dipeptidyl peptidase 1 isoform a preproprotein, partial [Homo sapiens]
List of domain hits
Name | Accession | Description | Interval | E-value | ||
CathepsinC_exc super family | cl07399 | Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ... |
1-32 | 4.08e-15 | ||
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor. The actual alignment was detected with superfamily member pfam08773: Pssm-ID: 462598 [Multi-domain] Cd Length: 118 Bit Score: 63.45 E-value: 4.08e-15
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Name | Accession | Description | Interval | E-value | ||
CathepsinC_exc | pfam08773 | Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ... |
1-32 | 4.08e-15 | ||
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor. Pssm-ID: 462598 [Multi-domain] Cd Length: 118 Bit Score: 63.45 E-value: 4.08e-15
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Name | Accession | Description | Interval | E-value | ||
CathepsinC_exc | pfam08773 | Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ... |
1-32 | 4.08e-15 | ||
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor. Pssm-ID: 462598 [Multi-domain] Cd Length: 118 Bit Score: 63.45 E-value: 4.08e-15
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Blast search parameters | ||||
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