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Conserved domains on  [gi|645912972|ref|NP_001280142|]
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tubulin beta chain isoform c [Homo sapiens]

Protein Classification

tubulin beta chain( domain architecture ID 1000324)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00010 super family cl30500
tubulin beta chain; Provisional
1-227 9.28e-149

tubulin beta chain; Provisional


The actual alignment was detected with superfamily member PTZ00010:

Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 422.26  E-value: 9.28e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   1 MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGP 80
Cdd:PTZ00010   1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972  81 FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVD----------------------------------- 125
Cdd:PTZ00010  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAEscdclqgfqithslgggtgsgmgtllisklreeyp 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972     --------------------------------------------------------------------------------
Cdd:PTZ00010 161 drimmtfsvfpspkvsdtvvepynatlsvhqlvenadesmcidnealydicfrtlklttptygdlnhlvsavmsgvtccl 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 126 --------------------------------------------------EQMLNVQN---------------------- 133
Cdd:PTZ00010 241 rfpgqlnsdlrklavnlvpfprlhffmmgfapltsrgsqqyrglsvpeltQQMFDAKNmmcaadprhgryltasalfrgr 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 134 ---------------KNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG 198
Cdd:PTZ00010 321 mstkevdeqmlnvqnKNSSYFVEWIPNNIKSSVCDIPPKGLKMSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTG 400
                        410       420
                 ....*....|....*....|....*....
gi 645912972 199 EGMDEMEFTEAESNMNDLVSEYQQYQDAT 227
Cdd:PTZ00010 401 EGMDEMEFTEAESNMNDLVSEYQQYQDAT 429
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-227 9.28e-149

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 422.26  E-value: 9.28e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   1 MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGP 80
Cdd:PTZ00010   1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972  81 FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVD----------------------------------- 125
Cdd:PTZ00010  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAEscdclqgfqithslgggtgsgmgtllisklreeyp 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972     --------------------------------------------------------------------------------
Cdd:PTZ00010 161 drimmtfsvfpspkvsdtvvepynatlsvhqlvenadesmcidnealydicfrtlklttptygdlnhlvsavmsgvtccl 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 126 --------------------------------------------------EQMLNVQN---------------------- 133
Cdd:PTZ00010 241 rfpgqlnsdlrklavnlvpfprlhffmmgfapltsrgsqqyrglsvpeltQQMFDAKNmmcaadprhgryltasalfrgr 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 134 ---------------KNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG 198
Cdd:PTZ00010 321 mstkevdeqmlnvqnKNSSYFVEWIPNNIKSSVCDIPPKGLKMSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTG 400
                        410       420
                 ....*....|....*....|....*....
gi 645912972 199 EGMDEMEFTEAESNMNDLVSEYQQYQDAT 227
Cdd:PTZ00010 401 EGMDEMEFTEAESNMNDLVSEYQQYQDAT 429
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-224 8.41e-135

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: 385.77  E-value: 8.41e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   2 REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPF 81
Cdd:cd02187    1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972  82 GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVD------------------------------------ 125
Cdd:cd02187   81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAEscdclqgfqlthslgggtgsglgtlllsklreeypd 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972     --------------------------------------------------------------------------------
Cdd:cd02187  161 rimstfsvlpspkvsdtvvepynavlslhqlvenadetfcidnealynicqrtlkltqptyddlnhlisqvmsgitsslr 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 126 -------------------------------------------------EQMLNVQN---------------------KN 135
Cdd:cd02187  241 fpgqlnsdlrklatnlvpfprlhfltpgfapltsrgsqqyrkltvpeltQQLFDAKNmmaacdprhgryltaaaifrgRI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 136 SSYFVE----------------WIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE 199
Cdd:cd02187  321 STKEVDeqmskvqnknssyfveWIPNNVKTSVCDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGE 400
                        410       420
                 ....*....|....*....|....*
gi 645912972 200 GMDEMEFTEAESNMNDLVSEYQQYQ 224
Cdd:cd02187  401 GMDEMEFTEAESNLNDLISEYQQYQ 425
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
3-126 6.13e-34

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: 120.79  E-value: 6.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972    3 EIVHIQAGQCGNQIGAKFWEVISDEHGIDptgtyhgdsdlqldRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGpfg 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCLEHGID--------------SLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG--- 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 645912972   83 qiFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVDE 126
Cdd:pfam00091  64 --FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEG 105
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
57-125 3.17e-23

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: 92.55  E-value: 3.17e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 645912972    57 GKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYT-----EGAELVDSVLDVVRKEVD 125
Cdd:smart00864   8 GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIREELE 81
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-227 9.28e-149

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 422.26  E-value: 9.28e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   1 MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGP 80
Cdd:PTZ00010   1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972  81 FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVD----------------------------------- 125
Cdd:PTZ00010  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAEscdclqgfqithslgggtgsgmgtllisklreeyp 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972     --------------------------------------------------------------------------------
Cdd:PTZ00010 161 drimmtfsvfpspkvsdtvvepynatlsvhqlvenadesmcidnealydicfrtlklttptygdlnhlvsavmsgvtccl 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 126 --------------------------------------------------EQMLNVQN---------------------- 133
Cdd:PTZ00010 241 rfpgqlnsdlrklavnlvpfprlhffmmgfapltsrgsqqyrglsvpeltQQMFDAKNmmcaadprhgryltasalfrgr 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 134 ---------------KNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG 198
Cdd:PTZ00010 321 mstkevdeqmlnvqnKNSSYFVEWIPNNIKSSVCDIPPKGLKMSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTG 400
                        410       420
                 ....*....|....*....|....*....
gi 645912972 199 EGMDEMEFTEAESNMNDLVSEYQQYQDAT 227
Cdd:PTZ00010 401 EGMDEMEFTEAESNMNDLVSEYQQYQDAT 429
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-224 8.41e-135

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: 385.77  E-value: 8.41e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   2 REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPF 81
Cdd:cd02187    1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972  82 GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVD------------------------------------ 125
Cdd:cd02187   81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAEscdclqgfqlthslgggtgsglgtlllsklreeypd 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972     --------------------------------------------------------------------------------
Cdd:cd02187  161 rimstfsvlpspkvsdtvvepynavlslhqlvenadetfcidnealynicqrtlkltqptyddlnhlisqvmsgitsslr 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 126 -------------------------------------------------EQMLNVQN---------------------KN 135
Cdd:cd02187  241 fpgqlnsdlrklatnlvpfprlhfltpgfapltsrgsqqyrkltvpeltQQLFDAKNmmaacdprhgryltaaaifrgRI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 136 SSYFVE----------------WIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE 199
Cdd:cd02187  321 STKEVDeqmskvqnknssyfveWIPNNVKTSVCDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGE 400
                        410       420
                 ....*....|....*....|....*
gi 645912972 200 GMDEMEFTEAESNMNDLVSEYQQYQ 224
Cdd:cd02187  401 GMDEMEFTEAESNLNDLISEYQQYQ 425
PLN00220 PLN00220
tubulin beta chain; Provisional
1-227 3.95e-132

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 379.94  E-value: 3.95e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   1 MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGP 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972  81 FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEV------------------------------------ 124
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAencdclqgfqvchslgggtgsgmgtlliskireeyp 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 125 DEQMLN-------------VQNKNSSYFVEWIPNNV-------------------------------------------- 147
Cdd:PLN00220 161 DRMMLTfsvfpspkvsdtvVEPYNATLSVHQLVENAdecmvldnealydicfrtlklttpsfgdlnhlisatmsgvtccl 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 148 -----------KTAVCDIP------------------------------------------------------------- 155
Cdd:PLN00220 241 rfpgqlnsdlrKLAVNLIPfprlhffmvgfapltsrgsqqyraltvpeltqqmwdaknmmcaadprhgryltasamfrgk 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 156 -------------------------------------PRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG 198
Cdd:PLN00220 321 mstkevdeqminvqnknssyfvewipnnvkssvcdipPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420
                 ....*....|....*....|....*....
gi 645912972 199 EGMDEMEFTEAESNMNDLVSEYQQYQDAT 227
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDAT 429
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-222 8.14e-46

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: 158.09  E-value: 8.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   2 REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGT--YHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSG 79
Cdd:cd02186    1 REIISIHVGQAGVQIGNACWELFCLEHGIQPDGQmpSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972  80 PFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVDE--------------------------QMLNVQ- 132
Cdd:cd02186   81 PYRQLFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQcdglqgflifhsvgggtgsgltslllERLSVDy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 133 -------------NKNSSYFVE------------------------------------WIPN------------------ 145
Cdd:cd02186  161 gkksklefsiypsPQVSTSVVEpynsvltthsllehsdcsilldnealydicrrqldiERPTytnlnrliaqvvssltas 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 146 ---------------------------------------------NVKT-----------------------AVC----- 152
Cdd:cd02186  241 lrfdgalnvdlnefqtnlvpyprihfplvsyapiisaekanheqlSVQEitnscfepanqmvkcdprhgkymACCllyrg 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 153 DIPPR-----------------------GLKMAVTF--------------------IGNSTAIQELFKRISEQFTAMFRR 189
Cdd:cd02186  321 DVVPKdvnaaiatiktkrtiqfvdwcptGFKVGINYqpptvvpgsdlakvdrsvcmLANSTAIAEAFQRLDHKFDLLYSK 400
                        410       420       430
                 ....*....|....*....|....*....|...
gi 645912972 190 KAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 222
Cdd:cd02186  401 RAFVHWYVGEGMEEGEFSEAREDLAALEKDYEE 433
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
2-125 2.38e-44

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: 153.85  E-value: 2.38e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   2 REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPF 81
Cdd:cd02188    1 REIITLQVGQCGNQIGSEFWKQLCSEHGISPDGSLEDFATDGNDRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNSPY 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 645912972  82 GQIFRPDNFVFGQ--SGAGNNWAKGhYTEGAELVDSVLDVVRKEVD 125
Cdd:cd02188   81 KNLFNPENIYLSKegGGAGNNWASG-YSQGEKVQEEILDIIDREAE 125
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
3-222 1.83e-39

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: 140.03  E-value: 1.83e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   3 EIVHIQAGQCGNQIGAKFWEVIsdehgidptgtyhgdsdlqldrisvyyneatggkyvpRAILVDLEPGTMDSVRSGPFG 82
Cdd:cd06059    1 EIITIQVGQCGNQIGDRFWELA-------------------------------------RAVLVDMEEGVINEVLKGPLG 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972  83 QIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVDE--------------------------QMLN------ 130
Cdd:cd06059   44 QLFDPNQFVTGVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKcdslqgffilhslgggtgsglgsyllELLEdeypkv 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 131 ---------------------------------------VQNKNSSYFVEWIP-------------NNV----------- 147
Cdd:cd06059  124 yrftfsvfpspdddnvitspynsvlalnhltehadcvlpIDNEALYDICNRQPatldidfppfddmNNLvaqllssltss 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 148 -------------------------------------------KTAVCDI---------------PPRGLKMAVTFIG-- 167
Cdd:cd06059  204 lrfegslnvdlneittnlvpfprlhfllpslspltsandvtlePLTLDQLfsdlfskdnqlvgcdPRHGTYLACALLLrg 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 168 -------------------------------------------------NSTAIQELFKRISEQFTAMFRRKAFLHWYTG 198
Cdd:cd06059  284 kvfslsdvrrnidrikpklkfiswnpdgfkvglcsvppvgqkysllflsNNTSIASTFERLIERFDKLYKRKAFLHHYTG 363
                        410       420
                 ....*....|....*....|....
gi 645912972 199 EGMDEMEFTEAESNMNDLVSEYQQ 222
Cdd:cd06059  364 EGMEEGDFSEARESLANLIQEYQE 387
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-126 1.04e-37

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 136.76  E-value: 1.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   1 MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGD--SDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRS 78
Cdd:PTZ00335   1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDknIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 645912972  79 GPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVDE 126
Cdd:PTZ00335  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADN 128
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-125 1.96e-37

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 136.09  E-value: 1.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   1 MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQL--DRISVYYNEATGGKYVPRAILVDLEPGTMDSVRS 78
Cdd:PLN00221   1 MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGgdDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 645912972  79 GPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVD 125
Cdd:PLN00221  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLAD 127
PLN00222 PLN00222
tubulin gamma chain; Provisional
2-125 2.62e-34

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 127.65  E-value: 2.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   2 REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPF 81
Cdd:PLN00222   3 REIITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGGDRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNSEY 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 645912972  82 GQIFRPDNFVFGQS--GAGNNWAKGhYTEGAELVDSVLDVVRKEVD 125
Cdd:PLN00222  83 RNLYNHENIFVSDHggGAGNNWASG-YHQGEQVEEDIMDMIDREAD 127
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
3-126 6.13e-34

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: 120.79  E-value: 6.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972    3 EIVHIQAGQCGNQIGAKFWEVISDEHGIDptgtyhgdsdlqldRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGpfg 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCLEHGID--------------SLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG--- 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 645912972   83 qiFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVDE 126
Cdd:pfam00091  64 --FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEG 105
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
4-124 6.77e-32

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: 120.83  E-value: 6.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   4 IVHIQAGQCGNQIGAKFWEVISDEhgidptGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQ 83
Cdd:cd02189    2 IVTVQVGQCGNQLGDELFDTLADE------ADSSASEGDQNSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRARSG 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 645912972  84 --IFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEV 124
Cdd:cd02189   76 awSYDPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREA 118
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
3-126 1.64e-31

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: 117.89  E-value: 1.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   3 EIVHIQAGQCGNQIGAKFWEVisdehgidptgtyhgdsdlqldrisvyyneatggkyvprAILVDLEPGTMDSVRSGPFG 82
Cdd:cd00286    1 EIVTIQVGQCGNQIGAAFWEQ---------------------------------------AVLVDLEPAVLDELLSGPLR 41
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 645912972  83 QIFRPDNFVFGQS--GAGNNWAKGHYTEGAELVDSVLDVVRKEVDE 126
Cdd:cd00286   42 QLFHPENIILIQKyhGAGNNWAKGHSVAGEEYQEEILDAIRKEVEE 87
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
2-124 2.07e-29

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: 114.26  E-value: 2.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   2 REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGK-YVP------RAILVDLEPGTMD 74
Cdd:cd02190    1 REIITVQVGQCGNQIGCRFWDLALREHAAYNKDGVYDDSMSSFFRNVDTRSGDPGDDgGSPikslkaRAVLIDMEEGVVN 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 645912972  75 SVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEV 124
Cdd:cd02190   81 ELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGPQYGESILEKLRRAA 130
PTZ00387 PTZ00387
epsilon tubulin; Provisional
1-126 3.54e-29

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 113.67  E-value: 3.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   1 MREIVHIQAGQCGNQIGAKFWEVISDEH-GIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSG 79
Cdd:PTZ00387   1 PREIVTVQVGQCGNQLGHRFWDVALKEHkKINANPQYDDARDSFFENVSENVNRPGKENLKARAVLVDMEEGVLNQILKS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 645912972  80 PFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEVDE 126
Cdd:PTZ00387  81 PLGDLFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQ 127
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
118-180 7.30e-25

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: 94.99  E-value: 7.30e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 645912972  118 DVVRKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKM---AVTFIGNSTAIQELFKRIS 180
Cdd:pfam03953  60 DVSPKDVHRAIQRIKEKRSAQFVEWCPTGIKVAICSQSPYVVPGskvSGLMLANTTSIAELFQRLL 125
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
57-125 3.17e-23

