acidic terminal segments, variant surface antigen of PfEMP1; ATS is the intracellular and ...
2593-3078
0e+00
acidic terminal segments, variant surface antigen of PfEMP1; ATS is the intracellular and relatively conserved acidic terminal segment of the Plasmodium falciparum erythrocyte membrane protein-1 (PfEMP1). this domain appears to be present in all variants of the highly polymorphic PfEMP1 proteins.
:
Pssm-ID: 373851 [Multi-domain] Cd Length: 446 Bit Score: 794.78 E-value: 0e+00
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ...
122-307
1.43e-87
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium vivax and Plasmodium knowlesi merozoites invade human erythrocytes that express Duffy blood group surface determinants. The Duffy receptor family is localized in micronemes, an organelle found in all organizms of the phylum Apicomplexa. This family is closely associated on PfEMP1 proteins with PFEMP, pfam03011.
:
Pssm-ID: 428465 [Multi-domain] Cd Length: 178 Bit Score: 283.78 E-value: 1.43e-87
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ...
2329-2464
4.26e-36
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been identified as the rosetting ligand of the malaria parasite P. falciparum. Rosetting is the adhesion of infected erythrocytes with uninfected erythrocytes in the vasculature of the infected organ, and is associated with severe malaria. PfEMP1 interacts with Complement Receptor One on uninfected erythrocytes to form rosettes. The extreme variation within these proteins and the grouping of var genes implies that var gene recombination preferentially occurs within var gene groups. These groups reflect a functional diversification that has evolved to cope with the varying conditions of transmission and host immune response met by the parasite. A recombination hotspot was uncovered between Duffy-binding-like (DBL) subdomains. Solution of the crystal structure of the N-terminal and first DBL region of PfEMP1 from the VarO variant of the PfEMP1 protein is found to be directly implicated in rosetting as the heparin-binding site.
:
Pssm-ID: 281064 Cd Length: 154 Bit Score: 135.32 E-value: 4.26e-36
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ...
1788-1985
1.94e-35
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium vivax and Plasmodium knowlesi merozoites invade human erythrocytes that express Duffy blood group surface determinants. The Duffy receptor family is localized in micronemes, an organelle found in all organizms of the phylum Apicomplexa. This family is closely associated on PfEMP1 proteins with PFEMP, pfam03011.
:
Pssm-ID: 428465 [Multi-domain] Cd Length: 178 Bit Score: 134.32 E-value: 1.94e-35
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ...
654-821
3.62e-30
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been identified as the rosetting ligand of the malaria parasite P. falciparum. Rosetting is the adhesion of infected erythrocytes with uninfected erythrocytes in the vasculature of the infected organ, and is associated with severe malaria. PfEMP1 interacts with Complement Receptor One on uninfected erythrocytes to form rosettes. The extreme variation within these proteins and the grouping of var genes implies that var gene recombination preferentially occurs within var gene groups. These groups reflect a functional diversification that has evolved to cope with the varying conditions of transmission and host immune response met by the parasite. A recombination hotspot was uncovered between Duffy-binding-like (DBL) subdomains. Solution of the crystal structure of the N-terminal and first DBL region of PfEMP1 from the VarO variant of the PfEMP1 protein is found to be directly implicated in rosetting as the heparin-binding site.
The actual alignment was detected with superfamily member pfam03011:
Pssm-ID: 281064 Cd Length: 154 Bit Score: 118.37 E-value: 3.62e-30
Cysteine-Rich Interdomain Region 1 gamma; Rosetting is the capacity of infected RBCs to bind ...
2260-2313
6.78e-15
Cysteine-Rich Interdomain Region 1 gamma; Rosetting is the capacity of infected RBCs to bind uninfected RBCs, which is consistently associated with severe malaria in African children. The rosette-forming PfEMP1 adhesins, namely IT4/R29, Palo Alto 89F5 VarO, 3D7/PF13_0003 and IT4/var60, belong to a specific sub-group called groupA/UpsA var genes and all four present a specific Duffy Binding-Like and and Cysteine-Rich Interdomain Region (DBL1alpha1-CIDR1gamma) double domain Head region found at the extracellular region of PfEMP1. This entry represents the CIDR1gamma domain which increases the binding affinity to VarO (Palo Alto VarO parasites).
:
Pssm-ID: 408346 Cd Length: 52 Bit Score: 71.15 E-value: 6.78e-15
acidic terminal segments, variant surface antigen of PfEMP1; ATS is the intracellular and ...
