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Conserved domains on  [gi|122725150|gb|ABM66464|]
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cell division FtsZ protein, partial [Grimontia hollisae]

Protein Classification

cell division protein FtsZ( domain architecture ID 11415192)

cell division protein FtsZ assembles into a Z ring that provides the framework for the cell division apparatus

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FtsZ COG0206
Cell division GTPase FtsZ [Cell cycle control, cell division, chromosome partitioning];
1-178 8.19e-97

Cell division GTPase FtsZ [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 439976 [Multi-domain]  Cd Length: 347  Bit Score: 283.93  E-value: 8.19e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150   1 EGVEFITVNTDAQALRKTSVSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADMVFIAAGMGGGTGTGAAP 80
Cdd:COG0206   36 EGVEFIAANTDAQALENSKAPTKIQLGEKLTRGLGAGANPEVGRKAAEESREEIREALEGADMVFITAGMGGGTGTGAAP 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150  81 VIAEVAKELGILTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLGRGITLLDAFAKANDVLRNAVQ 160
Cdd:COG0206  116 VIAEIAKELGALTVGVVTKPFSFEGKRRMRQAEEGIEELRKYVDTLIVIPNDKLLEVADKNTPLLEAFKKADDVLRQAVQ 195
                        170
                 ....*....|....*...
gi 122725150 161 GIAELITRPGLINVDFAD 178
Cdd:COG0206  196 GITDLITKPGLINLDFAD 213
 
Name Accession Description Interval E-value
FtsZ COG0206
Cell division GTPase FtsZ [Cell cycle control, cell division, chromosome partitioning];
1-178 8.19e-97

Cell division GTPase FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439976 [Multi-domain]  Cd Length: 347  Bit Score: 283.93  E-value: 8.19e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150   1 EGVEFITVNTDAQALRKTSVSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADMVFIAAGMGGGTGTGAAP 80
Cdd:COG0206   36 EGVEFIAANTDAQALENSKAPTKIQLGEKLTRGLGAGANPEVGRKAAEESREEIREALEGADMVFITAGMGGGTGTGAAP 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150  81 VIAEVAKELGILTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLGRGITLLDAFAKANDVLRNAVQ 160
Cdd:COG0206  116 VIAEIAKELGALTVGVVTKPFSFEGKRRMRQAEEGIEELRKYVDTLIVIPNDKLLEVADKNTPLLEAFKKADDVLRQAVQ 195
                        170
                 ....*....|....*...
gi 122725150 161 GIAELITRPGLINVDFAD 178
Cdd:COG0206  196 GITDLITKPGLINLDFAD 213
FtsZ_type1 cd02201
Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the ...
1-178 1.00e-89

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: 264.26  E-value: 1.00e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150   1 EGVEFITVNTDAQALRKTSVSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADMVFIAAGMGGGTGTGAAP 80
Cdd:cd02201   25 EGVEFIAINTDAQALEKSKAPNKIQIGEKLTRGLGAGGDPEVGRKAAEESREEIKEALKGADMVFITAGMGGGTGTGAAP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150  81 VIAEVAKELGILTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLGRGITLLDAFAKANDVLRNAVQ 160
Cdd:cd02201  105 VIAKIAKEMGALTVAVVTLPFSFEGKKRMRNAEEGLEELKKYVDTLIVIPNDKLLEIVGKNLPLLEAFKKADEVLAQAVK 184
                        170
                 ....*....|....*...
gi 122725150 161 GIAELITRPGLINVDFAD 178
Cdd:cd02201  185 GITDLITKPGLINLDFAD 202
ftsZ TIGR00065
cell division protein FtsZ; This family consists of cell division protein FtsZ, a GTPase found ...
1-178 7.05e-79

