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Conserved domains on  [gi|398010963|ref|XP_003858678|]
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beta tubulin, partial [Leishmania donovani]

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
 1-147 2.48e-118

tubulin beta chain; Provisional


The actual alignment was detected with superfamily member PTZ00010:

Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 340.60  E-value: 2.48e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   1 MREIVSCQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLERINVYFDESTGGRYVPRAVLMDLEPGTMDSVRAGP 80
Cdd:PTZ00010   1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398010963  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:PTZ00010  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGM 147
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
 1-147 2.48e-118

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 340.60  E-value: 2.48e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   1 MREIVSCQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLERINVYFDESTGGRYVPRAVLMDLEPGTMDSVRAGP 80
Cdd:PTZ00010   1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398010963  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:PTZ00010  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGM 147
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 2-147 1.14e-109

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: 317.97  E-value: 1.14e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   2 REIVSCQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLERINVYFDESTGGRYVPRAVLMDLEPGTMDSVRAGPY 81
Cdd:cd02187    1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398010963  82 GQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:cd02187   81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGL 146
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
 3-146 5.25e-51

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: 160.85  E-value: 5.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963    3 EIVSCQAGQCGNQIGSKFWEVISDEHGvdptgtyqgdsdlqLERINVYFDESTGGRYVPRAVLMDLEPGTMDSVRAGpyg 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCLEHG--------------IDSLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG--- 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398010963   83 qlFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSG 146
Cdd:pfam00091  64 --FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSG 125
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
 47-147 3.02e-37

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: 125.68  E-value: 3.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963    47 INVYFDEstgGRYVPRAVLMDLEPGTMDSVRAGPYGQLFRPDNFIFGQSGAGNNWAKGHYT-----EGAELIDSVLDVCR 121
Cdd:smart00864   1 KIKVFGV---GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77

                           90       100
                   ....*....|....*....|....*.
gi 398010963   122 KEAESCDclqGFQLSHSLGGGTGSGM 147
Cdd:smart00864  78 EELEGAD---GVFITAGMGGGTGTGA 100
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
 1-147 2.48e-118

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 340.60  E-value: 2.48e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   1 MREIVSCQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLERINVYFDESTGGRYVPRAVLMDLEPGTMDSVRAGP 80
Cdd:PTZ00010   1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398010963  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:PTZ00010  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGM 147
PLN00220 PLN00220
tubulin beta chain; Provisional
 1-147 1.39e-115

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 333.71  E-value: 1.39e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   1 MREIVSCQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLERINVYFDESTGGRYVPRAVLMDLEPGTMDSVRAGP 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398010963  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGM 147
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 2-147 1.14e-109

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: 317.97  E-value: 1.14e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   2 REIVSCQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLERINVYFDESTGGRYVPRAVLMDLEPGTMDSVRAGPY 81
Cdd:cd02187    1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398010963  82 GQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:cd02187   81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGL 146
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 2-147 4.00e-65

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: 204.31  E-value: 4.00e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   2 REIVSCQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLERINV--YFDESTGGRYVPRAVLMDLEPGTMDSVRAG 79
Cdd:cd02186    1 REIISIHVGQAGVQIGNACWELFCLEHGIQPDGQMPSDKTIGGDDDNFntFFSETGSGKYVPRAVFVDLEPTVIDEIRTG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398010963  80 PYGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:cd02186   81 PYRQLFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGL 148
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
 2-147 9.75e-64

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: 200.46  E-value: 9.75e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   2 REIVSCQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLERINVYFDESTGGRYVPRAVLMDLEPGTMDSVRAGPY 81
Cdd:cd02188    1 REIITLQVGQCGNQIGSEFWKQLCSEHGISPDGSLEDFATDGNDRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNSPY 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398010963  82 GQLFRPDNFIFGQ--SGAGNNWAKGhYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:cd02188   81 KNLFNPENIYLSKegGGAGNNWASG-YSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGM 147
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
 1-147 3.16e-54

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 176.44  E-value: 3.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   1 MREIVSCQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLE--RINVYFDESTGGRYVPRAVLMDLEPGTMDSVRA 78
Cdd:PTZ00335   1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEddAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398010963  79 GPYGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:PTZ00335  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGL 149
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
 3-147 2.43e-53

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: 172.77  E-value: 2.43e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   3 EIVSCQAGQCGNQIGSKFWEVIsdehgvdptgtyqgdsdlqlerinvyfdestggryvpRAVLMDLEPGTMDSVRAGPYG 82
Cdd:cd06059    1 EIITIQVGQCGNQIGDRFWELA-------------------------------------RAVLVDMEEGVINEVLKGPLG 43

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398010963  83 QLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:cd06059   44 QLFDPNQFVTGVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGL 108
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
 3-146 5.25e-51

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: 160.85  E-value: 5.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963    3 EIVSCQAGQCGNQIGSKFWEVISDEHGvdptgtyqgdsdlqLERINVYFDESTGGRYVPRAVLMDLEPGTMDSVRAGpyg 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCLEHG--------------IDSLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG--- 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398010963   83 qlFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSG 146
Cdd:pfam00091  64 --FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSG 125
PLN00221 PLN00221
tubulin alpha chain; Provisional
 1-147 2.85e-49

