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Conserved domains on  [gi|799386645|gb|AKA65676|]
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beta-tubulin, partial [Aspergillus pulverulentus]

Protein Classification

tubulin beta chain( domain architecture ID 1000324)

tubulin beta chain is part of tubulin, a dimer of alpha and beta chains, which is the major constituent of microtubules and binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00010 super family cl30500
tubulin beta chain; Provisional
1-317 0e+00

tubulin beta chain; Provisional


The actual alignment was detected with superfamily member PTZ00010:

Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 607.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   1 WQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNN 80
Cdd:PTZ00010  21 WEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGPYGQLFRPDNFIFGQSGAGNN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  81 WAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVV 160
Cdd:PTZ00010 101 WAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKVSDTVV 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 161 EPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPF 240
Cdd:PTZ00010 181 EPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPF 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799386645 241 PRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGRVSMKEVEDQMRNIQSKN 317
Cdd:PTZ00010 261 PRLHFFMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKN 337
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-317 0e+00

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 607.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   1 WQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNN 80
Cdd:PTZ00010  21 WEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGPYGQLFRPDNFIFGQSGAGNN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  81 WAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVV 160
Cdd:PTZ00010 101 WAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKVSDTVV 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 161 EPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPF 240
Cdd:PTZ00010 181 EPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPF 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799386645 241 PRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGRVSMKEVEDQMRNIQSKN 317
Cdd:PTZ00010 261 PRLHFFMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKN 337
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-317 0e+00

The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.


Pssm-ID: 276956 [Multi-domain]  Cd Length: 425  Bit Score: 602.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   1 WQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNN 80
Cdd:cd02187   20 WETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPYGQLFRPDNFVFGQSGAGNN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  81 WAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVV 160
Cdd:cd02187  100 WAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPDRIMSTFSVLPSPKVSDTVV 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 161 EPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPF 240
Cdd:cd02187  180 EPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLATNLVPF 259
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799386645 241 PRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGRVSMKEVEDQMRNIQSKN 317
Cdd:cd02187  260 PRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRISTKEVDEQMSKVQNKN 336
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
28-224 5.36e-59

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: 187.69  E-value: 5.36e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645    28 NVYFNEasgNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKGHYT-----EGAELVDQVVDVVRR 102
Cdd:smart00864   2 IKVFGV---GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIRE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   103 EAEACDclqGFQITHSlgggtgagmgtL----------LISKIREEFPDRmmaTFSVVPSPKVSDTVVEPYNATLSVHQL 172
Cdd:smart00864  79 ELEGAD---GVFITAG-----------MgggtgtgaapVIAEIAKEYGIL---TVAVVTKPFSFEGVVRPYNAELGLEEL 141
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 799386645   173 VEHSDETFCIDNEALYDICMRTLKLsNPSYGDLNHLVSAVMSGVTTCLRFPG 224
Cdd:smart00864 142 REHVDSLIVIDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
1-191 8.64e-48

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: 158.92  E-value: 8.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645    1 WQTISGEHGLDgsgvyngtsdlqleRMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGpfgqlFRPDNFVFGQSGAGNN 80
Cdd:pfam00091  19 WELLCLEHGID--------------SLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG-----FNPNKILLGKEGTGGN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   81 WAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSpKVSDTVV 160
Cdd:pfam00091  80 GAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGALTVAVVTFPF-GFSEGVV 158
                         170       180       190
                  ....*....|....*....|....*....|.
gi 799386645  161 EPYNATLSVHQLVEHSDETFCIDNEALYDIC 191
Cdd:pfam00091 159 RPYNAILGLKELIEHSDSVIVIDNDALYDIC 189
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-317 0e+00

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 607.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   1 WQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNN 80
Cdd:PTZ00010  21 WEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGPYGQLFRPDNFIFGQSGAGNN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  81 WAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVV 160
Cdd:PTZ00010 101 WAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKVSDTVV 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 161 EPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPF 240
Cdd:PTZ00010 181 EPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPF 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799386645 241 PRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGRVSMKEVEDQMRNIQSKN 317
Cdd:PTZ00010 261 PRLHFFMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKN 337
PLN00220 PLN00220
tubulin beta chain; Provisional
1-317 0e+00

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 605.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   1 WQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNN 80
Cdd:PLN00220  21 WEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGPYGQIFRPDNFVFGQSGAGNN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  81 WAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVV 160
Cdd:PLN00220 101 WAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVV 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 161 EPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPF 240
Cdd:PLN00220 181 EPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPF 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799386645 241 PRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGRVSMKEVEDQMRNIQSKN 317
Cdd:PLN00220 261 PRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKN 337
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-317 0e+00

The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.


