NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|470900603|emb|CCP61144|]
View 

eukaryotic betatubulin, partial [uncultured Nyctotherus sp.]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTZ00010 super family cl30500
tubulin beta chain; Provisional
 5-167 8.06e-119

tubulin beta chain; Provisional


The actual alignment was detected with superfamily member PTZ00010:

Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 342.91  E-value: 8.06e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPKVSDTVVEPY 84
Cdd:PTZ00010 104 GHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKVSDTVVEPY 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  85 NATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFPRL 164
Cdd:PTZ00010 184 NATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPFPRL 263


                 ...
gi 470900603 165 HFF 167
Cdd:PTZ00010 264 HFF 266
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
 5-167 8.06e-119

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 342.91  E-value: 8.06e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPKVSDTVVEPY 84
Cdd:PTZ00010 104 GHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKVSDTVVEPY 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  85 NATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFPRL 164
Cdd:PTZ00010 184 NATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPFPRL 263


                 ...
gi 470900603 165 HFF 167
Cdd:PTZ00010 264 HFF 266
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 5-167 1.35e-110

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: 321.05  E-value: 1.35e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPKVSDTVVEPY 84
Cdd:cd02187  103 GHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPDRIMSTFSVLPSPKVSDTVVEPY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  85 NATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFPRL 164
Cdd:cd02187  183 NAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLATNLVPFPRL 262


                 ...
gi 470900603 165 HFF 167
Cdd:cd02187  263 HFL 265
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
 1-145 8.43e-36

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: 122.98  E-value: 8.43e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603     1 QLGE----GHYT-----EGAELIDSVLDVVRKEAEGCDclqGFQITHslgggtgsgmgtlLISKVREEYPNRIMeTFSVF 71
Cdd:smart00864  47 QAGNnwtrGLGAgadpeVGREAAEESLDEIREELEGAD---GVFITAgmgggt-gtgaapVIAEIAKEYGILTV-AVVTK 121

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470900603    72 PspKVSDTVVEPYNATLSVHQLVENADEVQVVDNEALYDICFRTLKLtTPTYGGLNHLVSAAMSGVTCCLRFPG 145
Cdd:smart00864 122 P--FSFEGVVRPYNAELGLEELREHVDSLIVIDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
 5-112 4.81e-30

Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules.


Pssm-ID: 459669 [Multi-domain]  Cd Length: 190  Bit Score: 108.07  E-value: 4.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603    5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSpKVSDTVVEPY 84
Cdd:pfam00091  83 GYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGALTVAVVTFPF-GFSEGVVRPY 161

                          90       100
                  ....*....|....*....|....*...
gi 470900603   85 NATLSVHQLVENADEVQVVDNEALYDIC 112
Cdd:pfam00091 162 NAILGLKELIEHSDSVIVIDNDALYDIC 189
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
 5-167 8.06e-119

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 342.91  E-value: 8.06e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPKVSDTVVEPY 84
Cdd:PTZ00010 104 GHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKVSDTVVEPY 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  85 NATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFPRL 164
Cdd:PTZ00010 184 NATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPFPRL 263


                 ...
gi 470900603 165 HFF 167
Cdd:PTZ00010 264 HFF 266
PLN00220 PLN00220
tubulin beta chain; Provisional
 4-167 4.54e-117

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 338.34  E-value: 4.54e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   4 EGHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPKVSDTVVEP 83
Cdd:PLN00220 103 KGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEP 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  84 YNATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFPR 163
Cdd:PLN00220 183 YNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPR 262


                 ....
gi 470900603 164 LHFF 167
Cdd:PLN00220 263 LHFF 266
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 5-167 1.35e-110

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: 321.05  E-value: 1.35e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPKVSDTVVEPY 84
Cdd:cd02187  103 GHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPDRIMSTFSVLPSPKVSDTVVEPY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  85 NATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFPRL 164
Cdd:cd02187  183 NAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLATNLVPFPRL 262


                 ...
gi 470900603 165 HFF 167
Cdd:cd02187  263 HFL 265
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
 5-167 1.21e-63

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: 200.12  E-value: 1.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPKVSDTVVEPY 84
Cdd:cd06059   65 GYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYPKVYRFTFSVFPSPDDDNVITSPY 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  85 NATLSVHQLVENADEVQVVDNEALYDICFR---TLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPF 161
Cdd:cd06059  145 NSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLTSSLRFEGSLNVDLNEITTNLVPF 224


                 ....*.
gi 470900603 162 PRLHFF 167
Cdd:cd06059  225 PRLHFL 230
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
 5-167 3.38e-63

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: 197.24  E-value: 3.38e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPKVSdTVVEPY 84
Cdd:cd00286   65 GHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDEYPNRLVVTFSILPGPDEG-VIVYPY 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  85 NATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFPRL 164
Cdd:cd00286  144 NAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTEALRFEGSLNVDLRELAENLVPLPRG 223


                 ...
gi 470900603 165 HFF 167
Cdd:cd00286  224 HFL 226
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 5-166 2.89e-59

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: 190.06  E-value: 2.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPKVSDTVVEPY 84
Cdd:cd02186  105 GYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDYGKKSKLEFSIYPSPQVSTSVVEPY 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  85 NATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFPRL 164
Cdd:cd02186  185 NSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNVDLNEFQTNLVPYPRI 264


                 ..
gi 470900603 165 HF 166
Cdd:cd02186  265 HF 266
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
 3-166 4.68e-54

