Peptidases • Kalaharituber pfeilii F3 v1.0
| Annotations/Genomes | Total | Annotation Description | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
 Merops | 218 | 177 | 217 | 209 | 206 | 209 | 219 | 258 | 189 | 166 | 217 | 2,285 | |
| 5 | 5 | 9 | 5 | 4 | 4 | 6 | 9 | 4 | 3 | 7 | 61 | Water nucleophile; water bound by two Asp from monomer or dimer; all endopeptidases, from eukaryote organisms, viruses or virus-like organisms | |
| 1 | 1 | Water nucleophile; water bound by two Asp; all membrane-bound endopeptidases known only from eubacteria with active site on periplasmic side of cell membrane. | |||||||||||
| 4 | 3 | 3 | 1 | 1 | 7 | 7 | 4 | 2 | 4 | 36 | Water nucleophile; water bound by two Asp; all membrane-bound endopeptidases known only from eubacteria with active site on cytoplasmic side of cell membrane. | ||
| 19 | 18 | 23 | 26 | 22 | 21 | 27 | 21 | 20 | 18 | 23 | 238 | Cysteine nucleophile; catalytic residues in the order Cys, His, Asn (or Asp) in sequence | |
| 2 | 2 | 2 | 4 | 2 | 2 | 9 | 3 | 2 | 2 | 2 | 32 | Cysteine nucleophile; catalytic residues in the order His, Cys in sequence | |
| 2 | 3 | 1 | 1 | 2 | 1 | 1 | 2 | 1 | 3 | 17 | Cysteine nucleophile; catalytic residues in the order His, Glu (or Asp), Cys in sequence | ||
| 1 | 1 | 1 | 1 | 1 | 1 | 1 | 1 | 1 | 2 | 11 | Cysteine nucleophile; catalytic residues in the order Glu, Cys, His in sequence | ||
| 1 | 1 | 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 | 1 | 1 | 1 | 2 | 7 | Cysteine nucleophile; catalytic residues in the order Cys, His, His in sequence | |||||||
| 1 | 1 | 1 | 1 | 1 | 1 | 1 | 1 | 1 | 9 | Cysteine nucleophile; catalytic residues in the order His, Cys in sequence | |||
| 2 | 2 | Water nucleophile; water bound by Gln and Glu; all endopeptidases | |||||||||||
| 1 | 1 | Water nucleophile; water bound by Glu; all self-cleaving endopeptidases | |||||||||||
| 3 | 3 | 3 | 4 | 4 | 5 | 4 | 3 | 4 | 4 | 4 | 41 | Families of peptidase inhibitors not assigned to clans | |
| 1 | 1 | 2 | |||||||||||
| 1 | 1 | ||||||||||||
| 2 | 3 | 1 | 1 | 1 | 1 | 1 | 1 | 1 | 1 | 13 | |||
| 3 | 1 | 3 | 3 | 4 | 3 | 3 | 2 | 1 | 2 | 3 | 28 | ||
| 2 | 1 | 1 | 1 | 2 | 2 | 2 | 2 | 1 | 1 | 1 | 16 | Families of metallopeptidases not assigned to clans | |
| 15 | 6 | 12 | 15 | 16 | 18 | 13 | 14 | 10 | 8 | 14 | 141 | Water nucleophile; water bound by single zinc ion ligated to two His (within the motif HEXXH) and Glu, His or Asp | |
| 2 | 1 | 1 | 1 | 1 | 2 | 2 | 2 | 1 | 1 | 14 | Water nucleophile; water bound by single zinc ion ligated to His, Glu (within the motif HXXE) and His | ||
| 1 | 1 | Water nucleophile; water bound by single zinc ion ligated to His, Asp and His | |||||||||||
| 2 | 1 | 1 | 3 | 1 | 1 | 1 | 2 | 1 | 2 | 15 | 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 | |||||||||||
| 6 | 5 | 10 | 5 | 6 | 6 | 6 | 7 | 7 | 8 | 7 | 73 | Water nucleophile; water bound by two cobalt or manganese ions ligated by Asp, Asp, His, Glu, Glu | |
| 12 | 13 | 10 | 13 | 12 | 11 | 15 | 19 | 11 | 8 | 18 | 142 | Water nucleophile; water bound by two zinc ions ligated by His (or Asp), Asp, Glu, Asp (or Glu), His | |
| 5 | 6 | 5 | 5 | 5 | 5 | 6 | 8 | 6 | 6 | 5 | 62 | Water nucleophile; water bound by two zinc ions ligated by His, His or Asp, Lys or Glu, His, His. | |
| 4 | 4 | 8 | 4 | 3 | 4 | 4 | 4 | 4 | 4 | 4 | 47 | Water nucleophile; water bound by single zinc ion ligated to two His and Asp (within the motif HSHP(X)9D) | |
| 2 | 1 | 1 | 1 | 1 | 1 | 1 | 1 | 9 | Serine or cysteine nucleophile; catalytic residues in the order His, Asp, Ser (or Cys) in sequence; all endopeptidases | ||||
| 18 | 20 | 19 | 20 | 20 | 20 | 21 | 23 | 20 | 17 | 21 | 219 | Threonine, serine or cysteine nucleophile at the N-terminus of mature enzyme | |
| 4 | 4 | 5 | 5 | 8 | 9 | 2 | 6 | 4 | 4 | 3 | 54 | 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 | 1 | 1 | 3 | Serine or threonine nucleophile; N-terminal nucleophile | |||||||||
| 22 | 8 | 12 | 10 | 8 | 7 | 9 | 12 | 11 | 5 | 10 | 114 | Serine nucleophile; catalytic residues in the order Asp, His, Ser in sequence in family S8, but family S53 differs | |
| 61 | 41 | 57 | 52 | 60 | 58 | 49 | 77 | 41 | 41 | 58 | 595 | Serine nucleophile; catalytic residues in the order Ser, Asp, His in sequence | |
| 2 | 1 | 2 | 3 | 1 | 1 | 10 | Serine nucleophile; catalytic residues in the order Ser, Lys (within the motif SXXK) in sequence | ||||||
| 4 | 3 | 3 | 4 | 3 | 3 | 3 | 3 | 3 | 2 | 2 | 33 | Serine nucleophile; catalytic residues in the order Ser, Lys (or His) in sequence | |
| 1 | 1 | Serine nucleophile; catalytic residues in the order Ser, Lys in sequence | |||||||||||
| 1 | 1 | 1 | 2 | 1 | 1 | 1 | 1 | 2 | 1 | 1 | 13 | Serine nucleophile; catalytic residues in the order Ser, His, Asp in sequence | |
| 1 | 2 | 2 | 2 | 2 | 3 | 2 | 3 | 3 | 2 | 1 | 23 | Serine nucleophile; transmembrane protein with catalytic residues in the order Ser, His embedded in the membrane | |
| 1 | 1 | 1 | 3 | Families of peptidases of unknown catalytic mechanism not assigned to clans | |||||||||
| 1 | 1 | 2 | 1 | 1 | 3 | 1 | 2 | 1 | 1 | 14 | |||
| 10 | 15 | 11 | 13 | 12 | 12 | 13 | 11 | 16 | 11 | 13 | 137 | ||
| 1 | 1 | 2 | |||||||||||
| 1 | 1 | 1 | 1 | 4 | |||||||||
| 3 | 4 | 5 | 2 | 3 | 2 | 3 | 7 | 1 | 4 | 3 | 37 |
