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Conserved domains on  [gi|834400287|ref|NP_001032487|]
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tubulin beta-2b chain [Danio rerio]

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
28-457 0e+00

tubulin beta chain; Provisional


:

Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 948.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  28 MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSGP 107
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 108 FGQVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP 187
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 188 DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTTCL 267
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 268 RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRGR 347
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 348 MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG 427
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|
gi 834400287 428 EGMDEMEFTEAESNMNDLVSEYQQYQDATA 457
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATA 430
 
Name Accession Description Interval E-value
PLN00220 PLN00220
tubulin beta chain; Provisional
28-457 0e+00

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 948.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  28 MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSGP 107
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 108 FGQVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP 187
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 188 DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTTCL 267
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 268 RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRGR 347
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 348 MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG 427
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|
gi 834400287 428 EGMDEMEFTEAESNMNDLVSEYQQYQDATA 457
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATA 430
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
29-453 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: 906.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  29 REIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSGPF 108
Cdd:cd02187    1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 109 GQVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD 188
Cdd:cd02187   81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 189 RIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTTCLR 268
Cdd:cd02187  161 RIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 269 FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRGRM 348
Cdd:cd02187  241 FPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 349 SMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE 428
Cdd:cd02187  321 STKEVDEQMSKVQNKNSSYFVEWIPNNVKTSVCDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGE 400
                        410       420
                 ....*....|....*....|....*
gi 834400287 429 GMDEMEFTEAESNMNDLVSEYQQYQ 453
Cdd:cd02187  401 GMDEMEFTEAESNLNDLISEYQQYQ 425
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
288-409 3.61e-62

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: 198.22  E-value: 3.61e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  288 PRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSY 367
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 834400287  368 FVEWIPNNVKTAVCDIPPRGLKM---AATFIGNSTAIQELFKRIS 409
Cdd:pfam03953  81 FVEWCPTGIKVAICSQSPYVVPGskvSGLMLANTTSIAELFQRLL 125
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
74-271 4.41e-60

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: 195.01  E-value: 4.41e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287    74 INVYYNEasgGKYVPRAVLVDLEPGTMDSVRSGPFGQVFRPDNFVFGQSGAGNNWAKGHYT-----EGAELVDSVLDVVR 148
Cdd:smart00864   1 KIKVFGV---GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287   149 KEAESCDclqGFQLTHslgggtgsgmgtlLISKIREEYPDRimnTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYC 228
Cdd:smart00864  78 EELEGAD---GVFITAgmgggt-gtgaapVIAEIAKEYGIL---TVAVVTKPFSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 834400287   229 IDNEALYDICFRTLKLtTPSYGDLNHLVSATMSGVTTCLRFPG 271
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
 
Name Accession Description Interval E-value
PLN00220 PLN00220
tubulin beta chain; Provisional
28-457 0e+00

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 948.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  28 MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSGP 107
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 108 FGQVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP 187
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 188 DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTTCL 267
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 268 RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRGR 347
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 348 MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG 427
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|
gi 834400287 428 EGMDEMEFTEAESNMNDLVSEYQQYQDATA 457
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATA 430
PTZ00010 PTZ00010
tubulin beta chain; Provisional
28-457 0e+00

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 936.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  28 MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSGP 107
Cdd:PTZ00010   1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 108 FGQVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP 187
Cdd:PTZ00010  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 188 DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTTCL 267
Cdd:PTZ00010 161 DRIMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 268 RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRGR 347
Cdd:PTZ00010 241 RFPGQLNSDLRKLAVNLVPFPRLHFFMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 348 MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG 427
Cdd:PTZ00010 321 MSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSVCDIPPKGLKMSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|
gi 834400287 428 EGMDEMEFTEAESNMNDLVSEYQQYQDATA 457
Cdd:PTZ00010 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATV 430
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
29-453 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: 906.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  29 REIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSGPF 108
Cdd:cd02187    1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 109 GQVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD 188
Cdd:cd02187   81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 189 RIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTTCLR 268
Cdd:cd02187  161 RIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 269 FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRGRM 348
Cdd:cd02187  241 FPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 349 SMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE 428
Cdd:cd02187  321 STKEVDEQMSKVQNKNSSYFVEWIPNNVKTSVCDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGE 400
                        410       420
                 ....*....|....*....|....*
gi 834400287 429 GMDEMEFTEAESNMNDLVSEYQQYQ 453
Cdd:cd02187  401 GMDEMEFTEAESNLNDLISEYQQYQ 425
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
30-451 1.53e-167

