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Conserved domains on  [gi|1519315503|ref|NP_997195|]
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tubulin alpha-3E chain [Homo sapiens]

Protein Classification

tubulin alpha chain( domain architecture ID 11488404)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-440 0e+00

tubulin alpha chain; Provisional


:

Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 941.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRT 80
Cdd:PTZ00335    1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  81 GTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVD 160
Cdd:PTZ00335   81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 161 YSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:PTZ00335  161 YGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYR 320
Cdd:PTZ00335  241 SLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYA 400
Cdd:PTZ00335  321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYA 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1519315503 401 KWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEVGVDSV 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 [Multi-domain]  Cd Length: 448  Bit Score: 941.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRT 80
Cdd:PTZ00335    1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  81 GTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVD 160
Cdd:PTZ00335   81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 161 YSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:PTZ00335  161 YGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYR 320
Cdd:PTZ00335  241 SLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYA 400
Cdd:PTZ00335  321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYA 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1519315503 401 KWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEVGVDSV 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: 908.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   2 RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTG 81
Cdd:cd02186     1 REIISIHVGQAGVQIGNACWELFCLEHGIQPDGQMPSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  82 TYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDY 161
Cdd:cd02186    81 PYRQLFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 162 SKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITAS 241
Cdd:cd02186   161 GKKSKLEFSIYPSPQVSTSVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTAS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 242 LRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRG 321
Cdd:cd02186   241 LRFDGALNVDLNEFQTNLVPYPRIHFPLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 322 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYAK 401
Cdd:cd02186   321 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGSDLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSK 400
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1519315503 402 WAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEV 435
Cdd:cd02186   401 RAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEV 434
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
263-391 1.56e-76

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: 234.43  E-value: 1.56e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 263 PRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQ 342
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519315503 343 FVDWCPTGFKVGINYQPPTVVPGGDlakvqRAVCMLSNTTAIAEAWARL 391
Cdd:pfam03953  81 FVEWCPTGIKVAICSQSPYVVPGSK-----VSGLMLANTTSIAELFQRL 124
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
49-246 3.59e-67

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: 212.73  E-value: 3.59e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   49 FNTFFSETGAGkhvPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAASNYARGHYT-----IGKEIVDLVLDRIR 123
Cdd:smart00864   1 KIKVFGVGGGG---PNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  124 KLADLCtglQGFLIFHSFGGGTGSGFASLLMERLSvDYSKKSkLEFAIYPapQVSTAVVEPYNSILTTHTTLEHSDCAFM 203
Cdd:smart00864  78 EELEGA---DGVFITAGMGGGTGTGAAPVIAEIAK-EYGILT-VAVVTKP--FSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1519315503  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 [Multi-domain]  Cd Length: 448  Bit Score: 941.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRT 80
Cdd:PTZ00335    1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  81 GTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVD 160
Cdd:PTZ00335   81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 161 YSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:PTZ00335  161 YGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYR 320
Cdd:PTZ00335  241 SLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYA 400
Cdd:PTZ00335  321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYA 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1519315503 401 KWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEVGVDSV 440
Cdd:PTZ00335  401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAESA 440
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-450 0e+00

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 930.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRT 80
Cdd:PLN00221    1 MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  81 GTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVD 160
Cdd:PLN00221   81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 161 YSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:PLN00221  161 YGKKSKLGFTVYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYR 320
Cdd:PLN00221  241 SLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYA 400
Cdd:PLN00221  321 GDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTAVAEVFSRIDHKFDLMYA 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1519315503 401 KWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEVGVDSVEAEAEEGEAY 450
Cdd:PLN00221  401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAESAEGEGDEGEEY 450
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: 908.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   2 RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTG 81
Cdd:cd02186     1 REIISIHVGQAGVQIGNACWELFCLEHGIQPDGQMPSDKTIGGDDDNFNTFFSETGSGKYVPRAVFVDLEPTVIDEIRTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  82 TYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDY 161
Cdd:cd02186    81 PYRQLFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 162 SKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITAS 241
Cdd:cd02186   161 GKKSKLEFSIYPSPQVSTSVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTAS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 242 LRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRG 321
Cdd:cd02186   241 LRFDGALNVDLNEFQTNLVPYPRIHFPLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 322 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYAK 401
Cdd:cd02186   321 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGSDLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSK 400
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1519315503 402 WAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEV 435
Cdd:cd02186   401 RAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEV 434
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
3-434 4.80e-166

