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Conserved domains on  [gi|393715095|ref|NP_001257329|]
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tubulin alpha-1A chain isoform 2 [Homo sapiens]

Protein Classification

tubulin alpha chain( domain architecture ID 11488404)

tubulin alpha chain is a component of tubulin, the major constituent of microtubules that 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
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-405 0e+00

tubulin alpha chain; Provisional


:

Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 868.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095   1 MPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEII 80
Cdd:PTZ00335  36 MPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIV 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  81 DLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTL 160
Cdd:PTZ00335 116 DLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLL 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 161 EHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPV 240
Cdd:PTZ00335 196 EHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPI 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 241 ISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGI 320
Cdd:PTZ00335 276 ISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGI 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 321 NYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEV 400
Cdd:PTZ00335 356 NYQPPTVVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEV 435

                 ....*
gi 393715095 401 GVDSV 405
Cdd:PTZ00335 436 GAESA 440
 
Name Accession Description Interval E-value
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-405 0e+00

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 868.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095   1 MPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEII 80
Cdd:PTZ00335  36 MPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIV 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  81 DLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTL 160
Cdd:PTZ00335 116 DLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLL 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 161 EHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPV 240
Cdd:PTZ00335 196 EHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPI 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 241 ISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGI 320
Cdd:PTZ00335 276 ISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGI 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 321 NYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEV 400
Cdd:PTZ00335 356 NYQPPTVVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEV 435

                 ....*
gi 393715095 401 GVDSV 405
Cdd:PTZ00335 436 GAESA 440
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-400 0e+00

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: 836.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095   1 MPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEII 80
Cdd:cd02186   35 MPSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTGPYRQLFHPEQLISGKEDAANNFARGYYTIGKEII 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  81 DLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTL 160
Cdd:cd02186  115 DPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDYGKKSKLEFSIYPSPQVSTSVVEPYNSVLTTHSLL 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 161 EHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPV 240
Cdd:cd02186  195 EHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNVDLNEFQTNLVPYPRIHFPLVSYAPI 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 241 ISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGI 320
Cdd:cd02186  275 ISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGI 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 321 NYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEV 400
Cdd:cd02186  355 NYQPPTVVPGSDLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEV 434
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
228-357 1.71e-77

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: 235.97  E-value: 1.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  228 PRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQ 307
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 393715095  308 FVDWCPTGFKVGINYQPPTVVPGGDlakvqRAVCMLSNTTAIAEAWARLD 357
Cdd:pfam03953  81 FVEWCPTGIKVAICSQSPYVVPGSK-----VSGLMLANTTSIAELFQRLL 125
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
14-211 1.22e-68

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: 215.43  E-value: 1.22e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095    14 FNTFFSETGAGkhvPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYT-----IGKEIIDLVLDRIR 88
Cdd:smart00864   1 KIKVFGVGGGG---PNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095    89 KLADQCtglQGFLVFHsfgggtgsgftsLLMERLSvDYGKKSkLEFSIYPapQVSTAVVEPYNSILTTHTTLEHSDCAFM 168
Cdd:smart00864  78 EELEGA---DGVFITAgmgggtgtgaapVIAEIAK-EYGILT-VAVVTKP--FSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 393715095   169 VDNEAIYDICRRNLDIeRPTYTNLNRLIGQIVSSITASLRFDG 211
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
 
Name Accession Description Interval E-value
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-405 0e+00

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 868.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095   1 MPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEII 80
Cdd:PTZ00335  36 MPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIV 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  81 DLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTL 160
Cdd:PTZ00335 116 DLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLL 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 161 EHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPV 240
Cdd:PTZ00335 196 EHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPI 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 241 ISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGI 320
Cdd:PTZ00335 276 ISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGI 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 321 NYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEV 400
Cdd:PTZ00335 356 NYQPPTVVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEV 435

                 ....*
gi 393715095 401 GVDSV 405
Cdd:PTZ00335 436 GAESA 440
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-404 0e+00

