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Conserved domains on  [gi|1332784132|ref|WP_102766241|]
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cell division protein FtsZ [Paucibacter aquatile]

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];
3-345 3.29e-128

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


:

Pssm-ID: 439976 [Multi-domain]  Cd Length: 347  Bit Score: 373.68  E-value: 3.29e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   3 IEMIEEFDQGTQIKVIGVGGGGGNAVDHMIAQGVMGVEFICANTDAQALNRSKADQLLQLGST---GLGAGAKPEMGKAA 79
Cdd:COG0206     2 FELDDEEELKAKIKVIGVGGGGGNAVNRMIEAGLEGVEFIAANTDAQALENSKAPTKIQLGEKltrGLGAGANPEVGRKA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  80 AEEAEARIRESIQGAHMLFITAGMGGGTGTGAAPVIARVAKDMGILTVGVVTKPFEFEGGRRSKAADAGLAELEANVDSL 159
Cdd:COG0206    82 AEESREEIREALEGADMVFITAGMGGGTGTGAAPVIAEIAKELGALTVGVVTKPFSFEGKRRMRQAEEGIEELRKYVDTL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 160 IVVLNDKLLDVLGDDVTQDQAFAHANDVLKNAVGGISDIIHIPGLVNVDFEDVKTVMSEPGKAMMGTAQASGPDRAAKAA 239
Cdd:COG0206   162 IVIPNDKLLEVADKNTPLLEAFKKADDVLRQAVQGITDLITKPGLINLDFADVKTVMSNGGVALMGIGEASGENRAEEAA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 240 EAAVACPLLEGIDLSGARGVLVLIAASrANFKLSESRNAMNAIKRYASDDAHVIYGTAYDESLGDALRVTVIATGLSSQR 319
Cdd:COG0206   242 EKAISSPLLEDVSISGAKGVLVNITGG-SDLTLDEVNEAAEIIQEEADPDANIIFGAVIDESLGDEIRVTVIATGFDSEA 320
                         330       340
                  ....*....|....*....|....*.
gi 1332784132 320 ARQQPPLQVVQQTAQTQLRtgtYDVP 345
Cdd:COG0206   321 IVGEEETERPLEETEPAED---LDIP 343
 
Name Accession Description Interval E-value
FtsZ COG0206
Cell division GTPase FtsZ [Cell cycle control, cell division, chromosome partitioning];
3-345 3.29e-128

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


Pssm-ID: 439976 [Multi-domain]  Cd Length: 347  Bit Score: 373.68  E-value: 3.29e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   3 IEMIEEFDQGTQIKVIGVGGGGGNAVDHMIAQGVMGVEFICANTDAQALNRSKADQLLQLGST---GLGAGAKPEMGKAA 79
Cdd:COG0206     2 FELDDEEELKAKIKVIGVGGGGGNAVNRMIEAGLEGVEFIAANTDAQALENSKAPTKIQLGEKltrGLGAGANPEVGRKA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  80 AEEAEARIRESIQGAHMLFITAGMGGGTGTGAAPVIARVAKDMGILTVGVVTKPFEFEGGRRSKAADAGLAELEANVDSL 159
Cdd:COG0206    82 AEESREEIREALEGADMVFITAGMGGGTGTGAAPVIAEIAKELGALTVGVVTKPFSFEGKRRMRQAEEGIEELRKYVDTL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 160 IVVLNDKLLDVLGDDVTQDQAFAHANDVLKNAVGGISDIIHIPGLVNVDFEDVKTVMSEPGKAMMGTAQASGPDRAAKAA 239
Cdd:COG0206   162 IVIPNDKLLEVADKNTPLLEAFKKADDVLRQAVQGITDLITKPGLINLDFADVKTVMSNGGVALMGIGEASGENRAEEAA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 240 EAAVACPLLEGIDLSGARGVLVLIAASrANFKLSESRNAMNAIKRYASDDAHVIYGTAYDESLGDALRVTVIATGLSSQR 319
Cdd:COG0206   242 EKAISSPLLEDVSISGAKGVLVNITGG-SDLTLDEVNEAAEIIQEEADPDANIIFGAVIDESLGDEIRVTVIATGFDSEA 320
                         330       340
                  ....*....|....*....|....*.
gi 1332784132 320 ARQQPPLQVVQQTAQTQLRtgtYDVP 345
Cdd:COG0206   321 IVGEEETERPLEETEPAED---LDIP 343
FtsZ_type1 cd02201
Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the ...
26-314 1.92e-115