2593-3078
0e+00
acidic terminal segments, variant surface antigen of PfEMP1; ATS is the intracellular and relatively conserved acidic terminal segment of the Plasmodium falciparum erythrocyte membrane protein-1 (PfEMP1). this domain appears to be present in all variants of the highly polymorphic PfEMP1 proteins.
Pssm-ID: 373851 [Multi-domain] Cd Length: 446 Bit Score: 794.78 E-value: 0e+00
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ...
122-307
1.43e-87
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium vivax and Plasmodium knowlesi merozoites invade human erythrocytes that express Duffy blood group surface determinants. The Duffy receptor family is localized in micronemes, an organelle found in all organizms of the phylum Apicomplexa. This family is closely associated on PfEMP1 proteins with PFEMP, pfam03011.
Pssm-ID: 428465 [Multi-domain] Cd Length: 178 Bit Score: 283.78 E-value: 1.43e-87
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ...
1388-1569
3.33e-47
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium vivax and Plasmodium knowlesi merozoites invade human erythrocytes that express Duffy blood group surface determinants. The Duffy receptor family is localized in micronemes, an organelle found in all organizms of the phylum Apicomplexa. This family is closely associated on PfEMP1 proteins with PFEMP, pfam03011.
Pssm-ID: 428465 [Multi-domain] Cd Length: 178 Bit Score: 167.84 E-value: 3.33e-47
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ...
2329-2464
4.26e-36
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been identified as the rosetting ligand of the malaria parasite P. falciparum. Rosetting is the adhesion of infected erythrocytes with uninfected erythrocytes in the vasculature of the infected organ, and is associated with severe malaria. PfEMP1 interacts with Complement Receptor One on uninfected erythrocytes to form rosettes. The extreme variation within these proteins and the grouping of var genes implies that var gene recombination preferentially occurs within var gene groups. These groups reflect a functional diversification that has evolved to cope with the varying conditions of transmission and host immune response met by the parasite. A recombination hotspot was uncovered between Duffy-binding-like (DBL) subdomains. Solution of the crystal structure of the N-terminal and first DBL region of PfEMP1 from the VarO variant of the PfEMP1 protein is found to be directly implicated in rosetting as the heparin-binding site.
Pssm-ID: 281064 Cd Length: 154 Bit Score: 135.32 E-value: 4.26e-36
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ...
1788-1985
1.94e-35
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium vivax and Plasmodium knowlesi merozoites invade human erythrocytes that express Duffy blood group surface determinants. The Duffy receptor family is localized in micronemes, an organelle found in all organizms of the phylum Apicomplexa. This family is closely associated on PfEMP1 proteins with PFEMP, pfam03011.
Pssm-ID: 428465 [Multi-domain] Cd Length: 178 Bit Score: 134.32 E-value: 1.94e-35
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ...
654-821
3.62e-30
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been identified as the rosetting ligand of the malaria parasite P. falciparum. Rosetting is the adhesion of infected erythrocytes with uninfected erythrocytes in the vasculature of the infected organ, and is associated with severe malaria. PfEMP1 interacts with Complement Receptor One on uninfected erythrocytes to form rosettes. The extreme variation within these proteins and the grouping of var genes implies that var gene recombination preferentially occurs within var gene groups. These groups reflect a functional diversification that has evolved to cope with the varying conditions of transmission and host immune response met by the parasite. A recombination hotspot was uncovered between Duffy-binding-like (DBL) subdomains. Solution of the crystal structure of the N-terminal and first DBL region of PfEMP1 from the VarO variant of the PfEMP1 protein is found to be directly implicated in rosetting as the heparin-binding site.
Pssm-ID: 281064 Cd Length: 154 Bit Score: 118.37 E-value: 3.62e-30
Cysteine-Rich Interdomain Region 1 gamma; Rosetting is the capacity of infected RBCs to bind ...
2260-2313
6.78e-15
Cysteine-Rich Interdomain Region 1 gamma; Rosetting is the capacity of infected RBCs to bind uninfected RBCs, which is consistently associated with severe malaria in African children. The rosette-forming PfEMP1 adhesins, namely IT4/R29, Palo Alto 89F5 VarO, 3D7/PF13_0003 and IT4/var60, belong to a specific sub-group called groupA/UpsA var genes and all four present a specific Duffy Binding-Like and and Cysteine-Rich Interdomain Region (DBL1alpha1-CIDR1gamma) double domain Head region found at the extracellular region of PfEMP1. This entry represents the CIDR1gamma domain which increases the binding affinity to VarO (Palo Alto VarO parasites).
