cell division protein ZipA; This model represents the full length of bacterial cell division ...
4-277
9.17e-129
cell division protein ZipA; This model represents the full length of bacterial cell division protein ZipA. The N-terminal hydrophobic stretch is an uncleaved signal-anchor sequence. This is followed by an unconserved, variable length, low complexity region, and then a conserved C-terminal region of about 140 amino acids (see pfam04354) that interacts with the tubulin-like cell division protein FtsZ. [Cellular processes, Cell division]
:
Pssm-ID: 274030 [Multi-domain] Cd Length: 284 Bit Score: 367.31 E-value: 9.17e-129
cell division protein ZipA; This model represents the full length of bacterial cell division ...
4-277
9.17e-129
cell division protein ZipA; This model represents the full length of bacterial cell division protein ZipA. The N-terminal hydrophobic stretch is an uncleaved signal-anchor sequence. This is followed by an unconserved, variable length, low complexity region, and then a conserved C-terminal region of about 140 amino acids (see pfam04354) that interacts with the tubulin-like cell division protein FtsZ. [Cellular processes, Cell division]
Pssm-ID: 274030 [Multi-domain] Cd Length: 284 Bit Score: 367.31 E-value: 9.17e-129
ZipA C-terminal domain. ZipA, a membrane-anchored protein, is one of at least nine essential ...
148-277
9.96e-70
ZipA C-terminal domain. ZipA, a membrane-anchored protein, is one of at least nine essential gene products necessary for assembly of the septal ring which mediates cell division in E.coli. ZipA and FtsA directly bind FtsZ, a homolog of eukaryotic tubulins, at the prospective division site, followed by the sequential addition of FtsK, FtsQ, FtsL, FtsW, FtsI, and FtsN. ZipA contains three domains: a short N-terminal membrane-anchored domain, a central P/Q domain that is rich in proline and glutamine and a C-terminal domain, which comprises almost half the protein.
Pssm-ID: 238142 Cd Length: 130 Bit Score: 211.84 E-value: 9.96e-70
ZipA, C-terminal FtsZ-binding domain; This family represents the ZipA C-terminal domain. ZipA ...
150-276
3.94e-61
ZipA, C-terminal FtsZ-binding domain; This family represents the ZipA C-terminal domain. ZipA is involved in septum formation in bacterial cell division. Its C-terminal domain binds FtsZ, a major component of the bacterial septal ring. The structure of this domain is an alpha-beta fold with three alpha helices and a beta sheet of six antiparallel beta strands. The major loops protruding from the beta sheet surface are thought to form a binding site for FtsZ.
Pssm-ID: 427889 Cd Length: 127 Bit Score: 189.63 E-value: 3.94e-61
ZipA, C-terminal domain (FtsZ-binding); C-terminal domain of ZipA, a component of cell ...
148-277
8.95e-61
ZipA, C-terminal domain (FtsZ-binding); C-terminal domain of ZipA, a component of cell division in E.coli. It interacts with the FtsZ protein in one of the initial steps of septum formation. The structure of this domain is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands.
Pssm-ID: 129010 Cd Length: 131 Bit Score: 189.02 E-value: 8.95e-61
cell division protein ZipA; This model represents the full length of bacterial cell division ...
4-277
9.17e-129
cell division protein ZipA; This model represents the full length of bacterial cell division protein ZipA. The N-terminal hydrophobic stretch is an uncleaved signal-anchor sequence. This is followed by an unconserved, variable length, low complexity region, and then a conserved C-terminal region of about 140 amino acids (see pfam04354) that interacts with the tubulin-like cell division protein FtsZ. [Cellular processes, Cell division]
Pssm-ID: 274030 [Multi-domain] Cd Length: 284 Bit Score: 367.31 E-value: 9.17e-129
ZipA C-terminal domain. ZipA, a membrane-anchored protein, is one of at least nine essential ...
148-277
9.96e-70
ZipA C-terminal domain. ZipA, a membrane-anchored protein, is one of at least nine essential gene products necessary for assembly of the septal ring which mediates cell division in E.coli. ZipA and FtsA directly bind FtsZ, a homolog of eukaryotic tubulins, at the prospective division site, followed by the sequential addition of FtsK, FtsQ, FtsL, FtsW, FtsI, and FtsN. ZipA contains three domains: a short N-terminal membrane-anchored domain, a central P/Q domain that is rich in proline and glutamine and a C-terminal domain, which comprises almost half the protein.
Pssm-ID: 238142 Cd Length: 130 Bit Score: 211.84 E-value: 9.96e-70
ZipA, C-terminal FtsZ-binding domain; This family represents the ZipA C-terminal domain. ZipA ...
150-276
3.94e-61
ZipA, C-terminal FtsZ-binding domain; This family represents the ZipA C-terminal domain. ZipA is involved in septum formation in bacterial cell division. Its C-terminal domain binds FtsZ, a major component of the bacterial septal ring. The structure of this domain is an alpha-beta fold with three alpha helices and a beta sheet of six antiparallel beta strands. The major loops protruding from the beta sheet surface are thought to form a binding site for FtsZ.
Pssm-ID: 427889 Cd Length: 127 Bit Score: 189.63 E-value: 3.94e-61
ZipA, C-terminal domain (FtsZ-binding); C-terminal domain of ZipA, a component of cell ...
148-277
8.95e-61
ZipA, C-terminal domain (FtsZ-binding); C-terminal domain of ZipA, a component of cell division in E.coli. It interacts with the FtsZ protein in one of the initial steps of septum formation. The structure of this domain is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands.
Pssm-ID: 129010 Cd Length: 131 Bit Score: 189.02 E-value: 8.95e-61
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
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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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