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: 339.76  E-value: 1.92e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  26 NAVDHMIAQGVMGVEFICANTDAQALNRSKADQLLQLGST---GLGAGAKPEMGKAAAEEAEARIRESIQGAHMLFITAG 102
Cdd:cd02201    14 NAVNRMIESGLEGVEFIAINTDAQALEKSKAPNKIQIGEKltrGLGAGGDPEVGRKAAEESREEIKEALKGADMVFITAG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 103 MGGGTGTGAAPVIARVAKDMGILTVGVVTKPFEFEGGRRSKAADAGLAELEANVDSLIVVLNDKLLDVLGDDVTQDQAFA 182
Cdd:cd02201    94 MGGGTGTGAAPVIAKIAKEMGALTVAVVTLPFSFEGKKRMRNAEEGLEELKKYVDTLIVIPNDKLLEIVGKNLPLLEAFK 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 183 HANDVLKNAVGGISDIIHIPGLVNVDFEDVKTVMSEPGKAMMGTAQASGPDRAAKAAEAAVACPLLEGiDLSGARGVLVL 262
Cdd:cd02201   174 KADEVLAQAVKGITDLITKPGLINLDFADVKTVMKNGGLALMGIGEASGENRAEEAVEKALNSPLLED-DIKGAKGVLVN 252
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1332784132 263 IAASRaNFKLSESRNAMNAIKRYASDDAHVIYGTAYDESLGDALRVTVIATG 314
Cdd:cd02201   253 ITGGP-DLTLEEVNEAAEIITEKADPDANIIFGAVIDEELGDEIRVTVIATG 303
ftsZ TIGR00065
cell division protein FtsZ; This family consists of cell division protein FtsZ, a GTPase found ...
1-318 3.13e-90

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: 276.89  E-value: 3.13e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   1 MAIEMIEEFDQ-----GTQIKVIGVGGGGGNAVDHMIAQGVMGVEFICANTDAQALNRSKADQLLQLGST---GLGAGAK 72
Cdd:TIGR00065   1 MDEIETEFRELiqpsnKAKIKVIGVGGGGNNTVNRMLEEGVEGVEFIAINTDAQHLKTTKADKKILIGKKltrGLGAGGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  73 PEMGKAAAEEAEARIRESIQGAHMLFITAGMGGGTGTGAAPVIARVAKDMGILTVGVVTKPFEFEGGRRSKAADAGLAEL 152
Cdd:TIGR00065  81 PEIGRKAAEESRDEIRKLLEGADMVFITAGMGGGTGTGAAPVVAKIAKELGALTVAVVTKPFKFEGLKRRKKAEEGLERL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 153 EANVDSLIVVLNDKLLDVLGDDVTQDqAFAHANDVLKNAVGGISDIIHIPGLVNVDFEDVKTVMSEPGKAMMGTAQASGP 232
Cdd:TIGR00065 161 KQAVDTLIVIPNDKLLEVVPNLPLND-AFKVADDVLVRAVKGISELITKPGLINIDFADVRAVMSGGGVAMMGIGEALGE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 233 D---RAAKAAEAAVACPLLEGIDLSGARGVLVLIAASrANFKLSESRNAMNAIKRYASDDAHVIYGTAYDESLGDALRVT 309
Cdd:TIGR00065 240 DtanRAFEAVRKALSSPLLDVDKISGAKGALVHITGG-ADLTLLEAEEIQEIITSELDQDANIIWGAIIDPNLEDEIRVT 318

                  ....*....
gi 1332784132 310 VIATGLSSQ 318
Cdd:TIGR00065 319 IVATGVKSQ 327
PRK13018 PRK13018
cell division protein FtsZ; Provisional
4-317 5.63e-87

