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Conserved domains on  [gi|14210536|ref|NP_115914|]
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tubulin beta-6 chain isoform 1 [Homo sapiens]

Protein Classification

tubulin beta chain( domain architecture ID 11476486)

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
PLN00220 PLN00220
tubulin beta chain; Provisional
1-432 0e+00

tubulin beta chain; Provisional


:

Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 904.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    1 MREIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGP 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   81 FGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFP 160
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  161 DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTSL 240
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  241 RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRGP 320
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  321 MSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMASTFIGNSTAIQELFKRISEQFSAMFRRKAFLHWFTG 400
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|..
gi 14210536  401 EGMDEMEFTEAESNMNDLVSEYQQYQDATAND 432
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATADE 432
 
Name Accession Description Interval E-value
PLN00220 PLN00220
tubulin beta chain; Provisional
1-432 0e+00

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 904.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    1 MREIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGP 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   81 FGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFP 160
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  161 DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTSL 240
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  241 RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRGP 320
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  321 MSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMASTFIGNSTAIQELFKRISEQFSAMFRRKAFLHWFTG 400
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|..
gi 14210536  401 EGMDEMEFTEAESNMNDLVSEYQQYQDATAND 432
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATADE 432
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-426 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: 873.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   2 REIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGPF 81
Cdd:cd02187   1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  82 GQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPD 161
Cdd:cd02187  81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 162 RIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTSLR 241
Cdd:cd02187 161 RIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLR 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 242 FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRGPM 321
Cdd:cd02187 241 FPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRI 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 322 SMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMASTFIGNSTAIQELFKRISEQFSAMFRRKAFLHWFTGE 401
Cdd:cd02187 321 STKEVDEQMSKVQNKNSSYFVEWIPNNVKTSVCDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGE 400
                       410       420
                ....*....|....*....|....*
gi 14210536 402 GMDEMEFTEAESNMNDLVSEYQQYQ 426
Cdd:cd02187 401 GMDEMEFTEAESNLNDLISEYQQYQ 425
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
3-211 9.39e-63

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: 201.29  E-value: 9.39e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536     3 EIVHIQAGQCGNQIGTKFWEVISDEHGIDpaggyvgdsalqleRINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGpfg 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCLEHGID--------------SLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG--- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    83 qlFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPDR 162
Cdd:pfam00091  64 --FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGA 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 14210536   163 IMNTFSVMPSpKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDIC 211
Cdd:pfam00091 142 LTVAVVTFPF-GFSEGVVRPYNAILGLKELIEHSDSVIVIDNDALYDIC 189
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
47-244 8.92e-57

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: 185.77  E-value: 8.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536     47 INVYYNESssqKYVPRAALVDLEPGTMDSVRSGPFGQLFRPDNFIFGQTGAGNNWAKGHYT-----EGAELVDAVLDVVR 121
Cdd:smart00864   1 KIKVFGVG---GGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    122 KECEHCDclqGFQLTHslgggtgsgmgtlLISKIREEFPDRIMnTFSVMpsPKVSDTVVEPYNATLSVHQLVENTDETYC 201
Cdd:smart00864  78 EELEGAD---GVFITAgmgggt-gtgaapVIAEIAKEYGILTV-AVVTK--PFSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 14210536    202 IDNEALYDICFRTLKLtTPTYGDLNHLVSATMSGVTTSLRFPG 244
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
 
Name Accession Description Interval E-value
PLN00220 PLN00220
tubulin beta chain; Provisional
1-432 0e+00

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 904.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    1 MREIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGP 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   81 FGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFP 160
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  161 DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTSL 240
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  241 RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRGP 320
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  321 MSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMASTFIGNSTAIQELFKRISEQFSAMFRRKAFLHWFTG 400
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|..
gi 14210536  401 EGMDEMEFTEAESNMNDLVSEYQQYQDATAND 432
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATADE 432
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-433 0e+00

