Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
BSCOP2B SuperfamilyAcid proteases 8100328 3001059 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyAcid proteases 8100328 3001059 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BRVPe3o9aB1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: acid proteaseF: RVPECOD (1.6)
ARVPe3o9aA1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: acid proteaseF: RVPECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B2.40.70.10 Mainly Beta Beta Barrel Cathepsin D, subunit A domain 1CATH (4.3.0)
A2.40.70.10 Mainly Beta Beta Barrel Cathepsin D, subunit A domain 1CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00077Retroviral aspartyl protease (RVP)Retroviral aspartyl proteaseSingle domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a ...Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (Pfam:PF00026).
Domain