Protein Domain : IPR008761

Type:  Family Name:  Peptidase S37, tripeptidyl aminopeptidase
Description:  Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes []. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identified, these being grouped into clans on the basis of structural similarity and other functional evidence []. Structures are known for members of the clans and the structures indicate that some appear to be totally unrelated, suggesting different evolutionary origins for the serine peptidases [].Not withstanding their different evolutionary origins, there are similarities in the reaction mechanisms of several peptidases. Chymotrypsin, subtilisin and carboxypeptidase C have a catalytic triad of serine, aspartate and histidine in common: serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base []. The geometric orientations of the catalytic residues are similar between families, despite different protein folds []. The linear arrangements of the catalytic residues commonly reflect clan relationships. For example the catalytic triad in the chymotrypsin clan (PA) is ordered HDS, but is ordered DHS in the subtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) [, ].These group of serine peptidases belong to MEROPS peptidase family S37 (clan SC). The members of this group of secreted peptidases are restricted to bacteria. In Streptomyces lividansthe peptidase removes tripeptides from the N terminus of extracellular proteins (tripeptidyl aminopeptidase,Tap) [, ]. Short Name:  Peptidase_S37
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0 Child Features

0 Contains

1 Cross References

Identifier
PF05576

0 Found In

0 GO Annotation

0 Ontology Annotations

0 Parent Features

13 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
11918 I0Z7R1 PAC:27393045 Coccomyxa subellipsoidea C-169 395  
Bol036004 PAC:37357386 Brassica oleracea capitata 403  
Cz12g03180.t1 PAC:38240265 Chromochloris zofingiensis 293  
Lsat_1_v5_gn_1_61581.2 PAC:38946460 Lactuca sativa 504  
Carub.0006s2059.1.p PAC:39247934 Capsella rubella 438  
Isati.2329s0006.1.p PAC:39323255 Isatis tinctoria 499  
Isati.2329s0006.2.p PAC:39323256 Isatis tinctoria 461  
Isati.1378s0001.2.p PAC:39307761 Isatis tinctoria 367  
Isati.3106s0002.1.p PAC:39360575 Isatis tinctoria 315  
Eusyr.0014s0423.1.p PAC:39687048 Euclidium syriacum 423  
evm.model.AsparagusV1_03.1988 A0A5P1FCG5 PAC:40539881 Asparagus officinalis 485  
Bobra.0236s0008.1.p PAC:40724716 Botryococcus braunii 327  
Potri.001G213000.3.p PAC:42793151 Populus trichocarpa 356  

4 Publications

First Author Title Year Journal Volume Pages PubMed ID
            8439290
            7845208
            8920189
            7487044