cell division protein FtsZ; Provisional


Pssm-ID: 237273 [Multi-domain]  Cd Length: 378  Bit Score: 269.57  E-value: 5.63e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   4 EMIEEFDQGTQIKVIGVGGGGGNAVDHMIAQGVMGVEFICANTDAQALNRSKADQLLQLGST---GLGAGAKPEMGKAAA 80
Cdd:PRK13018   20 KASDDDFGNPKIVVVGCGGAGNNTINRLYEIGIEGAETIAINTDAQHLAMIKADKKILIGKSltrGLGAGGDPEVGRKAA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  81 EEAEARIRESIQGAHMLFITAGMGGGTGTGAAPVIARVAKDMGILTVGVVTKPFEFEGGRRSKAADAGLAELEANVDSLI 160
Cdd:PRK13018  100 EESRDEIKEVLKGADLVFVTAGMGGGTGTGAAPVVAEIAKEQGALVVGVVTKPFKFEGRARMQKAEEGIERLREAADTVI 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 161 VVLNDKLLDVLgDDVTQDQAFAHANDVLKNAVGGISDIIHIPGLVNVDFEDVKTVMSEPGKAMMGTAQASGPDRAAKAAE 240
Cdd:PRK13018  180 VIDNNRLLDIV-PNLPIADAFSVADEVIAETVKGITETITKPSLINLDFADVKSVMKGGGVAMMGVGEAKGQNRAMEAVR 258
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1332784132 241 AAVACPLLEgIDLSGARGVLVLIAASRaNFKLSESRNAMNAIKRYASDDAHVIYGTAYDESLGDALRVTVIATGLSS 317
Cdd:PRK13018  259 AALANPLLD-VDYRGAKGALVHITGGP-DLTLKEANEAASRITEELDPEANIIWGARIDPDMEGKVRVMVIMTGVKS 333
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
15-203 1.62e-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: 184.61  E-value: 1.62e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   15 IKVIGVGGGGGNAVDHMIAQGVmgVEFICANTDAQALNR-SKADQLLQLGST---GLGAGAKPEMGKAAAEEAEARIRES 90
Cdd:smart00864   2 IKVFGVGGGGPNAVNVDLEPGV--IDGVRANTDAQALNPeSLASGKIQAGNNwtrGLGAGADPEVGREAAEESLDEIREE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   91 IQGAHMLFITAGMGGGTGTGAAPVIARVAKDMGILTVGVVTKPFEFEGGRRSKAADAGLAELEANVDSLIVVLNDKLLDV 170
Cdd:smart00864  80 LEGADGVFITAGMGGGTGTGAAPVIAEIAKEYGILTVAVVTKPFSFEGVVRPYNAELGLEELREHVDSLIVIDNDALLDI 159
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1332784132  171 LGDDVTQDQAFAHANDVLKNAVGGISDIIHIPG 203
Cdd:smart00864 160 CGRKLPLRPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
1-172 8.18e-22

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: 92.28  E-value: 8.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   1 MAIEMIEEFDQGTQIKVIGVGGGGGNAVDHmIAQGVMgveficANTDAQALNRSKAD------QLLQLGSTGLGAGAKPE 74
Cdd:pfam00091  14 IGNALWELLCLEHGIDSLNVFFSESGSVEF-IPRSLA------IDTDPQALNEIKAGfnpnkiLLGKEGTGGNGAGGYPE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  75 MGKAAAEEAEARIRESIQGAHML---FITAGMGGGTGTGAAPVIARVAKDM--GILTVGVVTKPFEF-EGGRRSKAADAG 148
Cdd:pfam00091  87 IGREAAEESLEEIRKEVEGCDMLqgfFITASLGGGTGSGAAPVIAEILKELypGALTVAVVTFPFGFsEGVVRPYNAILG 166
                         170       180
                  ....*....|....*....|....
gi 1332784132 149 LAELEANVDSLIVVLNDKLLDVLG 172
Cdd:pfam00091 167 LKELIEHSDSVIVIDNDALYDICD 190
 
Name Accession Description Interval E-value
FtsZ COG0206
Cell division GTPase FtsZ [Cell cycle control, cell division, chromosome partitioning];
3-345 3.29e-128

