MULTISPECIES: alpha2-macroglobulin [Enterobacteriaceae]
Protein Classification
alpha-2-macroglobulin family protein( domain architecture ID 11457182)
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
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||||||||||||||||
| YfaS | COG2373 | Uncharacterized conserved protein YfaS, alpha-2-macroglobulin family [General function ... |
61-1652 | 0e+00 | ||||||||||||||||||||||
Uncharacterized conserved protein YfaS, alpha-2-macroglobulin family [General function prediction only]; : Pssm-ID: 441940 [Multi-domain] Cd Length: 1605 Bit Score: 1466.46 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||||||||||||||||
| YfaS | COG2373 | Uncharacterized conserved protein YfaS, alpha-2-macroglobulin family [General function ... |
61-1652 | 0e+00 | ||||||||||||||||||||||
Uncharacterized conserved protein YfaS, alpha-2-macroglobulin family [General function prediction only]; Pssm-ID: 441940 [Multi-domain] Cd Length: 1605 Bit Score: 1466.46 E-value: 0e+00
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| bMG1 | pfam17970 | Bacterial Alpha-2-macroglobulin MG1 domain; Alpha-2-macroglobulins (A2Ms) are plasma proteins ... |
59-163 | 2.30e-62 | ||||||||||||||||||||||
Bacterial Alpha-2-macroglobulin MG1 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 N-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 MG1 domain which is the farthest from the body of the structure. It is normally anchored to the inner membrane in vivo and connected to MG2 by a flexible linker. Pssm-ID: 465597 Cd Length: 105 Bit Score: 207.55 E-value: 2.30e-62
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| A2M_like | cd02891 | Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier ... |
1173-1436 | 1.43e-50 | ||||||||||||||||||||||
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: 180.66 E-value: 1.43e-50
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| Name | Accession | Description | Interval | E-value | ||||||||||||||||||||||
| YfaS | COG2373 | Uncharacterized conserved protein YfaS, alpha-2-macroglobulin family [General function ... |
61-1652 | 0e+00 | ||||||||||||||||||||||
Uncharacterized conserved protein YfaS, alpha-2-macroglobulin family [General function prediction only]; Pssm-ID: 441940 [Multi-domain] Cd Length: 1605 Bit Score: 1466.46 E-value: 0e+00
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| bMG1 | pfam17970 | Bacterial Alpha-2-macroglobulin MG1 domain; Alpha-2-macroglobulins (A2Ms) are plasma proteins ... |
59-163 | 2.30e-62 | ||||||||||||||||||||||
Bacterial Alpha-2-macroglobulin MG1 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 N-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 MG1 domain which is the farthest from the body of the structure. It is normally anchored to the inner membrane in vivo and connected to MG2 by a flexible linker. Pssm-ID: 465597 Cd Length: 105 Bit Score: 207.55 E-value: 2.30e-62
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| bMG5 | pfam17972 | Bacterial Alpha-2-macroglobulin MG5 domain; Alpha-2-macroglobulins (A2Ms) are plasma proteins ... |
485-610 | 9.55e-53 | ||||||||||||||||||||||
Bacterial Alpha-2-macroglobulin MG5 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 N-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 MG5 domain. Pssm-ID: 436183 Cd Length: 127 Bit Score: 181.17 E-value: 9.55e-53
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| A2M_like | cd02891 | Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier ... |
1173-1436 | 1.43e-50 | ||||||||||||||||||||||
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: 180.66 E-value: 1.43e-50
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| bMG6 | pfam17962 | Bacterial macroglobulin domain 6; This macroglobulin domain is found in bacterial alpha 2 ... |
616-741 | 3.21e-33 | ||||||||||||||||||||||
Bacterial macroglobulin domain 6; This macroglobulin domain is found in bacterial alpha 2 macroglobulin proteins. It adopts an Ig-like beta sandwich fold. Pssm-ID: 436175 Cd Length: 112 Bit Score: 124.67 E-value: 3.21e-33
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| bMG10 | pfam17973 | Bacterial Alpha-2-macroglobulin MG10 domain; Alpha-2-macroglobulins (A2Ms) are plasma proteins ... |
1505-1638 | 2.54e-25 | ||||||||||||||||||||||
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: 102.76 E-value: 2.54e-25
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| bMG3 | pfam11974 | Bacterial alpha-2-macroglobulin MG3 domain; This is the MG3 domain from bacterial ... |
289-383 | 3.61e-24 | ||||||||||||||||||||||
Bacterial alpha-2-macroglobulin MG3 domain; This is the MG3 domain from bacterial alpha2-macroglobulins. Pssm-ID: 432232 [Multi-domain] Cd Length: 102 Bit Score: 98.44 E-value: 3.61e-24
