NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1919556361|gb|QOS44251|]
View 

beta-tubulin, partial [Neonectria neomacrospora]

Protein Classification

tubulin beta chain( domain architecture ID 1000324)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTZ00010 super family cl30500
tubulin beta chain; Provisional
 1-97 1.08e-64

tubulin beta chain; Provisional


The actual alignment was detected with superfamily member PTZ00010:

Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 201.16  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEHGLDSNGVYAGNSELQLERMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQL 80
Cdd:PTZ00010    5 VHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGPYGQL 84

                          90
                  ....*....|....*..
gi 1919556361  81 FRPDNFVFGQSGAGNNW 97
Cdd:PTZ00010   85 FRPDNFIFGQSGAGNNW 101
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
 1-97 1.08e-64

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 201.16  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEHGLDSNGVYAGNSELQLERMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQL 80
Cdd:PTZ00010    5 VHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGPYGQL 84

                          90
                  ....*....|....*..
gi 1919556361  81 FRPDNFVFGQSGAGNNW 97
Cdd:PTZ00010   85 FRPDNFIFGQSGAGNNW 101
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 1-97 1.13e-63

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: 197.79  E-value: 1.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEHGLDSNGVYAGNSELQLERMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQL 80
Cdd:cd02187     4 IHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPYGQL 83

                          90
                  ....*....|....*..
gi 1919556361  81 FRPDNFVFGQSGAGNNW 97
Cdd:cd02187    84 FRPDNFVFGQSGAGNNW 100
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
 1-97 7.61e-22

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: 84.19  E-value: 7.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEHGLDsngvyagnselqleRMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGpfgql 80
Cdd:pfam00091   3 IVIGVGGAGNNIGNALWELLCLEHGID--------------SLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG----- 63

                          90
                  ....*....|....*..
gi 1919556361  81 FRPDNFVFGQSGAGNNW 97
Cdd:pfam00091  64 FNPNKILLGKEGTGGNG 80
 
Name Accession Description Interval E-value
PTZ00010 PTZ00010
tubulin beta chain; Provisional
 1-97 1.08e-64

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 201.16  E-value: 1.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEHGLDSNGVYAGNSELQLERMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQL 80
Cdd:PTZ00010    5 VHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGPYGQL 84

                          90
                  ....*....|....*..
gi 1919556361  81 FRPDNFVFGQSGAGNNW 97
Cdd:PTZ00010   85 FRPDNFIFGQSGAGNNW 101
PLN00220 PLN00220
tubulin beta chain; Provisional
 1-97 1.98e-64

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 200.43  E-value: 1.98e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEHGLDSNGVYAGNSELQLERMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQL 80
Cdd:PLN00220    5 LHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGPYGQI 84

                          90
                  ....*....|....*..
gi 1919556361  81 FRPDNFVFGQSGAGNNW 97
Cdd:PLN00220   85 FRPDNFVFGQSGAGNNW 101
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 1-97 1.13e-63

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: 197.79  E-value: 1.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEHGLDSNGVYAGNSELQLERMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQL 80
Cdd:cd02187     4 IHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPYGQL 83

                          90
                  ....*....|....*..
gi 1919556361  81 FRPDNFVFGQSGAGNNW 97
Cdd:cd02187    84 FRPDNFVFGQSGAGNNW 100
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
 3-97 1.60e-35

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: 124.58  E-value: 1.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   3 LQTGQCGNQIGAAFWQTISGEHGLDSNGVYAGNSELQLERMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFR 82
Cdd:cd02188     6 LQVGQCGNQIGSEFWKQLCSEHGISPDGSLEDFATDGNDRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNSPYKNLFN 85

                          90
                  ....*....|....*..
gi 1919556361  83 PDNFVFGQ--SGAGNNW 97
Cdd:cd02188    86 PENIYLSKegGGAGNNW 102
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 1-97 4.39e-27

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: 102.23  E-value: 4.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLqtGQCGNQIGAAFWQTISGEHGLDSNGVYAGNSELQLER--MSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFG 78
Cdd:cd02186     6 IHV--GQAGVQIGNACWELFCLEHGIQPDGQMPSDKTIGGDDdnFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTGPYR 83

                          90
                  ....*....|....*....
gi 1919556361  79 QLFRPDNFVFGQSGAGNNW 97
Cdd:cd02186    84 QLFHPEQLISGKEDAANNF 102
PLN00222 PLN00222
tubulin gamma chain; Provisional
 1-97 2.82e-26

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 99.92  E-value: 2.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEHGLDSNGVYAGNSELQLERMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQL 80
Cdd:PLN00222    6 ITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGGDRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNSEYRNL 85

                          90
                  ....*....|....*....
gi 1919556361  81 FRPDNFVFGQS--GAGNNW 97
Cdd:PLN00222   86 YNHENIFVSDHggGAGNNW 104
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
 1-97 2.20e-25

