Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
1586-1657
9.18e-13
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.
:
Pssm-ID: 465513 [Multi-domain] Cd Length: 72 Bit Score: 64.91 E-value: 9.18e-13
C-terminus of bacterial fibrinogen-binding adhesin; This is the C-terminal half of a bacterial ...
1389-1532
2.91e-12
C-terminus of bacterial fibrinogen-binding adhesin; This is the C-terminal half of a bacterial fibrinogen-binding adhesin SdrG. SdrG is a Gram-positive cell-wall-anchored adhesin that allows attachment of the bacterium to host tissues via specific binding to the beta-chain of human fibrinogen (Fg). SdrG binds to its ligand with a dynamic "dock, lock, and latch" mechanism which represents a general mode of ligand-binding for structurally related cell wall-anchored proteins in most Gram-positive bacteria. The C-terminal part of SdrG(276-596) is integral to the folding of the immunoglobulin-like whole to create the docking grooves necessary for Fg binding. The domain is associated with families of Cna_B, pfam05738.
The actual alignment was detected with superfamily member pfam10425:
Pssm-ID: 431277 [Multi-domain] Cd Length: 156 Bit Score: 66.29 E-value: 2.91e-12
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
583-648
2.65e-10
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.
:
Pssm-ID: 465513 [Multi-domain] Cd Length: 72 Bit Score: 57.98 E-value: 2.65e-10
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
1228-1509
1.21e-13
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 76.49 E-value: 1.21e-13
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
1586-1657
9.18e-13
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.
Pssm-ID: 465513 [Multi-domain] Cd Length: 72 Bit Score: 64.91 E-value: 9.18e-13
C-terminus of bacterial fibrinogen-binding adhesin; This is the C-terminal half of a bacterial ...
1389-1532
2.91e-12
C-terminus of bacterial fibrinogen-binding adhesin; This is the C-terminal half of a bacterial fibrinogen-binding adhesin SdrG. SdrG is a Gram-positive cell-wall-anchored adhesin that allows attachment of the bacterium to host tissues via specific binding to the beta-chain of human fibrinogen (Fg). SdrG binds to its ligand with a dynamic "dock, lock, and latch" mechanism which represents a general mode of ligand-binding for structurally related cell wall-anchored proteins in most Gram-positive bacteria. The C-terminal part of SdrG(276-596) is integral to the folding of the immunoglobulin-like whole to create the docking grooves necessary for Fg binding. The domain is associated with families of Cna_B, pfam05738.
Pssm-ID: 431277 [Multi-domain] Cd Length: 156 Bit Score: 66.29 E-value: 2.91e-12
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
583-648
2.65e-10
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.
Pssm-ID: 465513 [Multi-domain] Cd Length: 72 Bit Score: 57.98 E-value: 2.65e-10
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
1576-1707
4.30e-07
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.
Pssm-ID: 468234 [Multi-domain] Cd Length: 533 Bit Score: 54.76 E-value: 4.30e-07
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
879-1203
6.77e-05
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.
Pssm-ID: 468234 [Multi-domain] Cd Length: 533 Bit Score: 47.44 E-value: 6.77e-05
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
886-982
3.45e-03
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.
Pssm-ID: 468234 [Multi-domain] Cd Length: 533 Bit Score: 42.05 E-value: 3.45e-03
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
1131-1194
3.85e-15
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.
Pssm-ID: 465513 [Multi-domain] Cd Length: 72 Bit Score: 71.46 E-value: 3.85e-15
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
1228-1509
1.21e-13
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 76.49 E-value: 1.21e-13
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
1018-1086
1.78e-13
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.
Pssm-ID: 465513 [Multi-domain] Cd Length: 72 Bit Score: 66.84 E-value: 1.78e-13
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
1586-1657
9.18e-13
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.
Pssm-ID: 465513 [Multi-domain] Cd Length: 72 Bit Score: 64.91 E-value: 9.18e-13
C-terminus of bacterial fibrinogen-binding adhesin; This is the C-terminal half of a bacterial ...
1389-1532
2.91e-12
C-terminus of bacterial fibrinogen-binding adhesin; This is the C-terminal half of a bacterial fibrinogen-binding adhesin SdrG. SdrG is a Gram-positive cell-wall-anchored adhesin that allows attachment of the bacterium to host tissues via specific binding to the beta-chain of human fibrinogen (Fg). SdrG binds to its ligand with a dynamic "dock, lock, and latch" mechanism which represents a general mode of ligand-binding for structurally related cell wall-anchored proteins in most Gram-positive bacteria. The C-terminal part of SdrG(276-596) is integral to the folding of the immunoglobulin-like whole to create the docking grooves necessary for Fg binding. The domain is associated with families of Cna_B, pfam05738.
Pssm-ID: 431277 [Multi-domain] Cd Length: 156 Bit Score: 66.29 E-value: 2.91e-12
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
895-973
1.13e-11
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.
Pssm-ID: 465513 [Multi-domain] Cd Length: 72 Bit Score: 61.83 E-value: 1.13e-11
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
583-648
2.65e-10
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.
Pssm-ID: 465513 [Multi-domain] Cd Length: 72 Bit Score: 57.98 E-value: 2.65e-10
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
1576-1707
4.30e-07
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.
Pssm-ID: 468234 [Multi-domain] Cd Length: 533 Bit Score: 54.76 E-value: 4.30e-07
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
879-1203
6.77e-05
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.
Pssm-ID: 468234 [Multi-domain] Cd Length: 533 Bit Score: 47.44 E-value: 6.77e-05
SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This ...
1018-1060
2.46e-03
SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This domain has three calcium binding sites within a greek key beta sandwich fold.
Pssm-ID: 435789 [Multi-domain] Cd Length: 112 Bit Score: 39.51 E-value: 2.46e-03
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
886-982
3.45e-03
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.
Pssm-ID: 468234 [Multi-domain] Cd Length: 533 Bit Score: 42.05 E-value: 3.45e-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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