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: 472.46  E-value: 4.80e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   3 ECISIHVGQAGVQIGNACWELYclehgiqpdgqmpsdktigggddsfntffsetgagkhvpRAVFVDLEPTVVDEVRTGT 82
Cdd:cd06059     1 EIITIQVGQCGNQIGDRFWELA---------------------------------------RAVLVDMEEGVINEVLKGP 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  83 YRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYS 162
Cdd:cd06059    42 LGQLFDPNQFVTGVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYP 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 163 KKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRR---NLDIERPTYTNLNRLIGQIVSSIT 239
Cdd:cd06059   122 KVYRFTFSVFPSPDDDNVITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLT 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 240 ASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLY 319
Cdd:cd06059   202 SSLRFEGSLNVDLNEITTNLVPFPRLHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDNQLVGCDPRHGTYLACALLL 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 320 RGDVV-PKDVNAAIATIKTKRTiqFVDWCPTGFKVGINYQPPtvvpggdlAKVQRAVCMLSNTTAIAEAWARLVHKFDLM 398
Cdd:cd06059   282 RGKVFsLSDVRRNIDRIKPKLK--FISWNPDGFKVGLCSVPP--------VGQKYSLLFLSNNTSIASTFERLIERFDKL 351
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1519315503 399 YAKWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEE 434
Cdd:cd06059   352 YKRKAFLHHYTGEGMEEGDFSEARESLANLIQEYQE 387
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-428 4.08e-153

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: 441.24  E-value: 4.08e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   2 RECISIHVGQAGVQIGNACWELYCLEHGIQPDGqmpsdkTIGGGDD----SFNTFFSETGAGKHVPRAVFVDLEPTVVDE 77
Cdd:cd02187     1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDG------TYKGDSDlqleRINVYFNEASGGKYVPRAVLVDLEPGTIDS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  78 VRTGTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERL 157
Cdd:cd02187    75 VRSGPYGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 158 SVDYSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSS 237
Cdd:cd02187   155 REEYPDRIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 238 ITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCM 317
Cdd:cd02187   235 ITSSLRFPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 318 LYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGgdlakvqrAVCMLSNTTAIAEAWARLVHKFDL 397
Cdd:cd02187   315 IFRGRISTKEVDEQMSKVQNKNSSYFVEWIPNNVKTSVCDIPPRGLKM--------SATFIGNSTAIQELFKRLSEQFTA 386
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1519315503 398 MYAKWAFVHWYVGEGMEEGEFSEAREDLAAL 428
Cdd:cd02187   387 MFRRKAFLHWYTGEGMDEMEFTEAESNLNDL 417
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-439 1.88e-139

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 407.24  E-value: 1.88e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMpsdktIGGGD---DSFNTFFSETGAGKHVPRAVFVDLEPTVVDE 77
Cdd:PTZ00010    1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTY-----QGDSDlqlERINVYYNEATGGRYVPRAVLMDLEPGTMDS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  78 VRTGTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERL 157
Cdd:PTZ00010   76 VRAGPYGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 158 SVDYSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSS 237
Cdd:PTZ00010  156 REEYPDRIMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 238 ITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCM 317
Cdd:PTZ00010  236 VTCCLRFPGQLNSDLRKLAVNLVPFPRLHFFMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 318 LYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPggdlakvqRAVCMLSNTTAIAEAWARLVHKFDL 397
Cdd:PTZ00010  316 LFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSVCDIPPKGLK--------MSVTFIGNSTAIQEMFRRVGEQFTA 387
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1519315503 398 MYAKWAFVHWYVGEGMEEGEFSEAR---EDLAALEKDCEEVGVDS 439
Cdd:PTZ00010  388 MFRRKAFLHWYTGEGMDEMEFTEAEsnmNDLVSEYQQYQDATVEE 432
PLN00220 PLN00220
tubulin beta chain; Provisional
1-428 1.14e-131

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 387.26  E-value: 1.14e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   1 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGggDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRT 80
Cdd:PLN00220    1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQ--LERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  81 GTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVD 160
Cdd:PLN00220   79 GPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 161 YSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:PLN00220  159 YPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTC 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYR 320
Cdd:PLN00220  239 CLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTvvpggdlaKVQRAVCMLSNTTAIAEAWARLVHKFDLMYA 400
Cdd:PLN00220  319 GKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPK--------GLKMASTFIGNSTSIQEMFRRVSEQFTAMFR 390
                         410       420
                  ....*....|....*....|....*...
gi 1519315503 401 KWAFVHWYVGEGMEEGEFSEAREDLAAL 428
Cdd:PLN00220  391 RKAFLHWYTGEGMDEMEFTEAESNMNDL 418
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
3-381 6.18e-130