Pssm-ID: 276956 [Multi-domain]  Cd Length: 425  Bit Score: 602.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   1 WQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNN 80
Cdd:cd02187   20 WETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPYGQLFRPDNFVFGQSGAGNN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  81 WAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVV 160
Cdd:cd02187  100 WAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPDRIMSTFSVLPSPKVSDTVV 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 161 EPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPF 240
Cdd:cd02187  180 EPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLATNLVPF 259
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 799386645 241 PRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGRVSMKEVEDQMRNIQSKN 317
Cdd:cd02187  260 PRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRISTKEVDEQMSKVQNKN 336
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
7-317 3.51e-111

The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.


Pssm-ID: 276955 [Multi-domain]  Cd Length: 434  Bit Score: 329.50  E-value: 3.51e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   7 EHGL--DGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKG 84
Cdd:cd02186   26 EHGIqpDGQMPSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTGPYRQLFHPEQLISGKEDAANNFARG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  85 HYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVVEPYN 164
Cdd:cd02186  106 YYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDYGKKSKLEFSIYPSPQVSTSVVEPYN 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 165 ATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLH 244
Cdd:cd02186  186 SVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNVDLNEFQTNLVPYPRIH 265
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 799386645 245 FFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGRVSMKEVEDQMRNIQSKN 317
Cdd:cd02186  266 FPLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKR 338
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
42-318 1.10e-104

The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins. Also included in this group is the mitochondrial Misato/DML1 protein family, involved in mitochondrial fusion and in mitochondrial distribution and morphology.


Pssm-ID: 276963 [Multi-domain]  Cd Length: 387  Bit Score: 311.06  E-value: 1.10e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  42 RAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGG 121
Cdd:cd06059   23 RAVLVDMEEGVINEVLKGPLGQLFDPNQFVTGVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 122 GTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICMR---TLKLS 198
Cdd:cd06059  103 GTGSGLGSYLLELLEDEYPKVYRFTFSVFPSPDDDNVITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDID 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 199 NPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKN 278
Cdd:cd06059  183 FPPFDDMNNLVAQLLSSLTSSLRFEGSLNVDLNEITTNLVPFPRLHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDN 262
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 799386645 279 MMAASDFRNGRYLTCSAIFRGRV-SMKEVEDQMRNIQSKNQ 318
Cdd:cd06059  263 QLVGCDPRHGTYLACALLLRGKVfSLSDVRRNIDRIKPKLK 303
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
36-318 5.42e-104

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: 307.41  E-value: 5.42e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  36 GNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQS--GAGNNWAKGHYTEGAELVDQVVDVVRREAEACDCLQGF 113
Cdd:cd00286   15 GAAFWEQAVLVDLEPAVLDELLSGPLRQLFHPENIILIQKyhGAGNNWAKGHSVAGEEYQEEILDAIRKEVEECDELQGF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 114 QITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSdTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICMR 193
Cdd:cd00286   95 FITHSLGGGTGSGLGPLLAERLKDEYPNRLVVTFSILPGPDEG-VIVYPYNAALTLKTLTEHADCLLLVDNEALYDICPR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 194 TLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQM 273
Cdd:cd00286  174 PLHIDAPAYDHINELVAQRLGSLTEALRFEGSLNVDLRELAENLVPLPRGHFLMLGYAPLDSATSATPRSLRVKELTRRA 253
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 799386645 274 FDPKNMMAASDFRNGRYLTCSAIFRGRV--SMKEVEDQMRNIQSKNQ 318
Cdd:cd00286  254 FLPANLLVGCDPDHGEAIAALLVIRGPPdlSSKEVERAIARVKETLG 300
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-316 9.23e-99

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 298.16  E-value: 9.23e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   1 WQTISGEHGL--DGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAG 78
Cdd:PTZ00335  21 WELFCLEHGIqpDGQMPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  79 NNWAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDT 158
Cdd:PTZ00335 101 NNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 159 VVEPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMV 238
Cdd:PTZ00335 181 VVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDLTEFQTNLV 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799386645 239 PFPRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGRVSMKEVEDQMRNIQSK 316
Cdd:PTZ00335 261 PYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAIATIKTK 338
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-316 1.38e-93

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 285.16  E-value: 1.38e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   1 WQTISGEHGL--DGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAG 78
Cdd:PLN00221  21 WELYCLEHGIqpDGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  79 NNWAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDT 158
Cdd:PLN00221 101 NNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 159 VVEPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMV 238
Cdd:PLN00221 181 VVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTASLRFDGALNVDITEFQTNLV 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799386645 239 PFPRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGRVSMKEVEDQMRNIQSK 316
Cdd:PLN00221 261 PYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTK 338
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
1-317 1.19e-88

The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of tubulin superfamily. Gamma is a low abundance protein present within the cells in both various types of microtubule-organizing centers and cytoplasmic protein complexes. Gamma-tubulin recruits the alpha/beta-tubulin dimers that form the minus ends of microtubules and is thought to be involved in microtubule nucleation and capping.