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: 477.08  E-value: 1.53e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  30 EIVHLQAGQCGNQIGAKFWEVIsdehgidptgtyhgdsdlqldrinvyyneasggkyvpRAVLVDLEPGTMDSVRSGPFG 109
Cdd:cd06059    1 EIITIQVGQCGNQIGDRFWELA-------------------------------------RAVLVDMEEGVINEVLKGPLG 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 110 QVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDR 189
Cdd:cd06059   44 QLFDPNQFVTGVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYPKV 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 190 IMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFR---TLKLTTPSYGDLNHLVSATMSGVTTC 266
Cdd:cd06059  124 YRFTFSVFPSPDDDNVITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLTSS 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 267 LRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRG 346
Cdd:cd06059  204 LRFEGSLNVDLNEITTNLVPFPRLHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDNQLVGCDPRHGTYLACALLLRG 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 347 R-MSMKEVDEQMLNVQNKNSsyFVEWIPNNVKTAVCDIPPRGLKMAATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWY 425
Cdd:cd06059  284 KvFSLSDVRRNIDRIKPKLK--FISWNPDGFKVGLCSVPPVGQKYSLLFLSNNTSIASTFERLIERFDKLYKRKAFLHHY 361
                        410       420
                 ....*....|....*....|....*.
gi 834400287 426 TGEGMDEMEFTEAESNMNDLVSEYQQ 451
Cdd:cd06059  362 TGEGMEEGDFSEARESLANLIQEYQE 387
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
29-451 5.12e-161

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: 462.39  E-value: 5.12e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  29 REIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGT--YHGDSDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSG 106
Cdd:cd02186    1 REIISIHVGQAGVQIGNACWELFCLEHGIQPDGQmpSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 107 PFGQVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEY 186
Cdd:cd02186   81 PYRQLFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 187 PDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTTC 266
Cdd:cd02186  161 GKKSKLEFSIYPSPQVSTSVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 267 LRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRG 346
Cdd:cd02186  241 LRFDGALNVDLNEFQTNLVPYPRIHFPLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 347 RMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPP---RGLKMAATF-----IGNSTAIQELFKRISEQFTAMFRR 418
Cdd:cd02186  321 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPtvvPGSDLAKVDrsvcmLANSTAIAEAFQRLDHKFDLLYSK 400
                        410       420       430
                 ....*....|....*....|....*....|...
gi 834400287 419 KAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 451
Cdd:cd02186  401 RAFVHWYVGEGMEEGEFSEAREDLAALEKDYEE 433
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
28-451 7.47e-142

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 414.11  E-value: 7.47e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  28 MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGD--SDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRS 105
Cdd:PTZ00335   1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDknIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 106 GPFGQVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREE 185
Cdd:PTZ00335  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 186 YPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTT 265
Cdd:PTZ00335 161 YGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 266 CLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFR 345
Cdd:PTZ00335 241 SLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 346 GRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAV-----CDIPPRGL---KMAATFIGNSTAIQELFKRISEQFTAMFR 417
Cdd:PTZ00335 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGInyqppTVVPGGDLakvQRAVCMISNSTAIAEVFSRIDHKFDLMYA 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 834400287 418 RKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 451
Cdd:PTZ00335 401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEE 434
PLN00221 PLN00221
tubulin alpha chain; Provisional
28-451 2.04e-138

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 405.35  E-value: 2.04e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  28 MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQL--DRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRS 105
Cdd:PLN00221   1 MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGgdDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 106 GPFGQVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREE 185
Cdd:PLN00221  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 186 YPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTT 265
Cdd:PLN00221 161 YGKKSKLGFTVYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 266 CLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFR 345
Cdd:PLN00221 241 SLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 346 GRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPR--------GLKMAATFIGNSTAIQELFKRISEQFTAMFR 417
Cdd:PLN00221 321 GDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTvvpggdlaKVQRAVCMISNSTAVAEVFSRIDHKFDLMYA 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 834400287 418 RKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 451
Cdd:PLN00221 401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEE 434
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
30-398 3.01e-138