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 176.82  E-value: 4.68e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   3 GEGHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPKVSDTVVE 82
Cdd:PTZ00335 104 ARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVE 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  83 PYNATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFP 162
Cdd:PTZ00335 184 PYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDLTEFQTNLVPYP 263


                 ....
gi 470900603 163 RLHF 166
Cdd:PTZ00335 264 RIHF 267
PLN00221 PLN00221
tubulin alpha chain; Provisional
 5-166 1.25e-49

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 165.37  E-value: 1.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPKVSDTVVEPY 84
Cdd:PLN00221 106 GHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTAVVEPY 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  85 NATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFPRL 164
Cdd:PLN00221 186 NSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTASLRFDGALNVDITEFQTNLVPYPRI 265


                 ..
gi 470900603 165 HF 166
Cdd:PLN00221 266 HF 267
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
 7-167 2.14e-48

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: 161.56  E-value: 2.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   7 YTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSPK-VSDTVVEPYN 85
Cdd:cd02188  106 YSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRYPKKLIQTYSVFPNQEeSSDVVVQPYN 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  86 ATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFPRLH 165
Cdd:cd02188  186 SILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTSTLRFPGYMNNDLVSLISSLIPTPRLH 265


                 ..
gi 470900603 166 FF 167
Cdd:cd02188  266 FL 267
PLN00222 PLN00222
tubulin gamma chain; Provisional
 7-166 2.59e-39

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 138.44  E-value: 2.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   7 YTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPS-PKVSDTVVEPYN 85
Cdd:PLN00222 108 YHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRYSKKLVQTYSVFPNqMETSDVVVQPYN 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  86 ATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPTYGGLNHLVSAAMSGVTCCLRFPGQLNADLRKLAVNLIPFPRLH 165
Cdd:PLN00222 188 SLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTTTLRYPGYMNNDLVGLLASLIPTPRCH 267


                 .
gi 470900603 166 F 166
Cdd:PLN00222 268 F 268
PTZ00387 PTZ00387
epsilon tubulin; Provisional
 5-166 8.27e-36

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 129.07  E-value: 8.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSpKVSDTVVEPY 84
Cdd:PTZ00387 105 GHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEFPHVFRFCPVVFPS-AVDDVITSPY 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  85 NATLSVHQLVENADEVQVVDNEALYDICFRTLKL---------------------TTPT------YGGLNHLVSAAMSGV 137
Cdd:PTZ00387 184 NSFFALRELIEHADCVLPLDNDALANIADSALSRkkkklakgnikrgpqphkysvAKPTetkklpYDKMNNIVAQLLSNL 263

                        170       180
                 ....*....|....*....|....*....
gi 470900603 138 TCCLRFPGQLNADLRKLAVNLIPFPRLHF 166
Cdd:PTZ00387 264 TSSMRFEGSLNVDINEITTNLVPYPRLHF 292
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
 1-145 8.43e-36

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: 122.98  E-value: 8.43e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603     1 QLGE----GHYT-----EGAELIDSVLDVVRKEAEGCDclqGFQITHslgggtgsgmgtlLISKVREEYPNRIMeTFSVF 71
Cdd:smart00864  47 QAGNnwtrGLGAgadpeVGREAAEESLDEIREELEGAD---GVFITAgmgggt-gtgaapVIAEIAKEYGILTV-AVVTK 121

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470900603    72 PspKVSDTVVEPYNATLSVHQLVENADEVQVVDNEALYDICFRTLKLtTPTYGGLNHLVSAAMSGVTCCLRFPG 145
Cdd:smart00864 122 P--FSFEGVVRPYNAELGLEELREHVDSLIVIDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
 3-167 1.30e-34

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: 125.43  E-value: 1.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   3 GEGHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSpKVSDTVVE 82
Cdd:cd02190  108 AHGYHEYGPQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSGLGSYILELLEDEFPDVYRFVTSVFPS-GDDDVITS 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603  83 PYNATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTPT----------------------YGGLNHLVSAAMSGVTCC 140
Cdd:cd02190  187 PYNSVLALRELTEHADCVLPVENQALMDIVNKIKSSKDKGktgvlaainssgggqkkgkkkpFDDMNNIVANLLLNLTSS 266

                        170       180
                 ....*....|....*....|....*..
gi 470900603 141 LRFPGQLNADLRKLAVNLIPFPRLHFF 167
Cdd:cd02190  267 MRFEGSLNVDLNEITTNLVPFPRLHFL 293
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
 5-112 4.81e-30

Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules.


Pssm-ID: 459669 [Multi-domain]  Cd Length: 190  Bit Score: 108.07  E-value: 4.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603    5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSpKVSDTVVEPY 84
Cdd:pfam00091  83 GYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGALTVAVVTFPF-GFSEGVVRPY 161

                          90       100
                  ....*....|....*....|....*...
gi 470900603   85 NATLSVHQLVENADEVQVVDNEALYDIC 112
Cdd:pfam00091 162 NAILGLKELIEHSDSVIVIDNDALYDIC 189
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
 5-137 6.60e-17

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: 76.54  E-value: 6.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470900603   5 GHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPNRIMETFSVFPSpKVSDTVVEPY 84
Cdd:cd02189   98 GYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEYPKAYLLNTVVWPY-SSGEVPVQNY 176

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 470900603  85 NATLSVHQLVENADEVQVVDNEALYDICFRTLKLTTP-TYGGLNHLVSAAMSGV 137
Cdd:cd02189  177 NTLLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGV 230
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH