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Conserved domains on  [gi|159471706|ref|XP_001693997|]
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beta tubulin 2 [Chlamydomonas reinhardtii]

Protein Classification

PLN00220 family protein (domain architecture ID 11476486)

PLN00220 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN00220 PLN00220
tubulin beta chain; Provisional
1-430 0e+00

tubulin beta chain; Provisional


:

Pssm-ID: 215107  Cd Length: 447  Bit Score: 999.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   1 MREIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGP 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  81 YGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 161 DRMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITCCL 240
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 241 RFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRGR 320
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 321 MSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMSATFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHWYTG 400
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|
gi 159471706 401 EGMDEMEFTEAESNMNDLVSEYQQYQDASA 430
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATA 430
 
Name Accession Description Interval E-value
PLN00220 PLN00220
tubulin beta chain; Provisional
1-430 0e+00

tubulin beta chain; Provisional


Pssm-ID: 215107  Cd Length: 447  Bit Score: 999.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   1 MREIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGP 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  81 YGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 161 DRMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITCCL 240
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 241 RFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRGR 320
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 321 MSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMSATFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHWYTG 400
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|
gi 159471706 401 EGMDEMEFTEAESNMNDLVSEYQQYQDASA 430
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATA 430
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-426 0e+00

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  Cd Length: 425  Bit Score: 897.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   2 REIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGPY 81
Cdd:cd02187    1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  82 GQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPD 161
Cdd:cd02187   81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 162 RMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITCCLR 241
Cdd:cd02187  161 RIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 242 FPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRGRM 321
Cdd:cd02187  241 FPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 322 STKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMSATFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHWYTGE 401
Cdd:cd02187  321 STKEVDEQMSKVQNKNSSYFVEWIPNNVKTSVCDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGE 400
                        410       420
                 ....*....|....*....|....*
gi 159471706 402 GMDEMEFTEAESNMNDLVSEYQQYQ 426
Cdd:cd02187  401 GMDEMEFTEAESNLNDLISEYQQYQ 425
COG5023 COG5023
Tubulin [Cytoskeleton];
1-429 0e+00

Tubulin [Cytoskeleton];


Pssm-ID: 227356  Cd Length: 443  Bit Score: 701.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   1 MREIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGP 80
Cdd:COG5023    1 MREIITLQVGQCGNQIGNAFWETLCLEHGIGPDGTLLDSSDEGDERFDVFFYEASDGKFVPRAILVDLEPGVIDQVRNGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  81 YGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:COG5023   81 YGSLFHPENIIFGKEGAGNNWARGHYTVGKEIIDDVMDMIRREADGCDGLQGFLLLHSLGGGTGSGLGSLLLERLREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 161 DRMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITCCL 240
Cdd:COG5023  161 KKIKLTFSVFPAPKVSDVVVEPYNSVLTLHRLLENSDCTFVVDNEALYDICRRNLRIQNPSYDDLNQLISTVMSSVTTSL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 241 RFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRGR 320
Cdd:COG5023  241 RFPGYLNVDLRSIQTNLVPYPRLHFPLVSYTPFTSDGSAAHEKNSVSEVTNQLFDPKNQMVSCDPRKGRYMAVCLLFRGD 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 321 MSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPP---KGLKMSATFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHW 397
Cdd:COG5023  321 VDPRDVSRAVTRVQSKRTIQFVEWCPTGFKVAICKRPPsepAEVDVSGCMLSNTTSIAEAFKRIDDQFDLMFKKRAFLHW 400
                        410       420       430
                 ....*....|....*....|....*....|..
gi 159471706 398 YTGEGMDEMEFTEAESNMNDLVSEYQQYQDAS 429
Cdd:COG5023  401 YVGEGMEEGEFSEAREDVADLEEEYEAAEQDS 432
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
47-244 1.77e-60

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  Cd Length: 192  Bit Score: 198.48  E-value: 1.77e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706    47 INVYFNEatgGRYVPRAILMDLEPGTMDSVRSGPYGQIFRPDNFVFGQTGAGNNWAKGHYT-----EGAELIDSVLDVVR 121
Cdd:smart00864   1 KIKVFGV---GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   122 KEAESCDclqGFQVCHslgggtgsgmgtlLISKIREEYPDrmmLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMV 201
Cdd:smart00864  78 EELEGAD---GVFITAgmgggt-gtgaapVIAEIAKEYGI---LTVAVVTKPFSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 159471706   202 LDNEALYDICFRTLKLtTPTFGDLNHLISAVMSGITCCLRFPG 244
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
3-211 1.24e-59

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: 306575  Cd Length: 190  Bit Score: 196.28  E-value: 1.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706    3 EIVHIQGGQCGNQIGAKFWEVVSDEHGIDptgtyhgdsdlqleRINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGPYg 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCKEHGID--------------SLNVFFSESGSVEFIPRSIAIDTDPQALNEIKAGSL- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   83 qifrPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDR 162
Cdd:pfam00091  66 ----PNKIFLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGA 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 159471706  163 MMLTFSVVPSpKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDIC 211
Cdd:pfam00091 142 LTVAVVTFPF-GFSEGVVRPYNAILGLKELREHSDSVIVIDNDALLDIC 189
 
Name Accession Description Interval E-value
PLN00220 PLN00220
tubulin beta chain; Provisional
1-430 0e+00

tubulin beta chain; Provisional


Pssm-ID: 215107  Cd Length: 447  Bit Score: 999.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   1 MREIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGP 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  81 YGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 161 DRMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITCCL 240
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 241 RFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRGR 320
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 321 MSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMSATFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHWYTG 400
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|
gi 159471706 401 EGMDEMEFTEAESNMNDLVSEYQQYQDASA 430
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATA 430
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-430 0e+00

tubulin beta chain; Provisional


Pssm-ID: 240228  Cd Length: 445  Bit Score: 948.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   1 MREIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGP 80
Cdd:PTZ00010   1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  81 YGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:PTZ00010  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 161 DRMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITCCL 240
Cdd:PTZ00010 161 DRIMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 241 RFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRGR 320
Cdd:PTZ00010 241 RFPGQLNSDLRKLAVNLVPFPRLHFFMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 321 MSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMSATFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHWYTG 400
Cdd:PTZ00010 321 MSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSVCDIPPKGLKMSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|
gi 159471706 401 EGMDEMEFTEAESNMNDLVSEYQQYQDASA 430
Cdd:PTZ00010 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATV 430
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-426 0e+00

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  Cd Length: 425  Bit Score: 897.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   2 REIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGPY 81
Cdd:cd02187    1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  82 GQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPD 161
Cdd:cd02187   81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 162 RMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITCCLR 241
Cdd:cd02187  161 RIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 242 FPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRGRM 321
Cdd:cd02187  241 FPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 322 STKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMSATFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHWYTGE 401
Cdd:cd02187  321 STKEVDEQMSKVQNKNSSYFVEWIPNNVKTSVCDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGE 400
                        410       420
                 ....*....|....*....|....*
gi 159471706 402 GMDEMEFTEAESNMNDLVSEYQQYQ 426
Cdd:cd02187  401 GMDEMEFTEAESNLNDLISEYQQYQ 425
COG5023 COG5023
Tubulin [Cytoskeleton];
1-429 0e+00

Tubulin [Cytoskeleton];


Pssm-ID: 227356  Cd Length: 443  Bit Score: 701.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   1 MREIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGP 80
Cdd:COG5023    1 MREIITLQVGQCGNQIGNAFWETLCLEHGIGPDGTLLDSSDEGDERFDVFFYEASDGKFVPRAILVDLEPGVIDQVRNGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  81 YGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:COG5023   81 YGSLFHPENIIFGKEGAGNNWARGHYTVGKEIIDDVMDMIRREADGCDGLQGFLLLHSLGGGTGSGLGSLLLERLREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 161 DRMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITCCL 240
Cdd:COG5023  161 KKIKLTFSVFPAPKVSDVVVEPYNSVLTLHRLLENSDCTFVVDNEALYDICRRNLRIQNPSYDDLNQLISTVMSSVTTSL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 241 RFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRGR 320
Cdd:COG5023  241 RFPGYLNVDLRSIQTNLVPYPRLHFPLVSYTPFTSDGSAAHEKNSVSEVTNQLFDPKNQMVSCDPRKGRYMAVCLLFRGD 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 321 MSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPP---KGLKMSATFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHW 397
Cdd:COG5023  321 VDPRDVSRAVTRVQSKRTIQFVEWCPTGFKVAICKRPPsepAEVDVSGCMLSNTTSIAEAFKRIDDQFDLMFKKRAFLHW 400
                        410       420       430
                 ....*....|....*....|....*....|..
gi 159471706 398 YTGEGMDEMEFTEAESNMNDLVSEYQQYQDAS 429
Cdd:COG5023  401 YVGEGMEEGEFSEAREDVADLEEEYEAAEQDS 432
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-424 1.68e-161

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  Cd Length: 434  Bit Score: 467.02  E-value: 1.68e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   2 REIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINV--YFNEATGGRYVPRAILMDLEPGTMDSVRSG 79
Cdd:cd02186    1 REIISIHVGQAGVQIGNACWELFCLEHGIQPDGQMPSDKTIGGDDDNFntFFSETGSGKYVPRAVFVDLEPTVIDEIRTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  80 PYGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEY 159
Cdd:cd02186   81 PYRQLFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 160 PDRMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITCC 239
Cdd:cd02186  161 GKKSKLEFSIYPSPQVSTSVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 240 LRFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRG 319
Cdd:cd02186  241 LRFDGALNVDLNEFQTNLVPYPRIHFPLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 320 RMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPPKGL--------KMSATFIGNSTAIQEMFKRVSEQFTAMFRR 391
Cdd:cd02186  321 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVpgsdlakvDRSVCMLANSTAIAEAFQRLDHKFDLLYSK 400
                        410       420       430
                 ....*....|....*....|....*....|...
gi 159471706 392 KAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 424
Cdd:cd02186  401 RAFVHWYVGEGMEEGEFSEAREDLAALEKDYEE 433
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
3-424 4.83e-161

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  Cd Length: 387  Bit Score: 463.98  E-value: 4.83e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   3 EIVHIQGGQCGNQIGAKFWEVVsdehgidptgtyhgdsdlqlerinvyfneatggryvpRAILMDLEPGTMDSVRSGPYG 82
Cdd:cd06059    1 EIITIQVGQCGNQIGDRFWELA-------------------------------------RAVLVDMEEGVINEVLKGPLG 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  83 QIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDR 162
Cdd:cd06059   44 QLFDPNQFVTGVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYPKV 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 163 MMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFR---TLKLTTPTFGDLNHLISAVMSGITCC 239
Cdd:cd06059  124 YRFTFSVFPSPDDDNVITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLTSS 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 240 LRFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRG 319
Cdd:cd06059  204 LRFEGSLNVDLNEITTNLVPFPRLHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDNQLVGCDPRHGTYLACALLLRG 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 320 RMST-KEVDEQMLNVQNKNSsyFVEWIPNNVKSSVCDIPPKGLKMSATFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHWY 398
Cdd:cd06059  284 KVFSlSDVRRNIDRIKPKLK--FISWNPDGFKVGLCSVPPVGQKYSLLFLSNNTSIASTFERLIERFDKLYKRKAFLHHY 361
                        410       420
                 ....*....|....*....|....*.
gi 159471706 399 TGEGMDEMEFTEAESNMNDLVSEYQQ 424
Cdd:cd06059  362 TGEGMEEGDFSEARESLANLIQEYQE 387
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-424 2.45e-139

tubulin alpha chain; Provisional


Pssm-ID: 185562  Cd Length: 448  Bit Score: 411.02  E-value: 2.45e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   1 MREIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLE--RINVYFNEATGGRYVPRAILMDLEPGTMDSVRS 78
Cdd:PTZ00335   1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEddAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  79 GPYGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREE 158
Cdd:PTZ00335  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 159 YPDRMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITC 238
Cdd:PTZ00335 161 YGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 239 CLRFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFR 318
Cdd:PTZ00335 241 SLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 319 GRMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSV-----CDIPPKGL---KMSATFIGNSTAIQEMFKRVSEQFTAMFR 390
Cdd:PTZ00335 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGInyqppTVVPGGDLakvQRAVCMISNSTAIAEVFSRIDHKFDLMYA 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 159471706 391 RKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 424
Cdd:PTZ00335 401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEE 434
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-424 9.27e-132

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 391.48  E-value: 9.27e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   1 MREIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQL--ERINVYFNEATGGRYVPRAILMDLEPGTMDSVRS 78
Cdd:PLN00221   1 MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGgdDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  79 GPYGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREE 158
Cdd:PLN00221  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 159 YPDRMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITC 238
Cdd:PLN00221 161 YGKKSKLGFTVYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 239 CLRFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFR 318
Cdd:PLN00221 241 SLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 319 GRMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPPK--------GLKMSATFIGNSTAIQEMFKRVSEQFTAMFR 390
Cdd:PLN00221 321 GDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTvvpggdlaKVQRAVCMISNSTAVAEVFSRIDHKFDLMYA 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 159471706 391 RKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 424
Cdd:PLN00221 401 KRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEE 434
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
3-371 1.31e-128

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  Cd Length: 332  Bit Score: 379.06  E-value: 1.31e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   3 EIVHIQGGQCGNQIGAKFWEVvsdehgidptgtyhgdsdlqlerinvyfneatggryvprAILMDLEPGTMDSVRSGPYG 82
Cdd:cd00286    1 EIVTIQVGQCGNQIGAAFWEQ---------------------------------------AVLVDLEPAVLDELLSGPLR 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  83 QIFRPDNFVFGQ--TGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:cd00286   42 QLFHPENIILIQkyHGAGNNWAKGHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDEYP 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 161 DRMMLTFSVVPSPKVSdTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITCCL 240
Cdd:cd00286  122 NRLVVTFSILPGPDEG-VIVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTEAL 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 241 RFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRGR 320
Cdd:cd00286  201 RFEGSLNVDLRELAENLVPLPRGHFLMLGYAPLDSATSATPRSLRVKELTRRAFLPANLLVGCDPDHGEAIAALLVIRGP 280
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 159471706 321 --MSTKEVDEQMLNVQNKNSSYFvEWIPNNVKSSVCDIPPKGLKMSATFIGNS 371
Cdd:cd00286  281 pdLSSKEVERAIARVKETLGHLF-SWSPAGVKTGISPKPPAEGEVSVLALLNS 332
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
2-422 1.67e-128

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  Cd Length: 430  Bit Score: 382.27  E-value: 1.67e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   2 REIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGPY 81
Cdd:cd02188    1 REIITLQVGQCGNQIGSEFWKQLCSEHGISPDGSLEDFATDGNDRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNSPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  82 GQIFRPDNFVFGQ--TGAGNNWAKGhYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEY 159
Cdd:cd02188   81 KNLFNPENIYLSKegGGAGNNWASG-YSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 160 PDRMMLTFSVVPSPK-VSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITC 238
Cdd:cd02188  160 PKKLIQTYSVFPNQEeSSDVVVQPYNSILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 239 CLRFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTS-RGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALF 317
Cdd:cd02188  240 TLRFPGYMNNDLVSLISSLIPTPRLHFLMTSYTPLTSdQVASSVRKTTVLDVMRRLLQPKNRMVSTSTKNGCYISILNII 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 318 RGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPPKGL---KMSATFIGNSTAIQEMFKRVSEQFTAMFRRKAF 394
Cdd:cd02188  320 QGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSKKSPYVQtahRVSGLMLANHTSISSLFEKILSQYDKLRKRNAF 399
                        410       420       430
                 ....*....|....*....|....*....|.
gi 159471706 395 LHWYTGEGMDE---MEFTEAESNMNDLVSEY 422
Cdd:cd02188  400 LENYRKEDMFQdnlEEFDESREVVQSLIDEY 430
PLN00222 PLN00222
tubulin gamma chain; Provisional
2-423 2.49e-103

