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Conserved domains on  [gi|663085192|gb|AIE89840|]
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beta-tubulin, partial [Strobilurus esculentus]

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
1-198 5.68e-144

tubulin beta chain; Provisional


The actual alignment was detected with superfamily member PTZ00010:

Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 408.01  E-value: 5.68e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNA 80
Cdd:PTZ00010 106 YTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKVSDTVVEPYNA 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHF 160
Cdd:PTZ00010 186 TLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPFPRLHF 265
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 663085192 161 FMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMAAS 198
Cdd:PTZ00010 266 FMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAA 303
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-198 5.68e-144

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 408.01  E-value: 5.68e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNA 80
Cdd:PTZ00010 106 YTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKVSDTVVEPYNA 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHF 160
Cdd:PTZ00010 186 TLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPFPRLHF 265
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 663085192 161 FMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMAAS 198
Cdd:PTZ00010 266 FMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAA 303
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-198 2.27e-142

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: 403.10  E-value: 2.27e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNA 80
Cdd:cd02187  105 YTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPDRIMSTFSVLPSPKVSDTVVEPYNA 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHF 160
Cdd:cd02187  185 VLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLATNLVPFPRLHF 264
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 663085192 161 FMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMAAS 198
Cdd:cd02187  265 LTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAAC 302
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
4-139 2.32e-39

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: 133.00  E-value: 2.32e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192     4 GAELVDSVLDVVRKEAEGTDalqGFQITHSLgggtgagmgtlLISKIREEYPDRMMctySVVPSPKVSDTVVEPYNATLS 83
Cdd:smart00864  65 GREAAEESLDEIREELEGAD---GVFITAGMgggtg-tgaapVIAEIAKEYGILTV---AVVTKPFSFEGVVRPYNAELG 137
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 663085192    84 VHQLVENSDETFCIDNEALYDICFRTLKLsTPTYGDLNHLVSIVMSGITTCLRFPG 139
Cdd:smart00864 138 LEELREHVDSLIVIDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
1-106 3.48e-29

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: 106.92  E-value: 3.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192    1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSpKVSDTVVEPYNA 80
Cdd:pfam00091  85 PEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGALTVAVVTFPF-GFSEGVVRPYNA 163
                          90       100
                  ....*....|....*....|....*.
gi 663085192   81 TLSVHQLVENSDETFCIDNEALYDIC 106
Cdd:pfam00091 164 ILGLKELIEHSDSVIVIDNDALYDIC 189
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-198 5.68e-144

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 408.01  E-value: 5.68e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNA 80
Cdd:PTZ00010 106 YTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKVSDTVVEPYNA 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHF 160
Cdd:PTZ00010 186 TLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPFPRLHF 265
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 663085192 161 FMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMAAS 198
Cdd:PTZ00010 266 FMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAA 303
PLN00220 PLN00220
tubulin beta chain; Provisional
1-198 3.68e-143

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 406.13  E-value: 3.68e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNA 80
Cdd:PLN00220 106 YTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNA 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHF 160
Cdd:PLN00220 186 TLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHF 265
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 663085192 161 FMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMAAS 198
Cdd:PLN00220 266 FMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAA 303
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-198 2.27e-142

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: 403.10  E-value: 2.27e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNA 80
Cdd:cd02187  105 YTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPDRIMSTFSVLPSPKVSDTVVEPYNA 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHF 160
Cdd:cd02187  185 VLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLATNLVPFPRLHF 264
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 663085192 161 FMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMAAS 198
Cdd:cd02187  265 LTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAAC 302
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
1-197 4.43e-76

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: 231.53  E-value: 4.43e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSdTVVEPYNA 80
Cdd:cd00286   67 SVAGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDEYPNRLVVTFSILPGPDEG-VIVYPYNA 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHF 160
Cdd:cd00286  146 ALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTEALRFEGSLNVDLRELAENLVPLPRGHF 225
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 663085192 161 FMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMAA 197
Cdd:cd00286  226 LMLGYAPLDSATSATPRSLRVKELTRRAFLPANLLVG 262
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-196 4.65e-71

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: 221.64  E-value: 4.65e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNA 80
Cdd:cd02186  107 YTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDYGKKSKLEFSIYPSPQVSTSVVEPYNS 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHF 160
Cdd:cd02186  187 VLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNVDLNEFQTNLVPYPRIHF 266
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 663085192 161 FMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMA 196
Cdd:cd02186  267 PLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMV 302
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
1-197 2.37e-70

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: 218.61  E-value: 2.37e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNA 80
Cdd:cd06059   67 YVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYPKVYRFTFSVFPSPDDDNVITSPYNS 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFR---TLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPR 157
Cdd:cd06059  147 VLALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLTSSLRFEGSLNVDLNEITTNLVPFPR 226
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 663085192 158 LHFFMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMAA 197
Cdd:cd06059  227 LHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDNQLVG 266
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-196 2.82e-62

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 199.55  E-value: 2.82e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNA 80
Cdd:PTZ00335 108 YTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNS 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHF 160
Cdd:PTZ00335 188 VLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDLTEFQTNLVPYPRIHF 267
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 663085192 161 FMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMA 196
Cdd:PTZ00335 268 MLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMA 303
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-196 1.75e-58

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 189.63  E-value: 1.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPKVSDTVVEPYNA 80
Cdd:PLN00221 108 YTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTAVVEPYNS 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHF 160
Cdd:PLN00221 188 VLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTASLRFDGALNVDITEFQTNLVPYPRIHF 267
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 663085192 161 FMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMA 196
Cdd:PLN00221 268 MLSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMA 303
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
1-196 3.99e-57

