Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, ...
2-40
6.21e-11
Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.
:
Pssm-ID: 273479 [Multi-domain] Cd Length: 39 Bit Score: 57.88 E-value: 6.21e-11
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
312-770
4.18e-82
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
Pssm-ID: 271234 [Multi-domain] Cd Length: 339 Bit Score: 269.71 E-value: 4.18e-82
Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, ...
2-40
6.21e-11
Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.
Pssm-ID: 273479 [Multi-domain] Cd Length: 39 Bit Score: 57.88 E-value: 6.21e-11
SpGH101 family endo-alpha-N-acetylgalactosaminidase; Members of this family are streptococcal ...
1-148
5.88e-09
SpGH101 family endo-alpha-N-acetylgalactosaminidase; Members of this family are streptococcal surface proteins with a complex (and somewhat variable) architecture that includes a crosswall-targeting N-terminal YSIRK domain, a C-terminal cell wall-anchoring LPXTG domain, and a central endo-alpha-N-acetylgalactosaminidase that removes an O-linked disaccharide from host glycoproteins.
Pssm-ID: 439743 [Multi-domain] Cd Length: 1694 Bit Score: 60.35 E-value: 5.88e-09
YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and ...
7-32
1.94e-08
YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.
Pssm-ID: 428049 [Multi-domain] Cd Length: 26 Bit Score: 50.46 E-value: 1.94e-08
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1-137
8.30e-05
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 46.30 E-value: 8.30e-05
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1-133
1.54e-03
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.31 E-value: 1.54e-03
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
312-770
4.18e-82
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
Pssm-ID: 271234 [Multi-domain] Cd Length: 339 Bit Score: 269.71 E-value: 4.18e-82
Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, ...
2-40
6.21e-11
Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.
Pssm-ID: 273479 [Multi-domain] Cd Length: 39 Bit Score: 57.88 E-value: 6.21e-11
SpGH101 family endo-alpha-N-acetylgalactosaminidase; Members of this family are streptococcal ...
1-148
5.88e-09
SpGH101 family endo-alpha-N-acetylgalactosaminidase; Members of this family are streptococcal surface proteins with a complex (and somewhat variable) architecture that includes a crosswall-targeting N-terminal YSIRK domain, a C-terminal cell wall-anchoring LPXTG domain, and a central endo-alpha-N-acetylgalactosaminidase that removes an O-linked disaccharide from host glycoproteins.
Pssm-ID: 439743 [Multi-domain] Cd Length: 1694 Bit Score: 60.35 E-value: 5.88e-09
YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and ...
7-32
1.94e-08
YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.
Pssm-ID: 428049 [Multi-domain] Cd Length: 26 Bit Score: 50.46 E-value: 1.94e-08
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1-137
8.30e-05
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 46.30 E-value: 8.30e-05
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1-133
1.54e-03
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.31 E-value: 1.54e-03
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric ...
130-287
7.41e-03
Pentraxin / C-reactive protein / pentaxin family; This family form a doscoid pentameric structure. Human serum amyloid P demonstrates calcium-mediated ligand-binding.
Pssm-ID: 128463 Cd Length: 206 Bit Score: 38.79 E-value: 7.41e-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 thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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