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 895.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    1 MREIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGP 80
Cdd:PTZ00010   1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   81 FGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFP 160
Cdd:PTZ00010  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  161 DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTSL 240
Cdd:PTZ00010 161 DRIMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  241 RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRGP 320
Cdd:PTZ00010 241 RFPGQLNSDLRKLAVNLVPFPRLHFFMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  321 MSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMASTFIGNSTAIQELFKRISEQFSAMFRRKAFLHWFTG 400
Cdd:PTZ00010 321 MSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSVCDIPPKGLKMSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|...
gi 14210536  401 EGMDEMEFTEAESNMNDLVSEYQQYQDATANDG 433
Cdd:PTZ00010 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATVEEE 433
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-426 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: 873.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   2 REIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGPF 81
Cdd:cd02187   1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  82 GQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPD 161
Cdd:cd02187  81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 162 RIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTSLR 241
Cdd:cd02187 161 RIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLR 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 242 FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRGPM 321
Cdd:cd02187 241 FPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRI 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 322 SMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMASTFIGNSTAIQELFKRISEQFSAMFRRKAFLHWFTGE 401
Cdd:cd02187 321 STKEVDEQMSKVQNKNSSYFVEWIPNNVKTSVCDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGE 400
                       410       420
                ....*....|....*....|....*
gi 14210536 402 GMDEMEFTEAESNMNDLVSEYQQYQ 426
Cdd:cd02187 401 GMDEMEFTEAESNLNDLISEYQQYQ 425
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-424 2.33e-163

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: 467.40  E-value: 2.33e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   2 REIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERINV--YYNESSSQKYVPRAALVDLEPGTMDSVRSG 79
Cdd:cd02186   1 REIISIHVGQAGVQIGNACWELFCLEHGIQPDGQMPSDKTIGGDDDNFntFFSETGSGKYVPRAVFVDLEPTVIDEIRTG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  80 PFGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEF 159
Cdd:cd02186  81 PYRQLFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 160 PDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTS 239
Cdd:cd02186 161 GKKSKLEFSIYPSPQVSTSVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTAS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 240 LRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRG 319
Cdd:cd02186 241 LRFDGALNVDLNEFQTNLVPYPRIHFPLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRG 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 320 PMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPP---RGLKMASTF-----IGNSTAIQELFKRISEQFSAMFRR 391
Cdd:cd02186 321 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPtvvPGSDLAKVDrsvcmLANSTAIAEAFQRLDHKFDLLYSK 400
                       410       420       430
                ....*....|....*....|....*....|...
gi 14210536 392 KAFLHWFTGEGMDEMEFTEAESNMNDLVSEYQQ 424
Cdd:cd02186 401 RAFVHWYVGEGMEEGEFSEAREDLAALEKDYEE 433
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
3-424 1.16e-159

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: 456.28  E-value: 1.16e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   3 EIVHIQAGQCGNQIGTKFWEVIsdehgidpaggyvgdsalqlerinvyynesssqkyvpRAALVDLEPGTMDSVRSGPFG 82
Cdd:cd06059   1 EIITIQVGQCGNQIGDRFWELA-------------------------------------RAVLVDMEEGVINEVLKGPLG 43
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  83 QLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPDR 162
Cdd:cd06059  44 QLFDPNQFVTGVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYPKV 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 163 IMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFR---TLKLTTPTYGDLNHLVSATMSGVTTS 239
Cdd:cd06059 124 YRFTFSVFPSPDDDNVITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLTSS 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 240 LRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRG 319
Cdd:cd06059 204 LRFEGSLNVDLNEITTNLVPFPRLHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDNQLVGCDPRHGTYLACALLLRG 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 320 -PMSMKEVDEQMLAIQSKNSsyFVEWIPNNVKVAVCDIPPRGLKMASTFIGNSTAIQELFKRISEQFSAMFRRKAFLHWF 398
Cdd:cd06059 284 kVFSLSDVRRNIDRIKPKLK--FISWNPDGFKVGLCSVPPVGQKYSLLFLSNNTSIASTFERLIERFDKLYKRKAFLHHY 361
                       410       420
                ....*....|....*....|....*.
gi 14210536 399 TGEGMDEMEFTEAESNMNDLVSEYQQ 424
Cdd:cd06059 362 TGEGMEEGDFSEARESLANLIQEYQE 387
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-424 1.05e-140

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 410.25  E-value: 1.05e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    1 MREIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLE--RINVYYNESSSQKYVPRAALVDLEPGTMDSVRS 78
Cdd:PTZ00335   1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEddAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   79 GPFGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREE 158
Cdd:PTZ00335  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  159 FPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTT 238
Cdd:PTZ00335 161 YGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  239 SLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFR 318
Cdd:PTZ00335 241 SLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  319 GPMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAV-----CDIPPRGL---KMASTFIGNSTAIQELFKRISEQFSAMFR 390
Cdd:PTZ00335 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGInyqppTVVPGGDLakvQRAVCMISNSTAIAEVFSRIDHKFDLMYA 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 14210536  391 RKAFLHWFTGEGMDEMEFTEAESNMNDLVSEYQQ 424
Cdd:PTZ00335 401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEE 434
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-424 1.15e-136