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: 92.55  E-value: 3.17e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 645912972    57 GKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYT-----EGAELVDSVLDVVRKEVD 125
Cdd:smart00864   8 GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIREELE 81
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
139-223 3.57e-17

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: 79.98  E-value: 3.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 139 FVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTgEGMDEMEFTEAESNMNDLVS 218
Cdd:cd02190  366 FVSWNQDGWKIGLCSVPPVGQPYSLLCLANNTCIKPTFTEMHERFDKLYKRKAHLHHYT-QYMEQDDFDEALESLLDLIE 444

                 ....*
gi 645912972 219 EYQQY 223
Cdd:cd02190  445 EYKDL 449
PTZ00387 PTZ00387
epsilon tubulin; Provisional
134-226 1.74e-13

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 68.98  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 134 KNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTgEGMDEMEFTEAESNM 213
Cdd:PTZ00387 361 KEQLNMIYWNEDGFKTGLCNVSPLGQPYSLLCLANNCCIRNKFESMLERFNKLYKRKSHVHHYT-EYLEQAYFDETLETI 439
                         90
                 ....*....|...
gi 645912972 214 NDLVSEYQQYQDA 226
Cdd:PTZ00387 440 QNLIDDYAYLQTA 452
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
134-222 3.65e-10

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: 59.20  E-value: 3.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 134 KNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNM 213
Cdd:cd02189  345 KDPVLYSPWVPNPFNVSVSPRPFNGYEKSVTLLSNSQNIVGPLDSLLEKAWQMFKAGAYLHQYEKYGVEEEDFLDAFATL 424

                 ....*....
gi 645912972 214 NDLVSEYQQ 222
Cdd:cd02189  425 EQIIAAYKS 433
PLN00222 PLN00222
tubulin gamma chain; Provisional
115-221 2.68e-09

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 56.78  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972 115 SVLDVVRKEVD-----EQMLNVQNKNSSYFVEWIPNNVKTAVCDIPP--------RGLKMAvtfigNSTAIQELFKRISE 181
Cdd:PLN00222 321 SILNIIQGEVDptqvhKSLQRIRERKLANFIEWGPASIQVALSRKSPyvqtahrvSGLMLA-----NHTSIRHLFSKCLS 395
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 645912972 182 QFTAMFRRKAFLHWYTGEGM----DEMEFTEAESNMNDLVSEYQ 221
Cdd:PLN00222 396 QYDKLRKKQAFLDNYRKFPMfadnDLSEFDESREIVESLVDEYK 439
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
117-181 1.21e-08

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: 51.78  E-value: 1.21e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 645912972   117 LDVVRKEVDEQMLNVQNKNSS-YFVEWIPNNVKTavcdipprgLKMAVTFIGN-STAIQELFKRISE 181
Cdd:smart00865  63 PDLTLKEVNEAMERIREKADPdAFIIWGPVIDEE---------LGGDEIRVTViATGIGSLFKRLSE 120
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
2-78 5.51e-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: 38.39  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972    2 REIVHIQAGQCGNQIGAKFWEVisDEHGIdptgTYHGDSDL-QLDRiSVYY--NEATGG--KYVPRAILVDLePGTMDSV 76
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWNT--QESYF----TYDPNEEPsEVDH-DVLFreGETLDGqvTYTPRLLIYDL-KGSFGSL 72

                  ..
gi 645912972   77 RS 78
Cdd:pfam10644  73 RK 74
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
2-79 2.72e-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: 38.45  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 645912972   2 REIVHIQAGQCGNQIGAKFWEvISDEHgidptGTYHGDSDLQLDRI---SVYY------NEATggkYVPRAILVDLEpGT 72
Cdd:cd06060    1 REIVTLQLGHYANFVGTHFWN-IQESY-----FTYDEDEEAPPDHDvhdVLFRegetlqGEET---YTPRLLLVDLK-GS 70

                 ....*..
gi 645912972  73 MDSVRSG 79
Cdd:cd06060   71 LGSLRKE 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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