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: 238.37  E-value: 7.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150    1 EGVEFITVNTDAQALRKTSVSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADMVFIAAGMGGGTGTGAAP 80
Cdd:TIGR00065  42 EGVEFIAINTDAQHLKTTKADKKILIGKKLTRGLGAGGNPEIGRKAAEESRDEIRKLLEGADMVFITAGMGGGTGTGAAP 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150   81 VIAEVAKELGILTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLGRgITLLDAFAKANDVLRNAVQ 160
Cdd:TIGR00065 122 VVAKIAKELGALTVAVVTKPFKFEGLKRRKKAEEGLERLKQAVDTLIVIPNDKLLEVVPN-LPLNDAFKVADDVLVRAVK 200
                         170
                  ....*....|....*...
gi 122725150  161 GIAELITRPGLINVDFAD 178
Cdd:TIGR00065 201 GISELITKPGLINIDFAD 218
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
2-170 3.51e-69

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: 208.11  E-value: 3.51e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150     2 GVEFITVNTDAQALRKTS-VSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADMVFIAAGMGGGTGTGAAP 80
Cdd:smart00864  23 VIDGVRANTDAQALNPESlASGKIQAGNNWTRGLGAGADPEVGREAAEESLDEIREELEGADGVFITAGMGGGTGTGAAP 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150    81 VIAEVAKELGILTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLGRGITLLDAFAKANDVLRNAVQ 160
Cdd:smart00864 103 VIAEIAKEYGILTVAVVTKPFSFEGVVRPYNAELGLEELREHVDSLIVIDNDALLDICGRKLPLRPAFKDANDLLAQAVS 182
                          170
                   ....*....|
gi 122725150   161 GIAELITRPG 170
Cdd:smart00864 183 GITDLIRFPG 192
PRK13018 PRK13018
cell division protein FtsZ; Provisional
1-178 5.80e-65

cell division protein FtsZ; Provisional


Pssm-ID: 237273 [Multi-domain]  Cd Length: 378  Bit Score: 203.70  E-value: 5.80e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150   1 EGVEFITVNTDAQALRKTSVSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADMVFIAAGMGGGTGTGAAP 80
Cdd:PRK13018  53 EGAETIAINTDAQHLAMIKADKKILIGKSLTRGLGAGGDPEVGRKAAEESRDEIKEVLKGADLVFVTAGMGGGTGTGAAP 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150  81 VIAEVAKELGILTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLgRGITLLDAFAKANDVLRNAVQ 160
Cdd:PRK13018 133 VVAEIAKEQGALVVGVVTKPFKFEGRARMQKAEEGIERLREAADTVIVIDNNRLLDIV-PNLPIADAFSVADEVIAETVK 211
                        170
                 ....*....|....*...
gi 122725150 161 GIAELITRPGLINVDFAD 178
Cdd:PRK13018 212 GITETITKPSLINLDFAD 229
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
6-139 2.94e-30

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: 108.84  E-value: 2.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150    6 ITVNTDAQALRKTSVSTV---IQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADM---VFIAAGMGGGTGTGAA 79
Cdd:pfam00091  48 LAIDTDPQALNEIKAGFNpnkILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMlqgFFITASLGGGTGSGAA 127
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122725150   80 PVIAEVAKEL--GILTVAVVTKPFSF-EGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLG 139
Cdd:pfam00091 128 PVIAEILKELypGALTVAVVTFPFGFsEGVVRPYNAILGLKELIEHSDSVIVIDNDALYDICD 190
 
Name Accession Description Interval E-value
FtsZ COG0206
Cell division GTPase FtsZ [Cell cycle control, cell division, chromosome partitioning];
1-178 8.19e-97

Cell division GTPase FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439976 [Multi-domain]  Cd Length: 347  Bit Score: 283.93  E-value: 8.19e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150   1 EGVEFITVNTDAQALRKTSVSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADMVFIAAGMGGGTGTGAAP 80
Cdd:COG0206   36 EGVEFIAANTDAQALENSKAPTKIQLGEKLTRGLGAGANPEVGRKAAEESREEIREALEGADMVFITAGMGGGTGTGAAP 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150  81 VIAEVAKELGILTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLGRGITLLDAFAKANDVLRNAVQ 160
Cdd:COG0206  116 VIAEIAKELGALTVGVVTKPFSFEGKRRMRQAEEGIEELRKYVDTLIVIPNDKLLEVADKNTPLLEAFKKADDVLRQAVQ 195
                        170
                 ....*....|....*...
gi 122725150 161 GIAELITRPGLINVDFAD 178
Cdd:COG0206  196 GITDLITKPGLINLDFAD 213
FtsZ_type1 cd02201
Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the ...
1-178 1.00e-89

