InterPro : IPR000209

Name  Peptidase S8/S53 domain Short Name  Peptidase_S8/S53_dom
Type  Domain Description  This entry represents a domain found in serine peptidases belonging to the MEROPS peptidase families S8 (subfamilies S8A (subtilisin) and S8B (kexin)) and S53 (sedolisin), both of which are members of clan SB.The subtilisin family is the second largest serine protease family characterised to date. Over 200 subtilises are presently known, more than 170 of which with their complete amino acid sequence []. It is widespread, being found in eubacteria, archaebacteria, eukaryotes and viruses []. The vast majority of the family are endopeptidases, although there is an exopeptidase, tripeptidyl peptidase [, ]. Structures have been determined for several members of the subtilisin family: they exploit the same catalytic triad as the chymotrypsins, although the residues occur in a different order (HDS in chymotrypsin and DHS in subtilisin), but the structures show no other similarity [, ]. Some subtilisins are mosaic proteins, while others contain N- and C-terminal extensions that show no sequence similarity to any other known protein []. Based on sequence homology, a subdivision into six families has been proposed []. The proprotein-processing endopeptidases kexin, furin and related enzymesform a distinct subfamily known as the kexin subfamily (S8B). These preferentiallycleave C-terminally to paired basic amino acids. Members of this subfamilycan be identified by subtly different motifs around the active site [, ].Members of the kexin family, along with endopeptidases R, T and K from theyeast Tritirachium and cuticle-degrading peptidase from Metarhizium, requirethiol activation. This can be attributed to the presence of Cys-173 near tothe active histidine [].Only 1 viral member of the subtilisin family is known, a 56kDa protease from herpes virus 1, which infects the channel catfish []. Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, theyare considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The definingfeatures of these enzymes are a unique catalytic triad, Ser-Glu-Asp, as well as the presence of an aspartic acidresidue in the oxyanion hole. High-resolution crystal structures have now been solved for sedolisin from Pseudomonas sp. 101, as well as for kumamolisin from a thermophilic bacterium, Bacillus sp. MN-32. Mutations in the human gene leads to a fatal neurodegenerative disease [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

1 Child Features

Id Name Short Name Type
IPR030400 Sedolisin domain Sedolisin_dom Domain

2 Contains

Id Name Short Name Type
IPR003137 Protease-associated domain, PA Protease-assoc_domain Domain
IPR022398 Peptidase S8, subtilisin, His-active site Peptidase_S8_His-AS Active_site

24 Found In

Id Name Short Name Type
IPR015500 Peptidase S8, subtilisin-related Peptidase_S8_subtilisin-rel Family
IPR017292 Peptidase S8A, Vpr Peptidase_S8A_Vpr Family
IPR016625 Uncharacterised conserved protein UCP014872, subtilisin-related UCP014872_subtilisin-rel Family
IPR016916 Uncharacterised conserved protein UCP029389, subtilisin-related UCP029389_subtilisin-related Family
IPR012103 Peptidase S8A, bacillopeptidase F Pept_S8A_Bpr Family
IPR008357 Lantibiotic leader peptide-processing serine protease Lanit_process Family
IPR017001 Peptidase S53, physarolisin II, archaeal-type Pept_S53_physarolisin-II_arc Family
IPR017294 Peptidase S8A, subtilisin-related protease, kinetoplastidia Subtilisin-like_kinetoplast Family
IPR017295 Peptidase S8A, subtilisin-related, cyanobacteria-1 Pept_S8A_subtilisin_cyanobac-1 Family
IPR017296 Peptidase S8A, SAM-P45 Peptidase_S8A_SAM-P45 Family
IPR017297 Peptidase S8A, DPH-A Peptidase_S8A_DPH-A Family
IPR017306 Peptidase S8A, fervidolysin Peptidase_S8A_fervidolysin Family
IPR017308 Peptidase S8A, subtilisin-related, bacteroidetes Pept_S8_subtilisin_bacteroid Family
IPR017309 Peptidase S8A, subtilisin-related, proteobacteria Pept_S8A_subtilisin_proteobac Family
IPR017310 Peptidase S8A, subtilisin-related, clostridia Pept_S8A_subtilisin_clostridia Family
IPR017311 Peptidase S8A, subtilisin-related, shewanella Pept_S8A_subtilisin_shewanella Family
IPR017312 Peptidase S8A, subtilisin-related, shewanella-2 Pept_S8A_subtilisin_shewan-2 Family
IPR017313 Peptidase S8A, subtilisin-related, clostridia-2 Pept_S8A_subtilisin_clostrid-2 Family
IPR017314 Peptidase S8A, subtilisin-like peptidase 1, plasmodium Pept_S8A_PfSUB_1 Family
IPR017315 Peptidase S8A, subtilisin-related, proteobacteria-2 Pep_S8A_subtilisin_pbac-2 Family
IPR017316 Peptidase S8A, subtilisin-related, cyanobacteria-2 Pept_S8A_subtilisin_cyanobac-2 Family
IPR017317 Peptidase S8A, subtilisin-related, bacteroidetes-2 Pept_S8_subtilisin_bacteroid-2 Family
IPR017318 Peptidase S8A, subtilisin-related, campylobacter Pept_S8A_subtilisin_campylobac Family
IPR017319 Peptidase S8A, subtilisin-related, prokarya Pept_S8A_subtilisin_pro Family

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Rawlings ND Evolutionary families of peptidases. 1993 Biochem J 290 ( Pt 1) 205-18
Rawlings ND Families of serine peptidases. 1994 Methods Enzymol 244 19-61
Siezen RJ Subtilases: the superfamily of subtilisin-like serine proteases. 1997 Protein Sci 6 501-23
Wlodawer A Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases. 2003 Acta Biochim Pol 50 81-102



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)