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 858.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095   1 MPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEII 80
Cdd:PLN00221  36 MPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIV 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  81 DLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTL 160
Cdd:PLN00221 116 DLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTAVVEPYNSVLSTHSLL 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 161 EHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPV 240
Cdd:PLN00221 196 EHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTASLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPV 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 241 ISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGI 320
Cdd:PLN00221 276 ISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGI 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 321 NYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEV 400
Cdd:PLN00221 356 NYQPPTVVPGGDLAKVQRAVCMISNSTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEV 435

                 ....
gi 393715095 401 GVDS 404
Cdd:PLN00221 436 GAES 439
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-400 0e+00

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: 836.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095   1 MPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEII 80
Cdd:cd02186   35 MPSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTGPYRQLFHPEQLISGKEDAANNFARGYYTIGKEII 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  81 DLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTL 160
Cdd:cd02186  115 DPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDYGKKSKLEFSIYPSPQVSTSVVEPYNSVLTTHSLL 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 161 EHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPV 240
Cdd:cd02186  195 EHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNVDLNEFQTNLVPYPRIHFPLVSYAPI 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 241 ISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGI 320
Cdd:cd02186  275 ISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGI 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 321 NYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEV 400
Cdd:cd02186  355 NYQPPTVVPGSDLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEV 434
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
29-399 4.52e-164

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: 465.91  E-value: 4.52e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  29 RAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGG 108
Cdd:cd06059   23 RAVLVDMEEGVINEVLKGPLGQLFDPNQFVTGVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 109 GTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRR---NLDIE 185
Cdd:cd06059  103 GTGSGLGSYLLELLEDEYPKVYRFTFSVFPSPDDDNVITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDID 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 186 RPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN 265
Cdd:cd06059  183 FPPFDDMNNLVAQLLSSLTSSLRFEGSLNVDLNEITTNLVPFPRLHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDN 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 266 QMVKCDPRHGKYMACCLLYRGDVV-PKDVNAAIATIKTKRTiqFVDWCPTGFKVGINYQPPtvvpggdlAKVQRAVCMLS 344
Cdd:cd06059  263 QLVGCDPRHGTYLACALLLRGKVFsLSDVRRNIDRIKPKLK--FISWNPDGFKVGLCSVPP--------VGQKYSLLFLS 332
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 393715095 345 NTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEE 399
Cdd:cd06059  333 NNTSIASTFERLIERFDKLYKRKAFLHHYTGEGMEEGDFSEARESLANLIQEYQE 387
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
12-399 8.23e-143

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: 413.50  E-value: 8.23e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  12 DSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLA 91
Cdd:cd02187   44 ERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPYGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  92 DQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDN 171
Cdd:cd02187  124 ESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPDRIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDN 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 172 EAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQL 251
Cdd:cd02187  204 EALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQYRKL 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 252 SVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGg 331
Cdd:cd02187  284 TVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRISTKEVDEQMSKVQNKNSSYFVEWIPNNVKTSVCDIPPRGLKM- 362
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 393715095 332 dlakvqrAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEE 399
Cdd:cd02187  363 -------SATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNLNDLISEYQQ 423
PTZ00010 PTZ00010
tubulin beta chain; Provisional
2-399 1.83e-127

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 375.27  E-value: 1.83e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095   2 PSDKTIGGGD---DSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKE 78
Cdd:PTZ00010  32 PTGTYQGDSDlqlERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGPYGQLFRPDNFIFGQSGAGNNWAKGHYTEGAE 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  79 IIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHT 158
Cdd:PTZ00010 112 LIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKVSDTVVEPYNATLSVHQ 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 159 TLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYA 238
Cdd:PTZ00010 192 LVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPFPRLHFFMMGFA 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 239 PVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKV 318
Cdd:PTZ00010 272 PLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIKS 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 319 GINYQPPTVVPggdlakvqRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYE 398
Cdd:PTZ00010 352 SVCDIPPKGLK--------MSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQ 423

                 .
gi 393715095 399 E 399
Cdd:PTZ00010 424 Q 424
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
30-346 1.64e-125