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: 400.63  E-value: 3.01e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  30 EIVHLQAGQCGNQIGAKFWEVisdehgidptgtyhgdsdlqldrinvyyneasggkyvprAVLVDLEPGTMDSVRSGPFG 109
Cdd:cd00286    1 EIVTIQVGQCGNQIGAAFWEQ---------------------------------------AVLVDLEPAVLDELLSGPLR 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 110 QVFRPDNFVFGQS--GAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP 187
Cdd:cd00286   42 QLFHPENIILIQKyhGAGNNWAKGHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDEYP 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 188 DRIMNTFSVVPSPKVSdTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTTCL 267
Cdd:cd00286  122 NRLVVTFSILPGPDEG-VIVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTEAL 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 268 RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRGR 347
Cdd:cd00286  201 RFEGSLNVDLRELAENLVPLPRGHFLMLGYAPLDSATSATPRSLRVKELTRRAFLPANLLVGCDPDHGEAIAALLVIRGP 280
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 834400287 348 --MSMKEVDEQMLNVQNKNSSYFvEWIPNNVKTAVCDIPPRGLKMAATFIGNS 398
Cdd:cd00286  281 pdLSSKEVERAIARVKETLGHLF-SWSPAGVKTGISPKPPAEGEVSVLALLNS 332
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
29-449 6.71e-129

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: 380.35  E-value: 6.71e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  29 REIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSGPF 108
Cdd:cd02188    1 REIITLQVGQCGNQIGSEFWKQLCSEHGISPDGSLEDFATDGNDRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNSPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 109 GQVFRPDNFVFGQ--SGAGNNWAKGhYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEY 186
Cdd:cd02188   81 KNLFNPENIYLSKegGGAGNNWASG-YSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 187 PDRIMNTFSVVPSPK-VSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTT 265
Cdd:cd02188  160 PKKLIQTYSVFPNQEeSSDVVVQPYNSILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 266 CLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTS-RGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIF 344
Cdd:cd02188  240 TLRFPGYMNNDLVSLISSLIPTPRLHFLMTSYTPLTSdQVASSVRKTTVLDVMRRLLQPKNRMVSTSTKNGCYISILNII 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 345 RGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPP--------RGLKMAatfigNSTAIQELFKRISEQFTAMF 416
Cdd:cd02188  320 QGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSKKSPyvqtahrvSGLMLA-----NHTSISSLFEKILSQYDKLR 394
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 834400287 417 RRKAFLHWYTGEGMDE---MEFTEAESNMNDLVSEY 449
Cdd:cd02188  395 KRNAFLENYRKEDMFQdnlEEFDESREVVQSLIDEY 430
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
29-452 1.80e-103

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: 316.10  E-value: 1.80e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  29 REIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRiNV--YYNEASGGKYVP------RAVLVDLEPGTM 100
Cdd:cd02190    1 REIITVQVGQCGNQIGCRFWDLALREHAAYNKDGVYDDSMSSFFR-NVdtRSGDPGDDGGSPikslkaRAVLIDMEEGVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 101 DSVRSGPFGQVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLIS 180
Cdd:cd02190   80 NELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGPQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSGLGSYILE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 181 KIREEYPDRIMNTFSVVPSpKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTP------------- 247
Cdd:cd02190  160 LLEDEFPDVYRFVTSVFPS-GDDDVITSPYNSVLALRELTEHADCVLPVENQALMDIVNKIKSSKDKgktgvlaainssg 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 248 ---------SYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQ 318
Cdd:cd02190  239 ggqkkgkkkPFDDMNNIVANLLLNLTSSMRFEGSLNVDLNEITTNLVPFPRLHFLLSSLSPLYALADVRLPPRRLDQMFS 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 319 QMFDAKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEqmlNVQN-KNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGN 397
Cdd:cd02190  319 DAFSRDHQLLKADPKHGLYLACALLVRGNVSISDLRR---NIDRlKRQLKFVSWNQDGWKIGLCSVPPVGQPYSLLCLAN 395
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 834400287 398 STAIQELFKRISEQFTAMFRRKAFLHWYTgEGMDEMEFTEAESNMNDLVSEYQQY 452
Cdd:cd02190  396 NTCIKPTFTEMHERFDKLYKRKAHLHHYT-QYMEQDDFDEALESLLDLIEEYKDL 449
PLN00222 PLN00222
tubulin gamma chain; Provisional
29-450 1.34e-99

