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Conserved domains on  [gi|300244539|ref|NP_001177911|]
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tubulin alpha-1A chain [Danio rerio]

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
1-440 0e+00

tubulin alpha chain; Provisional


:

Pssm-ID: 185562  Cd Length: 448  Bit Score: 957.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
Cdd:PTZ00335   1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  81 GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD 160
Cdd:PTZ00335  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 161 YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:PTZ00335 161 YGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR 320
Cdd:PTZ00335 241 SLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA 400
Cdd:PTZ00335 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYA 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 300244539 401 KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSI 440
Cdd:PTZ00335 401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAESA 440
 
Name Accession Description Interval E-value
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-440 0e+00

tubulin alpha chain; Provisional


Pssm-ID: 185562  Cd Length: 448  Bit Score: 957.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
Cdd:PTZ00335   1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  81 GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD 160
Cdd:PTZ00335  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 161 YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:PTZ00335 161 YGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR 320
Cdd:PTZ00335 241 SLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA 400
Cdd:PTZ00335 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYA 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 300244539 401 KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSI 440
Cdd:PTZ00335 401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAESA 440
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-435 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: 923.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   2 RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTG 81
Cdd:cd02186    1 REIISIHVGQAGVQIGNACWELFCLEHGIQPDGQMPSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  82 TYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDY 161
Cdd:cd02186   81 PYRQLFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 162 GKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITAS 241
Cdd:cd02186  161 GKKSKLEFSIYPSPQVSTSVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 242 LRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRG 321
Cdd:cd02186  241 LRFDGALNVDLNEFQTNLVPYPRIHFPLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 322 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAK 401
Cdd:cd02186  321 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGSDLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSK 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 300244539 402 RAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEV 435
Cdd:cd02186  401 RAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEV 434
COG5023 COG5023
Tubulin [Cytoskeleton];
1-440 0e+00

Tubulin [Cytoskeleton];


Pssm-ID: 227356 [Multi-domain]  Cd Length: 443  Bit Score: 743.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTigGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
Cdd:COG5023    1 MREIITLQVGQCGNQIGNAFWETLCLEHGIGPDGTLLDSSD--EGDERFDVFFYEASDGKFVPRAILVDLEPGVIDQVRN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  81 GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD 160
Cdd:COG5023   79 GPYGSLFHPENIIFGKEGAGNNWARGHYTVGKEIIDDVMDMIRREADGCDGLQGFLLLHSLGGGTGSGLGSLLLERLREE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 161 YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:COG5023  159 YPKKIKLTFSVFPAPKVSDVVVEPYNSVLTLHRLLENSDCTFVVDNEALYDICRRNLRIQNPSYDDLNQLISTVMSSVTT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR 320
Cdd:COG5023  239 SLRFPGYLNVDLRSIQTNLVPYPRLHFPLVSYTPFTSDGSAAHEKNSVSEVTNQLFDPKNQMVSCDPRKGRYMAVCLLFR 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTvvpggDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA 400
Cdd:COG5023  319 GDVDPRDVSRAVTRVQSKRTIQFVEWCPTGFKVAICKRPPS-----EPAEVDVSGCMLSNTTSIAEAFKRIDDQFDLMFK 393
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 300244539 401 KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSI 440
Cdd:COG5023  394 KRAFLHWYVGEGMEEGEFSEAREDVADLEEEYEAAEQDSY 433
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
263-392 4.54e-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: 4.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  263 PRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQ 342
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 300244539  343 FVDWCPTGFKVGINYQPPTVVPGGDlakvqRAVCMLSNTTAIAEAWARLD 392
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 ...
49-246 3.11e-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: 3.11e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539    49 FNTFFSETGAGkhvPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYT-----IGKEIIDLVLDRIR 123
Cdd:smart00864   1 KIKVFGVGGGG---PNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   124 KLADQCtglQGFLVFHsfgggtgsgftsLLMERLSvDYGKKSkLEFSIYPapQVSTAVVEPYNSILTTHTTLEHSDCAFM 203
Cdd:smart00864  78 EELEGA---DGVFITAgmgggtgtgaapVIAEIAK-EYGILT-VAVVTKP--FSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 300244539   204 VDNEAIYDICRRNLDIeRPTYTNLNRLIGQIVSSITASLRFDG 246
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
 
