Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilySwaposin8025399 4001057 SCOP2 (2022-06-29)
ASCOP2 FamilyPepsin-like8030092 4002301 SCOP2 (2022-06-29)
ASCOP2 SuperfamilySaposin8037778 3000601 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyAcid proteases8042471 3001059 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyAcid proteases8042471 3001059 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyAcid proteases8042471 3001059 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyAcid proteases8042471 3001059 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyAcid proteases8042471 3001059 SCOP2B (2022-06-29)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.40.70.10 Mainly Beta Beta Barrel Cathepsin D, subunit A domain 1CATH (4.3.0)
A1.10.225.10 Mainly Alpha Orthogonal Bundle NK-Lysin Saposin-likeCATH (4.3.0)
B2.40.70.10 Mainly Beta Beta Barrel Cathepsin D, subunit A domain 1CATH (4.3.0)
B1.10.225.10 Mainly Alpha Orthogonal Bundle NK-Lysin Saposin-likeCATH (4.3.0)
C2.40.70.10 Mainly Beta Beta Barrel Cathepsin D, subunit A domain 1CATH (4.3.0)
C1.10.225.10 Mainly Alpha Orthogonal Bundle NK-Lysin Saposin-likeCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C
PF05184Saposin-like type B, region 1 (SapB_1)Saposin-like type B, region 1Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease, and pH sta ...Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease, and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity [1,2]. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes [3].
Domain
A, B, C
PF00026Eukaryotic aspartyl protease (Asp)Eukaryotic aspartyl protease- Family
A, B, C
PF03489Saposin-like type B, region 2 (SapB_2)Saposin-like type B, region 2- Family

Membrane Protein Annotation: OPM OPM Database Homepage