Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins ...
1433-1570
1.68e-52
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobulin-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD), which provides invasins with the specificity to bind to its host target molecules. InvE-AD adopts a C-type lectin-like domain (CTLD)fold with unique modifications. The core structure of the adhesion domain (AD) is made up of a globular alpha/beta fold and can be divided into three sub-sections. The first is a lasso-shaped loop structure termed the "adaptor ring" since it forms a ring-shaped platform that connects BIg21 pfam05688 with the two residual sub-sections in the AD. These two residual subsections are the "C-type lectin-like domain" and the "wedge module". InvE-CTLD lacks the ability to coordinate Ca2+, and motifs such as EPN, QPD, and WND that are responsible for the specificity of carbohydrate recognition are also absent, giving rise to the notion that the InvE-CTLD is not a carbohydrate binding domain.
Pssm-ID: 428588 [Multi-domain] Cd Length: 135 Bit Score: 180.61 E-value: 1.68e-52
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins ...
1433-1570
1.68e-52
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobulin-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD), which provides invasins with the specificity to bind to its host target molecules. InvE-AD adopts a C-type lectin-like domain (CTLD)fold with unique modifications. The core structure of the adhesion domain (AD) is made up of a globular alpha/beta fold and can be divided into three sub-sections. The first is a lasso-shaped loop structure termed the "adaptor ring" since it forms a ring-shaped platform that connects BIg21 pfam05688 with the two residual sub-sections in the AD. These two residual subsections are the "C-type lectin-like domain" and the "wedge module". InvE-CTLD lacks the ability to coordinate Ca2+, and motifs such as EPN, QPD, and WND that are responsible for the specificity of carbohydrate recognition are also absent, giving rise to the notion that the InvE-CTLD is not a carbohydrate binding domain.
Pssm-ID: 428588 [Multi-domain] Cd Length: 135 Bit Score: 180.61 E-value: 1.68e-52
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins ...
862-993
7.02e-45
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobulin-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD), which provides invasins with the specificity to bind to its host target molecules. InvE-AD adopts a C-type lectin-like domain (CTLD)fold with unique modifications. The core structure of the adhesion domain (AD) is made up of a globular alpha/beta fold and can be divided into three sub-sections. The first is a lasso-shaped loop structure termed the "adaptor ring" since it forms a ring-shaped platform that connects BIg21 pfam05688 with the two residual sub-sections in the AD. These two residual subsections are the "C-type lectin-like domain" and the "wedge module". InvE-CTLD lacks the ability to coordinate Ca2+, and motifs such as EPN, QPD, and WND that are responsible for the specificity of carbohydrate recognition are also absent, giving rise to the notion that the InvE-CTLD is not a carbohydrate binding domain.
Pssm-ID: 428588 [Multi-domain] Cd Length: 135 Bit Score: 159.04 E-value: 7.02e-45
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins ...
1143-1286
8.98e-44
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobulin-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD), which provides invasins with the specificity to bind to its host target molecules. InvE-AD adopts a C-type lectin-like domain (CTLD)fold with unique modifications. The core structure of the adhesion domain (AD) is made up of a globular alpha/beta fold and can be divided into three sub-sections. The first is a lasso-shaped loop structure termed the "adaptor ring" since it forms a ring-shaped platform that connects BIg21 pfam05688 with the two residual sub-sections in the AD. These two residual subsections are the "C-type lectin-like domain" and the "wedge module". InvE-CTLD lacks the ability to coordinate Ca2+, and motifs such as EPN, QPD, and WND that are responsible for the specificity of carbohydrate recognition are also absent, giving rise to the notion that the InvE-CTLD is not a carbohydrate binding domain.
Pssm-ID: 428588 [Multi-domain] Cd Length: 135 Bit Score: 155.96 E-value: 8.98e-44
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins ...