Name Accession Description Interval E-value
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-440 0e+00

tubulin alpha chain; Provisional


Pssm-ID: 185562  Cd Length: 448  Bit Score: 957.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
Cdd:PTZ00335   1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  81 GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD 160
Cdd:PTZ00335  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 161 YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:PTZ00335 161 YGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR 320
Cdd:PTZ00335 241 SLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA 400
Cdd:PTZ00335 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYA 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 300244539 401 KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSI 440
Cdd:PTZ00335 401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAESA 440
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-439 0e+00

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 946.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
Cdd:PLN00221   1 MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  81 GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD 160
Cdd:PLN00221  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 161 YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:PLN00221 161 YGKKSKLGFTVYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR 320
Cdd:PLN00221 241 SLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA 400
Cdd:PLN00221 321 GDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAVAEVFSRIDHKFDLMYA 400
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 300244539 401 KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDS 439
Cdd:PLN00221 401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAES 439
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-435 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: 923.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   2 RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTG 81
Cdd:cd02186    1 REIISIHVGQAGVQIGNACWELFCLEHGIQPDGQMPSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  82 TYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDY 161
Cdd:cd02186   81 PYRQLFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 162 GKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITAS 241
Cdd:cd02186  161 GKKSKLEFSIYPSPQVSTSVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 242 LRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRG 321
Cdd:cd02186  241 LRFDGALNVDLNEFQTNLVPYPRIHFPLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 322 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAK 401
Cdd:cd02186  321 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGSDLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSK 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 300244539 402 RAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEV 435
Cdd:cd02186  401 RAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEV 434
COG5023 COG5023
Tubulin [Cytoskeleton];
1-440 0e+00

Tubulin [Cytoskeleton];


Pssm-ID: 227356 [Multi-domain]  Cd Length: 443  Bit Score: 743.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTigGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
Cdd:COG5023    1 MREIITLQVGQCGNQIGNAFWETLCLEHGIGPDGTLLDSSD--EGDERFDVFFYEASDGKFVPRAILVDLEPGVIDQVRN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  81 GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD 160
Cdd:COG5023   79 GPYGSLFHPENIIFGKEGAGNNWARGHYTVGKEIIDDVMDMIRREADGCDGLQGFLLLHSLGGGTGSGLGSLLLERLREE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 161 YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:COG5023  159 YPKKIKLTFSVFPAPKVSDVVVEPYNSVLTLHRLLENSDCTFVVDNEALYDICRRNLRIQNPSYDDLNQLISTVMSSVTT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR 320
Cdd:COG5023  239 SLRFPGYLNVDLRSIQTNLVPYPRLHFPLVSYTPFTSDGSAAHEKNSVSEVTNQLFDPKNQMVSCDPRKGRYMAVCLLFR 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTvvpggDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA 400
Cdd:COG5023  319 GDVDPRDVSRAVTRVQSKRTIQFVEWCPTGFKVAICKRPPS-----EPAEVDVSGCMLSNTTSIAEAFKRIDDQFDLMFK 393
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 300244539 401 KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSI 440
Cdd:COG5023  394 KRAFLHWYVGEGMEEGEFSEAREDVADLEEEYEAAEQDSY 433
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
3-434 1.81e-172

