Summary for clan SP

Summary Structure Literature
Clan type peptidaseS59.001 - nucleoporin 145 (Homo sapiens), MEROPS Accession MER0020203 (peptidase unit: 710-937); PDB accession 1KO6
HistoryMEROPS 6.4 (24 September 2003)
DescriptionSerine nucleophile; catalytic residues in the order His, Ser within the motif HXS.
Contents of clanThe clan contains a single family of self-processing proteins.
EvidenceThe 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 foldThe 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 familiesThe fold is unique to clan SP.
Other databases SCOP82215


Family Family Type Peptidase Structure
S59 nucleoporin 145 (Homo sapiens) Yes

Distribution of clan SP among Kingdoms of Organisms