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 306.39  E-value: 1.34e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  29 REIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSGPF 108
Cdd:PLN00222   3 REIITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGGDRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNSEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 109 GQVFRPDNFVFGQS--GAGNNWAKGhYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEY 186
Cdd:PLN00222  83 RNLYNHENIFVSDHggGAGNNWASG-YHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 187 PDRIMNTFSVVPS-PKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPSYGDLNHLVSATMSGVTT 265
Cdd:PLN00222 162 SKKLVQTYSVFPNqMETSDVVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 266 CLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPL-TSRGSQQYRSLTVPELTQQMFDAKNMMAACDPR-----HGRYLT 339
Cdd:PLN00222 242 TLRYPGYMNNDLVGLLASLIPTPRCHFLMTGYTPLtVERQANVIRKTTVLDVMRRLLQTKNIMVSSYARtkeasQAKYIS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 340 VAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPP---RGLKMAATFIGNSTAIQELFKRISEQFTAMF 416
Cdd:PLN00222 322 ILNIIQGEVDPTQVHKSLQRIRERKLANFIEWGPASIQVALSRKSPyvqTAHRVSGLMLANHTSIRHLFSKCLSQYDKLR 401
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 834400287 417 RRKAFLHWYTGEGM----DEMEFTEAESNMNDLVSEYQ 450
Cdd:PLN00222 402 KKQAFLDNYRKFPMfadnDLSEFDESREIVESLVDEYK 439
PTZ00387 PTZ00387
epsilon tubulin; Provisional
28-455 2.16e-94

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 293.17  E-value: 2.16e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  28 MREIVHLQAGQCGNQIGAKFWEVISDEH-GIDPTGTYHGDSDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSG 106
Cdd:PTZ00387   1 PREIVTVQVGQCGNQLGHRFWDVALKEHkKINANPQYDDARDSFFENVSENVNRPGKENLKARAVLVDMEEGVLNQILKS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 107 PFGQVFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEY 186
Cdd:PTZ00387  81 PLGDLFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 187 PDRIMNTFSVVPSpKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPS------------------ 248
Cdd:PTZ00387 161 PHVFRFCPVVFPS-AVDDVITSPYNSFFALRELIEHADCVLPLDNDALANIADSALSRKKKKlakgnikrgpqphkysva 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 249 ---------YGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQ 319
Cdd:PTZ00387 240 kptetkklpYDKMNNIVAQLLSNLTSSMRFEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGPRRLDQMFKD 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 320 MFDAKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVqnKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGNST 399
Cdd:PTZ00387 320 CLDPDHQMVAATPEAGKYLATALIVRGPQNVSDVTRNILRL--KEQLNMIYWNEDGFKTGLCNVSPLGQPYSLLCLANNC 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 834400287 400 AIQELFKRISEQFTAMFRRKAFLHWYTgEGMDEMEFTEAESNMNDLVSEYQQYQDA 455
Cdd:PTZ00387 398 CIRNKFESMLERFNKLYKRKSHVHHYT-EYLEQAYFDETLETIQNLIDDYAYLQTA 452
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
31-451 1.86e-73

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: 237.93  E-value: 1.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  31 IVHLQAGQCGNQIGAKFWEVISDEhgidptGTYHGDSDLQLDRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSGPFGQ 110
Cdd:cd02189    2 IVTVQVGQCGNQLGDELFDTLADE------ADSSASEGDQNSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRARSG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 111 --VFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD 188
Cdd:cd02189   76 awSYDPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEYPK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 189 R-IMNTfsVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTP-SYGDLNHLVSATMSGV--- 263
Cdd:cd02189  156 AyLLNT--VVWPYSSGEVPVQNYNTLLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVllp 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 264 TTCLRFPGQLNAD-LRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRSLTVPEL---TQQMF----------DAKNMMAA 329
Cdd:cd02189  234 SSSPTSPSPLRRCpLGDLLEHLCPHPAYKLLTLRSLPQMPEPSRAFSTYTWPSLlkrLRQMLitgakleegiDWQLLDTS 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287 330 CDPRHGRYLTVAAIFRG--RMSMKEVDEQMLnvqnKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGNSTAIQELFKR 407
Cdd:cd02189  314 GSHNPNKSLAALLVLRGkdAMKVHSADLSAF----KDPVLYSPWVPNPFNVSVSPRPFNGYEKSVTLLSNSQNIVGPLDS 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 834400287 408 ISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 451
Cdd:cd02189  390 LLEKAWQMFKAGAYLHQYEKYGVEEEDFLDAFATLEQIIAAYKS 433
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
288-409 3.61e-62

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: 198.22  E-value: 3.61e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  288 PRLHFFMPGFAPLTSRGSQQYRSLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSY 367
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 834400287  368 FVEWIPNNVKTAVCDIPPRGLKM---AATFIGNSTAIQELFKRIS 409
Cdd:pfam03953  81 FVEWCPTGIKVAICSQSPYVVPGskvSGLMLANTTSIAELFQRLL 125
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
30-238 5.92e-62

