Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyDipeptidyl peptidase I (cathepsin C) exclusion domain8027418 4002113 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyDipeptidyl peptidase I (cathepsin C) exclusion domain8039797 3000840 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ACathepsinC_exce2djfA1 A: beta barrelsX: Lipocalins/StreptavidinH: Dipeptidyl peptidase I (cathepsin C), exclusion domain (From Topology)T: Dipeptidyl peptidase I (cathepsin C), exclusion domainF: CathepsinC_excECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B3.90.70.10 Alpha Beta Alpha-Beta Complex Cathepsin B Chain ACATH (4.3.0)
A2.40.128.80 Mainly Beta Beta Barrel Lipocalin Cathepsin C, exclusion domainCATH (4.3.0)
C2.40.50.170 Mainly Beta Beta Barrel OB fold (Dihydrolipoamide Acetyltransferase, E2P) Cysteine proteinases. Chain CCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00112Papain family cysteine protease (Peptidase_C1)Papain family cysteine protease- Domain
PF08773Cathepsin C exclusion domain (CathepsinC_exc)Cathepsin C exclusion domainCathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed ...Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands [1]. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor [1].
Domain
PF00112Papain family cysteine protease (Peptidase_C1)Papain family cysteine protease- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Dipeptidyl-peptidase 1
Dipeptidyl-peptidase 1
Dipeptidyl-peptidase 1

InterPro: Protein Family Classification InterPro Database Homepage

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosP53634
PharosP53634
PharosP53634