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 163.44  E-value: 2.85e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   1 MREIVSCQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQL--ERINVYFDESTGGRYVPRAVLMDLEPGTMDSVRA 78
Cdd:PLN00221   1 MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGgdDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398010963  79 GPYGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:PLN00221  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGL 149
PLN00222 PLN00222
tubulin gamma chain; Provisional
 2-147 1.06e-47

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 159.63  E-value: 1.06e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   2 REIVSCQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLERINVYFDESTGGRYVPRAVLMDLEPGTMDSVRAGPY 81
Cdd:PLN00222   3 REIITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGGDRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNSEY 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398010963  82 GQLFRPDNFIFGQS--GAGNNWAKGhYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:PLN00222  83 RNLYNHENIFVSDHggGAGNNWASG-YHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGM 149
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
 3-147 4.08e-47

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: 155.26  E-value: 4.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   3 EIVSCQAGQCGNQIGSKFWEVisdehgvdptgtyqgdsdlqlerinvyfdestggryvprAVLMDLEPGTMDSVRAGPYG 82
Cdd:cd00286    1 EIVTIQVGQCGNQIGAAFWEQ---------------------------------------AVLVDLEPAVLDELLSGPLR 41

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398010963  83 QLFRPDNFIFGQS--GAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:cd00286   42 QLFHPENIILIQKyhGAGNNWAKGHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGL 108
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
 4-147 4.32e-46

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: 154.73  E-value: 4.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   4 IVSCQAGQCGNQIGSKFWEVISDEhgvdptgTYQGDSDLQLERINVYFD-ESTGGRYVPRAVLMDLEPGTMDSVRAGPYG 82
Cdd:cd02189    2 IVTVQVGQCGNQLGDELFDTLADE-------ADSSASEGDQNSSATRFFsPFSDGKLKARCVLVDMEPKVVQQVLSRARS 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398010963  83 QL--FRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:cd02189   75 GAwsYDPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGL 141
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
 2-146 2.50e-45

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: 153.16  E-value: 2.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   2 REIVSCQAGQCGNQIGSKFWEVISDEHG-VDPTGTYQgDSDLQLERiNV--YFDESTGGRYVP------RAVLMDLEPGT 72
Cdd:cd02190    1 REIITVQVGQCGNQIGCRFWDLALREHAaYNKDGVYD-DSMSSFFR-NVdtRSGDPGDDGGSPikslkaRAVLIDMEEGV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398010963  73 MDSVRAGPYGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSG 146
Cdd:cd02190   79 VNELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGPQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSG 152
PTZ00387 PTZ00387
epsilon tubulin; Provisional
 1-147 1.53e-44

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 151.42  E-value: 1.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   1 MREIVSCQAGQCGNQIGSKFWEVISDEH-GVDPTGTYQgdsdlqlERINVYFDESTGGRYVP-------RAVLMDLEPGT 72
Cdd:PTZ00387   1 PREIVTVQVGQCGNQLGHRFWDVALKEHkKINANPQYD-------DARDSFFENVSENVNRPgkenlkaRAVLVDMEEGV 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398010963  73 MDSVRAGPYGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCRKEAESCDCLQGFQLSHSLGGGTGSGM 147
Cdd:PTZ00387  74 LNQILKSPLGDLFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGL 148
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
 47-147 3.02e-37

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: 125.68  E-value: 3.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963    47 INVYFDEstgGRYVPRAVLMDLEPGTMDSVRAGPYGQLFRPDNFIFGQSGAGNNWAKGHYT-----EGAELIDSVLDVCR 121
Cdd:smart00864   1 KIKVFGV---GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77

                           90       100
                   ....*....|....*....|....*.
gi 398010963   122 KEAESCDclqGFQLSHSLGGGTGSGM 147
Cdd:smart00864  78 EELEGAD---GVFITAGMGGGTGTGA 100
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
 2-96 2.61e-04

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: 39.61  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963   2 REIVSCQAGQCGNQIGSKFWEvISDEHgvdptGTYQGDSDLQLERIN--VYFDESTGGR----YVPRAVLMDLEpGTMDS 75
Cdd:cd06060    1 REIVTLQLGHYANFVGTHFWN-IQESY-----FTYDEDEEAPPDHDVhdVLFREGETLQgeetYTPRLLLVDLK-GSLGS 73

                         90       100
                 ....*....|....*....|.
gi 398010963  76 VRAgpYGQLFRPDNFIFGQSG 96
Cdd:cd06060   74 LRK--EGALYEEPDDDSSESQ 92
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
 2-78 1.97e-03

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: 35.69  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398010963    2 REIVSCQAGQCGNQIGSKFW----EVISDEHGVDPtgtYQGDSDLQL-ERINVYFDEStggrYVPRAVLMDLePGTMDSV 76
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWntqeSYFTYDPNEEP---SEVDHDVLFrEGETLDGQVT----YTPRLLIYDL-KGSFGSL 72


                  ..
gi 398010963   77 RA 78
Cdd:pfam10644  73 RK 74
 
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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