Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BPP-bindinge5czdB1 A: alpha bundlesX: ACP-likeH: Acyl-carrier protein (ACP) (From Topology)T: Acyl-carrier protein (ACP)F: PP-bindingECOD (1.6)
AEUF08355e5czdA2 A: a+b two layersX: Alpha-beta plaitsH: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)T: Probable ACP-binding domain of malonyl-CoA ACP transacylaseF: EUF08355ECOD (1.6)
AAcyl_transf_1_1ste5czdA1 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: FabD/lysophospholipase-likeF: Acyl_transf_1_1stECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B1.10.1200.10 Mainly Alpha Orthogonal Bundle Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein Chain ACATH (4.3.0)
A3.40.366.10 Alpha Beta 3-Layer(aba) Sandwich Malonyl-Coenzyme A Acyl Carrier Protein domain 2CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00550Phosphopantetheine attachment site (PP-binding)Phosphopantetheine attachment siteA 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes memb ...A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Domain
PF21124VinK acyltransferase small domain (VinK_C)VinK acyltransferase small domainThis family includes the VinK acyltransferase. VinK transfers a dipeptide group between two ACPs, VinL and VinP1LdACP, in vicenistatin biosynthesis [1]. This entry represents the small C-terminal domain [1]. VinK has two conserved catalytic residues, ...This family includes the VinK acyltransferase. VinK transfers a dipeptide group between two ACPs, VinL and VinP1LdACP, in vicenistatin biosynthesis [1]. This entry represents the small C-terminal domain [1]. VinK has two conserved catalytic residues, Ser-106 and His-216, at the interface between the large domain and small domain [1].
Domain