Alpha-2-macroglobulin bait region domain; Alpha-2-macroglobulins (A2Ms) are plasma proteins ...
467-610
5.94e-32
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: 121.30 E-value: 5.94e-32
Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments ...
682-750
4.84e-25
Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.
:
Pssm-ID: 237984 Cd Length: 70 Bit Score: 99.07 E-value: 4.84e-25
MG2 domain; This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin in eukaryotes. ...
126-219
3.40e-14
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: 68.88 E-value: 3.40e-14
Alpha-2-macroglobulin bait region domain; Alpha-2-macroglobulins (A2Ms) are plasma proteins ...
467-610
5.94e-32
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: 121.30 E-value: 5.94e-32
Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments ...
682-750
4.84e-25
Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.
Pssm-ID: 237984 Cd Length: 70 Bit Score: 99.07 E-value: 4.84e-25
MG2 domain; This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin in eukaryotes. ...
126-219
3.40e-14
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: 68.88 E-value: 3.40e-14
Anaphylotoxin-like domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated ...
698-732
2.94e-13
Anaphylotoxin-like domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.
Pssm-ID: 460347 Cd Length: 36 Bit Score: 64.22 E-value: 2.94e-13
Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments ...
698-732
4.19e-11
Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.
Pssm-ID: 197517 Cd Length: 35 Bit Score: 58.11 E-value: 4.19e-11
Alpha-2-macroglobulin bait region domain; Alpha-2-macroglobulins (A2Ms) are plasma proteins ...
467-610
5.94e-32
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: 121.30 E-value: 5.94e-32
Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments ...
682-750
4.84e-25
Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.
Pssm-ID: 237984 Cd Length: 70 Bit Score: 99.07 E-value: 4.84e-25
MG2 domain; This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin in eukaryotes. ...
126-219
3.40e-14
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: 68.88 E-value: 3.40e-14
Anaphylotoxin-like domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated ...
698-732
2.94e-13
Anaphylotoxin-like domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.
Pssm-ID: 460347 Cd Length: 36 Bit Score: 64.22 E-value: 2.94e-13
Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments ...
698-732
4.19e-11
Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.
Pssm-ID: 197517 Cd Length: 35 Bit Score: 58.11 E-value: 4.19e-11
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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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