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: 378.67  E-value: 6.18e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   3 ECISIHVGQAGVQIGNACWELYclehgiqpdgqmpsdktigggddsfntffsetgagkhvpraVFVDLEPTVVDEVRTGT 82
Cdd:cd00286     1 EIVTIQVGQCGNQIGAAFWEQA-----------------------------------------VLVDLEPAVLDELLSGP 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  83 YRQLFHPEQLITGKED--AASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVD 160
Cdd:cd00286    40 LRQLFHPENIILIQKYhgAGNNWAKGHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDE 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 161 YSKKSKLEFAIYPAPQVSTaVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA 240
Cdd:cd00286   120 YPNRLVVTFSILPGPDEGV-IVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTE 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 241 SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYR 320
Cdd:cd00286   199 ALRFEGSLNVDLRELAENLVPLPRGHFLMLGYAPLDSATSATPRSLRVKELTRRAFLPANLLVGCDPDHGEAIAALLVIR 278
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519315503 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 ...
2-423 1.58e-98

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: 301.77  E-value: 1.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   2 RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTigGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTG 81
Cdd:cd02188     1 REIITLQVGQCGNQIGSEFWKQLCSEHGISPDGSLEDFAT--DGNDRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  82 TYRQLFHPEQLITGKED--AASNYARGhYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSV 159
Cdd:cd02188    79 PYKNLFNPENIYLSKEGggAGNNWASG-YSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 160 DYSKKSKLEFAIYPA-PQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSI 238
Cdd:cd02188   158 RYPKKLIQTYSVFPNqEESSDVVVQPYNSILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSAS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 239 TASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKA-YHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCM 317
Cdd:cd02188   238 TSTLRFPGYMNNDLVSLISSLIPTPRLHFLMTSYTPLTSDQVAsSVRKTTVLDVMRRLLQPKNRMVSTSTKNGCYISILN 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 318 LYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPggdlakvQRAVC--MLSNTTAIAEAWARLVHKF 395
Cdd:cd02188   318 IIQGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSKKSPYVQT-------AHRVSglMLANHTSISSLFEKILSQY 390
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1519315503 396 DLMYAKWAFVHWYVGEGMEEG---EFSEARE 423
Cdd:cd02188   391 DKLRKRNAFLENYRKEDMFQDnleEFDESRE 421
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
2-431 7.23e-95

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: 292.99  E-value: 7.23e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   2 RECISIHVGQAGVQIGNACWELYCLEHGiqpdgqmpSDKTIGGGDDSFNTFFSETGAGKHVP-------------RAVFV 68
Cdd:cd02190     1 REIITVQVGQCGNQIGCRFWDLALREHA--------AYNKDGVYDDSMSSFFRNVDTRSGDPgddggspikslkaRAVLI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  69 DLEPTVVDEVRTGTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSG 148
Cdd:cd02190    73 DMEEGVVNELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGPQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 149 FASLLMERLSVDYSKKSKLEFAIYPAPQ--VSTAvvePYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTN 226
Cdd:cd02190   153 LGSYILELLEDEFPDVYRFVTSVFPSGDddVITS---PYNSVLALRELTEHADCVLPVENQALMDIVNKIKSSKDKGKTG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 227 ----------------------LNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHE 284
Cdd:cd02190   230 vlaainssgggqkkgkkkpfddMNNIVANLLLNLTSSMRFEGSLNVDLNEITTNLVPFPRLHFLLSSLSPLYALADVRLP 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 285 QLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIktKRTIQFVDWCPTGFKVGINYQPPTVVP 364
Cdd:cd02190   310 PRRLDQMFSDAFSRDHQLLKADPKHGLYLACALLVRGNVSISDLRRNIDRL--KRQLKFVSWNQDGWKIGLCSVPPVGQP 387
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519315503 365 ggdlakvqRAVCMLSNTTAIAEAWARLVHKFDLMYAKWAFVHWYVgEGMEEGEFSEAREDLAALEKD 431
Cdd:cd02190   388 --------YSLLCLANNTCIKPTFTEMHERFDKLYKRKAHLHHYT-QYMEQDDFDEALESLLDLIEE 445
PTZ00387 PTZ00387
epsilon tubulin; Provisional
1-438 1.96e-86