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


Pssm-ID: 439976 [Multi-domain]  Cd Length: 347  Bit Score: 373.68  E-value: 3.29e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   3 IEMIEEFDQGTQIKVIGVGGGGGNAVDHMIAQGVMGVEFICANTDAQALNRSKADQLLQLGST---GLGAGAKPEMGKAA 79
Cdd:COG0206     2 FELDDEEELKAKIKVIGVGGGGGNAVNRMIEAGLEGVEFIAANTDAQALENSKAPTKIQLGEKltrGLGAGANPEVGRKA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  80 AEEAEARIRESIQGAHMLFITAGMGGGTGTGAAPVIARVAKDMGILTVGVVTKPFEFEGGRRSKAADAGLAELEANVDSL 159
Cdd:COG0206    82 AEESREEIREALEGADMVFITAGMGGGTGTGAAPVIAEIAKELGALTVGVVTKPFSFEGKRRMRQAEEGIEELRKYVDTL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 160 IVVLNDKLLDVLGDDVTQDQAFAHANDVLKNAVGGISDIIHIPGLVNVDFEDVKTVMSEPGKAMMGTAQASGPDRAAKAA 239
Cdd:COG0206   162 IVIPNDKLLEVADKNTPLLEAFKKADDVLRQAVQGITDLITKPGLINLDFADVKTVMSNGGVALMGIGEASGENRAEEAA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 240 EAAVACPLLEGIDLSGARGVLVLIAASrANFKLSESRNAMNAIKRYASDDAHVIYGTAYDESLGDALRVTVIATGLSSQR 319
Cdd:COG0206   242 EKAISSPLLEDVSISGAKGVLVNITGG-SDLTLDEVNEAAEIIQEEADPDANIIFGAVIDESLGDEIRVTVIATGFDSEA 320
                         330       340
                  ....*....|....*....|....*.
gi 1332784132 320 ARQQPPLQVVQQTAQTQLRtgtYDVP 345
Cdd:COG0206   321 IVGEEETERPLEETEPAED---LDIP 343
FtsZ_type1 cd02201
Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the ...
26-314 1.92e-115

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: 339.76  E-value: 1.92e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  26 NAVDHMIAQGVMGVEFICANTDAQALNRSKADQLLQLGST---GLGAGAKPEMGKAAAEEAEARIRESIQGAHMLFITAG 102
Cdd:cd02201    14 NAVNRMIESGLEGVEFIAINTDAQALEKSKAPNKIQIGEKltrGLGAGGDPEVGRKAAEESREEIKEALKGADMVFITAG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 103 MGGGTGTGAAPVIARVAKDMGILTVGVVTKPFEFEGGRRSKAADAGLAELEANVDSLIVVLNDKLLDVLGDDVTQDQAFA 182
Cdd:cd02201    94 MGGGTGTGAAPVIAKIAKEMGALTVAVVTLPFSFEGKKRMRNAEEGLEELKKYVDTLIVIPNDKLLEIVGKNLPLLEAFK 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 183 HANDVLKNAVGGISDIIHIPGLVNVDFEDVKTVMSEPGKAMMGTAQASGPDRAAKAAEAAVACPLLEGiDLSGARGVLVL 262
Cdd:cd02201   174 KADEVLAQAVKGITDLITKPGLINLDFADVKTVMKNGGLALMGIGEASGENRAEEAVEKALNSPLLED-DIKGAKGVLVN 252
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1332784132 263 IAASRaNFKLSESRNAMNAIKRYASDDAHVIYGTAYDESLGDALRVTVIATG 314
Cdd:cd02201   253 ITGGP-DLTLEEVNEAAEIITEKADPDANIIFGAVIDEELGDEIRVTVIATG 303
ftsZ TIGR00065
cell division protein FtsZ; This family consists of cell division protein FtsZ, a GTPase found ...
1-318 3.13e-90

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: 276.89  E-value: 3.13e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   1 MAIEMIEEFDQ-----GTQIKVIGVGGGGGNAVDHMIAQGVMGVEFICANTDAQALNRSKADQLLQLGST---GLGAGAK 72
Cdd:TIGR00065   1 MDEIETEFRELiqpsnKAKIKVIGVGGGGNNTVNRMLEEGVEGVEFIAINTDAQHLKTTKADKKILIGKKltrGLGAGGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  73 PEMGKAAAEEAEARIRESIQGAHMLFITAGMGGGTGTGAAPVIARVAKDMGILTVGVVTKPFEFEGGRRSKAADAGLAEL 152
Cdd:TIGR00065  81 PEIGRKAAEESRDEIRKLLEGADMVFITAGMGGGTGTGAAPVVAKIAKELGALTVAVVTKPFKFEGLKRRKKAEEGLERL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 153 EANVDSLIVVLNDKLLDVLGDDVTQDqAFAHANDVLKNAVGGISDIIHIPGLVNVDFEDVKTVMSEPGKAMMGTAQASGP 232
Cdd:TIGR00065 161 KQAVDTLIVIPNDKLLEVVPNLPLND-AFKVADDVLVRAVKGISELITKPGLINIDFADVRAVMSGGGVAMMGIGEALGE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 233 D---RAAKAAEAAVACPLLEGIDLSGARGVLVLIAASrANFKLSESRNAMNAIKRYASDDAHVIYGTAYDESLGDALRVT 309
Cdd:TIGR00065 240 DtanRAFEAVRKALSSPLLDVDKISGAKGALVHITGG-ADLTLLEAEEIQEIITSELDQDANIIWGAIIDPNLEDEIRVT 318