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: 97.34  E-value: 2.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEhgldsngVYAGNSELQLERMSVY-FNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQ 79
Cdd:cd02189     3 VTVQVGQCGNQLGDELFDTLADE-------ADSSASEGDQNSSATRfFSPFSDGKLKARCVLVDMEPKVVQQVLSRARSG 75

                          90       100
                  ....*....|....*....|
gi 1919556361  80 L--FRPDNFVFGQSGAGNNW 97
Cdd:cd02189    76 AwsYDPKNVVCGQSGSGNNW 95
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
 3-97 2.88e-23

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: 91.53  E-value: 2.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   3 LQTGQCGNQIGAAFWQTISGEHG-LDSNGVYagnselqLERMSVYF-------NEASGNKYVP------RAVLVDLEPGT 68
Cdd:cd02190     6 VQVGQCGNQIGCRFWDLALREHAaYNKDGVY-------DDSMSSFFrnvdtrsGDPGDDGGSPikslkaRAVLIDMEEGV 78

                          90       100
                  ....*....|....*....|....*....
gi 1919556361  69 MDAVRAGPFGQLFRPDNFVFGQSGAGNNW 97
Cdd:cd02190    79 VNELLKGPLGDLFDETQLVTDVSGAGNNW 107
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
 1-97 3.85e-23

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: 90.72  E-value: 3.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTIsgehgldsngvyagnselqlermsvyfneasgnkyvpRAVLVDLEPGTMDAVRAGPFGQL 80
Cdd:cd06059     3 ITIQVGQCGNQIGDRFWELA-------------------------------------RAVLVDMEEGVINEVLKGPLGQL 45

                          90
                  ....*....|....*..
gi 1919556361  81 FRPDNFVFGQSGAGNNW 97
Cdd:cd06059    46 FDPNQFVTGVSGAGNNW 62
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
 1-97 7.61e-22

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: 84.19  E-value: 7.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEHGLDsngvyagnselqleRMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGpfgql 80
Cdd:pfam00091   3 IVIGVGGAGNNIGNALWELLCLEHGID--------------SLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG----- 63

                          90
                  ....*....|....*..
gi 1919556361  81 FRPDNFVFGQSGAGNNW 97
Cdd:pfam00091  64 FNPNKILLGKEGTGGNG 80
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
 3-97 5.79e-21

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 85.14  E-value: 5.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   3 LQTGQCGNQIGAAFWQTISGEHGLDSNGVYAGNSELQLE--RMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQL 80
Cdd:PTZ00335    7 IHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEddAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQL 86

                          90
                  ....*....|....*..
gi 1919556361  81 FRPDNFVFGQSGAGNNW 97
Cdd:PTZ00335   87 FHPEQLISGKEDAANNF 103
PLN00221 PLN00221
tubulin alpha chain; Provisional
 1-97 2.38e-20

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 83.70  E-value: 2.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEHGLDSNGVYAGNSELQL--ERMSVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFG 78
Cdd:PLN00221    5 ISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGgdDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYR 84

                          90
                  ....*....|....*....
gi 1919556361  79 QLFRPDNFVFGQSGAGNNW 97
Cdd:PLN00221   85 QLFHPEQLISGKEDAANNF 103
PTZ00387 PTZ00387
epsilon tubulin; Provisional
 1-97 2.59e-20

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 83.62  E-value: 2.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTISGEH-GLDSNGVYAgnselqlERMSVYFNEASGNKYVP-------RAVLVDLEPGTMDAV 72
Cdd:PTZ00387    5 VTVQVGQCGNQLGHRFWDVALKEHkKINANPQYD-------DARDSFFENVSENVNRPgkenlkaRAVLVDMEEGVLNQI 77

                          90       100
                  ....*....|....*....|....*
gi 1919556361  73 RAGPFGQLFRPDNFVFGQSGAGNNW 97
Cdd:PTZ00387   78 LKSPLGDLFDENFFVSDVSGAGNNW 102
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
 1-97 2.06e-16

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: 72.05  E-value: 2.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919556361   1 VHLQTGQCGNQIGAAFWQtisgehgldsngvyagnselqlermsvyfneasgnkyvpRAVLVDLEPGTMDAVRAGPFGQL 80
Cdd:cd00286     3 VTIQVGQCGNQIGAAFWE---------------------------------------QAVLVDLEPAVLDELLSGPLRQL 43

                          90
                  ....*....|....*....
gi 1919556361  81 FRPDNFVFGQS--GAGNNW 97
Cdd:cd00286    44 FHPENIILIQKyhGAGNNW 62
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
 1-64 8.42e-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: 35.69  E-value: 8.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1919556361   1 VHLQTGQCGNQIGAAFWQTisgehgLDSNGVYAGNSELQLERMSVYF--NEASGN--KYVPRAVLVDL 64
Cdd:pfam10644   4 ITLQFGNYSNYVGTHFWNT------QESYFTYDPNEEPSEVDHDVLFreGETLDGqvTYTPRLLIYDL 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH