erythrocyte membrane protein 1, PfEMP1 [Plasmodium falciparum 3D7]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| ATS | pfam15445 | acidic terminal segments, variant surface antigen of PfEMP1; ATS is the intracellular and ... |
2173-2646 | 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: 735.85 E-value: 0e+00
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| Duffy_binding | pfam05424 | Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ... |
132-336 | 2.57e-83 | ||||||||
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: 271.07 E-value: 2.57e-83
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| Duffy_binding | pfam05424 | Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ... |
903-1085 | 4.75e-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: 167.45 E-value: 4.75e-47
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| Duffy_binding super family | cl38187 | Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ... |
1325-1578 | 1.34e-29 | ||||||||
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. The actual alignment was detected with superfamily member pfam05424: Pssm-ID: 428465 [Multi-domain] Cd Length: 178 Bit Score: 117.37 E-value: 1.34e-29
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| PFEMP super family | cl03834 | PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ... |
642-805 | 1.50e-28 | ||||||||
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: 113.36 E-value: 1.50e-28
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| PFEMP super family | cl03834 | PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ... |
1913-2050 | 1.00e-22 | ||||||||
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: 96.80 E-value: 1.00e-22
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| CIDR1_gamma | pfam18562 | Cysteine-Rich Interdomain Region 1 gamma; Rosetting is the capacity of infected RBCs to bind ... |
1843-1895 | 1.43e-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: 72.69 E-value: 1.43e-15
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| NTS | pfam15447 | N-terminal segments of PfEMP1; This family, the N-terminal segment, is the most variable part ... |
21-64 | 8.39e-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: 58.56 E-value: 8.39e-11
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| Name | Accession | Description | Interval | E-value | ||||||||
| ATS | pfam15445 | acidic terminal segments, variant surface antigen of PfEMP1; ATS is the intracellular and ... |
2173-2646 | 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: 735.85 E-value: 0e+00
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| PTZ00176 | PTZ00176 | erythrocyte membrane protein 1 (PfEMP1); Provisional |
2179-2646 | 5.81e-143 | ||||||||
erythrocyte membrane protein 1 (PfEMP1); Provisional Pssm-ID: 140204 [Multi-domain] Cd Length: 1317 Bit Score: 483.77 E-value: 5.81e-143
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| Duffy_binding | pfam05424 | Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ... |
132-336 | 2.57e-83 | ||||||||
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: 271.07 E-value: 2.57e-83
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| PTZ00176 | PTZ00176 | erythrocyte membrane protein 1 (PfEMP1); Provisional |
21-421 | 2.04e-60 | ||||||||
erythrocyte membrane protein 1 (PfEMP1); Provisional Pssm-ID: 140204 [Multi-domain] Cd Length: 1317 Bit Score: 230.31 E-value: 2.04e-60
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| Duffy_binding | pfam05424 | Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ... |
903-1085 | 4.75e-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: 167.45 E-value: 4.75e-47
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| Duffy_binding | pfam05424 | Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ... |
1325-1578 | 1.34e-29 | ||||||||
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: 117.37 E-value: 1.34e-29
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| PFEMP | pfam03011 | PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ... |
642-805 | 1.50e-28 | ||||||||
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: 113.36 E-value: 1.50e-28
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| PFEMP | pfam03011 | PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ... |
1913-2050 | 1.00e-22 | ||||||||
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: 96.80 E-value: 1.00e-22
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| CIDR1_gamma | pfam18562 | Cysteine-Rich Interdomain Region 1 gamma; Rosetting is the capacity of infected RBCs to bind ... |
1843-1895 | 1.43e-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: 72.69 E-value: 1.43e-15
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| NTS | pfam15447 | N-terminal segments of PfEMP1; This family, the N-terminal segment, is the most variable part ... |
21-64 | 8.39e-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: 58.56 E-value: 8.39e-11
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| PTZ00176 | PTZ00176 | erythrocyte membrane protein 1 (PfEMP1); Provisional |