tubulin gamma chain; Provisional


Pssm-ID: 215108  Cd Length: 454  Bit Score: 318.71  E-value: 2.49e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   2 REIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGPY 81
Cdd:PLN00222   3 REIITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGGDRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNSEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  82 GQIFRPDNFVFGQTG--AGNNWAKGhYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEY 159
Cdd:PLN00222  83 RNLYNHENIFVSDHGggAGNNWASG-YHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 160 PDRMMLTFSVVPS-PKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITC 238
Cdd:PLN00222 162 SKKLVQTYSVFPNqMETSDVVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 239 CLRFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPL-TSRGSQQYRALTVPELTQQMWDAKNMMCAADPR-----HGRYLT 312
Cdd:PLN00222 242 TLRYPGYMNNDLVGLLASLIPTPRCHFLMTGYTPLtVERQANVIRKTTVLDVMRRLLQTKNIMVSSYARtkeasQAKYIS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 313 ASALFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPP---KGLKMSATFIGNSTAIQEMFKRVSEQFTAMF 389
Cdd:PLN00222 322 ILNIIQGEVDPTQVHKSLQRIRERKLANFIEWGPASIQVALSRKSPyvqTAHRVSGLMLANHTSIRHLFSKCLSQYDKLR 401
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 159471706 390 RRKAFLHWYTGEGM----DEMEFTEAESNMNDLVSEYQ 423
Cdd:PLN00222 402 KKQAFLDNYRKFPMfadnDLSEFDESREIVESLVDEYK 439
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
2-425 1.26e-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  Cd Length: 449  Bit Score: 308.78  E-value: 1.26e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   2 REIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERiNV--YFNEATGGRYVP------RAILMDLEPGTM 73
Cdd:cd02190    1 REIITVQVGQCGNQIGCRFWDLALREHAAYNKDGVYDDSMSSFFR-NVdtRSGDPGDDGGSPikslkaRAVLIDMEEGVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  74 DSVRSGPYGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLIS 153
Cdd:cd02190   80 NELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGPQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSGLGSYILE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 154 KIREEYPDRMMLTFSVVPSpKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPT------------ 221
Cdd:cd02190  160 LLEDEFPDVYRFVTSVFPS-GDDDVITSPYNSVLALRELTEHADCVLPVENQALMDIVNKIKSSKDKGktgvlaainssg 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 222 ----------FGDLNHLISAVMSGITCCLRFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQ 291
Cdd:cd02190  239 ggqkkgkkkpFDDMNNIVANLLLNLTSSMRFEGSLNVDLNEITTNLVPFPRLHFLLSSLSPLYALADVRLPPRRLDQMFS 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 292 QMWDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEqmlNVQN-KNSSYFVEWIPNNVKSSVCDIPPKGLKMSATFIGN 370
Cdd:cd02190  319 DAFSRDHQLLKADPKHGLYLACALLVRGNVSISDLRR---NIDRlKRQLKFVSWNQDGWKIGLCSVPPVGQPYSLLCLAN 395
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 159471706 371 STAIQEMFKRVSEQFTAMFRRKAFLHWYTgEGMDEMEFTEAESNMNDLVSEYQQY 425
Cdd:cd02190  396 NTCIKPTFTEMHERFDKLYKRKAHLHHYT-QYMEQDDFDEALESLLDLIEEYKDL 449
PTZ00387 PTZ00387
epsilon tubulin; Provisional
1-428 1.65e-91

epsilon tubulin; Provisional


Pssm-ID: 240395  Cd Length: 465  Bit Score: 288.16  E-value: 1.65e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   1 MREIVHIQGGQCGNQIGAKFWEVVSDEH-GIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSG 79
Cdd:PTZ00387   1 PREIVTVQVGQCGNQLGHRFWDVALKEHkKINANPQYDDARDSFFENVSENVNRPGKENLKARAVLVDMEEGVLNQILKS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  80 PYGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEY 159
Cdd:PTZ00387  81 PLGDLFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 160 PDRMMLTFSVVPSpKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKL---------------------T 218
Cdd:PTZ00387 161 PHVFRFCPVVFPS-AVDDVITSPYNSFFALRELIEHADCVLPLDNDALANIADSALSRkkkklakgnikrgpqphkysvA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 219 TPT------FGDLNHLISAVMSGITCCLRFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQ 292
Cdd:PTZ00387 240 KPTetkklpYDKMNNIVAQLLSNLTSSMRFEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGPRRLDQMFKD 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 293 MWDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVqnKNSSYFVEWIPNNVKSSVCDIPPKGLKMSATFIGNST 372
Cdd:PTZ00387 320 CLDPDHQMVAATPEAGKYLATALIVRGPQNVSDVTRNILRL--KEQLNMIYWNEDGFKTGLCNVSPLGQPYSLLCLANNC 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 159471706 373 AIQEMFKRVSEQFTAMFRRKAFLHWYTgEGMDEMEFTEAESNMNDLVSEYQQYQDA 428
Cdd:PTZ00387 398 CIRNKFESMLERFNKLYKRKSHVHHYT-EYLEQAYFDETLETIQNLIDDYAYLQTA 452
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
4-424 1.93e-69