Pssm-ID: 408346 Cd Length: 52 Bit Score: 71.15 E-value: 6.78e-15
N-terminal segments of PfEMP1; This family, the N-terminal segment, is the most variable part ...
22-57
4.42e-11
N-terminal segments of PfEMP1; This family, the N-terminal segment, is the most variable part of the variant surface antigen family of Plasmodium falciparum, the erythrocyte membrane protein-1 (PfEMP1) proteins. PfEMP1 is an important target for protective immunity and is implicated in the pathology of malaria through its ability to adhere to host endothelial receptors. A structural and functional study of the N-terminal domain of PfEMP1 from the VarO variant comprising the N-terminal segment (NTS) and the first DBL domain (DBL1alpha1), shows this region is directly implicated in rosetting. NTS, previously thought to be a structurally independent component of PfEMP1, forms an integral part of the DBL1alpha domain that is found to be the important heparin-binding site. This family is closely associated with PFEMP, pfam03011, and Duffy_binding, pfam05424.
Pssm-ID: 406013 [Multi-domain] Cd Length: 36 Bit Score: 59.72 E-value: 4.42e-11
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
2711-2734
1.25e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 41.33 E-value: 1.25e-03
acidic terminal segments, variant surface antigen of PfEMP1; ATS is the intracellular and ...
2593-3078
0e+00
acidic terminal segments, variant surface antigen of PfEMP1; ATS is the intracellular and relatively conserved acidic terminal segment of the Plasmodium falciparum erythrocyte membrane protein-1 (PfEMP1). this domain appears to be present in all variants of the highly polymorphic PfEMP1 proteins.
Pssm-ID: 373851 [Multi-domain] Cd Length: 446 Bit Score: 794.78 E-value: 0e+00
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ...
122-307
1.43e-87
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium vivax and Plasmodium knowlesi merozoites invade human erythrocytes that express Duffy blood group surface determinants. The Duffy receptor family is localized in micronemes, an organelle found in all organizms of the phylum Apicomplexa. This family is closely associated on PfEMP1 proteins with PFEMP, pfam03011.
Pssm-ID: 428465 [Multi-domain] Cd Length: 178 Bit Score: 283.78 E-value: 1.43e-87
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ...
1388-1569
3.33e-47
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium vivax and Plasmodium knowlesi merozoites invade human erythrocytes that express Duffy blood group surface determinants. The Duffy receptor family is localized in micronemes, an organelle found in all organizms of the phylum Apicomplexa. This family is closely associated on PfEMP1 proteins with PFEMP, pfam03011.
Pssm-ID: 428465 [Multi-domain] Cd Length: 178 Bit Score: 167.84 E-value: 3.33e-47
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ...
961-1135
7.01e-44
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium vivax and Plasmodium knowlesi merozoites invade human erythrocytes that express Duffy blood group surface determinants. The Duffy receptor family is localized in micronemes, an organelle found in all organizms of the phylum Apicomplexa. This family is closely associated on PfEMP1 proteins with PFEMP, pfam03011.
Pssm-ID: 428465 [Multi-domain] Cd Length: 178 Bit Score: 158.59 E-value: 7.01e-44
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ...
2329-2464
4.26e-36
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been identified as the rosetting ligand of the malaria parasite P. falciparum. Rosetting is the adhesion of infected erythrocytes with uninfected erythrocytes in the vasculature of the infected organ, and is associated with severe malaria. PfEMP1 interacts with Complement Receptor One on uninfected erythrocytes to form rosettes. The extreme variation within these proteins and the grouping of var genes implies that var gene recombination preferentially occurs within var gene groups. These groups reflect a functional diversification that has evolved to cope with the varying conditions of transmission and host immune response met by the parasite. A recombination hotspot was uncovered between Duffy-binding-like (DBL) subdomains. Solution of the crystal structure of the N-terminal and first DBL region of PfEMP1 from the VarO variant of the PfEMP1 protein is found to be directly implicated in rosetting as the heparin-binding site.
Pssm-ID: 281064 Cd Length: 154 Bit Score: 135.32 E-value: 4.26e-36
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ...
1788-1985
1.94e-35
Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium vivax and Plasmodium knowlesi merozoites invade human erythrocytes that express Duffy blood group surface determinants. The Duffy receptor family is localized in micronemes, an organelle found in all organizms of the phylum Apicomplexa. This family is closely associated on PfEMP1 proteins with PFEMP, pfam03011.