899-1159 | 3.73e-09 | ||||||||
erythrocyte membrane protein 1 (PfEMP1); Provisional Pssm-ID: 140204 [Multi-domain] Cd Length: 1317 Bit Score: 62.75 E-value: 3.73e-09
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2290-2321 | 3.88e-07 | ||||||||
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: 51.34 E-value: 3.88e-07
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| Hia | COG5295 | Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
2290-2322 | 6.09e-04 | ||||||||
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 45.53 E-value: 6.09e-04
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| Name | Accession | Description | Interval | E-value | ||||||||
| ATS | pfam15445 | acidic terminal segments, variant surface antigen of PfEMP1; ATS is the intracellular and ... |
2173-2646 | 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: 735.85 E-value: 0e+00
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| PTZ00176 | PTZ00176 | erythrocyte membrane protein 1 (PfEMP1); Provisional |
2179-2646 | 5.81e-143 | ||||||||
erythrocyte membrane protein 1 (PfEMP1); Provisional Pssm-ID: 140204 [Multi-domain] Cd Length: 1317 Bit Score: 483.77 E-value: 5.81e-143
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| Duffy_binding | pfam05424 | Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ... |
132-336 | 2.57e-83 | ||||||||
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: 271.07 E-value: 2.57e-83
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| PTZ00176 | PTZ00176 | erythrocyte membrane protein 1 (PfEMP1); Provisional |
21-421 | 2.04e-60 | ||||||||
erythrocyte membrane protein 1 (PfEMP1); Provisional Pssm-ID: 140204 [Multi-domain] Cd Length: 1317 Bit Score: 230.31 E-value: 2.04e-60
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| Duffy_binding | pfam05424 | Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ... |
903-1085 | 4.75e-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: 167.45 E-value: 4.75e-47
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| Duffy_binding | pfam05424 | Duffy binding domain; This domain is found in Plasmodium Duffy binding proteins. Plasmodium ... |
1325-1578 | 1.34e-29 | ||||||||
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: 117.37 E-value: 1.34e-29
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| PFEMP | pfam03011 | PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ... |
642-805 | 1.50e-28 | ||||||||
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: 113.36 E-value: 1.50e-28
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| PFEMP | pfam03011 | PFEMP1 DBL domain; PfEMP1 (Plasmodium falciparum erythrocyte membrane protein) has been ... |
1913-2050 | 1.00e-22 | ||||||||
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: 96.80 E-value: 1.00e-22
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| CIDR1_gamma | pfam18562 | Cysteine-Rich Interdomain Region 1 gamma; Rosetting is the capacity of infected RBCs to bind ... |
1843-1895 | 1.43e-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: 72.69 E-value: 1.43e-15
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| NTS | pfam15447 | N-terminal segments of PfEMP1; This family, the N-terminal segment, is the most variable part ... |
21-64 | 8.39e-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: 58.56 E-value: 8.39e-11
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| PTZ00176 | PTZ00176 | erythrocyte membrane protein 1 (PfEMP1); Provisional |
98-378 | 2.07e-09 | ||||||||
erythrocyte membrane protein 1 (PfEMP1); Provisional Pssm-ID: 140204 [Multi-domain] Cd Length: 1317 Bit Score: 63.52 E-value: 2.07e-09
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| PTZ00176 | PTZ00176 | erythrocyte membrane protein 1 (PfEMP1); Provisional |
899-1159 | 3.73e-09 | ||||||||
erythrocyte membrane protein 1 (PfEMP1); Provisional Pssm-ID: 140204 [Multi-domain] Cd Length: 1317 Bit Score: 62.75 E-value: 3.73e-09
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| PTZ00176 | PTZ00176 | erythrocyte membrane protein 1 (PfEMP1); Provisional |
878-1150 | 9.12e-09 | ||||||||
erythrocyte membrane protein 1 (PfEMP1); Provisional Pssm-ID: 140204 [Multi-domain] Cd Length: 1317 Bit Score: 61.20 E-value: 9.12e-09
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2290-2321 | 3.88e-07 | ||||||||
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: 51.34 E-value: 3.88e-07
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2290-2321 | 5.88e-07 | ||||||||
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: 50.57 E-value: 5.88e-07
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2290-2322 | 6.86e-07 | ||||||||
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: 50.57 E-value: 6.86e-07
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2290-2322 | 1.27e-06 | ||||||||
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: 49.80 E-value: 1.27e-06
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2291-2322 | 1.58e-06 | ||||||||
