Summary for clan SP
| Clan type peptidase | S59.001 - nucleoporin 145 (Homo sapiens), MEROPS Accession MER0020203 (peptidase unit: 710-937); PDB accession 1KO6 |
| History | MEROPS 6.4 (24 September 2003) |
| Description | Serine nucleophile; catalytic residues in the order His, Ser within the motif HXS. |
| Contents of clan | The clan contains a single family of self-processing proteins. |
| Evidence | The protein fold (see below) of nucleoporin 145 (S59.001) is unlike those of other peptidases. |
| Catalytic mechanism | (See family S59.) |
| Peptidase activity | (See family S59.) |
| Protein fold | The tertiary structure has been determined for the C-terminal, autolytic domain of nucleoporin 145 (S59.001; Hodel et al., 2002). This structure does not include the catalytic serine. The nucleoporin fold contains two layered beta sheets, of two and six strands. The catalytic histidine is in the larger strand near the C-terminus. |
| Homologous non-peptidase families | The fold is unique to clan SP. |
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Other databases
| SCOP | 82215 |
Families
| S59 |
nucleoporin 145 (Homo sapiens) |
Yes |
Distribution of clan SP among Kingdoms of Organisms
