3.4.21.B56: Pyrococcus horikoshii membrane protease PH1510
This is an abbreviated version!
For detailed information about Pyrococcus horikoshii membrane protease PH1510, go to the full flat file.
Word Map on EC 3.4.21.B56
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3.4.21.B56
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hyperthermophilic
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archaeon
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dyad
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hemolytic
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anemia
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stomatocytosis
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ser-lys
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erythrocyte
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superposition
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coiled-coil
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symmetry-related
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ob-fold
- 3.4.21.B56
-
hyperthermophilic
- archaeon
-
dyad
-
hemolytic
-
anemia
-
stomatocytosis
- ser-lys
- erythrocyte
-
superposition
-
coiled-coil
-
symmetry-related
-
ob-fold
Reaction
Synonyms
1510-C, 1510-N, membrane stomatin-specific protease, PH1510, PH1510p, stomatin operon partner protein, Stomatin/STOPP, STOPP, STOPP PH1510
ECTree
3.4.21.B56 Pyrococcus horikoshii membrane protease PH1510Advanced search results
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General Information on EC 3.4.21.B56 - Pyrococcus horikoshii membrane protease PH1510
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
physiological function
the enzyme may be involved in the quality control of membrane proteins, e.g. stomatin, prohibitin, flotillin, and HflK/C domain proteins found in the lipid raft microdomains of various cellular membranes
additional information
additional information
C-terminal soluble enzyme domain 1510-C, residues 371-441 of PH1510, functions as a scaffold protein to form the multimeric assembly of STOPP and stomatin
additional information
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C-terminal soluble enzyme domain 1510-C, residues 371-441 of PH1510, functions as a scaffold protein to form the multimeric assembly of STOPP and stomatin
additional information
the N-terminal region of PH1510 (residues 16-236, i.e. 1510-N) is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138). The hexameric subcomplex I from archaeal proteasome consists of coiled-coil segments and oligonucleotide binding-fold domains, molecular modeling of hexameric oligonucleotide binding domains of enzyme 1510-C, domain structure, overview. Conserved residues at the domain surface may play key roles in maintaining protein-protein interactions of enzyme and substrate
additional information
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the N-terminal region of PH1510 (residues 16-236, i.e. 1510-N) is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138). The hexameric subcomplex I from archaeal proteasome consists of coiled-coil segments and oligonucleotide binding-fold domains, molecular modeling of hexameric oligonucleotide binding domains of enzyme 1510-C, domain structure, overview. Conserved residues at the domain surface may play key roles in maintaining protein-protein interactions of enzyme and substrate
additional information
the N-terminal region of PH1510p is a serine protease with a catalytic Ser-Lys dyad, Ser97 and Lys138
additional information
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the N-terminal region of PH1510p is a serine protease with a catalytic Ser-Lys dyad, Ser97 and Lys138