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: 488.64  E-value: 1.81e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   3 ECISIHVGQAGVQIGNACWELYclehgiqpdgqmpsdktigggddsfntffsetgagkhvpRAVFVDLEPTVIDEVRTGT 82
Cdd:cd06059    1 EIITIQVGQCGNQIGDRFWELA---------------------------------------RAVLVDMEEGVINEVLKGP 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  83 YRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYG 162
Cdd:cd06059   42 LGQLFDPNQFVTGVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYP 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 163 KKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRR---NLDIERPTYTNLNRLIGQIVSSIT 239
Cdd:cd06059  122 KVYRFTFSVFPSPDDDNVITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLT 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 240 ASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLY 319
Cdd:cd06059  202 SSLRFEGSLNVDLNEITTNLVPFPRLHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDNQLVGCDPRHGTYLACALLL 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 320 RGDVV-PKDVNAAIATIKTKRTiqFVDWCPTGFKVGINYQPPtvvpggdlAKVQRAVCMLSNTTAIAEAWARLDHKFDLM 398
Cdd:cd06059  282 RGKVFsLSDVRRNIDRIKPKLK--FISWNPDGFKVGLCSVPP--------VGQKYSLLFLSNNTSIASTFERLIERFDKL 351
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 300244539 399 YAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEE 434
Cdd:cd06059  352 YKRKAFLHHYTGEGMEEGDFSEARESLANLIQEYQE 387
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-434 2.28e-159

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: 457.03  E-value: 2.28e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   2 RECISIHVGQAGVQIGNACWELYCLEHGIQPDGqmpsdkTIGGGDD----SFNTFFSETGAGKHVPRAVFVDLEPTVIDE 77
Cdd:cd02187    1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDG------TYKGDSDlqleRINVYFNEASGGKYVPRAVLVDLEPGTIDS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  78 VRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERL 157
Cdd:cd02187   75 VRSGPYGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 158 SVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSS 237
Cdd:cd02187  155 REEYPDRIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 238 ITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCL 317
Cdd:cd02187  235 ITSSLRFPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 318 LYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGgdlakvqrAVCMLSNTTAIAEAWARLDHKFDL 397
Cdd:cd02187  315 IFRGRISTKEVDEQMSKVQNKNSSYFVEWIPNNVKTSVCDIPPRGLKM--------SATFIGNSTAIQELFKRLSEQFTA 386
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 300244539 398 MYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEE 434
Cdd:cd02187  387 MFRRKAFLHWYTGEGMDEMEFTEAESNLNDLISEYQQ 423
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-434 1.83e-142

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 414.94  E-value: 1.83e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMpsdktIGGGD---DSFNTFFSETGAGKHVPRAVFVDLEPTVIDE 77
Cdd:PTZ00010   1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTY-----QGDSDlqlERINVYYNEATGGRYVPRAVLMDLEPGTMDS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  78 VRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERL 157
Cdd:PTZ00010  76 VRAGPYGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 158 SVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSS 237
Cdd:PTZ00010 156 REEYPDRIMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 238 ITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCL 317
Cdd:PTZ00010 236 VTCCLRFPGQLNSDLRKLAVNLVPFPRLHFFMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 318 LYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPggdlakvqRAVCMLSNTTAIAEAWARLDHKFDL 397
Cdd:PTZ00010 316 LFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSVCDIPPKGLK--------MSVTFIGNSTAIQEMFRRVGEQFTA 387
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 300244539 398 MYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEE 434
Cdd:PTZ00010 388 MFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 424
PLN00220 PLN00220
tubulin beta chain; Provisional
1-434 1.73e-136

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 399.58  E-value: 1.73e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGggDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQ--LERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  81 GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD 160
Cdd:PLN00220  79 GPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 161 YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:PLN00220 159 YPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTC 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR 320
Cdd:PLN00220 239 CLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFR 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTvvpggdlaKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA 400
Cdd:PLN00220 319 GKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPK--------GLKMASTFIGNSTSIQEMFRRVSEQFTAMFR 390
                        410       420       430
                 ....*....|....*....|....*....|....
gi 300244539 401 KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEE 434
Cdd:PLN00220 391 RKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 424
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
3-381 1.65e-131

