRX]
|
|
|
BINDING
|
|
91
|
|
91
|
|
/ligand="Ca(2+)" /ligand_id="29108" /ligand_label="#1
|
|
binds
|
|
[HCUEDKQNMYWSTRX]
|
|
|
end case
DISULFID
|
|
6
|
|
125
|
|
|
|
disulf
|
|
C-x*-C
|
|
|
DISULFID
|
|
30
|
|
114
|
|
|
|
disulf
|
|
C-x*-C
|
|
|
DISULFID
|
|
64
|
|
80
|
|
|
|
disulf
|
|
C-x*-C
|
|
|
DISULFID
|
|
76
|
|
94
|
|
|
|
disulf
|
|
C-x*-C
|
|
|
Additional information
[?]
Size range |
110-140 amino acids |
Related rules |
None |
Repeats |
1 |
Topology |
Undefined |
Example |
Q659U0 (LYSC_LEPWE) |
Scope |
Eukaryota; Metazoa |
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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