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: 365.96  E-value: 1.64e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  30 AVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKED--AANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFG 107
Cdd:cd00286   22 AVLVDLEPAVLDELLSGPLRQLFHPENIILIQKYhgAGNNWAKGHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 108 GGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTaVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERP 187
Cdd:cd00286  102 GGTGSGLGPLLAERLKDEYPNRLVVTFSILPGPDEGV-IVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAP 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 188 TYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQM 267
Cdd:cd00286  181 AYDHINELVAQRLGSLTEALRFEGSLNVDLRELAENLVPLPRGHFLMLGYAPLDSATSATPRSLRVKELTRRAFLPANLL 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 268 VKCDPRHGKYMACCLLYRG--DVVPKDVNAAIATIKTKRTIQFvDWCPTGFKVGINYQPPtvvpggdlAKVQRAVCMLSN 345
Cdd:cd00286  261 VGCDPDHGEAIAALLVIRGppDLSSKEVERAIARVKETLGHLF-SWSPAGVKTGISPKPP--------AEGEVSVLALLN 331

                 .
gi 393715095 346 T 346
Cdd:cd00286  332 S 332
PLN00220 PLN00220
tubulin beta chain; Provisional
15-399 6.81e-123

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 363.76  E-value: 6.81e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  15 NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC 94
Cdd:PLN00220  48 NVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENC 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  95 TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI 174
Cdd:PLN00220 128 DCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEAL 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 175 YDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA 254
Cdd:PLN00220 208 YDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVP 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 255 EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTvvpggdla 334
Cdd:PLN00220 288 ELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPK-------- 359
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 393715095 335 KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEE 399
Cdd:PLN00220 360 GLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 424
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
11-400 8.29e-92

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: 284.13  E-value: 8.29e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  11 DDSFNTFFSETGAGKHVP-------------RAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGK 77
Cdd:cd02190   37 DDSMSSFFRNVDTRSGDPgddggspikslkaRAVLIDMEEGVVNELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGP 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  78 EIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQ--VSTAvvePYNSILT 155
Cdd:cd02190  117 QYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSGLGSYILELLEDEFPDVYRFVTSVFPSGDddVITS---PYNSVLA 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 156 THTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTN----------------------LNRLIGQIVSSITASLRFDGAL 213
Cdd:cd02190  194 LRELTEHADCVLPVENQALMDIVNKIKSSKDKGKTGvlaainssgggqkkgkkkpfddMNNIVANLLLNLTSSMRFEGSL 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 214 NVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDV 293
Cdd:cd02190  274 NVDLNEITTNLVPFPRLHFLLSSLSPLYALADVRLPPRRLDQMFSDAFSRDHQLLKADPKHGLYLACALLVRGNVSISDL 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 294 NAAIATIktKRTIQFVDWCPTGFKVGINYQPPTVVPggdlakvqRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWY 373
Cdd:cd02190  354 RRNIDRL--KRQLKFVSWNQDGWKIGLCSVPPVGQP--------YSLLCLANNTCIKPTFTEMHERFDKLYKRKAHLHHY 423
                        410       420
                 ....*....|....*....|....*..
gi 393715095 374 VgEGMEEGEFSEAREDMAALEKDYEEV 400
Cdd:cd02190  424 T-QYMEQDDFDEALESLLDLIEEYKDL 449
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
10-397 6.15e-83

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: 260.55  E-value: 6.15e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  10 GDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKED--AANNYARGhYTIGKEIIDLVLDRI 87
Cdd:cd02188   42 GNDRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNSPYKNLFNPENIYLSKEGggAGNNWASG-YSQGEKVQEEILDII 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  88 RKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPA-PQVSTAVVEPYNSILTTHTTLEHSDCA 166
Cdd:cd02188  121 DREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRYPKKLIQTYSVFPNqEESSDVVVQPYNSILTLKRLTLNADCV 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 167 FMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKA 246
Cdd:cd02188  201 VVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTSTLRFPGYMNNDLVSLISSLIPTPRLHFLMTSYTPLTSDQVA 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 247 -YHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPP 325
Cdd:cd02188  281 sSVRKTTVLDVMRRLLQPKNRMVSTSTKNGCYISILNIIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSKKSP 360
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 393715095 326 TVVPggdlakvQRAVC--MLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEG---EFSEAREDMAALEKDY 397
Cdd:cd02188  361 YVQT-------AHRVSglMLANHTSISSLFEKILSQYDKLRKRNAFLENYRKEDMFQDnleEFDESREVVQSLIDEY 430
PTZ00387 PTZ00387
epsilon tubulin; Provisional
11-400 4.56e-81

