Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyCell wall binding repeat8036367 3000365 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF19127e4x36A2 A: beta duplicates or obligate multimersX: beta-hairpin stack (From Topology)H: beta-hairpin stack (From Topology)T: beta-hairpin stackF: PF19127ECOD (1.6)
APF01510e4x36A3 A: a+b three layersX: N-acetylmuramoyl-L-alanine amidase-like (From Topology)H: N-acetylmuramoyl-L-alanine amidase-like (From Topology)T: N-acetylmuramoyl-L-alanine amidase-likeF: PF01510ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.80.10 Alpha Beta 3-Layer(aba) Sandwich Lysozyme-like Peptidoglycan recognition protein-likeCATH (4.3.0)
A2.10.270.10 Mainly Beta Ribbon left handed beta-beta-3-solenoid Cholin BindingCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF01473Putative cell wall binding repeat (Choline_bind_1)Putative cell wall binding repeat- Repeat
PF19127Choline-binding repeat (Choline_bind_3)Choline-binding repeat- Repeat
PF01510N-acetylmuramoyl-L-alanine amidase (Amidase_2)N-acetylmuramoyl-L-alanine amidaseThis family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The ...This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Autolysin