Pssm-ID: 276957 [Multi-domain]  Cd Length: 430  Bit Score: 271.72  E-value: 1.19e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   1 WQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQ--SGAG 78
Cdd:cd02188   20 WKQLCSEHGISPDGSLEDFATDGNDRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNSPYKNLFNPENIYLSKegGGAG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  79 NNWAKGhYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPK-VSD 157
Cdd:cd02188  100 NNWASG-YSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRYPKKLIQTYSVFPNQEeSSD 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 158 TVVEPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNM 237
Cdd:cd02188  179 VVVQPYNSILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTSTLRFPGYMNNDLVSLISSL 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 238 VPFPRLHFFMVGFAPLTS-RGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGRVSMKEVEDQMRNIQSK 316
Cdd:cd02188  259 IPTPRLHFLMTSYTPLTSdQVASSVRKTTVLDVMRRLLQPKNRMVSTSTKNGCYISILNIIQGEVDPTQVHKSLQRIRER 338

                 .
gi 799386645 317 N 317
Cdd:cd02188  339 K 339
PLN00222 PLN00222
tubulin gamma chain; Provisional
1-318 3.89e-72

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 230.12  E-value: 3.89e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   1 WQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSG--AG 78
Cdd:PLN00222  22 WKQLCLEHGISKDGILEDFATQGGDRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNSEYRNLYNHENIFVSDHGggAG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  79 NNWAKGhYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPS-PKVSD 157
Cdd:PLN00222 102 NNWASG-YHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRYSKKLVQTYSVFPNqMETSD 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 158 TVVEPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNM 237
Cdd:PLN00222 181 VVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTTTLRYPGYMNNDLVGLLASL 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 238 VPFPRLHFFMVGFAPL-TSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRN-----GRYLTCSAIFRGRVSMKEVEDQMR 311
Cdd:PLN00222 261 IPTPRCHFLMTGYTPLtVERQANVIRKTTVLDVMRRLLQTKNIMVSSYARTkeasqAKYISILNIIQGEVDPTQVHKSLQ 340

                 ....*..
gi 799386645 312 NIQSKNQ 318
Cdd:PLN00222 341 RIRERKL 347
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
42-314 2.56e-60

The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The epsilon-tubulins which are widespread but not ubiquitous among eukaryotes play a role in basal body/centriole morphogenesis.


Pssm-ID: 276959 [Multi-domain]  Cd Length: 449  Bit Score: 199.00  E-value: 2.56e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  42 RAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGG 121
Cdd:cd02190   68 RAVLIDMEEGVVNELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGPQYGESILEKLRRAAEKCDSLQSFFLLHSLGG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 122 GTGAGMGTLLISKIREEFPDRMMATFSVVPSpKVSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLSNP- 200
Cdd:cd02190  148 GTGSGLGSYILELLEDEFPDVYRFVTSVFPS-GDDDVITSPYNSVLALRELTEHADCVLPVENQALMDIVNKIKSSKDKg 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 201 ---------------------SYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLtsrgaY 259
Cdd:cd02190  227 ktgvlaainssgggqkkgkkkPFDDMNNIVANLLLNLTSSMRFEGSLNVDLNEITTNLVPFPRLHFLLSSLSPL-----Y 301
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 260 SFRAVTVPELTQ-QMFD----PKNMMAASDFRNGRYLTCSAIFRGRVsmkEVEDQMRNIQ 314
Cdd:cd02190  302 ALADVRLPPRRLdQMFSdafsRDHQLLKADPKHGLYLACALLVRGNV---SISDLRRNID 358
PTZ00387 PTZ00387
epsilon tubulin; Provisional
1-313 3.83e-60

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 199.18  E-value: 3.83e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   1 WQTISGEH-GLDGSGVYNGTSDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGN 79
Cdd:PTZ00387  21 WDVALKEHkKINANPQYDDARDSFFENVSENVNRPGKENLKARAVLVDMEEGVLNQILKSPLGDLFDENFFVSDVSGAGN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  80 NWAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSpKVSDTV 159
Cdd:PTZ00387 101 NWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEFPHVFRFCPVVFPS-AVDDVI 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 160 VEPYNATLSVHQLVEHSDETFCIDNEALYDICMRTLKLS----------------------------NPsYGDLNHLVSA 211
Cdd:PTZ00387 180 TSPYNSFFALRELIEHADCVLPLDNDALANIADSALSRKkkklakgnikrgpqphkysvakptetkkLP-YDKMNNIVAQ 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 212 VMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYL 291
Cdd:PTZ00387 259 LLSNLTSSMRFEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGPRRLDQMFKDCLDPDHQMVAATPEAGKYL 338
                        330       340
                 ....*....|....*....|..
gi 799386645 292 TCSAIFRGRVsmkEVEDQMRNI 313
Cdd:PTZ00387 339 ATALIVRGPQ---NVSDVTRNI 357
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
28-224 5.36e-59