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: 49.42 E-value: 1.58e-06
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2290-2321 | 3.41e-06 | ||||||||
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: 48.65 E-value: 3.41e-06
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2291-2322 | 4.88e-06 | ||||||||
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: 47.88 E-value: 4.88e-06
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2290-2321 | 6.33e-06 | ||||||||
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: 47.88 E-value: 6.33e-06
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2290-2319 | 7.04e-06 | ||||||||
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: 47.49 E-value: 7.04e-06
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2291-2322 | 1.06e-05 | ||||||||
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: 47.10 E-value: 1.06e-05
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2291-2322 | 1.35e-05 | ||||||||
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: 46.72 E-value: 1.35e-05
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2291-2322 | 1.43e-05 | ||||||||
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: 46.72 E-value: 1.43e-05
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2291-2322 | 1.87e-05 | ||||||||
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: 46.33 E-value: 1.87e-05
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2291-2322 | 2.72e-05 | ||||||||
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: 45.95 E-value: 2.72e-05
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| LbR_Ice_bind | cd12796 | Ice-binding protein, left-handed beta-roll; The ice-binding protein of the grass Lolium ... |
2290-2321 | 2.82e-05 | ||||||||
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: 45.47 E-value: 2.82e-05
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2293-2321 | 4.45e-05 | ||||||||
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: 45.18 E-value: 4.45e-05
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| YadA_head | pfam05658 | YadA head domain repeat (2 copies); This entry represents two copies of a fourteen residue ... |
2296-2322 | 6.22e-05 | ||||||||
YadA head domain repeat (2 copies); This entry represents two copies of a fourteen residue repeat that makes up the head domain of bacterial haemagglutinins and invasins. Pssm-ID: 461707 [Multi-domain] Cd Length: 27 Bit Score: 41.85 E-value: 6.22e-05
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| LbR_Ice_bind | cd12796 | Ice-binding protein, left-handed beta-roll; The ice-binding protein of the grass Lolium ... |
2290-2321 | 6.24e-05 | ||||||||
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: 44.70 E-value: 6.24e-05
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| LbR_Ice_bind | cd12796 | Ice-binding protein, left-handed beta-roll; The ice-binding protein of the grass Lolium ... |
2289-2321 | 8.51e-05 | ||||||||
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: 44.31 E-value: 8.51e-05
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| LbR_Ice_bind | cd12796 | Ice-binding protein, left-handed beta-roll; The ice-binding protein of the grass Lolium ... |
2291-2334 | 2.12e-04 | ||||||||
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: 43.16 E-value: 2.12e-04
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| LbR-like | cd12813 | Left-handed beta-roll, including virulence factors and various other proteins; This family ... |
2290-2319 | 2.19e-04 | ||||||||
Left-handed beta-roll, including virulence factors and various other proteins; This family contains a variety of protein domains with a left-handed beta-roll structure including cell surface adhesion proteins, bacterial virulence factors, and ice-binding proteins, and other activities. UspA1 Head And Neck Domain and YadA of Yersinia 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 beta-rolls 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. The collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface 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. 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. These domains form a left handed beta roll made up of a series of short repeated elements. Pssm-ID: 240610 [Multi-domain] Cd Length: 99 Bit Score: 42.53 E-value: 2.19e-04
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| LbR-like | cd12813 | Left-handed beta-roll, including virulence factors and various other proteins; This family ... |
2290-2322 | 2.33e-04 | ||||||||
Left-handed beta-roll, including virulence factors and various other proteins; This family contains a variety of protein domains with a left-handed beta-roll structure including cell surface adhesion proteins, bacterial virulence factors, and ice-binding proteins, and other activities. UspA1 Head And Neck Domain and YadA of Yersinia 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 beta-rolls 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. The collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface 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. 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. These domains form a left handed beta roll made up of a series of short repeated elements. Pssm-ID: 240610 [Multi-domain] Cd Length: 99 Bit Score: 42.53 E-value: 2.33e-04