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: 382.53  E-value: 1.65e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   3 ECISIHVGQAGVQIGNACWELYclehgiqpdgqmpsdktigggddsfntffsetgagkhvpraVFVDLEPTVIDEVRTGT 82
Cdd:cd00286    1 EIVTIQVGQCGNQIGAAFWEQA-----------------------------------------VLVDLEPAVLDELLSGP 39
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  83 YRQLFHPEQLITGKED--AANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD 160
Cdd:cd00286   40 LRQLFHPENIILIQKYhgAGNNWAKGHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDE 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 161 YGKKSKLEFSIYPAPQVSTaVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:cd00286  120 YPNRLVVTFSILPGPDEGV-IVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTE 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR 320
Cdd:cd00286  199 ALRFEGSLNVDLRELAENLVPLPRGHFLMLGYAPLDSATSATPRSLRVKELTRRAFLPANLLVGCDPDHGEAIAALLVIR 278
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300244539 321 G--DVVPKDVNAAIATIKTKRTIQFvDWCPTGFKVGINYQPPtvvpggdlAKVQRAVCMLSNT 381
Cdd:cd00286  279 GppDLSSKEVERAIARVKETLGHLF-SWSPAGVKTGISPKPP--------AEGEVSVLALLNS 332
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
2-432 1.28e-100

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: 307.16  E-value: 1.28e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   2 RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTigGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTG 81
Cdd:cd02188    1 REIITLQVGQCGNQIGSEFWKQLCSEHGISPDGSLEDFAT--DGNDRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  82 TYRQLFHPEQLITGKED--AANNYARGhYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSV 159
Cdd:cd02188   79 PYKNLFNPENIYLSKEGggAGNNWASG-YSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 160 DYGKKSKLEFSIYPA-PQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSI 238
Cdd:cd02188  158 RYPKKLIQTYSVFPNqEESSDVVVQPYNSILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSAS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 239 TASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKA-YHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCL 317
Cdd:cd02188  238 TSTLRFPGYMNNDLVSLISSLIPTPRLHFLMTSYTPLTSDQVAsSVRKTTVLDVMRRLLQPKNRMVSTSTKNGCYISILN 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 318 LYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPggdlakvQRAVC--MLSNTTAIAEAWARLDHKF 395
Cdd:cd02188  318 IIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSKKSPYVQT-------AHRVSglMLANHTSISSLFEKILSQY 390
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 300244539 396 DLMYAKRAFVHWYVGEGMEEG---EFSEAREDMAALEKDY 432
Cdd:cd02188  391 DKLRKRNAFLENYRKEDMFQDnleEFDESREVVQSLIDEY 430
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
2-435 1.55e-99

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: 304.93  E-value: 1.55e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   2 RECISIHVGQAGVQIGNACWELYCLEHGiqpdgqmpSDKTIGGGDDSFNTFFSETGAGKHVP-------------RAVFV 68
Cdd:cd02190    1 REIITVQVGQCGNQIGCRFWDLALREHA--------AYNKDGVYDDSMSSFFRNVDTRSGDPgddggspikslkaRAVLI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  69 DLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSG 148
Cdd:cd02190   73 DMEEGVVNELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGPQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 149 FTSLLMERLSVDYGKKSKLEFSIYPAPQ--VSTAvvePYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTN 226
Cdd:cd02190  153 LGSYILELLEDEFPDVYRFVTSVFPSGDddVITS---PYNSVLALRELTEHADCVLPVENQALMDIVNKIKSSKDKGKTG 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 227 ----------------------LNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHE 284
Cdd:cd02190  230 vlaainssgggqkkgkkkpfddMNNIVANLLLNLTSSMRFEGSLNVDLNEITTNLVPFPRLHFLLSSLSPLYALADVRLP 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 285 QLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIktKRTIQFVDWCPTGFKVGINYQPPTVVP 364
Cdd:cd02190  310 PRRLDQMFSDAFSRDHQLLKADPKHGLYLACALLVRGNVSISDLRRNIDRL--KRQLKFVSWNQDGWKIGLCSVPPVGQP 387
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300244539 365 ggdlakvqRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVgEGMEEGEFSEAREDMAALEKDYEEV 435
Cdd:cd02190  388 --------YSLLCLANNTCIKPTFTEMHERFDKLYKRKAHLHHYT-QYMEQDDFDEALESLLDLIEEYKDL 449
PTZ00387 PTZ00387
epsilon tubulin; Provisional
1-435 9.18e-91