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 399.95  E-value: 1.15e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    1 MREIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQL--ERINVYYNESSSQKYVPRAALVDLEPGTMDSVRS 78
Cdd:PLN00221   1 MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGgdDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   79 GPFGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREE 158
Cdd:PLN00221  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  159 FPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTT 238
Cdd:PLN00221 161 YGKKSKLGFTVYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  239 SLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFR 318
Cdd:PLN00221 241 SLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  319 GPMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPR--------GLKMASTFIGNSTAIQELFKRISEQFSAMFR 390
Cdd:PLN00221 321 GDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTvvpggdlaKVQRAVCMISNSTAVAEVFSRIDHKFDLMYA 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 14210536  391 RKAFLHWFTGEGMDEMEFTEAESNMNDLVSEYQQ 424
Cdd:PLN00221 401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEE 434
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
3-371 6.01e-133

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: 385.99  E-value: 6.01e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   3 EIVHIQAGQCGNQIGTKFWEVisdehgidpaggyvgdsalqlerinvyynesssqkyvprAALVDLEPGTMDSVRSGPFG 82
Cdd:cd00286   1 EIVTIQVGQCGNQIGAAFWEQ---------------------------------------AVLVDLEPAVLDELLSGPLR 41
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  83 QLFRPDNFIFGQ--TGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFP 160
Cdd:cd00286  42 QLFHPENIILIQkyHGAGNNWAKGHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDEYP 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 161 DRIMNTFSVMPSPKVSdTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTSL 240
Cdd:cd00286 122 NRLVVTFSILPGPDEG-VIVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTEAL 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 241 RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRGP 320
Cdd:cd00286 201 RFEGSLNVDLRELAENLVPLPRGHFLMLGYAPLDSATSATPRSLRVKELTRRAFLPANLLVGCDPDHGEAIAALLVIRGP 280
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 14210536 321 --MSMKEVDEQMLAIQSKNSSYFvEWIPNNVKVAVCDIPPRGLKMASTFIGNS 371
Cdd:cd00286 281 pdLSSKEVERAIARVKETLGHLF-SWSPAGVKTGISPKPPAEGEVSVLALLNS 332
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
2-422 1.61e-126

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: 373.41  E-value: 1.61e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   2 REIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGgYVGDSALQLE-RINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGP 80
Cdd:cd02188   1 REIITLQVGQCGNQIGSEFWKQLCSEHGISPDG-SLEDFATDGNdRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNSP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  81 FGQLFRPDNFIFGQ--TGAGNNWAKGhYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREE 158
Cdd:cd02188  80 YKNLFNPENIYLSKegGGAGNNWASG-YSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 159 FPDRIMNTFSVMPSPK-VSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVT 237
Cdd:cd02188 159 YPKKLIQTYSVFPNQEeSSDVVVQPYNSILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSAST 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 238 TSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTS-RGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATV 316
Cdd:cd02188 239 STLRFPGYMNNDLVSLISSLIPTPRLHFLMTSYTPLTSdQVASSVRKTTVLDVMRRLLQPKNRMVSTSTKNGCYISILNI 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 317 FRGPMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRgLKMASTFIG----NSTAIQELFKRISEQFSAMFRRK 392
Cdd:cd02188 319 IQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSKKSPY-VQTAHRVSGlmlaNHTSISSLFEKILSQYDKLRKRN 397
                       410       420       430
                ....*....|....*....|....*....|...
gi 14210536 393 AFLHWFTGEGMDE---MEFTEAESNMNDLVSEY 422
Cdd:cd02188 398 AFLENYRKEDMFQdnlEEFDESREVVQSLIDEY 430
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
2-425 1.80e-99

