NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|76257849|gb|ABA41242|]
View 

alpha-tubulin, partial [Mantoniella squamata]

Protein Classification

tubulin alpha chain( domain architecture ID 11476498)

tubulin alpha chain dimerizes with the beta chain to form tubulin, the major constituent of microtubules

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-395 0e+00

tubulin alpha chain; Provisional


:

Pssm-ID: 177802  Cd Length: 450  Bit Score: 940.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    1 CWELYCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDA 80
Cdd:PLN00221  20 CWELYCLEHGIQPDGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   81 ANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVST 160
Cdd:PLN00221 100 ANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVST 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  161 AVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQTNL 240
Cdd:PLN00221 180 AVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTASLRFDGALNVDITEFQTNL 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  241 VPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKR 320
Cdd:PLN00221 260 VPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKR 339
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76257849  321 TIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVLRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGME 395
Cdd:PLN00221 340 TIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGME 414
 
Name Accession Description Interval E-value
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-395 0e+00

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 940.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    1 CWELYCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDA 80
Cdd:PLN00221  20 CWELYCLEHGIQPDGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   81 ANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVST 160
Cdd:PLN00221 100 ANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVST 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  161 AVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQTNL 240
Cdd:PLN00221 180 AVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTASLRFDGALNVDITEFQTNL 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  241 VPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKR 320
Cdd:PLN00221 260 VPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKR 339
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76257849  321 TIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVLRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGME 395
Cdd:PLN00221 340 TIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGME 414
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-395 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: 847.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   1 CWELYCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDA 80
Cdd:cd02186  19 CWELFCLEHGIQPDGQMPSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTGPYRQLFHPEQLISGKEDA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  81 ANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVST 160
Cdd:cd02186  99 ANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDYGKKSKLEFSIYPSPQVST 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 161 AVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQTNL 240
Cdd:cd02186 179 SVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNVDLNEFQTNL 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 241 VPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKR 320
Cdd:cd02186 259 VPYPRIHFPLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKR 338
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76257849 321 TIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVLRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGME 395
Cdd:cd02186 339 TIQFVDWCPTGFKVGINYQPPTVVPGSDLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSKRAFVHWYVGEGME 413
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
30-227 2.71e-74

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: 229.30  E-value: 2.71e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849     30 FNTFFSETGAGkhvPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYT-----IGKEIVDLCLDRIR 104
Cdd:smart00864   1 KIKVFGVGGGG---PNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    105 KLADNCtglQGFMVFNAVGGCTGSGLGSLLLERLSvDYGKKSkLGFTIYPspQVSTAVVEPYNSVLSTHSLLEHTDVAVM 184
Cdd:smart00864  78 EELEGA---DGVFITAGMGGGTGTGAAPVIAEIAK-EYGILT-VAVVTKP--FSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 76257849    185 LDNEAIYDICRRSLDIeRPTYTNLSRLVGQVISSLTASLRFDG 227
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
244-373 7.23e-74

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: 225.96  E-value: 7.23e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   244 PRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQ 323
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 76257849   324 FVDWCPTGFKCGINYQPPTVVPGGDlakvlRAVCMISNSTAIAEVFSRLD 373
Cdd:pfam03953  81 FVEWCPTGIKVAICSQSPYVVPGSK-----VSGLMLANTTSIAELFQRLL 125
 
Name Accession Description Interval E-value
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-395 0e+00

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 940.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    1 CWELYCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDA 80
Cdd:PLN00221  20 CWELYCLEHGIQPDGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   81 ANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVST 160
Cdd:PLN00221 100 ANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVST 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  161 AVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQTNL 240
Cdd:PLN00221 180 AVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTASLRFDGALNVDITEFQTNL 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  241 VPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKR 320
Cdd:PLN00221 260 VPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKR 339
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76257849  321 TIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVLRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGME 395
Cdd:PLN00221 340 TIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGME 414
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-395 0e+00

