heme uptake protein IsdC; Isd proteins are iron-regulated surface proteins found in Bacillus, ...
1-237
4.99e-105
heme uptake protein IsdC; Isd proteins are iron-regulated surface proteins found in Bacillus, Staphylococcus and Listeria species and are responsible for heme scavenging from hemoproteins. The IsdC protein consists of an N-terminal hydrophobic signal sequence, a central NEAT (NEAr Transporter, pfam05031) domain, which confers the ability to bind heme, and a C-terminal SrtB processing signal which targets the protein to the cell wall. IsdC is believed to make a direct contact with, and transfer heme to, the heme-binding component (IsdE) of an ABC transporter in the cytoplasmic membrane, and to receive heme from other NEAT-containing heme-binding proteins also localized in the cell wall.
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Pssm-ID: 274705 [Multi-domain] Cd Length: 217 Bit Score: 302.59 E-value: 4.99e-105
heme uptake protein IsdC; Isd proteins are iron-regulated surface proteins found in Bacillus, ...
1-237
4.99e-105
heme uptake protein IsdC; Isd proteins are iron-regulated surface proteins found in Bacillus, Staphylococcus and Listeria species and are responsible for heme scavenging from hemoproteins. The IsdC protein consists of an N-terminal hydrophobic signal sequence, a central NEAT (NEAr Transporter, pfam05031) domain, which confers the ability to bind heme, and a C-terminal SrtB processing signal which targets the protein to the cell wall. IsdC is believed to make a direct contact with, and transfer heme to, the heme-binding component (IsdE) of an ABC transporter in the cytoplasmic membrane, and to receive heme from other NEAT-containing heme-binding proteins also localized in the cell wall.
Pssm-ID: 274705 [Multi-domain] Cd Length: 217 Bit Score: 302.59 E-value: 4.99e-105
Iron Transport-associated domain; NEAT domains are heme and/or hemoprotein-binding modules ...
31-146
5.54e-46
Iron Transport-associated domain; NEAT domains are heme and/or hemoprotein-binding modules highly conserved in secondary structure. They have roles in hemoprotein binding, heme extraction and heme transfer
Pssm-ID: 428269 [Multi-domain] Cd Length: 116 Bit Score: 148.95 E-value: 5.54e-46
NEAr Transport domain, a component of cell surface proteins; NEAr Transporter (NEAT) domain; ...
34-150
4.68e-37
NEAr Transport domain, a component of cell surface proteins; NEAr Transporter (NEAT) domain; used by pathogenic bacteria to to scavenge heme-iron from host hemoproteins. The NEAT domain is a component of cell surface proteins (iron regulated surface determinants, or Isd, such as IsdA and IsdC) in various gram-positive bacteria, and may be arranged in tandem repeats.
Pssm-ID: 132993 [Multi-domain] Cd Length: 117 Bit Score: 126.27 E-value: 4.68e-37
heme uptake protein IsdC; Isd proteins are iron-regulated surface proteins found in Bacillus, ...
1-237
4.99e-105
heme uptake protein IsdC; Isd proteins are iron-regulated surface proteins found in Bacillus, Staphylococcus and Listeria species and are responsible for heme scavenging from hemoproteins. The IsdC protein consists of an N-terminal hydrophobic signal sequence, a central NEAT (NEAr Transporter, pfam05031) domain, which confers the ability to bind heme, and a C-terminal SrtB processing signal which targets the protein to the cell wall. IsdC is believed to make a direct contact with, and transfer heme to, the heme-binding component (IsdE) of an ABC transporter in the cytoplasmic membrane, and to receive heme from other NEAT-containing heme-binding proteins also localized in the cell wall.
Pssm-ID: 274705 [Multi-domain] Cd Length: 217 Bit Score: 302.59 E-value: 4.99e-105
Iron Transport-associated domain; NEAT domains are heme and/or hemoprotein-binding modules ...
31-146
5.54e-46
Iron Transport-associated domain; NEAT domains are heme and/or hemoprotein-binding modules highly conserved in secondary structure. They have roles in hemoprotein binding, heme extraction and heme transfer
Pssm-ID: 428269 [Multi-domain] Cd Length: 116 Bit Score: 148.95 E-value: 5.54e-46
NEAr Transport domain, a component of cell surface proteins; NEAr Transporter (NEAT) domain; ...
34-150
4.68e-37
NEAr Transport domain, a component of cell surface proteins; NEAr Transporter (NEAT) domain; used by pathogenic bacteria to to scavenge heme-iron from host hemoproteins. The NEAT domain is a component of cell surface proteins (iron regulated surface determinants, or Isd, such as IsdA and IsdC) in various gram-positive bacteria, and may be arranged in tandem repeats.
Pssm-ID: 132993 [Multi-domain] Cd Length: 117 Bit Score: 126.27 E-value: 4.68e-37
sortase B cell surface sorting signal; Two different classes of sorting signal, both analogous ...
206-234
1.92e-11
sortase B cell surface sorting signal; Two different classes of sorting signal, both analogous to the sortase A signal LPXTG, may be recognized by the sortase SrtB. These are given as NXZTN and NPKXZ. Proteins sorted by this class of sortase are less common than the sortase A and LPXTG system. This model describes a number of cell surface protein C-terminal regions from Gram-positive bacteria that appear to be sortase B (SrtB) sorting signals.
Pssm-ID: 213766 Cd Length: 29 Bit Score: 56.83 E-value: 1.92e-11
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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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.
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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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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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