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 283.15  E-value: 9.18e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   1 MRECISIHVGQAGVQIGNACWELYCLEH-GIQPDGQMpsdktigggDDSFNTFFSETGAGKHVP-------RAVFVDLEP 72
Cdd:PTZ00387   1 PREIVTVQVGQCGNQLGHRFWDVALKEHkKINANPQY---------DDARDSFFENVSENVNRPgkenlkaRAVLVDMEE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  73 TVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSL 152
Cdd:PTZ00387  72 GVLNQILKSPLGDLFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 153 LMERLSVDYGKKSKLEFSIYPApQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIER----------- 221
Cdd:PTZ00387 152 ILGMLEDEFPHVFRFCPVVFPS-AVDDVITSPYNSFFALRELIEHADCVLPLDNDALANIADSALSRKKkklakgnikrg 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 222 ----------PT------YTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQ 285
Cdd:PTZ00387 231 pqphkysvakPTetkklpYDKMNNIVAQLLSNLTSSMRFEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGP 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 286 LSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAtiKTKRTIQFVDWCPTGFKVGINYQPPTVVPg 365
Cdd:PTZ00387 311 RRLDQMFKDCLDPDHQMVAATPEAGKYLATALIVRGPQNVSDVTRNIL--RLKEQLNMIYWNEDGFKTGLCNVSPLGQP- 387
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 366 gdlakvqRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVgEGMEEGEFSEAREDMAALEKDYEEV 435
Cdd:PTZ00387 388 -------YSLLCLANNCCIRNKFESMLERFNKLYKRKSHVHHYT-EYLEQAYFDETLETIQNLIDDYAYL 449
PLN00222 PLN00222
tubulin gamma chain; Provisional
2-432 1.22e-83

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 264.40  E-value: 1.22e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   2 RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGgdDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTG 81
Cdd:PLN00222   3 REIITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGG--DRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  82 TYRQLFHPEQLITGKED--AANNYARGhYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSV 159
Cdd:PLN00222  81 EYRNLYNHENIFVSDHGggAGNNWASG-YHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALND 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 160 DYGKKSKLEFSIYPA-PQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSI 238
Cdd:PLN00222 160 RYSKKLVQTYSVFPNqMETSDVVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSAS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 239 TASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPV-ISAEKAYHEQLSVAEITNACFEPANQMVKCDPR-----HGKY 312
Cdd:PLN00222 240 TTTLRYPGYMNNDLVGLLASLIPTPRCHFLMTGYTPLtVERQANVIRKTTVLDVMRRLLQTKNIMVSSYARtkeasQAKY 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 313 MACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVqravcMLSNTTAIAEAWARLD 392
Cdd:PLN00222 320 ISILNIIQGEVDPTQVHKSLQRIRERKLANFIEWGPASIQVALSRKSPYVQTAHRVSGL-----MLANHTSIRHLFSKCL 394
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 300244539 393 HKFDLMYAKRAFVHWYVGEGM----EEGEFSEAREDMAALEKDY 432
Cdd:PLN00222 395 SQYDKLRKKQAFLDNYRKFPMfadnDLSEFDESREIVESLVDEY 438
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
263-392 4.54e-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: 4.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  263 PRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQ 342
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 300244539  343 FVDWCPTGFKVGINYQPPTVVPGGDlakvqRAVCMLSNTTAIAEAWARLD 392
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 ...
49-246 3.11e-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: 3.11e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539    49 FNTFFSETGAGkhvPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYT-----IGKEIIDLVLDRIR 123
Cdd:smart00864   1 KIKVFGVGGGG---PNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   124 KLADQCtglQGFLVFHsfgggtgsgftsLLMERLSvDYGKKSkLEFSIYPapQVSTAVVEPYNSILTTHTTLEHSDCAFM 203
Cdd:smart00864  78 EELEGA---DGVFITAgmgggtgtgaapVIAEIAK-EYGILT-VAVVTKP--FSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 300244539   204 VDNEAIYDICRRNLDIeRPTYTNLNRLIGQIVSSITASLRFDG 246
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
3-213 5.26e-66