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 271.98  E-value: 1.96e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   1 MRECISIHVGQAGVQIGNACWELYCLEH-GIQPDGQMpsdktigggDDSFNTFFSETGAGKHVP-------RAVFVDLEP 72
Cdd:PTZ00387    1 PREIVTVQVGQCGNQLGHRFWDVALKEHkKINANPQY---------DDARDSFFENVSENVNRPgkenlkaRAVLVDMEE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  73 TVVDEVRTGTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASL 152
Cdd:PTZ00387   72 GVLNQILKSPLGDLFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 153 LMERLSVDYSKKSKLEFAIYPApQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIER----------- 221
Cdd:PTZ00387  152 ILGMLEDEFPHVFRFCPVVFPS-AVDDVITSPYNSFFALRELIEHADCVLPLDNDALANIADSALSRKKkklakgnikrg 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 222 ----------PT------YTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQ 285
Cdd:PTZ00387  231 pqphkysvakPTetkklpYDKMNNIVAQLLSNLTSSMRFEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGP 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 286 LSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIAtiKTKRTIQFVDWCPTGFKVGINYQPPTVVPg 365
Cdd:PTZ00387  311 RRLDQMFKDCLDPDHQMVAATPEAGKYLATALIVRGPQNVSDVTRNIL--RLKEQLNMIYWNEDGFKTGLCNVSPLGQP- 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 366 gdlakvqRAVCMLSNTTAIAEAWARLVHKFDLMYAKWAFVHWYVgEGMEEGEFSEARE-------DLAALEKDCEEVGVD 438
Cdd:PTZ00387  388 -------YSLLCLANNCCIRNKFESMLERFNKLYKRKSHVHHYT-EYLEQAYFDETLEtiqnlidDYAYLQTAEPPKDLP 459
PLN00222 PLN00222
tubulin gamma chain; Provisional
2-433 1.09e-82

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 261.70  E-value: 1.09e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   2 RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGgdDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTG 81
Cdd:PLN00222    3 REIITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGG--DRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  82 TYRQLFHPEQLITGKED--AASNYARGhYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSV 159
Cdd:PLN00222   81 EYRNLYNHENIFVSDHGggAGNNWASG-YHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALND 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 160 DYSKKSKLEFAIYPA-PQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSI 238
Cdd:PLN00222  160 RYSKKLVQTYSVFPNqMETSDVVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSAS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 239 TASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPV-ISAEKAYHEQLSVAEITNACFEPANQMVKCDPR-----HGKY 312
Cdd:PLN00222  240 TTTLRYPGYMNNDLVGLLASLIPTPRCHFLMTGYTPLtVERQANVIRKTTVLDVMRRLLQTKNIMVSSYARtkeasQAKY 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 313 MACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVqravcMLSNTTAIAEAWARLV 392
Cdd:PLN00222  320 ISILNIIQGEVDPTQVHKSLQRIRERKLANFIEWGPASIQVALSRKSPYVQTAHRVSGL-----MLANHTSIRHLFSKCL 394
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1519315503 393 HKFDLMYAKWAFVHWYVGEGM----EEGEFSEARE---DLAALEKDCE 433
Cdd:PLN00222  395 SQYDKLRKKQAFLDNYRKFPMfadnDLSEFDESREiveSLVDEYKACE 442
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
263-391 1.56e-76

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: 234.43  E-value: 1.56e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 263 PRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQ 342
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519315503 343 FVDWCPTGFKVGINYQPPTVVPGGDlakvqRAVCMLSNTTAIAEAWARL 391
Cdd:pfam03953  81 FVEWCPTGIKVAICSQSPYVVPGSK-----VSGLMLANTTSIAELFQRL 124
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
49-246 3.59e-67

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: 212.73  E-value: 3.59e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   49 FNTFFSETGAGkhvPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAASNYARGHYT-----IGKEIVDLVLDRIR 123
Cdd:smart00864   1 KIKVFGVGGGG---PNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  124 KLADLCtglQGFLIFHSFGGGTGSGFASLLMERLSvDYSKKSkLEFAIYPapQVSTAVVEPYNSILTTHTTLEHSDCAFM 203
Cdd:smart00864  78 EELEGA---DGVFITAGMGGGTGTGAAPVIAEIAK-EYGILT-VAVVTKP--FSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1519315503  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 5.85e-65