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 256.96  E-value: 4.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  11 DDSFNTFFSETGAGKHVP-------RAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLV 83
Cdd:PTZ00387  38 DDARDSFFENVSENVNRPgkenlkaRAVLVDMEEGVLNQILKSPLGDLFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  84 LDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPApQVSTAVVEPYNSILTTHTTLEHS 163
Cdd:PTZ00387 118 SESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEFPHVFRFCPVVFPS-AVDDVITSPYNSFFALRELIEHA 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 164 DCAFMVDNEAIYDICRRNLDIER---------------------PT------YTNLNRLIGQIVSSITASLRFDGALNVD 216
Cdd:PTZ00387 197 DCVLPLDNDALANIADSALSRKKkklakgnikrgpqphkysvakPTetkklpYDKMNNIVAQLLSNLTSSMRFEGSLNVD 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 217 LTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAA 296
Cdd:PTZ00387 277 INEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGPRRLDQMFKDCLDPDHQMVAATPEAGKYLATALIVRGPQNVSDVTRN 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 297 IAtiKTKRTIQFVDWCPTGFKVGINYQPPTVVPggdlakvqRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVgE 376
Cdd:PTZ00387 357 IL--RLKEQLNMIYWNEDGFKTGLCNVSPLGQP--------YSLLCLANNCCIRNKFESMLERFNKLYKRKSHVHHYT-E 425
                        410       420
                 ....*....|....*....|....
gi 393715095 377 GMEEGEFSEAREDMAALEKDYEEV 400
Cdd:PTZ00387 426 YLEQAYFDETLETIQNLIDDYAYL 449
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
228-357 1.71e-77

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: 235.97  E-value: 1.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  228 PRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQ 307
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 393715095  308 FVDWCPTGFKVGINYQPPTVVPGGDlakvqRAVCMLSNTTAIAEAWARLD 357
Cdd:pfam03953  81 FVEWCPTGIKVAICSQSPYVVPGSK-----VSGLMLANTTSIAELFQRLL 125
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
14-211 1.22e-68

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: 215.43  E-value: 1.22e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095    14 FNTFFSETGAGkhvPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYT-----IGKEIIDLVLDRIR 88
Cdd:smart00864   1 KIKVFGVGGGG---PNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095    89 KLADQCtglQGFLVFHsfgggtgsgftsLLMERLSvDYGKKSkLEFSIYPapQVSTAVVEPYNSILTTHTTLEHSDCAFM 168
Cdd:smart00864  78 EELEGA---DGVFITAgmgggtgtgaapVIAEIAK-EYGILT-VAVVTKP--FSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 393715095   169 VDNEAIYDICRRNLDIeRPTYTNLNRLIGQIVSSITASLRFDG 211
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
PLN00222 PLN00222
tubulin gamma chain; Provisional
10-397 3.61e-68