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: 304.93  E-value: 1.80e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   2 REIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERI-------NVYYNESSSQKYVPRAALVDLEPGTMD 74
Cdd:cd02190   1 REIITVQVGQCGNQIGCRFWDLALREHAAYNKDGVYDDSMSSFFRNvdtrsgdPGDDGGSPIKSLKARAVLIDMEEGVVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  75 SVRSGPFGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISK 154
Cdd:cd02190  81 ELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGPQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSGLGSYILEL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 155 IREEFPDRIMNTFSVMPSpKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPT------------- 221
Cdd:cd02190 161 LEDEFPDVYRFVTSVFPS-GDDDVITSPYNSVLALRELTEHADCVLPVENQALMDIVNKIKSSKDKGktgvlaainssgg 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 222 ---------YGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQ 292
Cdd:cd02190 240 gqkkgkkkpFDDMNNIVANLLLNLTSSMRFEGSLNVDLNEITTNLVPFPRLHFLLSSLSPLYALADVRLPPRRLDQMFSD 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 293 MFDARNMMAACDPRHGRYLTVATVFRGPMSMKEVDEQMLAIQSKNSsyFVEWIPNNVKVAVCDIPPRGLKMASTFIGNST 372
Cdd:cd02190 320 AFSRDHQLLKADPKHGLYLACALLVRGNVSISDLRRNIDRLKRQLK--FVSWNQDGWKIGLCSVPPVGQPYSLLCLANNT 397
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 14210536 373 AIQELFKRISEQFSAMFRRKAFLHWFTgEGMDEMEFTEAESNMNDLVSEYQQY 425
Cdd:cd02190 398 CIKPTFTEMHERFDKLYKRKAHLHHYT-QYMEQDDFDEALESLLDLIEEYKDL 449
PLN00222 PLN00222
tubulin gamma chain; Provisional
2-423 3.60e-97

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 299.07  E-value: 3.60e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    2 REIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQLERINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGPF 81
Cdd:PLN00222   3 REIITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGGDRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNSEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   82 GQLFRPDNFIFGQTG--AGNNWAKGhYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEF 159
Cdd:PLN00222  83 RNLYNHENIFVSDHGggAGNNWASG-YHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  160 PDRIMNTFSVMPS-PKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTT 238
Cdd:PLN00222 162 SKKLVQTYSVFPNqMETSDVVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  239 SLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPL-TSRGSQQYRALTVPELTQQMFDARNMMAACDPR-----HGRYLT 312
Cdd:PLN00222 242 TLRYPGYMNNDLVGLLASLIPTPRCHFLMTGYTPLtVERQANVIRKTTVLDVMRRLLQTKNIMVSSYARtkeasQAKYIS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  313 VATVFRGPMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPP---RGLKMASTFIGNSTAIQELFKRISEQFSAMF 389
Cdd:PLN00222 322 ILNIIQGEVDPTQVHKSLQRIRERKLANFIEWGPASIQVALSRKSPyvqTAHRVSGLMLANHTSIRHLFSKCLSQYDKLR 401
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 14210536  390 RRKAFLHWFTGEGM----DEMEFTEAESNMNDLVSEYQ 423
Cdd:PLN00222 402 KKQAFLDNYRKFPMfadnDLSEFDESREIVESLVDEYK 439
PTZ00387 PTZ00387
epsilon tubulin; Provisional
1-428 6.30e-95

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 293.55  E-value: 6.30e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    1 MREIVHIQAGQCGNQIGTKFWEVISDEHGIDPAGGYVGDSALQL-ERINVYYNESSSQKYVPRAALVDLEPGTMDSVRSG 79
Cdd:PTZ00387   1 PREIVTVQVGQCGNQLGHRFWDVALKEHKKINANPQYDDARDSFfENVSENVNRPGKENLKARAVLVDMEEGVLNQILKS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   80 PFGQLFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEF 159
Cdd:PTZ00387  81 PLGDLFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  160 PDRIMNTFSVMPSpKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKL---------------------T 218
Cdd:PTZ00387 161 PHVFRFCPVVFPS-AVDDVITSPYNSFFALRELIEHADCVLPLDNDALANIADSALSRkkkklakgnikrgpqphkysvA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  219 TPT------YGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQ 292
Cdd:PTZ00387 240 KPTetkklpYDKMNNIVAQLLSNLTSSMRFEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGPRRLDQMFKD 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  293 MFDARNMMAACDPRHGRYLTVATVFRGPMSMKEVDEQMLAIqsKNSSYFVEWIPNNVKVAVCDIPPRGLKMASTFIGNST 372
Cdd:PTZ00387 320 CLDPDHQMVAATPEAGKYLATALIVRGPQNVSDVTRNILRL--KEQLNMIYWNEDGFKTGLCNVSPLGQPYSLLCLANNC 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 14210536  373 AIQELFKRISEQFSAMFRRKAFLHWFTgEGMDEMEFTEAESNMNDLVSEYQQYQDA 428
Cdd:PTZ00387 398 CIRNKFESMLERFNKLYKRKSHVHHYT-EYLEQAYFDETLETIQNLIDDYAYLQTA 452
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
4-424 1.02e-68

