FtsZ/tubulin family protein may be involved in polymer formation, similar to the cell-division GTPase FtsZ or the tubulin-like filament-forming GTPase TubZ
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
11-277
1.81e-14
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.
The actual alignment was detected with superfamily member cd02201:
Pssm-ID: 471962 [Multi-domain] Cd Length: 303 Bit Score: 72.05 E-value: 1.81e-14
Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the ...
11-277
1.81e-14
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: 72.05 E-value: 1.81e-14
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
176-282
2.44e-07
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: 48.31 E-value: 2.44e-07
FtsZ family, C-terminal domain; This family includes the bacterial FtsZ family of proteins. ...
197-279
4.39e-05
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: 41.42 E-value: 4.39e-05
Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the ...
11-277
1.81e-14
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: 72.05 E-value: 1.81e-14
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
176-282
2.44e-07
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: 48.31 E-value: 2.44e-07
FtsZ family, C-terminal domain; This family includes the bacterial FtsZ family of proteins. ...
197-279
4.39e-05
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: 41.42 E-value: 4.39e-05
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.
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