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 223.18  E-value: 3.61e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  10 GDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKED--AANNYARGhYTIGKEIIDLVLDRI 87
Cdd:PLN00222  44 GGDRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNSEYRNLYNHENIFVSDHGggAGNNWASG-YHQGEQVEEDIMDMI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  88 RKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPA-PQVSTAVVEPYNSILTTHTTLEHSDCA 166
Cdd:PLN00222 123 DREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRYSKKLVQTYSVFPNqMETSDVVVQPYNSLLTLKRLTLNADCV 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 167 FMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPV-ISAEK 245
Cdd:PLN00222 203 VVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTTTLRYPGYMNNDLVGLLASLIPTPRCHFLMTGYTPLtVERQA 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 246 AYHEQLSVAEITNACFEPANQMVKCDPR-----HGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGI 320
Cdd:PLN00222 283 NVIRKTTVLDVMRRLLQTKNIMVSSYARtkeasQAKYISILNIIQGEVDPTQVHKSLQRIRERKLANFIEWGPASIQVAL 362
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 321 NYQPPTVVPGGDLAKVqravcMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGM----EEGEFSEAREDMAALEKD 396
Cdd:PLN00222 363 SRKSPYVQTAHRVSGL-----MLANHTSIRHLFSKCLSQYDKLRKKQAFLDNYRKFPMfadnDLSEFDESREIVESLVDE 437

                 .
gi 393715095 397 Y 397
Cdd:PLN00222 438 Y 438
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
12-178 5.49e-50

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: 167.40  E-value: 5.49e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095   12 DSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGtyrqlFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLA 91
Cdd:pfam00091  29 DSLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG-----FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095   92 DQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPApQVSTAVVEPYNSILTTHTTLEHSDCAFMVDN 171
Cdd:pfam00091 104 EGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGALTVAVVTFPF-GFSEGVVRPYNAILGLKELIEHSDSVIVIDN 182

                  ....*..
gi 393715095  172 EAIYDIC 178
Cdd:pfam00091 183 DALYDIC 189
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
11-399 1.52e-37

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: 141.25  E-value: 1.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  11 DDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFH--PEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIR 88
Cdd:cd02189   36 NSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRARSGAWSydPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095  89 KLADQCTGLQGFLVFHSFGGgtgsgftsLLMERLSVDYGKKSKLEFSIypAPQvSTA--VVEPYNSILTTHTTLEHSDCA 166
Cdd:cd02189  116 REAERCDRLSGFLVLHSLAGgtgsglgsRVTELLRDEYPKAYLLNTVV--WPY-SSGevPVQNYNTLLTLSHLQESSDGI 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 167 FMVDNEAIYDICRRNLDIERP-TYTNLNRLIG-QIVSSI--TASLRFDGALNVD-LTEFQTNLVPYPriHFPLAT--YAP 239
Cdd:cd02189  193 LLFENDDLHKICSKLLGLKNPvSFSDINRVIArQLAGVLlpSSSPTSPSPLRRCpLGDLLEHLCPHP--AYKLLTlrSLP 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 240 VISAE-------------KAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTi 306
Cdd:cd02189  271 QMPEPsrafstytwpsllKRLRQMLITGAKLEEGIDWQLLDTSGSHNPNKSLAALLVLRGKDAMKVHSADLSAFKDPVL- 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095 307 qFVDWCPTGFkvginyqpPTVVPGGDLAKVQRAVCMLSNTTAIAeawARLDH---KFDLMYAKRAFVHWYVGEGMEEGEF 383
Cdd:cd02189  350 -YSPWVPNPF--------NVSVSPRPFNGYEKSVTLLSNSQNIV---GPLDSlleKAWQMFKAGAYLHQYEKYGVEEEDF 417
                        410
                 ....*....|....*.
gi 393715095 384 SEAREDMAALEKDYEE 399
Cdd:cd02189  418 LDAFATLEQIIAAYKS 433
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
213-358 6.61e-27

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: 103.78  E-value: 6.61e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095   213 LNVDLTEFQTNLVPYPrihFPLATYAPVISAEKAyheqLSVAE--ITNACFEPANQMVKCDPRHgkYMACCLlyrgDVVP 290
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASGENRA----LEAAElaISSPLLEDSNIMGAKGVLV--NITGGP----DLTL 67
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393715095   291 KDVNAAIATIKTKRT-IQFVDWCptgfkvginyqpPTVVPggdlaKVQRAVCMLSN-TTAIAEAWARLDH 358
Cdd:smart00865  68 KEVNEAMERIREKADpDAFIIWG------------PVIDE-----ELGGDEIRVTViATGIGSLFKRLSE 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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