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 921.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    1 CWELYCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDA 80
Cdd:PTZ00335  20 CWELFCLEHGIQPDGQMPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   81 ANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVST 160
Cdd:PTZ00335 100 ANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVST 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  161 AVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQTNL 240
Cdd:PTZ00335 180 AVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDLTEFQTNL 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  241 VPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKR 320
Cdd:PTZ00335 260 VPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAIATIKTKR 339
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76257849  321 TIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVLRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGME 395
Cdd:PTZ00335 340 TIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYAKRAFVHWYVGEGME 414
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-395 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: 847.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   1 CWELYCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDA 80
Cdd:cd02186  19 CWELFCLEHGIQPDGQMPSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTGPYRQLFHPEQLISGKEDA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  81 ANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVST 160
Cdd:cd02186  99 ANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDYGKKSKLEFSIYPSPQVST 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 161 AVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQTNL 240
Cdd:cd02186 179 SVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNVDLNEFQTNL 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 241 VPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKR 320
Cdd:cd02186 259 VPYPRIHFPLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKR 338
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76257849 321 TIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVLRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGME 395
Cdd:cd02186 339 TIQFVDWCPTGFKVGINYQPPTVVPGSDLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSKRAFVHWYVGEGME 413
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
45-395 2.31e-159

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: 453.20  E-value: 2.31e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  45 RCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGG 124
Cdd:cd06059  23 RAVLVDMEEGVINEVLKGPLGQLFDPNQFVTGVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGG 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 125 CTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRR---SLDIE 201
Cdd:cd06059 103 GTGSGLGSYLLELLEDEYPKVYRFTFSVFPSPDDDNVITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDID 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 202 RPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPAS 281
Cdd:cd06059 183 FPPFDDMNNLVAQLLSSLTSSLRFEGSLNVDLNEITTNLVPFPRLHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDN 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 282 MMAKCDPRHGKYMACCLMYRGDVV-PKDVNAAVATIKTKRTiqFVDWCPTGFKCGINYQPPTVVPggdlakvlRAVCMIS 360
Cdd:cd06059 263 QLVGCDPRHGTYLACALLLRGKVFsLSDVRRNIDRIKPKLK--FISWNPDGFKVGLCSVPPVGQK--------YSLLFLS 332
                       330       340       350
                ....*....|....*....|....*....|....*
gi 76257849 361 NSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGME 395
Cdd:cd06059 333 NNTSIASTFERLIERFDKLYKRKAFLHHYTGEGME 367
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-395 5.35e-157

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: 448.55  E-value: 5.35e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   2 WELYCLEHGIQPDGqmpsdkTIGGGDDAF----NTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGK 77
Cdd:cd02187  20 WETISKEHGIDPDG------TYKGDSDLQleriNVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPYGQLFRPDNFVFGQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  78 EDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQ 157
Cdd:cd02187  94 SGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPDRIMSTFSVLPSPK 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 158 VSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQ 237
Cdd:cd02187 174 VSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLA 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 238 TNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIK 317
Cdd:cd02187 254 TNLVPFPRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRISTKEVDEQMSKVQ 333
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76257849 318 TKRTIQFVDWCPTGFKCGINYQPPTVVPGgdlakvlrAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGME 395
Cdd:cd02187 334 NKNSSYFVEWIPNNVKTSVCDIPPRGLKM--------SATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGEGMD 403
PTZ00010 PTZ00010
tubulin beta chain; Provisional
2-395 1.15e-138

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 403.00  E-value: 1.15e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    2 WELYCLEHGIQPDGQMpsdktIGGGD---DAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKE 78
Cdd:PTZ00010  21 WEVISDEHGIDPTGTY-----QGDSDlqlERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGPYGQLFRPDNFIFGQS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   79 DAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQV 158
Cdd:PTZ00010  96 GAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSPKV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  159 STAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQT 238
Cdd:PTZ00010 176 SDTVVEPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAV 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  239 NLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKT 318
Cdd:PTZ00010 256 NLVPFPRLHFFMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQN 335
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76257849  319 KRTIQFVDWCPTGFKCGINYQPPTVVPggdlakvlRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGME 395
Cdd:PTZ00010 336 KNSSYFVEWIPNNIKSSVCDIPPKGLK--------MSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTGEGMD 404
PLN00220 PLN00220
tubulin beta chain; Provisional
2-395 2.18e-131

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 384.56  E-value: 2.18e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    2 WELYCLEHGIQPDGQMPSDKTIGggDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAA 81
Cdd:PLN00220  21 WEVVCDEHGIDPTGTYHGDSDLQ--LERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGPYGQIFRPDNFVFGQSGAG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   82 NNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTA 161
Cdd:PLN00220  99 NNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  162 VVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQTNLV 241
Cdd:PLN00220 179 VVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLI 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  242 PYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRT 321
Cdd:PLN00220 259 PFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNS 338
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 76257849  322 IQFVDWCPTGFKCGINYQPPTvvpGGDLAKVLravcmISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGME 395
Cdd:PLN00220 339 SYFVEWIPNNVKSSVCDIPPK---GLKMASTF-----IGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMD 404
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
47-362 3.62e-120

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: 351.71  E-value: 3.62e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  47 VFLDLEPTVIDEVRTGTYRQLFHPEQLISGKED--AANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGG 124
Cdd:cd00286  23 VLVDLEPAVLDELLSGPLRQLFHPENIILIQKYhgAGNNWAKGHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLGG 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 125 CTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTaVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPT 204
Cdd:cd00286 103 GTGSGLGPLLAERLKDEYPNRLVVTFSILPGPDEGV-IVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPA 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 205 YTNLSRLVGQVISSLTASLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMA 284
Cdd:cd00286 182 YDHINELVAQRLGSLTEALRFEGSLNVDLRELAENLVPLPRGHFLMLGYAPLDSATSATPRSLRVKELTRRAFLPANLLV 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 285 KCDPRHGKYMACCLMYRG--DVVPKDVNAAVATIKTKRTIQFvDWCPTGFKCGINYQPPtvvpggdlAKVLRAVCMISNS 362
Cdd:cd00286 262 GCDPDHGEAIAALLVIRGppDLSSKEVERAIARVKETLGHLF-SWSPAGVKTGISPKPP--------AEGEVSVLALLNS 332
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
1-395 1.37e-96

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: 294.83  E-value: 1.37e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   1 CWELYCLEHGIQPDGQMPSDKTigGGDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKED- 79
Cdd:cd02188  19 FWKQLCSEHGISPDGSLEDFAT--DGNDRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNSPYKNLFNPENIYLSKEGg 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  80 -AANNFARGhYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYP-SPQ 157
Cdd:cd02188  97 gAGNNWASG-YSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRYPKKLIQTYSVFPnQEE 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 158 VSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQ 237
Cdd:cd02188 176 SSDVVVQPYNSILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTSTLRFPGYMNNDLVSLI 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 238 TNLVPYPRIHFMLSSYAPVISAEKA-YHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATI 316
Cdd:cd02188 256 SSLIPTPRLHFLMTSYTPLTSDQVAsSVRKTTVLDVMRRLLQPKNRMVSTSTKNGCYISILNIIQGEVDPTQVHKSLQRI 335
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 317 KTKRTIQFVDWCPTGFKCGINYQPPTV-----VPGGdlakvlravcMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVG 391
Cdd:cd02188 336 RERKLANFIPWGPASIQVALSKKSPYVqtahrVSGL----------MLANHTSISSLFEKILSQYDKLRKRNAFLENYRK 405

                ....
gi 76257849 392 EGME 395
Cdd:cd02188 406 EDMF 409
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
27-395 5.58e-96

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: 294.15  E-value: 5.58e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  27 DDAFNTFFSETGAGKHVP-------------RCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGK 93
Cdd:cd02190  37 DDSMSSFFRNVDTRSGDPgddggspikslkaRAVLIDMEEGVVNELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGP 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  94 EIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQ--VSTAvvePYNSVLS 171
Cdd:cd02190 117 QYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSGLGSYILELLEDEFPDVYRFVTSVFPSGDddVITS---PYNSVLA 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 172 THSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSR----------------------LVGQVISSLTASLRFDGAL 229
Cdd:cd02190 194 LRELTEHADCVLPVENQALMDIVNKIKSSKDKGKTGVLAainssgggqkkgkkkpfddmnnIVANLLLNLTSSMRFEGSL 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 230 NVDITEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDV 309
Cdd:cd02190 274 NVDLNEITTNLVPFPRLHFLLSSLSPLYALADVRLPPRRLDQMFSDAFSRDHQLLKADPKHGLYLACALLVRGNVSISDL 353
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 310 NAAVATIktKRTIQFVDWCPTGFKCGINYQPPTVVPggdlakvlRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWY 389
Cdd:cd02190 354 RRNIDRL--KRQLKFVSWNQDGWKIGLCSVPPVGQP--------YSLLCLANNTCIKPTFTEMHERFDKLYKRKAHLHHY 423

                ....*.
gi 76257849 390 VgEGME 395
Cdd:cd02190 424 T-QYME 428
PTZ00387 PTZ00387
epsilon tubulin; Provisional
2-395 5.88e-84

