Protein Domain : IPR008751

Type:  Domain Name:  Peptidase C53, pestivirus Npro
Description:  Cysteine peptidases have characteristic molecular topologies, which can be seen not only in their three-dimensional structures, but commonly also in the two-dimensional structures. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins which are evolutionary related), and further sub-divided into families, on the basis of the architecture of their catalytic dyad or triad []. This group of cysteine peptidases belong to MEROPS peptidase family C53 (clan C-). The active site residues occur in the order E, H, C in the sequence which is unlike that in any other family. They are unique to pestiviruses. The N-terminal cysteine peptidase (Npro) encoded by the bovine viral diarrhoea virus genome is responsible for the self-cleavage that releases the N terminus of the core protein. This unique protease is dispensable for viral replication, and its coding region can be replaced by a ubiquitin gene directly fused in frame to the core [, , , ]. Short Name:  Peptidase_C53
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0 Child Features

0 Contains

2 Cross Referencess

Identifier
PF05550
PD003091

0 Found In

2 GO Annotations

GO Term Gene Name
GO:0016032 IPR008751
GO:0019082 IPR008751

2 Ontology Annotations

GO Term Gene Name
GO:0016032 IPR008751
GO:0019082 IPR008751

0 Parent Features

8 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Brdisv1pangenome1002369m.p PAC:33622127 Brachypodium distachyon Pangenome 119  
CKAN_01156000 A0A3S3NMQ9 PAC:42708344 Cinnamomum kanehirae 267  
CKAN_00125700 A0A3S3LWU0 PAC:42703969 Cinnamomum kanehirae 251  
CKAN_00126000 A0A443N3D6 PAC:42701598 Cinnamomum kanehirae 285  
CKAN_00091500 A0A3S3MPW4 PAC:42703541 Cinnamomum kanehirae 187  
CepurR40.VG062000.1.p PAC:43024368 Ceratodon purpureus R40 98  
ELECO.r07.2AG0142840.1 PAC:44179402 Eleusine coracana 232  
ELECO.r07.2BG0198290.1 PAC:44192172 Eleusine coracana 232  

5 Publications

First Author Title Year Journal Volume Pages PubMed ID
            11517925
            11711606
            8972567
            9499122
            10864644