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: 207.07  E-value: 5.85e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   3 ECISIHVGQAGVQIGNACWELYCLEHGIqpdgqmpsdktigggdDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGt 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCLEHGI----------------DSLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  83 yrqlFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYS 162
Cdd:pfam00091  64 ----FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYP 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1519315503 163 KKSKLEFAIYPApQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDIC 213
Cdd:pfam00091 140 GALTVAVVTFPF-GFSEGVVRPYNAILGLKELIEHSDSVIVIDNDALYDIC 189
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
4-426 7.56e-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: 156.27  E-value: 7.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503   4 CISIHVGQAGVQIGNACWELYCLEhgiqpdGQMPSDKtiGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTY 83
Cdd:cd02189     2 IVTVQVGQCGNQLGDELFDTLADE------ADSSASE--GDQNSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRAR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  84 RQLFH--PEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDY 161
Cdd:cd02189    74 SGAWSydPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 162 SKKSKLEFAIypAPQvSTA--VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERP-TYTNLNRLIG-QIVSS 237
Cdd:cd02189   154 PKAYLLNTVV--WPY-SSGevPVQNYNTLLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIArQLAGV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 238 I--TASLRFDGALNVD-LTEFQTNLVPYPriHFPLAT--YAPVISAE-------------KAYHEQLSVAEITNACFEPA 299
Cdd:cd02189   231 LlpSSSPTSPSPLRRCpLGDLLEHLCPHP--AYKLLTlrSLPQMPEPsrafstytwpsllKRLRQMLITGAKLEEGIDWQ 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 300 NQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTiqFVDWCPTGFkvginyqpPTVVPGGDLAKVQRAVCMLS 379
Cdd:cd02189   309 LLDTSGSHNPNKSLAALLVLRGKDAMKVHSADLSAFKDPVL--YSPWVPNPF--------NVSVSPRPFNGYEKSVTLLS 378
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1519315503 380 NTTAIAEAWARLVHKFDLMYAKWAFVHWYVGEGMEEGEFSEAREDLA 426
Cdd:cd02189   379 NSQNIVGPLDSLLEKAWQMFKAGAYLHQYEKYGVEEEDFLDAFATLE 425
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
248-393 1.06e-26

Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. These proteins are GTPases and are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division, it is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea. This is the C-terminal domain.


Pssm-ID: 214868 [Multi-domain]  Cd Length: 120  Bit Score: 103.78  E-value: 1.06e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  248 LNVDLTEFQTNLVPYPrihFPLATYAPVISAEKAyheqLSVAE--ITNACFEPANQMVKCDPRHgkYMACCMlyrgDVVP 325
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASGENRA----LEAAElaISSPLLEDSNIMGAKGVLV--NITGGP----DLTL 67
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503  326 KDVNAAIATIKTKRT-IQFVDWCptgfkvginyqpPTVVPggdlaKVQRAVCMLSN-TTAIAEAWARLVH 393
Cdd:smart00865  68 KEVNEAMERIREKADpDAFIIWG------------PVIDE-----ELGGDEIRVTViATGIGSLFKRLSE 120
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
108-200 5.83e-04

Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family of GTPases and is localized to the the outer membrane of mitochondria. It has a role in mitochondrial fusion and in mitochondrial distribution and morphology. Mutations in its Drosophila homolog (misato) lead to irregular chromosome segregation during mitosis. Deletion of the budding yeast homolog DML1 is lethal and unregulate expression of DML1 leads to mitochondrial dispersion and abnormalities in cell morphology. The Misato/DML1 protein family is conserved from yeast to human, but its exact function is still unknown.


Pssm-ID: 276964 [Multi-domain]  Cd Length: 539  Bit Score: 42.31  E-value: 5.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315503 108 YTIGKEIV------DLVLDRIRKLADLCTGLQGFLI-------FhsfgggtgSGFASLLMERLSVDYSKKSKLEFAIYPA 174
Cdd:cd06060   177 FSQGEELFsdleelEEFEDRLRFFVEECDSLQGFQIlvdtddgF--------GGVAAKLLENLRDEYGKKSILTPGLSPA 248
                          90       100       110
                  ....*....|....*....|....*....|
gi 1519315503 175 PQVSTAVVEPY----NSILTTHTTLEHSDC 200
Cdd:cd06060   249 SPPDPDSQRRIkrllNDALSLSSLSEHSSL 278
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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