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| LbR_Ice_bind | cd12796 | Ice-binding protein, left-handed beta-roll; The ice-binding protein of the grass Lolium ... |
2290-2321 | 2.54e-04 | ||||||||
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: 42.77 E-value: 2.54e-04
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| LbR-like | cd12813 | Left-handed beta-roll, including virulence factors and various other proteins; This family ... |
2290-2322 | 2.59e-04 | ||||||||
Left-handed beta-roll, including virulence factors and various other proteins; This family contains a variety of protein domains with a left-handed beta-roll structure including cell surface adhesion proteins, bacterial virulence factors, and ice-binding proteins, and other activities. UspA1 Head And Neck Domain and YadA of Yersinia 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 beta-rolls 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. The collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface 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. 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. These domains form a left handed beta roll made up of a series of short repeated elements. Pssm-ID: 240610 [Multi-domain] Cd Length: 99 Bit Score: 42.53 E-value: 2.59e-04
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| LbR-like | cd12813 | Left-handed beta-roll, including virulence factors and various other proteins; This family ... |
2290-2322 | 3.50e-04 | ||||||||
Left-handed beta-roll, including virulence factors and various other proteins; This family contains a variety of protein domains with a left-handed beta-roll structure including cell surface adhesion proteins, bacterial virulence factors, and ice-binding proteins, and other activities. UspA1 Head And Neck Domain and YadA of Yersinia 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 beta-rolls 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. The collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface 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. 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. These domains form a left handed beta roll made up of a series of short repeated elements. Pssm-ID: 240610 [Multi-domain] Cd Length: 99 Bit Score: 42.15 E-value: 3.50e-04
|
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| LbR_Ice_bind | cd12796 | Ice-binding protein, left-handed beta-roll; The ice-binding protein of the grass Lolium ... |
2290-2333 | 5.26e-04 | ||||||||
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: 42.00 E-value: 5.26e-04
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| Hia | COG5295 | Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
2290-2322 | 6.09e-04 | ||||||||
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 45.53 E-value: 6.09e-04
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| Hia | COG5295 | Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
2288-2324 | 6.25e-04 | ||||||||
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 45.15 E-value: 6.25e-04
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| Hia | COG5295 | Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
2291-2328 | 7.21e-04 | ||||||||
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 45.15 E-value: 7.21e-04
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| LbR_Ice_bind | cd12796 | Ice-binding protein, left-handed beta-roll; The ice-binding protein of the grass Lolium ... |
2290-2321 | 1.21e-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: 40.84 E-value: 1.21e-03
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| KLF18_N | cd21575 | N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ... |
2294-2470 | 1.83e-03 | ||||||||
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains. Pssm-ID: 410566 [Multi-domain] Cd Length: 276 Bit Score: 42.75 E-value: 1.83e-03
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| LbR_Ice_bind | cd12796 | Ice-binding protein, left-handed beta-roll; The ice-binding protein of the grass Lolium ... |
2373-2472 | 2.25e-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: 40.07 E-value: 2.25e-03
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| Hia | COG5295 | Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ... |
2290-2330 | 3.12e-03 | ||||||||
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures]; Pssm-ID: 444098 [Multi-domain] Cd Length: 785 Bit Score: 42.84 E-value: 3.12e-03
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| LbR_YadA-like | cd12820 | YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ... |
2291-2313 | 3.60e-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: 3.60e-03
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