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: 395044 [Multi-domain]  Cd Length: 190  Bit Score: 209.77  E-value: 5.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539    3 ECISIHVGQAGVQIGNACWELYCLEHGIqpdgqmpsdktigggdDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGt 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCLEHGI----------------DSLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   83 yrqlFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYG 162
Cdd:pfam00091  64 ----FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYP 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 300244539  163 KKSKLEFSIYPAPqVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDIC 213
Cdd:pfam00091 140 GALTVAVVTFPFP-FSEGVVRPYNAILGLKELIEHSDSVIVIDNDALYDIC 189
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
4-434 8.35e-45

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: 161.66  E-value: 8.35e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   4 CISIHVGQAGVQIGNACWELYCLEhgiqpdGQMPSDKtiGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTY 83
Cdd:cd02189    2 IVTVQVGQCGNQLGDELFDTLADE------ADSSASE--GDQNSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRAR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539  84 RQLFH--PEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGgtgsgftsLLMERLSVDY 161
Cdd:cd02189   74 SGAWSydPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGgtgsglgsRVTELLRDEY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 162 GKKSKLEFSIypAPQvSTA--VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERP-TYTNLNRLIG-QIVSS 237
Cdd:cd02189  154 PKAYLLNTVV--WPY-SSGevPVQNYNTLLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIArQLAGV 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 238 I--TASLRFDGALNVD-LTEFQTNLVPYPriHFPLAT--YAPVISAE-------------KAYHEQLSVAEITNACFEPA 299
Cdd:cd02189  231 LlpSSSPTSPSPLRRCpLGDLLEHLCPHP--AYKLLTlrSLPQMPEPsrafstytwpsllKRLRQMLITGAKLEEGIDWQ 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539 300 NQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTiqFVDWCPTGFkvginyqpPTVVPGGDLAKVQRAVCMLS 379
Cdd:cd02189  309 LLDTSGSHNPNKSLAALLVLRGKDAMKVHSADLSAFKDPVL--YSPWVPNPF--------NVSVSPRPFNGYEKSVTLLS 378
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 300244539 380 NTTAIAeawARLDH---KFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEE 434
Cdd:cd02189  379 NSQNIV---GPLDSlleKAWQMFKAGAYLHQYEKYGVEEEDFLDAFATLEQIIAAYKS 433
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
248-393 6.69e-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: 104.17  E-value: 6.69e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   248 LNVDLTEFQTNLVPYPrihFPLATYAPVISAEKAyheqLSVAE--ITNACFEPANQMVKCDPRHgkYMACCLlyrgDVVP 325
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASGENRA----LEAAElaISSPLLEDSNIMGAKGVLV--NITGGP----DLTL 67
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300244539   326 KDVNAAIATIKTKRT-IQFVDWCptgfkvginyqpPTVVPggdlaKVQRAVCMLSN-TTAIAEAWARLDH 393
Cdd:smart00865  68 KEVNEAMERIREKADpDAFIIWG------------PVIDE-----ELGGDEIRVTViATGIGSLFKRLSE 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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