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 263.51  E-value: 5.88e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    2 WELYCLEH-GIQPDGQMpsdktigggDDAFNTFFSETGAGKHVP-------RCVFLDLEPTVIDEVRTGTYRQLFHPEQL 73
Cdd:PTZ00387  21 WDVALKEHkKINANPQY---------DDARDSFFENVSENVNRPgkenlkaRAVLVDMEEGVLNQILKSPLGDLFDENFF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   74 ISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIY 153
Cdd:PTZ00387  92 VSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEFPHVFRFCPVVF 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  154 PSpQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIER---------------------PT------YT 206
Cdd:PTZ00387 172 PS-AVDDVITSPYNSFFALRELIEHADCVLPLDNDALANIADSALSRKKkklakgnikrgpqphkysvakPTetkklpYD 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  207 NLSRLVGQVISSLTASLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKC 286
Cdd:PTZ00387 251 KMNNIVAQLLSNLTSSMRFEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGPRRLDQMFKDCLDPDHQMVAA 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  287 DPRHGKYMACCLMYRGDVVPKDVNAAVAtiKTKRTIQFVDWCPTGFKCGINYQPPTVVPggdlakvlRAVCMISNSTAIA 366
Cdd:PTZ00387 331 TPEAGKYLATALIVRGPQNVSDVTRNIL--RLKEQLNMIYWNEDGFKTGLCNVSPLGQP--------YSLLCLANNCCIR 400
                        410       420
                 ....*....|....*....|....*....
gi 76257849  367 EVFSRLDHKFDLMYAKRAFVHWYVgEGME 395
Cdd:PTZ00387 401 NKFESMLERFNKLYKRKSHVHHYT-EYLE 428
PLN00222 PLN00222
tubulin gamma chain; Provisional
2-394 5.16e-79

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 250.53  E-value: 5.16e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    2 WELYCLEHGIQPDGQMPSDKTIGGgdDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKED-- 79
Cdd:PLN00222  22 WKQLCLEHGISKDGILEDFATQGG--DRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNSEYRNLYNHENIFVSDHGgg 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   80 AANNFARGhYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPS-PQV 158
Cdd:PLN00222 100 AGNNWASG-YHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRYSKKLVQTYSVFPNqMET 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  159 STAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRSLDIERPTYTNLSRLVGQVISSLTASLRFDGALNVDITEFQT 238
Cdd:PLN00222 179 SDVVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTTTLRYPGYMNNDLVGLLA 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  239 NLVPYPRIHFMLSSYAPV-ISAEKAYHEQLSVAEITNSAYEPASMMAKCDPR-----HGKYMACCLMYRGDVVPKDVNAA 312
Cdd:PLN00222 259 SLIPTPRCHFLMTGYTPLtVERQANVIRKTTVLDVMRRLLQTKNIMVSSYARtkeasQAKYISILNIIQGEVDPTQVHKS 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  313 VATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVlravcMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGE 392
Cdd:PLN00222 339 LQRIRERKLANFIEWGPASIQVALSRKSPYVQTAHRVSGL-----MLANHTSIRHLFSKCLSQYDKLRKKQAFLDNYRKF 413

                 ..
gi 76257849  393 GM 394
Cdd:PLN00222 414 PM 415
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
30-227 2.71e-74

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: 229.30  E-value: 2.71e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849     30 FNTFFSETGAGkhvPRCVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYT-----IGKEIVDLCLDRIR 104
Cdd:smart00864   1 KIKVFGVGGGG---PNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    105 KLADNCtglQGFMVFNAVGGCTGSGLGSLLLERLSvDYGKKSkLGFTIYPspQVSTAVVEPYNSVLSTHSLLEHTDVAVM 184
Cdd:smart00864  78 EELEGA---DGVFITAGMGGGTGTGAAPVIAEIAK-EYGILT-VAVVTKP--FSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 76257849    185 LDNEAIYDICRRSLDIeRPTYTNLSRLVGQVISSLTASLRFDG 227
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
244-373 7.23e-74

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: 225.96  E-value: 7.23e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849   244 PRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAYEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQ 323
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 76257849   324 FVDWCPTGFKCGINYQPPTVVPGGDlakvlRAVCMISNSTAIAEVFSRLD 373
Cdd:pfam03953  81 FVEWCPTGIKVAICSQSPYVVPGSK-----VSGLMLANTTSIAELFQRLL 125
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
1-194 6.18e-71

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: 220.55  E-value: 6.18e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849     1 CWELYCLEHGIqpdgqmpsdktigggdDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGtyrqlFHPEQLISGKEDA 80
Cdd:pfam00091  18 LWELLCLEHGI----------------DSLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG-----FNPNKILLGKEGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    81 ANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKKSKLGFTIYPSpQVST 160
Cdd:pfam00091  77 GGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGALTVAVVTFPF-GFSE 155
                         170       180       190
                  ....*....|....*....|....*....|....
gi 76257849   161 AVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDIC 194
Cdd:pfam00091 156 GVVRPYNAILGLKELIEHSDSVIVIDNDALYDIC 189
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
27-395 4.22e-43