                  ....*....
gi 1332784132 310 VIATGLSSQ 318
Cdd:TIGR00065 319 IVATGVKSQ 327
PRK13018 PRK13018
cell division protein FtsZ; Provisional
4-317 5.63e-87

cell division protein FtsZ; Provisional


Pssm-ID: 237273 [Multi-domain]  Cd Length: 378  Bit Score: 269.57  E-value: 5.63e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   4 EMIEEFDQGTQIKVIGVGGGGGNAVDHMIAQGVMGVEFICANTDAQALNRSKADQLLQLGST---GLGAGAKPEMGKAAA 80
Cdd:PRK13018   20 KASDDDFGNPKIVVVGCGGAGNNTINRLYEIGIEGAETIAINTDAQHLAMIKADKKILIGKSltrGLGAGGDPEVGRKAA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  81 EEAEARIRESIQGAHMLFITAGMGGGTGTGAAPVIARVAKDMGILTVGVVTKPFEFEGGRRSKAADAGLAELEANVDSLI 160
Cdd:PRK13018  100 EESRDEIKEVLKGADLVFVTAGMGGGTGTGAAPVVAEIAKEQGALVVGVVTKPFKFEGRARMQKAEEGIERLREAADTVI 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 161 VVLNDKLLDVLgDDVTQDQAFAHANDVLKNAVGGISDIIHIPGLVNVDFEDVKTVMSEPGKAMMGTAQASGPDRAAKAAE 240
Cdd:PRK13018  180 VIDNNRLLDIV-PNLPIADAFSVADEVIAETVKGITETITKPSLINLDFADVKSVMKGGGVAMMGVGEAKGQNRAMEAVR 258
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1332784132 241 AAVACPLLEgIDLSGARGVLVLIAASRaNFKLSESRNAMNAIKRYASDDAHVIYGTAYDESLGDALRVTVIATGLSS 317
Cdd:PRK13018  259 AALANPLLD-VDYRGAKGALVHITGGP-DLTLKEANEAASRITEELDPEANIIWGARIDPDMEGKVRVMVIMTGVKS 333
FtsZ_CetZ-like cd02191
Subfamily of FitZ and Cell-structure-related euryarchaeota tubulin/FtsZ homolog-like; FtsZ is ...
15-314 1.29e-57

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: 191.62  E-value: 1.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  15 IKVIGVGGGGGNAVDHMIAQGV-----MGVEFICANTDAQALNRSKADQLLQLG---STGLGAGAKPEMGKAAAEEAEAR 86
Cdd:cd02191     3 IVVIGVGQAGGNLASALQSFDRetgfgAGVETVAINTAAQDLKSLKAKETLLIGqdrTNGHGVGGNPELGAQAAEEDQEE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  87 IRESIQG---AHMLFITAGMGGGTGTGAAPVIARVAKDMGI-LTVGVVTKPFEFEGGRRSKAADAGLAELEANVDSLIVV 162
Cdd:cd02191    83 IMEALEGrveADMIFVTTGLGGGTGSGGAPVLAEALKKVYDvLTVAVVTLPFADEGALYMQNAGEGLRTLAEEADALILV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 163 LNDKLLDVLGDdvtQDQAFAHANDVLKNAVGGISDIIHIPGLVNVDFEDVKTVMSEPGKAMMGTAQASG-PDRAAKAAEA 241
Cdd:cd02191   163 DNEKLRSIGGS---LSEAYDAINEVLARRVGGLLEAIEATGLSVVDFADVKTVMNSGGMAMLGYGSADAsINRAREATRR 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1332784132 242 AVACPLLEgIDLSGARGVLVLIAASRANFKLSESRNAMNAIKRYAsDDAHVIYGTAYDESLgdALRVTVIATG 314
Cdd:cd02191   240 ALRTPLLL-PDASGADGALVVIAGEPDTLPLKEVERVRRWVEDET-GSATVRGGDVIDESG--RLRVLVVLTG 308
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
15-203 1.62e-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: 184.61  E-value: 1.62e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   15 IKVIGVGGGGGNAVDHMIAQGVmgVEFICANTDAQALNR-SKADQLLQLGST---GLGAGAKPEMGKAAAEEAEARIRES 90
Cdd:smart00864   2 IKVFGVGGGGPNAVNVDLEPGV--IDGVRANTDAQALNPeSLASGKIQAGNNwtrGLGAGADPEVGREAAEESLDEIREE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   91 IQGAHMLFITAGMGGGTGTGAAPVIARVAKDMGILTVGVVTKPFEFEGGRRSKAADAGLAELEANVDSLIVVLNDKLLDV 170
Cdd:smart00864  80 LEGADGVFITAGMGGGTGTGAAPVIAEIAKEYGILTVAVVTKPFSFEGVVRPYNAELGLEELREHVDSLIVIDNDALLDI 159
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1332784132  171 LGDDVTQDQAFAHANDVLKNAVGGISDIIHIPG 203
Cdd:smart00864 160 CGRKLPLRPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
205-321 1.32e-32

