Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane ...
573-966
1.01e-58
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane proteins) family, as described in Bartonella, consists of autotransporter surface proteins including collagen-binding autotransporter adhesins VompA and VompC.
The actual alignment was detected with superfamily member NF033870:
Pssm-ID: 411434 [Multi-domain] Cd Length: 356 Bit Score: 205.41 E-value: 1.01e-58
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
278-844
1.05e-22
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
The actual alignment was detected with superfamily member NF033481:
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 105.33 E-value: 1.05e-22
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane ...
573-966
1.01e-58
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane proteins) family, as described in Bartonella, consists of autotransporter surface proteins including collagen-binding autotransporter adhesins VompA and VompC.
Pssm-ID: 411434 [Multi-domain] Cd Length: 356 Bit Score: 205.41 E-value: 1.01e-58
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
278-844
1.05e-22
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 105.33 E-value: 1.05e-22
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
223-790
3.09e-18
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 90.69 E-value: 3.09e-18
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
290-813
2.06e-16
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 84.92 E-value: 2.06e-16
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
652-719
1.14e-11
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: 62.90 E-value: 1.14e-11
YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a ...
907-965
1.83e-09
YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a family of surface-exposed bacterial proteins. YadA, an adhesin from Yersinia, was the first member of this family to be characterized. UspA2 from Moraxella was second. The Eib immunoglobulin-binding proteins from E. coli were third, followed by the DsrA proteins of Haemophilus ducreyi and others. These proteins are homologous at their C-terminal and have predicted signal sequences, but they diverge elsewhere. The C-terminal 9 amino acids, consisting of alternating hydrophobic amino acids ending in F or W, comprise a targeting motif for the outer membrane of the Gram negative cell envelope. This region is important for oligomerization.
Pssm-ID: 427576 [Multi-domain] Cd Length: 60 Bit Score: 54.49 E-value: 1.83e-09
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
221-607
6.30e-09
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 60.26 E-value: 6.30e-09
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
652-779
1.04e-08
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 59.49 E-value: 1.04e-08
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
652-811
1.49e-08
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 59.11 E-value: 1.49e-08
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane ...
223-363
3.27e-06
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane proteins) family, as described in Bartonella, consists of autotransporter surface proteins including collagen-binding autotransporter adhesins VompA and VompC.
Pssm-ID: 411434 [Multi-domain] Cd Length: 356 Bit Score: 50.56 E-value: 3.27e-06
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane ...
235-476
2.23e-05
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane proteins) family, as described in Bartonella, consists of autotransporter surface proteins including collagen-binding autotransporter adhesins VompA and VompC.
Pssm-ID: 411434 [Multi-domain] Cd Length: 356 Bit Score: 47.86 E-value: 2.23e-05
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
653-761
9.11e-04
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 43.32 E-value: 9.11e-04
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane ...
573-966
1.01e-58
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane proteins) family, as described in Bartonella, consists of autotransporter surface proteins including collagen-binding autotransporter adhesins VompA and VompC.
Pssm-ID: 411434 [Multi-domain] Cd Length: 356 Bit Score: 205.41 E-value: 1.01e-58
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
278-844
1.05e-22
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 105.33 E-value: 1.05e-22
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
223-790
3.09e-18
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 90.69 E-value: 3.09e-18
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
290-813
2.06e-16
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 84.92 E-value: 2.06e-16
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
652-719
1.14e-11
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: 62.90 E-value: 1.14e-11
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
652-719
1.29e-11
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: 62.51 E-value: 1.29e-11
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
652-719
9.50e-11
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: 60.20 E-value: 9.50e-11
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
655-719
2.92e-10
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: 58.66 E-value: 2.92e-10
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
655-719
5.81e-10
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: 57.89 E-value: 5.81e-10
YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a ...
907-965
1.83e-09
YadA-like membrane anchor domain; This region represents the C-terminal 120 amino acids of a family of surface-exposed bacterial proteins. YadA, an adhesin from Yersinia, was the first member of this family to be characterized. UspA2 from Moraxella was second. The Eib immunoglobulin-binding proteins from E. coli were third, followed by the DsrA proteins of Haemophilus ducreyi and others. These proteins are homologous at their C-terminal and have predicted signal sequences, but they diverge elsewhere. The C-terminal 9 amino acids, consisting of alternating hydrophobic amino acids ending in F or W, comprise a targeting motif for the outer membrane of the Gram negative cell envelope. This region is important for oligomerization.
Pssm-ID: 427576 [Multi-domain] Cd Length: 60 Bit Score: 54.49 E-value: 1.83e-09
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
221-607
6.30e-09
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 60.26 E-value: 6.30e-09
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
652-779
1.04e-08
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 59.49 E-value: 1.04e-08
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
652-811
1.49e-08
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 59.11 E-value: 1.49e-08
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
666-724
4.28e-08
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: 52.50 E-value: 4.28e-08
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane ...
223-363
3.27e-06
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane proteins) family, as described in Bartonella, consists of autotransporter surface proteins including collagen-binding autotransporter adhesins VompA and VompC.
Pssm-ID: 411434 [Multi-domain] Cd Length: 356 Bit Score: 50.56 E-value: 3.27e-06
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane ...
235-476
2.23e-05
Vomp family autotransporter C-terminal domain; The Vomp (variably expressed outer-membrane proteins) family, as described in Bartonella, consists of autotransporter surface proteins including collagen-binding autotransporter adhesins VompA and VompC.
Pssm-ID: 411434 [Multi-domain] Cd Length: 356 Bit Score: 47.86 E-value: 2.23e-05
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an ...
653-761
9.11e-04
trimeric autotransporter adhesin Ata; Ata (Acinetobacter trimeric autotransporter) has an architecture that consists of a long signal peptide, a repetitive passenger domain that varies in length from strain to strain, and a C-terminal domain of four transmembrane beta stands that forms one third of the pore for autotransporter activity and anchoring in the outer membrane.
Pssm-ID: 411124 [Multi-domain] Cd Length: 1862 Bit Score: 43.32 E-value: 9.11e-04
YadA-like, left-handed beta-roll; This group contains the collagen-binding domain virulence ...
652-692
1.28e-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: 1.28e-03
YadA head domain repeat (2 copies); This entry represents two copies of a fourteen residue ...
662-688
4.00e-03
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: 35.68 E-value: 4.00e-03
Left-handed beta-roll, including virulence factors and various other proteins; This family ...
657-719
5.93e-03
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: 37.14 E-value: 5.93e-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.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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