Stage IV sporulation protein SpoIVA, required for spore cortex formation and coat assembly ...
1-492
0e+00
Stage IV sporulation protein SpoIVA, required for spore cortex formation and coat assembly [Cell cycle control, cell division, chromosome partitioning];
:
Pssm-ID: 444533 [Multi-domain] Cd Length: 492 Bit Score: 936.12 E-value: 0e+00
Stage IV sporulation protein SpoIVA, required for spore cortex formation and coat assembly ...
1-492
0e+00
Stage IV sporulation protein SpoIVA, required for spore cortex formation and coat assembly [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444533 [Multi-domain] Cd Length: 492 Bit Score: 936.12 E-value: 0e+00
stage IV sporulation protein A; A comparative genome analysis of all sequenced genomes of ...
1-492
0e+00
stage IV sporulation protein A; A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This protein, a member of this panel, is designated stage IV sporulation protein A. It acts in the mother cell compartment and plays a role in spore coat morphogenesis. [Cellular processes, Sporulation and germination]
Pssm-ID: 131883 [Multi-domain] Cd Length: 492 Bit Score: 861.80 E-value: 0e+00
Stage IV sporulation protein A, ATPase domain; SpoIVA is designated stage IV sporulation ...
1-237
2.70e-169
Stage IV sporulation protein A, ATPase domain; SpoIVA is designated stage IV sporulation protein A. It acts in the mother cell compartment and plays a role in spore coat morphogenesis. A comparative genome analysis of all sequenced genomes of Firmicutes shows that the proteins are strictly conserved among the sub-set of endospore-forming species. This protein assembles into static polymers driven by ATP hydrolysis and is anchored to the outer forespore membrane through its C-terminal domain. This entry represents the ATPase domain located at the N-terminal of SpoIVA. It contains a conserved 'sensor' threonine residue that is involved in coordinating a Mg+2 ion.
Pssm-ID: 462826 Cd Length: 237 Bit Score: 476.55 E-value: 2.70e-169
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
21-217
5.20e-03
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 37.82 E-value: 5.20e-03
Stage IV sporulation protein SpoIVA, required for spore cortex formation and coat assembly ...
1-492
0e+00
Stage IV sporulation protein SpoIVA, required for spore cortex formation and coat assembly [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444533 [Multi-domain] Cd Length: 492 Bit Score: 936.12 E-value: 0e+00
stage IV sporulation protein A; A comparative genome analysis of all sequenced genomes of ...
1-492
0e+00
stage IV sporulation protein A; A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This protein, a member of this panel, is designated stage IV sporulation protein A. It acts in the mother cell compartment and plays a role in spore coat morphogenesis. [Cellular processes, Sporulation and germination]
Pssm-ID: 131883 [Multi-domain] Cd Length: 492 Bit Score: 861.80 E-value: 0e+00
Stage IV sporulation protein A, ATPase domain; SpoIVA is designated stage IV sporulation ...
1-237
2.70e-169
Stage IV sporulation protein A, ATPase domain; SpoIVA is designated stage IV sporulation protein A. It acts in the mother cell compartment and plays a role in spore coat morphogenesis. A comparative genome analysis of all sequenced genomes of Firmicutes shows that the proteins are strictly conserved among the sub-set of endospore-forming species. This protein assembles into static polymers driven by ATP hydrolysis and is anchored to the outer forespore membrane through its C-terminal domain. This entry represents the ATPase domain located at the N-terminal of SpoIVA. It contains a conserved 'sensor' threonine residue that is involved in coordinating a Mg+2 ion.
Pssm-ID: 462826 Cd Length: 237 Bit Score: 476.55 E-value: 2.70e-169
Stage IV sporulation protein A, middle domain; This is the structural middle domain of Stage ...
238-416
1.20e-91
Stage IV sporulation protein A, middle domain; This is the structural middle domain of Stage IV sporulation protein A (SpoIVA) which follows the ATPase domain and the predicted secondary structure suggests that it is composed of two symmetrical units containing alpha-helices and beta-strands. SpoIVA acts in the mother cell compartment and plays a role in spore coat morphogenesis. A comparative genome analysis of all sequenced genomes of Firmicutes shows that the proteins are strictly conserved among the sub-set of endospore-forming species.
Pssm-ID: 466587 Cd Length: 179 Bit Score: 276.59 E-value: 1.20e-91
Sporulation stage IV protein A, C-terminal; SpoIVA (Sporulation stage IV protein A) acts in ...
417-492
3.03e-41
Sporulation stage IV protein A, C-terminal; SpoIVA (Sporulation stage IV protein A) acts in the mother cell compartment and plays a role in spore coat morphogenesis. A comparative genome analysis of all sequenced genomes of Firmicutes shows that the proteins are strictly conserved among the sub-set of endospore-forming species. This entry represents the C-terminal domain of SpoIVA, which plays a key role in targeting the protein to the outer forespore membrane, in particular the five hydrophobic residues at the extreme C-terminal are essential for this function. Structure predictions suggest that it has three conserved alpha helices followed by a beta-hairpin.
Pssm-ID: 466588 [Multi-domain] Cd Length: 76 Bit Score: 142.20 E-value: 3.03e-41
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
21-217
5.20e-03
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 37.82 E-value: 5.20e-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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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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