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  Cd Length: 433  Bit Score: 229.46  E-value: 1.93e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   4 IVHIQGGQCGNQIGAKFWEVVSDEhgidptGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGPYGQ 83
Cdd:cd02189    2 IVTVQVGQCGNQLGDELFDTLADE------ADSSASEGDQNSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRARSG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  84 --IFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPD 161
Cdd:cd02189   76 awSYDPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEYPK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 162 RMMLTFSVVPSpKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTP-TFGDLNHLISAVMSGI---- 236
Cdd:cd02189  156 AYLLNTVVWPY-SSGEVPVQNYNTLLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVllps 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 237 -TCCLRFPGQLNaDLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELtqqMWDAKNMMCAADP---------- 305
Cdd:cd02189  235 sSPTSPSPLRRC-PLGDLLEHLCPHPAYKLLTLRSLPQMPEPSRAFSTYTWPSL---LKRLRQMLITGAKleegidwqll 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706 306 ------RHGRYLTASALFRG--RMSTKEVDEQMLnvqnKNSSYFVEWIPNNVKSSVCDIPPKGLKMSATFIGNSTAIQEM 377
Cdd:cd02189  311 dtsgshNPNKSLAALLVLRGkdAMKVHSADLSAF----KDPVLYSPWVPNPFNVSVSPRPFNGYEKSVTLLSNSQNIVGP 386
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 159471706 378 FKRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQ 424
Cdd:cd02189  387 LDSLLEKAWQMFKAGAYLHQYEKYGVEEEDFLDAFATLEQIIAAYKS 433
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
47-244 1.77e-60

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  Cd Length: 192  Bit Score: 198.48  E-value: 1.77e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706    47 INVYFNEatgGRYVPRAILMDLEPGTMDSVRSGPYGQIFRPDNFVFGQTGAGNNWAKGHYT-----EGAELIDSVLDVVR 121
Cdd:smart00864   1 KIKVFGV---GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   122 KEAESCDclqGFQVCHslgggtgsgmgtlLISKIREEYPDrmmLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMV 201
Cdd:smart00864  78 EELEGAD---GVFITAgmgggt-gtgaapVIAEIAKEYGI---LTVAVVTKPFSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 159471706   202 LDNEALYDICFRTLKLtTPTFGDLNHLISAVMSGITCCLRFPG 244
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
3-211 1.24e-59

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: 306575  Cd Length: 190  Bit Score: 196.28  E-value: 1.24e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706    3 EIVHIQGGQCGNQIGAKFWEVVSDEHGIDptgtyhgdsdlqleRINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGPYg 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCKEHGID--------------SLNVFFSESGSVEFIPRSIAIDTDPQALNEIKAGSL- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   83 qifrPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDR 162
Cdd:pfam00091  66 ----PNKIFLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGA 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 159471706  163 MMLTFSVVPSpKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDIC 211
Cdd:pfam00091 142 LTVAVVTFPF-GFSEGVVRPYNAILGLKELREHSDSVIVIDNDALLDIC 189
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
261-382 8.58e-57

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: 309177  Cd Length: 125  Bit Score: 186.27  E-value: 8.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706  261 PRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSY 340
Cdd:pfam03953   1 PRLHFLLTSYAPLTSDNKASHEKTSVLEVTRQLFDPKNQMVSCDPRNGKYMACALLYRGDVDPKEVNKAIQRIKEKRSAQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 159471706  341 FVEWIPNNVKSSVCDIPPKGLKM---SATFIGNSTAIQEMFKRVS 382
Cdd:pfam03953  81 FVEWCPTGIKVGICSVSPYVVPGskvSGLMLANTTSIAELFQRLL 125
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
246-383 2.83e-25

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  Cd Length: 120  Bit Score: 100.70  E-value: 2.83e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159471706   246 LNADLRKLAVNLIPFPrlhFFMVGFTPLTSrgsqQYRALTVPELTQ--QMWDAKNMMCAADPRHgrYLTASAlfrgRMST 323
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASG----ENRALEAAELAIssPLLEDSNIMGAKGVLV--NITGGP----DLTL 67
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 159471706   324 KEVDEQMLNVQNKNSS-YFVEWIPNNVKSsvcdippkgLKMSATFIGN-STAIQEMFKRVSE 383
Cdd:smart00865  68 KEVNEAMERIREKADPdAFIIWGPVIDEE---------LGGDEIRVTViATGIGSLFKRLSE 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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