597-722
3.82e-42
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobulin-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD), which provides invasins with the specificity to bind to its host target molecules. InvE-AD adopts a C-type lectin-like domain (CTLD)fold with unique modifications. The core structure of the adhesion domain (AD) is made up of a globular alpha/beta fold and can be divided into three sub-sections. The first is a lasso-shaped loop structure termed the "adaptor ring" since it forms a ring-shaped platform that connects BIg21 pfam05688 with the two residual sub-sections in the AD. These two residual subsections are the "C-type lectin-like domain" and the "wedge module". InvE-CTLD lacks the ability to coordinate Ca2+, and motifs such as EPN, QPD, and WND that are responsible for the specificity of carbohydrate recognition are also absent, giving rise to the notion that the InvE-CTLD is not a carbohydrate binding domain.
Pssm-ID: 428588 [Multi-domain] Cd Length: 135 Bit Score: 151.34 E-value: 3.82e-42
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins ...
330-460
3.14e-38
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobulin-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD), which provides invasins with the specificity to bind to its host target molecules. InvE-AD adopts a C-type lectin-like domain (CTLD)fold with unique modifications. The core structure of the adhesion domain (AD) is made up of a globular alpha/beta fold and can be divided into three sub-sections. The first is a lasso-shaped loop structure termed the "adaptor ring" since it forms a ring-shaped platform that connects BIg21 pfam05688 with the two residual sub-sections in the AD. These two residual subsections are the "C-type lectin-like domain" and the "wedge module". InvE-CTLD lacks the ability to coordinate Ca2+, and motifs such as EPN, QPD, and WND that are responsible for the specificity of carbohydrate recognition are also absent, giving rise to the notion that the InvE-CTLD is not a carbohydrate binding domain.
Pssm-ID: 428588 [Multi-domain] Cd Length: 135 Bit Score: 140.17 E-value: 3.14e-38
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) ...
224-327
1.38e-35
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) found in InvasinE (InvE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobuli-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD) pfam05689, which provides invasins with the specificity to bind to its host target molecules. The overall structure of InvE shows that it comprises of three domain architecture in which the domains BIg20 (Bacterial Immunoglobulin-like 20) and BIg21 adopt two layer beta-sandwich fold resembling eukaryotic members of Immunoglobulin-superfamily (IgSF), while the AD is a globular, alpha/beta-domain. The structure of BIg21 belongs to the I2 set of IgSF with a unique modification in the C-E interstrand loop, important for its interaction with AD. BIg21 and AD form a functional super-domain as well, necessary to target the host receptor.
Pssm-ID: 428587 [Multi-domain] Cd Length: 108 Bit Score: 131.24 E-value: 1.38e-35
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) ...
1027-1140
3.41e-33
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) found in InvasinE (InvE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobuli-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD) pfam05689, which provides invasins with the specificity to bind to its host target molecules. The overall structure of InvE shows that it comprises of three domain architecture in which the domains BIg20 (Bacterial Immunoglobulin-like 20) and BIg21 adopt two layer beta-sandwich fold resembling eukaryotic members of Immunoglobulin-superfamily (IgSF), while the AD is a globular, alpha/beta-domain. The structure of BIg21 belongs to the I2 set of IgSF with a unique modification in the C-E interstrand loop, important for its interaction with AD. BIg21 and AD form a functional super-domain as well, necessary to target the host receptor.
Pssm-ID: 428587 [Multi-domain] Cd Length: 108 Bit Score: 124.69 E-value: 3.41e-33
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins ...
1730-1864
4.40e-32
Adhesion domain; This entry represents the Adhesion domain found in InvasinE (invE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobulin-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD), which provides invasins with the specificity to bind to its host target molecules. InvE-AD adopts a C-type lectin-like domain (CTLD)fold with unique modifications. The core structure of the adhesion domain (AD) is made up of a globular alpha/beta fold and can be divided into three sub-sections. The first is a lasso-shaped loop structure termed the "adaptor ring" since it forms a ring-shaped platform that connects BIg21 pfam05688 with the two residual sub-sections in the AD. These two residual subsections are the "C-type lectin-like domain" and the "wedge module". InvE-CTLD lacks the ability to coordinate Ca2+, and motifs such as EPN, QPD, and WND that are responsible for the specificity of carbohydrate recognition are also absent, giving rise to the notion that the InvE-CTLD is not a carbohydrate binding domain.