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: 199.75  E-value: 5.92e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287   30 EIVHLQAGQCGNQIGAKFWEVISDEHGIDptgtyhgdsdlqldRINVYYNEASGGKYVPRAVLVDLEPGTMDSVRSGpfg 109
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCLEHGID--------------SLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG--- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  110 qvFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDR 189
Cdd:pfam00091  64 --FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGA 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 834400287  190 IMNTFSVVPSpKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDIC 238
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 ...
74-271 4.41e-60

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: 195.01  E-value: 4.41e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287    74 INVYYNEasgGKYVPRAVLVDLEPGTMDSVRSGPFGQVFRPDNFVFGQSGAGNNWAKGHYT-----EGAELVDSVLDVVR 148
Cdd:smart00864   1 KIKVFGV---GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287   149 KEAESCDclqGFQLTHslgggtgsgmgtlLISKIREEYPDRimnTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYC 228
Cdd:smart00864  78 EELEGAD---GVFITAgmgggt-gtgaapVIAEIAKEYGIL---TVAVVTKPFSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 834400287   229 IDNEALYDICFRTLKLtTPSYGDLNHLVSATMSGVTTCLRFPG 271
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 ...
273-410 5.08e-30

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: 113.03  E-value: 5.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287   273 LNADLRKLAVNMVPFPrlhFFMPGFAPLTSrgsqQYRSLTVPELTQ--QMFDAKNMMAACDPRHgrYLTVAAifrgRMSM 350
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASG----ENRALEAAELAIssPLLEDSNIMGAKGVLV--NITGGP----DLTL 67
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 834400287   351 KEVDEQMLNVQNKNSS-YFVEWIPNNVKTavcdipprgLKMAATFIGN-STAIQELFKRISE 410
Cdd:smart00865  68 KEVNEAMERIREKADPdAFIIWGPVIDEE---------LGGDEIRVTViATGIGSLFKRLSE 120
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
29-105 1.62e-04

Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved domains, segments I, II and III. Segments I and III are common to Tubulins pfam00091, but segment II aligns with myosin heavy chain sequences from D. melanogaster (PIR C35815), rabbit (SP P04460), and human (PIR S12458). Segment II of misato is a major contributor to its greater length compared with the various tubulins. The most significant sequence similarities to this 54-amino acid region are from a motif found in the heavy chains of myosins from different organizms. A comparison of segment II with the vertebrate myosin heavy chains reveals that it is homologous to a myosin peptide in the hinge region linking the S2 and LMM domains. Segment II also contains heptad repeats which are characteriztic of the myosin tail alpha-helical coiled-coils. This myosin-like homology may be due only to the fact that both myosin and Misato carry coiled-coils, which appear similar but are not necessarily homologous (Wood V, personal communication).


Pssm-ID: 431412 [Multi-domain]  Cd Length: 115  Bit Score: 41.08  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287   29 REIVHLQAGQCGNQIGAKFWEVisDEHGIdptgTYHGDSDL-QLDRiNVYY--NEASGG--KYVPRAVLVDLePGTMDSV 103
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWNT--QESYF----TYDPNEEPsEVDH-DVLFreGETLDGqvTYTPRLLIYDL-KGSFGSL 72

                  ..
gi 834400287  104 RS 105
Cdd:pfam10644  73 RK 74
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
29-106 3.42e-03

Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family of GTPases and is localized to the the outer membrane of mitochondria. It has a role in mitochondrial fusion and in mitochondrial distribution and morphology. Mutations in its Drosophila homolog (misato) lead to irregular chromosome segregation during mitosis. Deletion of the budding yeast homolog DML1 is lethal and unregulate expression of DML1 leads to mitochondrial dispersion and abnormalities in cell morphology. The Misato/DML1 protein family is conserved from yeast to human, but its exact function is still unknown.


Pssm-ID: 276964 [Multi-domain]  Cd Length: 539  Bit Score: 39.99  E-value: 3.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 834400287  29 REIVHLQAGQCGNQIGAKFWEvISDEHgidptGTYHGDSDLQLDRIN--VYYNEASGGK----YVPRAVLVDLEpGTMDS 102
Cdd:cd06060    1 REIVTLQLGHYANFVGTHFWN-IQESY-----FTYDEDEEAPPDHDVhdVLFREGETLQgeetYTPRLLLVDLK-GSLGS 73

                 ....
gi 834400287 103 VRSG 106
Cdd:cd06060   74 LRKE 77
 
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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