Peptidases • Magnaporthiopsis poae ATCC 64411
| Annotations/Genomes | Total | Annotation Description | |||||||
|---|---|---|---|---|---|---|---|---|---|
 Merops | 266 | 337 | 275 | 242 | 358 | 295 | 1,773 | ||
| 15 | 18 | 17 | 19 | 20 | 21 | 110 | Water nucleophile; water bound by two Asp from monomer or dimer; all endopeptidases, from eukaryote organisms, viruses or virus-like organisms | ||
| 1 | 1 | 2 | Water nucleophile; water bound by two Asp; all membrane-bound endopeptidases known only from eubacteria with active site on periplasmic side of cell membrane. | ||||||
| 2 | 2 | 2 | 5 | 4 | 2 | 17 | Water nucleophile; water bound by two Asp; all membrane-bound endopeptidases known only from eubacteria with active site on cytoplasmic side of cell membrane. | ||
| 1 | 1 | 2 | Water nucleophile; water bound by Asp and His; all membrane-bound endopeptidases known only from eubacteria with active site on periplasmic side of cell membrane. | ||||||
| 14 | 15 | 16 | 16 | 24 | 18 | 103 | Cysteine nucleophile; catalytic residues in the order Cys, His, Asn (or Asp) in sequence | ||
| 2 | 3 | 3 | 3 | 4 | 3 | 18 | Cysteine nucleophile; catalytic residues in the order His, Cys in sequence | ||
| 2 | 3 | 1 | 1 | 1 | 8 | Cysteine nucleophile; catalytic residues in the order His, Glu (or Asp), Cys in sequence | |||
| 1 | 1 | 1 | 1 | 1 | 1 | 6 | Cysteine nucleophile; catalytic residues in the order Glu, Cys, His in sequence | ||
| 1 | 1 | Cysteine nucleophile; catalytic residues in the order His, Cys in sequence | |||||||
| 1 | 2 | 3 | Cysteine nucleophile; catalytic residues in the order Cys, His, His in sequence | ||||||
| 1 | 1 | 1 | 3 | Cysteine nucleophile; catalytic residues in the order His, Cys in sequence | |||||
| 4 | 1 | 1 | 2 | 4 | 4 | 16 | Water nucleophile; water bound by Gln and Glu; all endopeptidases | ||
| 1 | 1 | 2 | Water nucleophile; water bound by Glu; all self-cleaving endopeptidases | ||||||
| 4 | 4 | 2 | 3 | 4 | 3 | 20 | Families of peptidase inhibitors not assigned to clans | ||
| 1 | 1 | ||||||||
| 1 | 2 | 3 | 2 | 2 | 10 | ||||
| 1 | 6 | 3 | 1 | 4 | 4 | 19 | |||
| 2 | 2 | ||||||||
| 3 | 3 | 1 | 2 | 3 | 4 | 16 | Families of metallopeptidases not assigned to clans | ||
| 9 | 23 | 11 | 12 | 19 | 14 | 88 | Water nucleophile; water bound by single zinc ion ligated to two His (within the motif HEXXH) and Glu, His or Asp | ||
| 3 | 4 | 4 | 2 | 3 | 4 | 20 | Water nucleophile; water bound by single zinc ion ligated to His, Glu (within the motif HXXE) and His | ||
| 2 | 2 | 1 | 2 | 2 | 2 | 11 | Water nucleophile; water bound by single zinc ion ligated to two His (within the motif HXXEH) and Glu | ||
| 6 | 8 | 3 | 10 | 9 | 7 | 43 | Water nucleophile; water bound by two cobalt or manganese ions ligated by Asp, Asp, His, Glu, Glu | ||
| 16 | 19 | 24 | 14 | 23 | 19 | 115 | Water nucleophile; water bound by two zinc ions ligated by His (or Asp), Asp, Glu, Asp (or Glu), His | ||
| 6 | 6 | 7 | 10 | 21 | 10 | 60 | Water nucleophile; water bound by two zinc ions ligated by His, His or Asp, Lys or Glu, His, His. | ||
| 2 | 1 | 3 | Water nucleophile; water bound by single zinc ion ligated to two His (within the motif HEXXH) and Asp; membrane proteins with intramembrane active site. | ||||||
| 1 | 1 | Water nucleophile; water bound by single zinc ion ligated to two His and Asp (within the motifs HXXXD and HXH) | |||||||
| 3 | 3 | 2 | 4 | 3 | 4 | 19 | Water nucleophile; water bound by single zinc ion ligated to two His and Asp (within the motif HSHP(X)9D) | ||
| 1 | 1 | Water nucleophile; water bound by single zinc ion ligated to Asp, His and His. | |||||||
| 3 | 3 | 1 | 1 | 8 | Serine or cysteine nucleophile; catalytic residues in the order His, Asp, Ser (or Cys) in sequence; all endopeptidases | ||||
| 21 | 21 | 17 | 23 | 25 | 22 | 129 | Threonine, serine or cysteine nucleophile at the N-terminus of mature enzyme | ||
| 7 | 4 | 5 | 2 | 7 | 3 | 28 | 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 | 1 | 4 | Serine or threonine nucleophile; N-terminal nucleophile | |||||
| 2 | 1 | 3 | Families of serine peptidases not assigned to clans | ||||||
| 12 | 20 | 17 | 8 | 25 | 16 | 98 | Serine nucleophile; catalytic residues in the order Asp, His, Ser in sequence in family S8, but family S53 differs | ||
| 107 | 120 | 86 | 71 | 106 | 104 | 594 | Serine nucleophile; catalytic residues in the order Ser, Asp, His in sequence | ||
| 5 | 3 | 5 | 5 | 7 | 6 | 31 | Serine nucleophile; catalytic residues in the order Ser, Lys (within the motif SXXK) in sequence | ||
| 3 | 3 | 3 | 2 | 2 | 3 | 16 | Serine nucleophile; catalytic residues in the order Ser, Lys (or His) in sequence | ||
| 1 | 1 | 1 | 1 | 1 | 1 | 6 | Serine nucleophile; catalytic residues in the order Ser, His, Asp in sequence | ||
| 2 | 2 | Serine nucleophile; catalytic residues in the order Ser, Glu, His | |||||||
| 2 | 3 | 3 | 4 | 2 | 3 | 17 | Serine nucleophile; transmembrane protein with catalytic residues in the order Ser, His embedded in the membrane | ||
| 7 | 4 | 2 | 13 | Families of peptidases of unknown catalytic mechanism not assigned to clans | |||||
| 1 | 1 | 1 | 2 | 1 | 1 | 7 | |||
| 14 | 11 | 9 | 13 | 15 | 10 | 72 | |||
| 1 | 1 | ||||||||
| 1 | 1 | ||||||||
| 1 | 8 | 8 | 1 | 4 | 22 |