Pssm-ID: 428588 [Multi-domain] Cd Length: 135 Bit Score: 122.45 E-value: 4.40e-32
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) ...
1317-1430
3.14e-29
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) found in InvasinE (InvE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobuli-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD) pfam05689, which provides invasins with the specificity to bind to its host target molecules. The overall structure of InvE shows that it comprises of three domain architecture in which the domains BIg20 (Bacterial Immunoglobulin-like 20) and BIg21 adopt two layer beta-sandwich fold resembling eukaryotic members of Immunoglobulin-superfamily (IgSF), while the AD is a globular, alpha/beta-domain. The structure of BIg21 belongs to the I2 set of IgSF with a unique modification in the C-E interstrand loop, important for its interaction with AD. BIg21 and AD form a functional super-domain as well, necessary to target the host receptor.
Pssm-ID: 428587 [Multi-domain] Cd Length: 108 Bit Score: 113.14 E-value: 3.14e-29
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) ...
1598-1726
5.72e-28
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) found in InvasinE (InvE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobuli-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD) pfam05689, which provides invasins with the specificity to bind to its host target molecules. The overall structure of InvE shows that it comprises of three domain architecture in which the domains BIg20 (Bacterial Immunoglobulin-like 20) and BIg21 adopt two layer beta-sandwich fold resembling eukaryotic members of Immunoglobulin-superfamily (IgSF), while the AD is a globular, alpha/beta-domain. The structure of BIg21 belongs to the I2 set of IgSF with a unique modification in the C-E interstrand loop, important for its interaction with AD. BIg21 and AD form a functional super-domain as well, necessary to target the host receptor.
Pssm-ID: 428587 [Multi-domain] Cd Length: 108 Bit Score: 109.67 E-value: 5.72e-28
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) ...
484-594
5.23e-26
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) found in InvasinE (InvE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobuli-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD) pfam05689, which provides invasins with the specificity to bind to its host target molecules. The overall structure of InvE shows that it comprises of three domain architecture in which the domains BIg20 (Bacterial Immunoglobulin-like 20) and BIg21 adopt two layer beta-sandwich fold resembling eukaryotic members of Immunoglobulin-superfamily (IgSF), while the AD is a globular, alpha/beta-domain. The structure of BIg21 belongs to the I2 set of IgSF with a unique modification in the C-E interstrand loop, important for its interaction with AD. BIg21 and AD form a functional super-domain as well, necessary to target the host receptor.
Pssm-ID: 428587 [Multi-domain] Cd Length: 108 Bit Score: 103.89 E-value: 5.23e-26
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) ...
750-859
1.14e-24
Bacterial Immunoglobulin-like 21; This entry represents BIg21(Bacterial Immunoglobulin-like 21) found in InvasinE (InvE). Invasins are members of the inverse autotransporter (IAT) family also referred to as type Ve secretion system. In general, they consist of an N-terminal beta-barrel-like domain, which is responsible for attachment of invasin to the outer membrane region of bacteria, repetitive Immunoglobuli-like (Ig) domains, which vary significantly in number among all the invasins, and the C-terminal domain/adhesion domain (AD) pfam05689, which provides invasins with the specificity to bind to its host target molecules. The overall structure of InvE shows that it comprises of three domain architecture in which the domains BIg20 (Bacterial Immunoglobulin-like 20) and BIg21 adopt two layer beta-sandwich fold resembling eukaryotic members of Immunoglobulin-superfamily (IgSF), while the AD is a globular, alpha/beta-domain. The structure of BIg21 belongs to the I2 set of IgSF with a unique modification in the C-E interstrand loop, important for its interaction with AD. BIg21 and AD form a functional super-domain as well, necessary to target the host receptor.
Pssm-ID: 428587 [Multi-domain] Cd Length: 108 Bit Score: 100.04 E-value: 1.14e-24
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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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.
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(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.
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