Structural Classification of Proteins
Family: Prokaryotic proteases
Lineage:
Root:
scop
Class:
All beta proteins
[48724]
Fold:
Trypsin-like serine proteases
[50493]
barrel, closed; n=6, S=8; greek-key
duplication: consists of two domains of the same fold
Superfamily:
Trypsin-like serine proteases
[50494]
uperfamily
Family:
Prokaryotic proteases
[50495]
Protein Domains:
Achromobacter protease [50496]
Achromobacter lyticus, strain m497-1
[TaxId: 224]
[50497] (2)
alpha-Lytic protease [50498]
Lysobacter enzymogenes, 495
[TaxId: 69]
[50499] (41)
Protease A [50500]
Streptomyces griseus, strain k1
[TaxId: 1911]
[50501] (5)
Glutamic acid-specific protease [50502]
Streptomyces griseus
[TaxId: 1911]
[50503] (1)
Trypsin [50504]
Streptomyces griseus, strain k1
[TaxId: 1911]
[50505] (3)
Serine proteinase [50506]
Streptomyces fradiae
[TaxId: 1906]
[50507] (1)
Protease B [50508]
Streptomyces griseus, strain k1
[TaxId: 1911]
[50509] (29)
Streptogrisin B
Epidermolytic (exfoliative) toxin A [50510]
probable glutamic acid-specific protease
Staphylococcus aureus
[TaxId: 1280]
[50511] (4)
Exfoliative toxin B [50512]
Staphylococcus aureus
[TaxId: 1280]
[50513] (2)
V8 protease [101809]
glutamic acid-specific protease
Staphylococcus aureus
[TaxId: 1280]
[101810] (3)
SQ
P04188
69-284
Glutamyl endopeptidase [101811]
Bacillus intermedius
[TaxId: 1400]
[101812] (2)
Protease Do (DegP, HtrA), catalytic domain [74969]
Escherichia coli
[TaxId: 562]
[74970] (14)
Thermotoga maritima
[TaxId: 2336]
[89339] (1)
Mitochondrial serine protease HtrA2, catalytic domain [74971]
Human (Homo sapiens)
[TaxId: 9606]
[74972] (1)
Stress sensor protease DegS, catalytic domain [110236]
Escherichia coli
[TaxId: 562]
[110237] (31)
SQ
P31137
37-354 ! SQ
P31137
Protease PepD [141383]
Mycobacterium tuberculosis
[TaxId: 1773]
[141384] (6)
SQ
O53896
154-374
Rv0983
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Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright
© 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk