Peptidases • Aspergillus homomorphus CBS 101889 v1.0
| Annotations/Genomes | Total | Annotation Description | |||||
|---|---|---|---|---|---|---|---|
 Merops | 274 | 317 | 388 | 291 | 414 | 1,684 | |
| 4 | 10 | 15 | 4 | 13 | 46 | Water nucleophile; water bound by two Asp from monomer or dimer; all endopeptidases, from eukaryote organisms, viruses or virus-like organisms | |
| 1 | 1 | 4 | 2 | 8 | Water nucleophile; water bound by two Asp; all membrane-bound endopeptidases known only from eubacteria with active site on periplasmic side of cell membrane. | ||
| 1 | 8 | 8 | 33 | 6 | 56 | Water nucleophile; water bound by two Asp; all membrane-bound endopeptidases known only from eubacteria with active site on cytoplasmic side of cell membrane. | |
| 50 | 31 | 34 | 10 | 34 | 159 | Cysteine nucleophile; catalytic residues in the order Cys, His, Asn (or Asp) in sequence | |
| 3 | 2 | 3 | 3 | 3 | 14 | Cysteine nucleophile; catalytic residues in the order His, Cys in sequence | |
| 1 | 1 | 1 | 2 | 5 | Cysteine nucleophile; catalytic residues in the order His, Glu (or Asp), Cys in sequence | ||
| 1 | 1 | 1 | 3 | Cysteine nucleophile; catalytic residues in the order Glu, Cys, His in sequence | |||
| 1 | 1 | 2 | Cysteine nucleophile; active peptidase is a homodimer with active site His and Glu from one monomer and Cys from the other. Catalytic residues in the order His, Glu, Cys in each monomer. | ||||
| 2 | 7 | 5 | 4 | 3 | 21 | Water nucleophile; water bound by Gln and Glu; all endopeptidases | |
| 1 | 1 | Water nucleophile; water bound by Glu; all self-cleaving endopeptidases | |||||
| 7 | 5 | 5 | 5 | 4 | 26 | Families of peptidase inhibitors not assigned to clans | |
| 1 | 1 | ||||||
| 1 | 1 | ||||||
| 2 | 1 | 1 | 3 | 7 | |||
| 2 | 3 | 4 | 1 | 10 | |||
| 1 | 1 | ||||||
| 13 | 11 | 7 | 7 | 14 | 52 | Families of metallopeptidases not assigned to clans | |
| 13 | 16 | 14 | 16 | 25 | 84 | Water nucleophile; water bound by single zinc ion ligated to two His (within the motif HEXXH) and Glu, His or Asp | |
| 1 | 1 | 1 | 2 | 5 | Water nucleophile; water bound by single zinc ion ligated to His, Glu (within the motif HXXE) and His | ||
| 1 | 1 | 2 | Water nucleophile; water bound by single zinc ion ligated to two His (within the motif HXXEH) and Glu | ||||
| 1 | 1 | Water nucleophile; water bound by two zinc ions ligated by Lys, Asp, Asp, Asp, Glu | |||||
| 4 | 6 | 8 | 5 | 7 | 30 | Water nucleophile; water bound by two cobalt or manganese ions ligated by Asp, Asp, His, Glu, Glu | |
| 17 | 24 | 26 | 40 | 26 | 133 | Water nucleophile; water bound by two zinc ions ligated by His (or Asp), Asp, Glu, Asp (or Glu), His | |
| 7 | 7 | 17 | 8 | 13 | 52 | Water nucleophile; water bound by two zinc ions ligated by His, His or Asp, Lys or Glu, His, His. | |
| 1 | 1 | Water nucleophile; water bound by single zinc ion ligated to two His (within the motif HEXXH) and Asp; membrane proteins with intramembrane active site. | |||||
| 3 | 4 | 5 | 1 | 1 | 14 | Water nucleophile; water bound by single zinc ion ligated to two His and Asp (within the motif HSHP(X)9D) | |
| 1 | 1 | 1 | 3 | Water nucleophile; water bound by single zinc ion ligated to Asp, His and His. | |||
| 1 | 1 | Asparagine nucleophile; catalytic residues in the order Asn, Glu in sequence; all self-processing endopeptidases | |||||
| 2 | 1 | 3 | 6 | Serine or cysteine nucleophile; catalytic residues in the order His, Asp, Ser (or Cys) in sequence; all endopeptidases | |||
| 20 | 22 | 20 | 17 | 26 | 105 | Threonine, serine or cysteine nucleophile at the N-terminus of mature enzyme | |
| 6 | 8 | 8 | 4 | 9 | 35 | Serine or cysteine nucleophile; catalytic residues in the order Cys (or Ser), His, Glu in sequence. | |
| 1 | 1 | Cysteine nucleophile at the N-terminus of mature enzyme; catalytic residues in the order Cys, Thr, His | |||||
| 1 | 2 | 3 | Serine or threonine nucleophile; N-terminal nucleophile | ||||
| 1 | 1 | Families of serine peptidases not assigned to clans | |||||
| 8 | 10 | 12 | 4 | 9 | 43 | Serine nucleophile; catalytic residues in the order Asp, His, Ser in sequence in family S8, but family S53 differs | |
| 59 | 109 | 160 | 61 | 153 | 542 | Serine nucleophile; catalytic residues in the order Ser, Asp, His in sequence | |
| 1 | 7 | 10 | 1 | 7 | 26 | Serine nucleophile; catalytic residues in the order Ser, Lys (within the motif SXXK) in sequence | |
| 3 | 4 | 3 | 1 | 7 | 18 | Serine nucleophile; catalytic residues in the order Ser, Lys (or His) in sequence | |
| 5 | 1 | 2 | 2 | 3 | 13 | Serine nucleophile; catalytic residues in the order Ser, His, Asp in sequence | |
| 1 | 1 | 2 | Serine nucleophile; catalytic residues in the order Ser, Glu, His | ||||
| 1 | 2 | 1 | 2 | 1 | 7 | Serine nucleophile; transmembrane protein with catalytic residues in the order Ser, His embedded in the membrane | |
| 2 | 3 | 3 | 9 | 17 | Families of peptidases of unknown catalytic mechanism not assigned to clans | ||
| 1 | 1 | 1 | 1 | 1 | 5 | ||
| 11 | 8 | 9 | 8 | 19 | 55 | ||
| 1 | 1 | ||||||
| 1 | 1 | 2 | |||||
| 18 | 4 | 38 | 3 | 63 |