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: 187.69  E-value: 5.36e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645    28 NVYFNEasgNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKGHYT-----EGAELVDQVVDVVRR 102
Cdd:smart00864   2 IKVFGV---GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIRE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   103 EAEACDclqGFQITHSlgggtgagmgtL----------LISKIREEFPDRmmaTFSVVPSPKVSDTVVEPYNATLSVHQL 172
Cdd:smart00864  79 ELEGAD---GVFITAG-----------MgggtgtgaapVIAEIAKEYGIL---TVAVVTKPFSFEGVVRPYNAELGLEEL 141
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 799386645   173 VEHSDETFCIDNEALYDICMRTLKLsNPSYGDLNHLVSAVMSGVTTCLRFPG 224
Cdd:smart00864 142 REHVDSLIVIDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
1-191 8.64e-48

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: 158.92  E-value: 8.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645    1 WQTISGEHGLDgsgvyngtsdlqleRMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGpfgqlFRPDNFVFGQSGAGNN 80
Cdd:pfam00091  19 WELLCLEHGID--------------SLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG-----FNPNKILLGKEGTGGN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   81 WAKGHYTEGAELVDQVVDVVRREAEACDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSpKVSDTVV 160
Cdd:pfam00091  80 GAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGALTVAVVTFPF-GFSEGVV 158
                         170       180       190
                  ....*....|....*....|....*....|.
gi 799386645  161 EPYNATLSVHQLVEHSDETFCIDNEALYDIC 191
Cdd:pfam00091 159 RPYNAILGLKELIEHSDSVIVIDNDALYDIC 189
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
20-299 2.44e-40

The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. Delta-tubulin plays an essential role in forming the triplet microtubules of centrioles and basal bodies.


Pssm-ID: 276958 [Multi-domain]  Cd Length: 433  Bit Score: 145.87  E-value: 2.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  20 SDLQLERMNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQL--FRPDNFVFGQSGAGNNWAKGHYTEGAELVDQVV 97
Cdd:cd02189   32 EGDQNSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRARSGAwsYDPKNVVCGQSGSGNNWALGYYVHGPSLLEDIL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645  98 DVVRREAEACDCLQGFQITHSLgggtgagmgtLLISKIREEFPDRMMATFSVVPSpKVSDTVVEPYNATLSVHQLVEHSD 177
Cdd:cd02189  112 EALRREAERCDRLSGFLVLHSLaggtgsglgsRVTELLRDEYPKAYLLNTVVWPY-SSGEVPVQNYNTLLTLSHLQESSD 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 178 ETFCIDNEALYDICMRTLKLSNP-SYGDLNHLVSAVMSGV---TTCLRFPGQLNSD-LRKLAVNMVPFPRLHFFMVGFAP 252
Cdd:cd02189  191 GILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVllpSSSPTSPSPLRRCpLGDLLEHLCPHPAYKLLTLRSLP 270
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645 253 LTSRGAYSFRAVTVPEL---TQQMF----------DPKNMMAASDFRNGRYLTCSAIFRG 299
Cdd:cd02189  271 QMPEPSRAFSTYTWPSLlkrLRQMLitgakleegiDWQLLDTSGSHNPNKSLAALLVLRG 330
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
241-318 1.78e-35

Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins 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. (The FtsZ GTPases have been split into their won family).


Pssm-ID: 397858 [Multi-domain]  Cd Length: 125  Bit Score: 124.65  E-value: 1.78e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 799386645  241 PRLHFFMVGFAPLTSRGAYSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCSAIFRGRVSMKEVEDQMRNIQSKNQ 318
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRS 78
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
226-317 1.02e-19

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: 82.98  E-value: 1.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 799386645   226 LNSDLRKLAVNMVPFPrlhFFMVGFAPLTSRgaysFRAVTVPELTQ--QMFDPKNMMAASDFRNgrYLTCSAifrgRVSM 303
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASGE----NRALEAAELAIssPLLEDSNIMGAKGVLV--NITGGP----DLTL 67
                           90
                   ....*....|....
gi 799386645   304 KEVEDQMRNIQSKN 317
Cdd:smart00865  68 KEVNEAMERIREKA 81
 
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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