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| MG2 | pfam01835 | MG2 domain; This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin in eukaryotes. ... |
388-481 | 1.32e-22 | ||||||||||||||||||||||
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: 93.53 E-value: 1.32e-22
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| ISOPREN_C2_like | cd00688 | This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
1173-1434 | 1.91e-21 | ||||||||||||||||||||||
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two broadly specific proteinase inhibitors alpha2-macroglobulin (alpha (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and C5 components of vertebrate complement. Class II terpene cyclases include squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY), these integral membrane proteins catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. The protein prenyltransferases include protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II) which catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Alpha (2)-M is a major carrier protein in serum and involved in the immobilization and entrapment of proteases. PZP is a pregnancy associated protein. Alpha (2)-M and PZP are known to bind to and, may modulate, the activity of placental protein-14 in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system. Pssm-ID: 238362 [Multi-domain] Cd Length: 300 Bit Score: 96.85 E-value: 1.91e-21
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| A2M_BRD | pfam07703 | Alpha-2-macroglobulin bait region domain; Alpha-2-macroglobulins (A2Ms) are plasma proteins ... |
758-906 | 3.96e-15 | ||||||||||||||||||||||
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: 73.92 E-value: 3.96e-15
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| A2M | pfam00207 | Alpha-2-macroglobulin family; This family includes the C-terminal region of the ... |
974-1057 | 6.00e-06 | ||||||||||||||||||||||
Alpha-2-macroglobulin family; This family includes the C-terminal region of the alpha-2-macroglobulin family. Pssm-ID: 459711 [Multi-domain] Cd Length: 91 Bit Score: 46.04 E-value: 6.00e-06
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| COG1470 | COG1470 | Uncharacterized membrane protein [Function unknown]; |
1016-1143 | 1.13e-04 | ||||||||||||||||||||||
Uncharacterized membrane protein [Function unknown]; Pssm-ID: 441079 [Multi-domain] Cd Length: 475 Bit Score: 46.78 E-value: 1.13e-04
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| complement_C3_C4_C5 | cd02896 | Proteins similar to C3, C4 and C5 of vertebrate complement. The vertebrate complement system, ... |
1177-1258 | 2.55e-04 | ||||||||||||||||||||||
Proteins similar to C3, C4 and C5 of vertebrate complement. The vertebrate complement system, comprised of a large number of distinct plasma proteins, 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: 239226 [Multi-domain] Cd Length: 297 Bit Score: 44.96 E-value: 2.55e-04
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| TED_complement | pfam07678 | A-macroglobulin TED domain; This entry corresponds to the TED domain of the complement ... |
1184-1276 | 3.92e-04 | ||||||||||||||||||||||
A-macroglobulin TED domain; This entry corresponds to the TED domain of the complement components such as C3, C4 and C5. This domain contains a short highly conserved region of proteinase-binding alpha-macro-globulins contains the cysteine and a glutamine of a thiol-ester bond that is cleaved at the moment of proteinase binding, and mediates the covalent binding of the alpha-macro-globulin to the proteinase. The GCGEQ motif is highly conserved. Pssm-ID: 462227 [Multi-domain] Cd Length: 311 Bit Score: 44.60 E-value: 3.92e-04
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| A2M_2 | cd02897 | Proteins similar to alpha2-macroglobulin (alpha (2)-M). This group also contains the pregnancy ... |
1184-1264 | 3.05e-03 | ||||||||||||||||||||||
Proteins similar to alpha2-macroglobulin (alpha (2)-M). This group also contains the pregnancy zone protein (PZP). Alpha(2)-M and PZP are broadly specific proteinase inhibitors. Alpha (2)-M is a major carrier protein in serum. The structural thioester of alpha (2)-M, is involved in the immobilization and entrapment of proteases. 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 contributing to fetal survival. It has been suggested that thioester bond cleavage promotes the binding of PZ and alpha (2)-M to the CD91 receptor clearing them from circulation. Pssm-ID: 239227 Cd Length: 292 Bit Score: 41.41 E-value: 3.05e-03
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