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: 119.19  E-value: 1.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  205 VNVDFEDVKTVMSEPGKAMMGTAQASGPDRAAKAAEAAVACPLLEGIDLSGARGVLVLIAASrANFKLSESRNAMNAIKR 284
Cdd:smart00865   1 INVDFADVKTVMVPMGFAMMGIGPASGENRALEAAELAISSPLLEDSNIMGAKGVLVNITGG-PDLTLKEVNEAMERIRE 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1332784132  285 YASDDAHVIYGTAYDESL-GDALRVTVIATGLSSQRAR 321
Cdd:smart00865  80 KADPDAFIIWGPVIDEELgGDEIRVTVIATGIGSLFKR 117
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
1-172 8.18e-22

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: 92.28  E-value: 8.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132   1 MAIEMIEEFDQGTQIKVIGVGGGGGNAVDHmIAQGVMgveficANTDAQALNRSKAD------QLLQLGSTGLGAGAKPE 74
Cdd:pfam00091  14 IGNALWELLCLEHGIDSLNVFFSESGSVEF-IPRSLA------IDTDPQALNEIKAGfnpnkiLLGKEGTGGNGAGGYPE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  75 MGKAAAEEAEARIRESIQGAHML---FITAGMGGGTGTGAAPVIARVAKDM--GILTVGVVTKPFEF-EGGRRSKAADAG 148
Cdd:pfam00091  87 IGREAAEESLEEIRKEVEGCDMLqgfFITASLGGGTGSGAAPVIAEILKELypGALTVAVVTFPFGFsEGVVRPYNAILG 166
                         170       180
                  ....*....|....*....|....
gi 1332784132 149 LAELEANVDSLIVVLNDKLLDVLG 172
Cdd:pfam00091 167 LKELIEHSDSVIVIDNDALYDICD 190
FtsZ_C pfam12327
FtsZ family, C-terminal domain; This family includes the bacterial FtsZ family of proteins. ...
220-316 1.32e-20

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: 85.72  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 220 GKAMMGTAQASGPDRAAKAAEAAVACPLLEgIDLSGARGVLVLIAASRaNFKLSESRNAMNAIKRYASDDAHVIYGTAYD 299
Cdd:pfam12327   1 GVAMMGTGEASGENRAEEAAEAAISSPLLD-VDLSGARGVLVNITGGP-DLTLFEANEAAETIREEVDPDANIIFGTVID 78
                          90
                  ....*....|....*..
gi 1332784132 300 ESLGDALRVTVIATGLS 316
Cdd:pfam12327  79 PELEDEIRVTVVATGID 95
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
45-229 7.45e-07

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: 50.87  E-value: 7.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132  45 NTDAQALNRSKADQLLQ--------LGSTGLGAGAKPEMGKAAAEEaeaRIRESIQGA-----------HMLFITAGMGG 105
Cdd:cd00286    26 DLEPAVLDELLSGPLRQlfhpeniiLIQKYHGAGNNWAKGHSVAGE---EYQEEILDAirkeveecdelQGFFITHSLGG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332784132 106 GTGTGAAPVIARVAKDM--GILTVGVVTKPFEFEG-GRRSKAADAGLAELEANVDSLIVVLNDKLLDVLGDDVTQDQ-AF 181
Cdd:cd00286   103 GTGSGLGPLLAERLKDEypNRLVVTFSILPGPDEGvIVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDApAY 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1332784132 182 AHANDVLKNAVGGISDIIHIPGLVNVDFED--VKTVMSEPGK-AMMGTAQA 229
Cdd:cd00286   183 DHINELVAQRLGSLTEALRFEGSLNVDLRElaENLVPLPRGHfLMLGYAPL 233
 
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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