immunoglobulin (Ig)-like domain-containing alpha-2-macroglobulin family protein may be a broad-spectrum protease inhibitor, similar to alpha-2-macroglobulin from Escherichia coli (A2MG, YfhM) and similar proteins from proteobacteria
MG2 domain; This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin in eukaryotes. ...
314-410
9.31e-19
MG2 domain; This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin in eukaryotes. 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.
Pssm-ID: 426464 [Multi-domain] Cd Length: 95 Bit Score: 82.75 E-value: 9.31e-19
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
542-617
1.05e-03
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 39.40 E-value: 1.05e-03
MG2 domain; This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin in eukaryotes. ...
314-410
9.31e-19
MG2 domain; This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin in eukaryotes. 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.
Pssm-ID: 426464 [Multi-domain] Cd Length: 95 Bit Score: 82.75 E-value: 9.31e-19
Alpha-2-macroglobulin bait region domain; Alpha-2-macroglobulins (A2Ms) are plasma proteins ...
630-776
3.25e-17
Alpha-2-macroglobulin bait region domain; 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. 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 recognized as the Venus flytrap mechanism.
Pssm-ID: 462235 [Multi-domain] Cd Length: 139 Bit Score: 79.70 E-value: 3.25e-17
Bacterial Alpha-2-macroglobulin MG10 domain; Alpha-2-macroglobulins (A2Ms) are plasma proteins ...
1352-1487
7.77e-04
Bacterial Alpha-2-macroglobulin MG10 domain; 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. Bacterial A2Ms are located in the periplasm where they are believed to provide protection to the cell by trapping external proteases through a covalent interaction with an activated thioester. This domain is found on the C-terminal region in A2Ms in bacteria. Structure analysis of Salmonella enterica ser A2Ms (SA-A2Ms) show that they are composed of 13 domains, all of which fold as variants of beta sandwiches with the exception of the TED, which consists of 14 alpha helices. Most of the beta sandwich domains appear to serve a structural role and are referred to as the macroglobulin-like (MG) domains. This is the MG10 domain. MG10 is markedly different from the other MG domains in that it has more beta strands and an alpha helix. The position of MG10 is stabilized by, in addition to other hydrogen bonds, the formation of a beta sheet with MG9.
Pssm-ID: 465598 Cd Length: 128 Bit Score: 41.13 E-value: 7.77e-04
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
542-617
1.05e-03
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.
Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 39.40 E-value: 1.05e-03
Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier ...
1027-1124
3.06e-03
Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier protein in serum. It is a broadly specific proteinase inhibitor. The structural thioester of alpha (2)-M, is involved in the immobilization and entrapment of proteases. This group contains another broadly specific proteinase inhibitor: pregnancy zone protein (PZP). PZP is a trace protein in the plasma of non-pregnant females and males which is elevated in pregnancy. Alpha (2)-M and PZ bind to placental protein-14 and may modulate its activity in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system. This group also contains C3, C4 and C5 of vertebrate complement. The vertebrate complement is an effector of both the acquired and innate immune systems The point of convergence of the classical, alternative and lectin pathways of the complement system is the proteolytic activation of C3. C4 plays a key role in propagating the classical and lectin pathways. C5 participates in the classical and alternative pathways. The thioester bond located within the structure of C3 and C4 is central to the function of complement. C5 does not contain an active thioester bond.
Pssm-ID: 239221 [Multi-domain] Cd Length: 282 Bit Score: 41.22 E-value: 3.06e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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