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Conserved domains on  [gi|75399196|sp|Q8KNP3|]
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RecName: Full=Tubulin-like protein TubZ; AltName: Full=FtsZ-like protein TubZ-Bt

Protein Classification

FtsZ/tubulin family protein( domain architecture ID 3)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tubulin_FtsZ_Cetz-like super family cl10017
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
24-319 3.42e-08

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 cd02202:

Pssm-ID: 471962 [Multi-domain]  Cd Length: 357  Bit Score: 55.33  E-value: 3.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196  24 RWGVIGAGQKGNKEADLFAGYKFSNGTTCYP-TLAVNFAESDMMHLQNIIKEDRIHFdglkgaartpsvvtdlfdPETNP 102
Cdd:cd02202   2 KLAVIGVGQAGGRIADALLRAERRSGRSIVVnALAVNTDRADLSGLDHIPEERRILI------------------GDTET 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196 103 NANGyLDKLaQELGRKFTNEEGEVI-----------VDQFLICLGAGGGVGTGWGSLVLQLIREqFFPCPVSMLISLPSG 171
Cdd:cd02202  64 GGHG-VGGD-NELGAEVAEEDIDELlraldtapfseADAFLVVAGLGGGTGSGAAPVLAEELKE-RYDKPVYALGVLPAA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196 172 DPDEIN--NALVLLseiDEFMREQDrlfgnsdikplaNVIVNDNTQMQRIIESQKGTKDLKNRyvnwkEVAnDNVVSTLH 249
Cdd:cd02202 141 EEGGRYalNAARSL---RSLVELAD------------AVILFDNDAWRRSGESIAEAYDRINE-----EIA-ERLGALLA 199
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196 250 EINIIPENYGSDNVTyDPSDLIKLLSiPGRFLTIGKARiakfdlHSLENSIKRSLDEGFFSAEHQFETAT 319
Cdd:cd02202 200 AGEVDAPKSVGESVL-DASDIINTLS-GGGVATIGYAS------EDLPTDGRSGSGLLLGESDSDVDEQE 261
 
Name Accession Description Interval E-value
CetZ_tubulin-like cd02202
Cell-structure-related euryarchaeota tubulin/FtsZ homologs; CetZ proteins comprise a distinct ...
24-319 3.42e-08

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: 55.33  E-value: 3.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196  24 RWGVIGAGQKGNKEADLFAGYKFSNGTTCYP-TLAVNFAESDMMHLQNIIKEDRIHFdglkgaartpsvvtdlfdPETNP 102
Cdd:cd02202   2 KLAVIGVGQAGGRIADALLRAERRSGRSIVVnALAVNTDRADLSGLDHIPEERRILI------------------GDTET 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196 103 NANGyLDKLaQELGRKFTNEEGEVI-----------VDQFLICLGAGGGVGTGWGSLVLQLIREqFFPCPVSMLISLPSG 171
Cdd:cd02202  64 GGHG-VGGD-NELGAEVAEEDIDELlraldtapfseADAFLVVAGLGGGTGSGAAPVLAEELKE-RYDKPVYALGVLPAA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196 172 DPDEIN--NALVLLseiDEFMREQDrlfgnsdikplaNVIVNDNTQMQRIIESQKGTKDLKNRyvnwkEVAnDNVVSTLH 249
Cdd:cd02202 141 EEGGRYalNAARSL---RSLVELAD------------AVILFDNDAWRRSGESIAEAYDRINE-----EIA-ERLGALLA 199
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196 250 EINIIPENYGSDNVTyDPSDLIKLLSiPGRFLTIGKARiakfdlHSLENSIKRSLDEGFFSAEHQFETAT 319
Cdd:cd02202 200 AGEVDAPKSVGESVL-DASDIINTLS-GGGVATIGYAS------EDLPTDGRSGSGLLLGESDSDVDEQE 261
 
Name Accession Description Interval E-value
CetZ_tubulin-like cd02202
Cell-structure-related euryarchaeota tubulin/FtsZ homologs; CetZ proteins comprise a distinct ...
24-319 3.42e-08

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: 55.33  E-value: 3.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196  24 RWGVIGAGQKGNKEADLFAGYKFSNGTTCYP-TLAVNFAESDMMHLQNIIKEDRIHFdglkgaartpsvvtdlfdPETNP 102
Cdd:cd02202   2 KLAVIGVGQAGGRIADALLRAERRSGRSIVVnALAVNTDRADLSGLDHIPEERRILI------------------GDTET 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196 103 NANGyLDKLaQELGRKFTNEEGEVI-----------VDQFLICLGAGGGVGTGWGSLVLQLIREqFFPCPVSMLISLPSG 171
Cdd:cd02202  64 GGHG-VGGD-NELGAEVAEEDIDELlraldtapfseADAFLVVAGLGGGTGSGAAPVLAEELKE-RYDKPVYALGVLPAA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196 172 DPDEIN--NALVLLseiDEFMREQDrlfgnsdikplaNVIVNDNTQMQRIIESQKGTKDLKNRyvnwkEVAnDNVVSTLH 249
Cdd:cd02202 141 EEGGRYalNAARSL---RSLVELAD------------AVILFDNDAWRRSGESIAEAYDRINE-----EIA-ERLGALLA 199
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75399196 250 EINIIPENYGSDNVTyDPSDLIKLLSiPGRFLTIGKARiakfdlHSLENSIKRSLDEGFFSAEHQFETAT 319
Cdd:cd02202 200 AGEVDAPKSVGESVL-DASDIINTLS-GGGVATIGYAS------EDLPTDGRSGSGLLLGESDSDVDEQE 261
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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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