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: 264.26  E-value: 1.00e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150   1 EGVEFITVNTDAQALRKTSVSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADMVFIAAGMGGGTGTGAAP 80
Cdd:cd02201   25 EGVEFIAINTDAQALEKSKAPNKIQIGEKLTRGLGAGGDPEVGRKAAEESREEIKEALKGADMVFITAGMGGGTGTGAAP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150  81 VIAEVAKELGILTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLGRGITLLDAFAKANDVLRNAVQ 160
Cdd:cd02201  105 VIAKIAKEMGALTVAVVTLPFSFEGKKRMRNAEEGLEELKKYVDTLIVIPNDKLLEIVGKNLPLLEAFKKADEVLAQAVK 184
                        170
                 ....*....|....*...
gi 122725150 161 GIAELITRPGLINVDFAD 178
Cdd:cd02201  185 GITDLITKPGLINLDFAD 202
ftsZ TIGR00065
cell division protein FtsZ; This family consists of cell division protein FtsZ, a GTPase found ...
1-178 7.05e-79

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: 238.37  E-value: 7.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150    1 EGVEFITVNTDAQALRKTSVSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADMVFIAAGMGGGTGTGAAP 80
Cdd:TIGR00065  42 EGVEFIAINTDAQHLKTTKADKKILIGKKLTRGLGAGGNPEIGRKAAEESRDEIRKLLEGADMVFITAGMGGGTGTGAAP 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150   81 VIAEVAKELGILTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLGRgITLLDAFAKANDVLRNAVQ 160
Cdd:TIGR00065 122 VVAKIAKELGALTVAVVTKPFKFEGLKRRKKAEEGLERLKQAVDTLIVIPNDKLLEVVPN-LPLNDAFKVADDVLVRAVK 200
                         170
                  ....*....|....*...
gi 122725150  161 GIAELITRPGLINVDFAD 178
Cdd:TIGR00065 201 GISELITKPGLINIDFAD 218
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
2-170 3.51e-69

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: 208.11  E-value: 3.51e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150     2 GVEFITVNTDAQALRKTS-VSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADMVFIAAGMGGGTGTGAAP 80
Cdd:smart00864  23 VIDGVRANTDAQALNPESlASGKIQAGNNWTRGLGAGADPEVGREAAEESLDEIREELEGADGVFITAGMGGGTGTGAAP 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150    81 VIAEVAKELGILTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLGRGITLLDAFAKANDVLRNAVQ 160
Cdd:smart00864 103 VIAEIAKEYGILTVAVVTKPFSFEGVVRPYNAELGLEELREHVDSLIVIDNDALLDICGRKLPLRPAFKDANDLLAQAVS 182
                          170
                   ....*....|
gi 122725150   161 GIAELITRPG 170
Cdd:smart00864 183 GITDLIRFPG 192
PRK13018 PRK13018
cell division protein FtsZ; Provisional
1-178 5.80e-65

cell division protein FtsZ; Provisional


Pssm-ID: 237273 [Multi-domain]  Cd Length: 378  Bit Score: 203.70  E-value: 5.80e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150   1 EGVEFITVNTDAQALRKTSVSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADMVFIAAGMGGGTGTGAAP 80
Cdd:PRK13018  53 EGAETIAINTDAQHLAMIKADKKILIGKSLTRGLGAGGDPEVGRKAAEESRDEIKEVLKGADLVFVTAGMGGGTGTGAAP 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150  81 VIAEVAKELGILTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLgRGITLLDAFAKANDVLRNAVQ 160
Cdd:PRK13018 133 VVAEIAKEQGALVVGVVTKPFKFEGRARMQKAEEGIERLREAADTVIVIDNNRLLDIV-PNLPIADAFSVADEVIAETVK 211
                        170
                 ....*....|....*...
gi 122725150 161 GIAELITRPGLINVDFAD 178
Cdd:PRK13018 212 GITETITKPSLINLDFAD 229
FtsZ_CetZ-like cd02191
Subfamily of FitZ and Cell-structure-related euryarchaeota tubulin/FtsZ homolog-like; FtsZ is ...
2-178 9.10e-54

