Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AAAA_32_3rde4fwhA3 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: AAA_32_3rdECOD (1.6)
ALon_C_Ne4fwhA6 A: a+b two layersX: Ribosomal protein S5 domain 2-like (From Topology)H: Ribosomal protein S5 domain 2-like (From Topology)T: Ribosomal protein S5 domain 2-likeF: Lon_C_NECOD (1.6)
AAAA_32_1ste4fwhA2 A: a+b two layersX: Lon-like protease MtaLonC helical domain (From Topology)H: Lon-like protease MtaLonC helical domain (From Topology)T: Lon-like protease MtaLonC helical domainF: AAA_32_1stECOD (1.6)
AAAA_32_2nde4fwhA4 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: AAA_32_2ndECOD (1.6)
ALon_C_C_1e4fwhA5 A: a/b three-layered sandwichesX: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)H: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)T: C-terminal subdomain in Lon-related proteases catalytic domainsF: Lon_C_C_1ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A1.10.8.60 Mainly Alpha Orthogonal Bundle Helicase, Ruva Protein domain 3CATH (4.3.0)
A3.30.230.10 Alpha Beta 2-Layer Sandwich Ribosomal Protein S5 domain 2CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF05362Lon protease (S16) C-terminal proteolytic domain (Lon_C)Lon protease (S16) C-terminal proteolytic domainThe Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activit ...The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.
Domain
PF13654LonB-like, AAA domain (AAA_32)LonB-like, AAA domainThis entry includes a wide variety of AAA domains, including some that have lost essential nucleotide binding residues in the P-loop. This domain is found in Lon proteases from archaea and bacteria [1].Domain
PF20436Archaeal LonB, AAA+ ATPase LID domain (LonB_AAA-LID)Archaeal LonB, AAA+ ATPase LID domainThe species-specific Lon-insertion domain (LID) is characteristic of Lon proteases (also known as endopeptidase La) and is fused to the AAA+ module [1]. Bacterial and eukaryotic Lons (LonA) have a LID at the N-terminal of AAA+ module; in archaeal Lon ...The species-specific Lon-insertion domain (LID) is characteristic of Lon proteases (also known as endopeptidase La) and is fused to the AAA+ module [1]. Bacterial and eukaryotic Lons (LonA) have a LID at the N-terminal of AAA+ module; in archaeal Lons (LonB) the LID, represented in this entry, is inserted within the AAA+ module in a series of transmembrane segments known as the membrane-anchoring region (MA). In the Lon-like protease LonC, which does not have ATPase activity, the LID is also within the AAA-like module similar to LonBs; in this case, it is predicted to contain coiled-coil regions rather than transmembrane segments [1].
Domain