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: 224.84  E-value: 1.02e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   4 IVHIQAGQCGNQIGTKFWEVISDEhGIDPAGGYVGDSALQLERinvyyNESSSQKYVPRAALVDLEPGTMDSVRSGPFGQ 83
Cdd:cd02189   2 IVTVQVGQCGNQLGDELFDTLADE-ADSSASEGDQNSSATRFF-----SPFSDGKLKARCVLVDMEPKVVQQVLSRARSG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536  84 L--FRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPD 161
Cdd:cd02189  76 AwsYDPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEYPK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 162 R-IMNTfSVMPSpKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTP-TYGDLNHLVSATMSGV--- 236
Cdd:cd02189 156 AyLLNT-VVWPY-SSGEVPVQNYNTLLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVllp 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 237 TTSLRFPGQLNAD-LRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPEL---TQQMF----------DARNMMAA 302
Cdd:cd02189 234 SSSPTSPSPLRRCpLGDLLEHLCPHPAYKLLTLRSLPQMPEPSRAFSTYTWPSLlkrLRQMLitgakleegiDWQLLDTS 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536 303 CDPRHGRYLTVATVFRGPMSMKEVDEQMLAIqsKNSSYFVEWIPNNVKVAVCDIPPRGLKMASTFIGNSTAIQELFKRIS 382
Cdd:cd02189 314 GSHNPNKSLAALLVLRGKDAMKVHSADLSAF--KDPVLYSPWVPNPFNVSVSPRPFNGYEKSVTLLSNSQNIVGPLDSLL 391
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 14210536 383 EQFSAMFRRKAFLHWFTGEGMDEMEFTEAESNMNDLVSEYQQ 424
Cdd:cd02189 392 EKAWQMFKAGAYLHQYEKYGVEEEDFLDAFATLEQIIAAYKS 433
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
3-211 9.39e-63

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: 201.29  E-value: 9.39e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536     3 EIVHIQAGQCGNQIGTKFWEVISDEHGIDpaggyvgdsalqleRINVYYNESSSQKYVPRAALVDLEPGTMDSVRSGpfg 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCLEHGID--------------SLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG--- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    83 qlFRPDNFIFGQTGAGNNWAKGHYTEGAELVDAVLDVVRKECEHCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPDR 162
Cdd:pfam00091  64 --FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGA 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 14210536   163 IMNTFSVMPSpKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDIC 211
Cdd:pfam00091 142 LTVAVVTFPF-GFSEGVVRPYNAILGLKELIEHSDSVIVIDNDALYDIC 189
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
261-382 7.14e-59

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: 188.98  E-value: 7.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536   261 PRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDARNMMAACDPRHGRYLTVATVFRGPMSMKEVDEQMLAIQSKNSSY 340
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 14210536   341 FVEWIPNNVKVAVCDIPPRGLKM---ASTFIGNSTAIQELFKRIS 382
Cdd:pfam03953  81 FVEWCPTGIKVAICSQSPYVVPGskvSGLMLANTTSIAELFQRLL 125
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
47-244 8.92e-57

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: 185.77  E-value: 8.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536     47 INVYYNESssqKYVPRAALVDLEPGTMDSVRSGPFGQLFRPDNFIFGQTGAGNNWAKGHYT-----EGAELVDAVLDVVR 121
Cdd:smart00864   1 KIKVFGVG---GGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    122 KECEHCDclqGFQLTHslgggtgsgmgtlLISKIREEFPDRIMnTFSVMpsPKVSDTVVEPYNATLSVHQLVENTDETYC 201
Cdd:smart00864  78 EELEGAD---GVFITAgmgggt-gtgaapVIAEIAKEYGILTV-AVVTK--PFSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 14210536    202 IDNEALYDICFRTLKLtTPTYGDLNHLVSATMSGVTTSLRFPG 244
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
246-383 3.13e-28

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: 108.02  E-value: 3.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14210536    246 LNADLRKLAVNMVPFPrlhFFMPGFAPLTSrgsqQYRALTVPELTQ--QMFDARNMMAACDPRHgrYLTVATvfrgPMSM 323
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASG----ENRALEAAELAIssPLLEDSNIMGAKGVLV--NITGGP----DLTL 67
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14210536    324 KEVDEQMLAIQSKNSS-YFVEWIPNNVKVavcdipprgLKMASTFIGN-STAIQELFKRISE 383
Cdd:smart00865  68 KEVNEAMERIREKADPdAFIIWGPVIDEE---------LGGDEIRVTViATGIGSLFKRLSE 120
 
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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