Sequence similarity between netrin UNC-6 and C345C complement protein family members, and hence the existence of the UNC-6 module, was first reported in [1]. Subsequently, many additional members of the family were identified on the basis of sequence ...
Sequence similarity between netrin UNC-6 and C345C complement protein family members, and hence the existence of the UNC-6 module, was first reported in [1]. Subsequently, many additional members of the family were identified on the basis of sequence similarity between the C-terminal domains of netrins, complement proteins C3, C4, C5, secreted frizzled-related proteins, and type I pro-collagen C-proteinase enhancer proteins (PCOLCEs), which are homologous with the N-terminal domains of tissue inhibitors of metalloproteinases (TIMPs). The TIMPs are classified as a separate family in Pfam (Pfam:PF00965) [2]. This expanded domain family has been named as the NTR module [2].
This entry represents the first segment of the CUB domain from complement component C3, which is completed but a second segment represented in Pfam:PF21308. The CUB domain is interrupted by the TE domain. The CUB domain forms a massive, tightly packe ...
This entry represents the first segment of the CUB domain from complement component C3, which is completed but a second segment represented in Pfam:PF21308. The CUB domain is interrupted by the TE domain. The CUB domain forms a massive, tightly packed super domain with the TE and MG8 domains [1-5]. These entry also includes venom factors, also known as Complement C3 homologues. These are complement-activating proteins with structural and functional similarities to complement component C3b, the activated form of C3 [6].
Complement component 3, CUB domain, second segment
Complement C3 is major component in the both the classical and alternative complement activation pathways. C3 is cleaved into two chains (alpha and beta) by C3 convertases. This entry represents the second segment of the CUB domain, which is complete ...
Complement C3 is major component in the both the classical and alternative complement activation pathways. C3 is cleaved into two chains (alpha and beta) by C3 convertases. This entry represents the second segment of the CUB domain, which is completed by Pfam:PF21406 [2]. The CUB domain is interrupted by the TE domain. The CUB, TE and MG8 domains form a massive, tightly packed super domain. This entry also includes venom factors, also known as Complement C3 homologues. These are complement-activating proteins with structural and functional similarities to complement component C3b, the activated form of C3 [6].
This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin in eukaryotes [1]. Alpha-2-macroglobulins (A2Ms) are plasma proteins that trap and inhibit a broad range of proteases and are major components of the eukaryotic innate immune system. How ...
This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin in eukaryotes [1]. Alpha-2-macroglobulins (A2Ms) are plasma proteins that trap and inhibit a broad range of proteases and are major components of the eukaryotic innate immune system. However, A2M-like proteins were identified in pathogenically invasive bacteria and species that colonize higher eukaryotes. This domain is found in eukaryotic and bacterial proteins. In human A2Ms, this domain is termed macroglobulin-like (MG) domain 2 and in Salmonella enterica ser A2Ms, this is domain 4 [2] [3].
Alpha-2-macroglobulins (A2Ms) are plasma proteins that trap and inhibit a broad range of proteases and are major components of the eukaryotic innate immune system. However, A2M-like proteins were identified in pathogenically invasive bacteria and spe ...
Alpha-2-macroglobulins (A2Ms) are plasma proteins that trap and inhibit a broad range of proteases and are major components of the eukaryotic innate immune system. However, A2M-like proteins were identified in pathogenically invasive bacteria and species that colonize higher eukaryotes. This domain is found in eukaryotic and bacterial proteins. In human A2Ms, this domain encompasses macroglobulin-like domain MG5 and 6 including bait region. In Salmonella enterica ser A2Ms, this domain encompasses MG7 and MG8 including the bait region [1] [2]. The Bait region is cleaved by proteases, followed by a large conformational change that blocks the target protease within a cage-like complex. This model of protease entrapment is recognised as the Venus flytrap mechanism [1].
This domain is found at the C-terminal end of human Properdin (CFP, for Complement factor P) and similar animal proteins. CFP is a positive regulator of the alternate pathway (AP) of complement. It contains six thrombospondin repeat type I (TSP 1-6 d ...
This domain is found at the C-terminal end of human Properdin (CFP, for Complement factor P) and similar animal proteins. CFP is a positive regulator of the alternate pathway (AP) of complement. It contains six thrombospondin repeat type I (TSP 1-6 domains and an N-terminal domain (Pfam:PF18487). This entry represents the last TSP type I domain, which binds to the first TSP type I domain (Pfam:PF00090), contributing to multimerisation [1-5].
