Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the ...
32-323
6.31e-134
Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the eukaryotic tubulins and is essential for cell division in prokaryotes. FtsZ is capable of polymerizing in a GTP-driven process into structures similar to those formed by tubulin. FtsZ forms a ring-shaped septum at the site of bacterial cell division, which is required for constriction of cell membrane and cell envelope to yield two daughter cells.
Pssm-ID: 276961 [Multi-domain] Cd Length: 303 Bit Score: 387.14 E-value: 6.31e-134
cell division protein FtsZ; This family consists of cell division protein FtsZ, a GTPase found ...
32-324
6.48e-101
cell division protein FtsZ; This family consists of cell division protein FtsZ, a GTPase found in bacteria, the chloroplast of plants, and in archaebacteria. Structurally similar to tubulin, FtsZ undergoes GTP-dependent polymerization into filaments that form a cytoskeleton involved in septum synthesis. [Cellular processes, Cell division]
Pssm-ID: 272884 [Multi-domain] Cd Length: 349 Bit Score: 304.62 E-value: 6.48e-101
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
32-213
9.85e-56
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the bacterial FtsZ family of proteins. These proteins are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division, it is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases, this entry is the GTPase domain. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea.
Pssm-ID: 214867 [Multi-domain] Cd Length: 192 Bit Score: 183.07 E-value: 9.85e-56
FtsZ family, C-terminal domain; This family includes the bacterial FtsZ family of proteins. ...
230-325
3.77e-30
FtsZ family, C-terminal domain; This family includes the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ is a GTPase, like tubulin. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea.
Pssm-ID: 463534 [Multi-domain] Cd Length: 95 Bit Score: 112.30 E-value: 3.77e-30
Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the ...
32-323
6.31e-134
Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the eukaryotic tubulins and is essential for cell division in prokaryotes. FtsZ is capable of polymerizing in a GTP-driven process into structures similar to those formed by tubulin. FtsZ forms a ring-shaped septum at the site of bacterial cell division, which is required for constriction of cell membrane and cell envelope to yield two daughter cells.
Pssm-ID: 276961 [Multi-domain] Cd Length: 303 Bit Score: 387.14 E-value: 6.31e-134
cell division protein FtsZ; This family consists of cell division protein FtsZ, a GTPase found ...
32-324
6.48e-101
cell division protein FtsZ; This family consists of cell division protein FtsZ, a GTPase found in bacteria, the chloroplast of plants, and in archaebacteria. Structurally similar to tubulin, FtsZ undergoes GTP-dependent polymerization into filaments that form a cytoskeleton involved in septum synthesis. [Cellular processes, Cell division]
Pssm-ID: 272884 [Multi-domain] Cd Length: 349 Bit Score: 304.62 E-value: 6.48e-101
Subfamily of FitZ and Cell-structure-related euryarchaeota tubulin/FtsZ homolog-like; FtsZ is ...
32-323
4.29e-59
Subfamily of FitZ and Cell-structure-related euryarchaeota tubulin/FtsZ homolog-like; FtsZ is a GTPase that is similar to the eukaryotic tubulins and is essential for cell division in prokaryotes. CetZ-like proteins are related to tubulin and FtsZ and co-exists with FtsZ in many archaea. However, a recent study found that Cetz proteins (formerly annotated FtsZ type 2) are not required for cell division. Instead, CetZ proteins are shown to be involved in controlling archaeal cell shape dynamics. The results from inactivation studies of CetZ proteins in Haloferax volcanii suggest that CetZ1 is essential for normal swimming motility and rod-cell development.
Pssm-ID: 276960 [Multi-domain] Cd Length: 308 Bit Score: 195.86 E-value: 4.29e-59
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
32-213
9.85e-56
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the bacterial FtsZ family of proteins. These proteins are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division, it is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases, this entry is the GTPase domain. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea.
Pssm-ID: 214867 [Multi-domain] Cd Length: 192 Bit Score: 183.07 E-value: 9.85e-56
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
215-326
1.24e-41
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. These proteins are GTPases and are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division, it is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea. This is the C-terminal domain.
Pssm-ID: 214868 [Multi-domain] Cd Length: 120 Bit Score: 143.46 E-value: 1.24e-41
FtsZ family, C-terminal domain; This family includes the bacterial FtsZ family of proteins. ...
230-325
3.77e-30
FtsZ family, C-terminal domain; This family includes the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ is a GTPase, like tubulin. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea.
Pssm-ID: 463534 [Multi-domain] Cd Length: 95 Bit Score: 112.30 E-value: 3.77e-30
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
43-182
2.39e-24
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules.
Pssm-ID: 459669 [Multi-domain] Cd Length: 190 Bit Score: 99.60 E-value: 2.39e-24
Cell-structure-related euryarchaeota tubulin/FtsZ homologs; CetZ proteins comprise a distinct ...
46-323
9.64e-11
Cell-structure-related euryarchaeota tubulin/FtsZ homologs; CetZ proteins comprise a distinct tubulin/FtsZ family. The crystal structures of CetZ contain the FtsZ/tubulin superfamily fold and its family members have mosaic of tubulin-like and FtsZ-like amino acid residues. However, a recent study found that CetZ proteins (formerly annotated FtsZ type 2) are not required for cell division, whereas FtsZ proteins play an important role. Instead, CetZ proteins are shown to be involved in controlling archaeal cell shape dynamics. The results from inactivation studies of CetZ proteins in Haloferax volcanii suggest that CetZ1 is essential for normal swimming motility and rod-cell development.
Pssm-ID: 276962 [Multi-domain] Cd Length: 357 Bit Score: 63.03 E-value: 9.64e-11
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
49-323
1.63e-06
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, gamma-, delta-, epsilon, and zeta-tubulins as well as FtsZ and CetZ, all of which are involved in polymer formation. Tubulin is the major component of microtubules, but also exists as a heterodimer and as a curved oligomer. Microtubules exist in all eukaryotic cells and are responsible for many functions, including cellular transport, cell motility, and mitosis. FtsZ forms a ring-shaped septum at the site of bacterial cell division, which is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria, archaea, and chloroplasts. A recent study found that CetZ proteins, formerly annotated FtsZ type 2, are not required for cell division, whereas FtsZ proteins play an important role. Instead, CetZ proteins are shown to be involved in controlling archaeal cell shape dynamics. The results from inactivation studies of CetZ proteins in Haloferax volcanii suggest that CetZ1 is essential for normal swimming motility and rod-cell development.
Pssm-ID: 276954 [Multi-domain] Cd Length: 332 Bit Score: 49.71 E-value: 1.63e-06
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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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,
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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.
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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
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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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