Pssm-ID: 428465 [Multi-domain] Cd Length: 178 Bit Score: 134.32 E-value: 1.94e-35
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ...
654-821
3.62e-30
PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been identified as the rosetting ligand of the malaria parasite P. falciparum. Rosetting is the adhesion of infected erythrocytes with uninfected erythrocytes in the vasculature of the infected organ, and is associated with severe malaria. PfEMP1 interacts with Complement Receptor One on uninfected erythrocytes to form rosettes. The extreme variation within these proteins and the grouping of var genes implies that var gene recombination preferentially occurs within var gene groups. These groups reflect a functional diversification that has evolved to cope with the varying conditions of transmission and host immune response met by the parasite. A recombination hotspot was uncovered between Duffy-binding-like (DBL) subdomains. Solution of the crystal structure of the N-terminal and first DBL region of PfEMP1 from the VarO variant of the PfEMP1 protein is found to be directly implicated in rosetting as the heparin-binding site.
Pssm-ID: 281064 Cd Length: 154 Bit Score: 118.37 E-value: 3.62e-30
Cysteine-Rich Interdomain Region 1 gamma; Rosetting is the capacity of infected RBCs to bind ...
2260-2313
6.78e-15
Cysteine-Rich Interdomain Region 1 gamma; Rosetting is the capacity of infected RBCs to bind uninfected RBCs, which is consistently associated with severe malaria in African children. The rosette-forming PfEMP1 adhesins, namely IT4/R29, Palo Alto 89F5 VarO, 3D7/PF13_0003 and IT4/var60, belong to a specific sub-group called groupA/UpsA var genes and all four present a specific Duffy Binding-Like and and Cysteine-Rich Interdomain Region (DBL1alpha1-CIDR1gamma) double domain Head region found at the extracellular region of PfEMP1. This entry represents the CIDR1gamma domain which increases the binding affinity to VarO (Palo Alto VarO parasites).
Pssm-ID: 408346 Cd Length: 52 Bit Score: 71.15 E-value: 6.78e-15
N-terminal segments of PfEMP1; This family, the N-terminal segment, is the most variable part ...
22-57
4.42e-11
N-terminal segments of PfEMP1; This family, the N-terminal segment, is the most variable part of the variant surface antigen family of Plasmodium falciparum, the erythrocyte membrane protein-1 (PfEMP1) proteins. PfEMP1 is an important target for protective immunity and is implicated in the pathology of malaria through its ability to adhere to host endothelial receptors. A structural and functional study of the N-terminal domain of PfEMP1 from the VarO variant comprising the N-terminal segment (NTS) and the first DBL domain (DBL1alpha1), shows this region is directly implicated in rosetting. NTS, previously thought to be a structurally independent component of PfEMP1, forms an integral part of the DBL1alpha domain that is found to be the important heparin-binding site. This family is closely associated with PFEMP, pfam03011, and Duffy_binding, pfam05424.
Pssm-ID: 406013 [Multi-domain] Cd Length: 36 Bit Score: 59.72 E-value: 4.42e-11
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
2711-2734
1.25e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 41.33 E-value: 1.25e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
2711-2734
2.89e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 40.17 E-value: 2.89e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
2711-2734
2.92e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 40.17 E-value: 2.92e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
2711-2735
2.97e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 40.17 E-value: 2.97e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
2711-2735
4.77e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 39.79 E-value: 4.77e-03
Ice-binding protein, left-handed beta-roll; The ice-binding protein of the grass Lolium ...
2709-2734
5.06e-03
Ice-binding protein, left-handed beta-roll; The ice-binding protein of the grass Lolium perenne (LpIBP) discourages the recrystallization of ice. Ice-binding proteins produced by organisms to prevent the growing of ice are termed to anti-freeze proteins. LpIBP consists of an unusual left-handed beta roll. Ice-binding is mediated by a flat beta-sheet on one side of the helix.
Pssm-ID: 240609 [Multi-domain] Cd Length: 114 Bit Score: 39.30 E-value: 5.06e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
2710-2735
5.40e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 39.40 E-value: 5.40e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
2711-2734
6.67e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 39.02 E-value: 6.67e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
2711-2734
7.93e-03
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.
Pssm-ID: 240612 [Multi-domain] Cd Length: 126 Bit Score: 39.02 E-value: 7.93e-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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
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.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
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(specific hits) are drawn in bright colors.
Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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)
mapped to the query sequence.
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
(illustrated example)
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
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
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
(CDART).
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