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: 172.74  E-value: 9.10e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150   2 GVEFITVNTDAQALRKTSVSTVIQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEG---ADMVFIAAGMGGGTGTGA 78
Cdd:cd02191   31 GVETVAINTAAQDLKSLKAKETLLIGQDRTNGHGVGGNPELGAQAAEEDQEEIMEALEGrveADMIFVTTGLGGGTGSGG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150  79 APVIAEVAKELGI-LTVAVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLGrgiTLLDAFAKANDVLRN 157
Cdd:cd02191  111 APVLAEALKKVYDvLTVAVVTLPFADEGALYMQNAGEGLRTLAEEADALILVDNEKLRSIGG---SLSEAYDAINEVLAR 187
                        170       180
                 ....*....|....*....|.
gi 122725150 158 AVQGIAELITRPGLINVDFAD 178
Cdd:cd02191  188 RVGGLLEAIEATGLSVVDFAD 208
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
6-139 2.94e-30

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: 108.84  E-value: 2.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150    6 ITVNTDAQALRKTSVSTV---IQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEGADM---VFIAAGMGGGTGTGAA 79
Cdd:pfam00091  48 LAIDTDPQALNEIKAGFNpnkILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMlqgFFITASLGGGTGSGAA 127
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122725150   80 PVIAEVAKEL--GILTVAVVTKPFSF-EGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKVLG 139
Cdd:pfam00091 128 PVIAEILKELypGALTVAVVTFPFGFsEGVVRPYNAILGLKELIEHSDSVIVIDNDALYDICD 190
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
30-176 5.44e-10

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: 57.03  E-value: 5.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150  30 ITKGLGAGANPQVGRESA-MEDREAIKAELE-------GADMVFIAAGMGGGTGTGAAPVIAEVAKEL--GILTVAVVTK 99
Cdd:cd00286   52 IQKYHGAGNNWAKGHSVAgEEYQEEILDAIRkeveecdELQGFFITHSLGGGTGSGLGPLLAERLKDEypNRLVVTFSIL 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122725150 100 PFSFEGKK-RMAFAEQGIDELSKHVDSLITIPNEKLLKVLGRGITLLD-AFAKANDVLRNAVQGIAELITRPGLINVDF 176
Cdd:cd00286  132 PGPDEGVIvYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDApAYDHINELVAQRLGSLTEALRFEGSLNVDL 210
CetZ_tubulin-like cd02202
Cell-structure-related euryarchaeota tubulin/FtsZ homologs; CetZ proteins comprise a distinct ...
3-152 4.79e-09

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: 54.17  E-value: 4.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122725150   3 VEFITVNTDAQALRKTSVSTV---IQIGGDITKGLGAGANPQVGRESAMEDREAIKAELEG-----ADMVFIAAGMGGGT 74
Cdd:cd02202   32 VNALAVNTDRADLSGLDHIPEerrILIGDTETGGHGVGGDNELGAEVAEEDIDELLRALDTapfseADAFLVVAGLGGGT 111
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122725150  75 GTGAAPVIAEVAKELGILTV-AVVTKPFSFEGKKRMAFAEQGIDELSKHVDSLITIPNEKLLKvlgRGITLLDAFAKAN 152
Cdd:cd02202  112 GSGAAPVLAEELKERYDKPVyALGVLPAAEEGGRYALNAARSLRSLVELADAVILFDNDAWRR---SGESIAEAYDRIN 187
 
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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