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: 185.44  E-value: 3.99e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSPK-VSDTVVEPYN 79
Cdd:cd02188  106 YSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRYPKKLIQTYSVFPNQEeSSDVVVQPYN 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  80 ATLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLH 159
Cdd:cd02188  186 SILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTSTLRFPGYMNNDLVSLISSLIPTPRLH 265
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 663085192 160 FFMTGFAPLT-ARGSQQYRAVTVPELTQQMFDAKNMMA 196
Cdd:cd02188  266 FLMTSYTPLTsDQVASSVRKTTVLDVMRRLLQPKNRMV 303
PLN00222 PLN00222
tubulin gamma chain; Provisional
1-198 4.09e-47

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 160.01  E-value: 4.09e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPS-PKVSDTVVEPYN 79
Cdd:PLN00222 108 YHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRYSKKLVQTYSVFPNqMETSDVVVQPYN 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  80 ATLSVHQLVENSDETFCIDNEALYDICFRTLKLSTPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLH 159
Cdd:PLN00222 188 SLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTTTLRYPGYMNNDLVGLLASLIPTPRCH 267
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 663085192 160 FFMTGFAPL-TARGSQQYRAVTVPELTQQMFDAKNMMAAS 198
Cdd:PLN00222 268 FLMTGYTPLtVERQANVIRKTTVLDVMRRLLQTKNIMVSS 307
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
4-139 2.32e-39

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: 133.00  E-value: 2.32e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192     4 GAELVDSVLDVVRKEAEGTDalqGFQITHSLgggtgagmgtlLISKIREEYPDRMMctySVVPSPKVSDTVVEPYNATLS 83
Cdd:smart00864  65 GREAAEESLDEIREELEGAD---GVFITAGMgggtg-tgaapVIAEIAKEYGILTV---AVVTKPFSFEGVVRPYNAELG 137
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 663085192    84 VHQLVENSDETFCIDNEALYDICFRTLKLsTPTYGDLNHLVSIVMSGITTCLRFPG 139
Cdd:smart00864 138 LEELREHVDSLIVIDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
PTZ00387 PTZ00387
epsilon tubulin; Provisional
4-191 2.52e-34

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 126.38  E-value: 2.52e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   4 GAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSpKVSDTVVEPYNATLS 83
Cdd:PTZ00387 110 GDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEFPHVFRFCPVVFPS-AVDDVITSPYNSFFA 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  84 VHQLVENSDETFCIDNEALYDICFRTLKLST---------------------PT------YGDLNHLVSIVMSGITTCLR 136
Cdd:PTZ00387 189 LRELIEHADCVLPLDNDALANIADSALSRKKkklakgnikrgpqphkysvakPTetkklpYDKMNNIVAQLLSNLTSSMR 268
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663085192 137 FPGQLNSDLRKLAVNMVPFPRLHFFMTGFAPLTARgsqqYRAVTVPELTQQMFDA 191
Cdd:PTZ00387 269 FEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSL----KDVAVGPRRLDQMFKD 319
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
9-198 1.56e-33

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: 123.89  E-value: 1.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   9 DSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSpKVSDTVVEPYNATLSVHQLV 88
Cdd:cd02190  120 ESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSGLGSYILELLEDEFPDVYRFVTSVFPS-GDDDVITSPYNSVLALRELT 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  89 ENSDETFCIDNEALYDICFRTLKLSTPT----------------------YGDLNHLVSIVMSGITTCLRFPGQLNSDLR 146
Cdd:cd02190  199 EHADCVLPVENQALMDIVNKIKSSKDKGktgvlaainssgggqkkgkkkpFDDMNNIVANLLLNLTSSMRFEGSLNVDLN 278
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663085192 147 KLAVNMVPFPRLHFFMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMAAS 198
Cdd:cd02190  279 EITTNLVPFPRLHFLLSSLSPLYALADVRLPPRRLDQMFSDAFSRDHQLLKA 330
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
1-106 3.48e-29

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: 106.92  E-value: 3.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192    1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSpKVSDTVVEPYNA 80
Cdd:pfam00091  85 PEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGALTVAVVTFPF-GFSEGVVRPYNA 163
                          90       100
                  ....*....|....*....|....*.
gi 663085192   81 TLSVHQLVENSDETFCIDNEALYDIC 106
Cdd:pfam00091 164 ILGLKELIEHSDSVIVIDNDALYDIC 189
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
1-189 1.85e-19

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: 85.01  E-value: 1.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192   1 YTEGAELVDSVLDVVRKEAEGTDALQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMCTYSVVPSpKVSDTVVEPYNA 80
Cdd:cd02189  100 YVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEYPKAYLLNTVVWPY-SSGEVPVQNYNT 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663085192  81 TLSVHQLVENSDETFCIDNEALYDICFRTLKLSTP-TYGDLN-----HLVSIVMSGITTCLRFPGQLNSdLRKLAVNMVP 154
Cdd:cd02189  179 LLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINrviarQLAGVLLPSSSPTSPSPLRRCP-LGDLLEHLCP 257
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 663085192 155 FPRLHFFmTGF-APLTARGSQQYRAVTVPEL---TQQMF 189
Cdd:cd02189  258 HPAYKLL-TLRsLPQMPEPSRAFSTYTWPSLlkrLRQML 295
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
156-198 1.95e-16

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: 71.88  E-value: 1.95e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 663085192  156 PRLHFFMTGFAPLTARGSQQYRAVTVPELTQQMFDAKNMMAAS 198
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSC 43
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
141-197 3.03e-11

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: 57.94  E-value: 3.03e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 663085192   141 LNSDLRKLAVNMVPFPrlhFFMTGFAPLTArgsqQYRAVTVPELTQ--QMFDAKNMMAA 197
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASG----ENRALEAAELAIssPLLEDSNIMGA 52
 
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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