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: 155.50  E-value: 4.22e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  27 DDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRTGTYRQLFH--PEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIR 104
Cdd:cd02189  36 NSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRARSGAWSydPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALR 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 105 KLADNCTGLQGFMVFNAVGGCTGSGLGSLLLERLSVDYGKksklgftiypSPQVSTAV---------VEPYNSVLSTHSL 175
Cdd:cd02189 116 REAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEYPK----------AYLLNTVVwpyssgevpVQNYNTLLTLSHL 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 176 LEHTDVAVMLDNEAIYDICRRSLDIERP-TYTNLSRLVGQVISSL---TASLRFDGALNVD-ITEFQTNLVPYPRIHFML 250
Cdd:cd02189 186 QESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVllpSSSPTSPSPLRRCpLGDLLEHLCPHPAYKLLT 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849 251 SSYAPVISAEKAYHEQLSVAE---------ITNSAYEPASMMAKCDPRHGKYMACCLMY----RGDVVPKDVNAAVATIK 317
Cdd:cd02189 266 LRSLPQMPEPSRAFSTYTWPSllkrlrqmlITGAKLEEGIDWQLLDTSGSHNPNKSLAAllvlRGKDAMKVHSADLSAFK 345
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76257849 318 TKRTiqFVDWCPTGFkcginyqpPTVVPGGDLAKVLRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGME 395
Cdd:cd02189 346 DPVL--YSPWVPNPF--------NVSVSPRPFNGYEKSVTLLSNSQNIVGPLDSLLEKAWQMFKAGAYLHQYEKYGVE 413
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
229-374 1.15e-23

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: 94.92  E-value: 1.15e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    229 LNVDITEFQTNLVPYPrihFMLSSYAPVISAEKAyheqLSVAEITNSA--YEPASMMAKCDPRHgkYMACCLmyrgDVVP 306
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASGENRA----LEAAELAISSplLEDSNIMGAKGVLV--NITGGP----DLTL 67
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    307 KDVNAAVATIKTKRT-IQFVDWCptgfkcginyqpPTVVPggdlaKVLRAVCMISN-STAIAEVFSRLDH 374
Cdd:smart00865  68 KEVNEAMERIREKADpDAFIIWG------------PVIDE-----ELGGDEIRVTViATGIGSLFKRLSE 120
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
89-183 4.03e-09

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: 58.10  E-value: 4.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849  89 YTIGKEIV------DLCLDRIRKLADNCTGLQGFMVFNAV-GGctGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTA 161
Cdd:cd06060 177 FSQGEELFsdleelEEFEDRLRFFVEECDSLQGFQILVDTdDG--FGGVAAKLLENLRDEYGKKSILTPGLSPASPPDPD 254
                        90       100
                ....*....|....*....|....*.
gi 76257849 162 VVEPY----NSVLSTHSLLEHTDVAV 183
Cdd:cd06060 255 SQRRIkrllNDALSLSSLSEHSSLFV 280
Tubulin_3 pfam14881
Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the ...
65-146 6.29e-04

Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Misato from Drosophila and Dml1p from fungi are descendants of an ancestral tubulin-like protein, and exhibit regions with similarity to members of a GTPase family that includes eukaryotic tubulin and prokaryotic FtsZ. Dml1p and Misato have been co-opted into a role in mtDNA inheritance in yeast, and into a cell division-related mechanism in flies, respectively. Dml1p might additionally function in the partitioning of the mitochondrial organelle itself, or in the segregation of chromosomes, thereby explaining its essential requirement. This domain subject to extensive post-translational modifications.


Pssm-ID: 434281 [Multi-domain]  Cd Length: 180  Bit Score: 40.44  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76257849    65 RQLFHPEQLISGKEDAANN----FARghYTIGKEI-------VDLcLDR-IRKLADNCTGLQGFMVFNAVGGCTGsGLGS 132
Cdd:pfam14881  17 RVFYHPRSIVQLNEYELNSqlmpFED--WSVGEELfreldkeHDL-LDRdLRPFAEECDQLQGLQVFTGSDDAWG-GFAA 92
                          90
                  ....*....|....
gi 76257849   133 LLLERLSVDYGKKS 146
Cdd:pfam14881  93 RYLERLRDEYGKKS 106
 
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