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Conserved domains on  [gi|15233429|ref|NP_193821|]
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tubulin beta-9 chain [Arabidopsis thaliana]

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
1-431 0e+00

tubulin beta chain; Provisional


:

Pssm-ID: 215107  Cd Length: 447  Bit Score: 980.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    1 MREILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGP 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   81 FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  161 DRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTCCL 240
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGK 320
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  321 MSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|.
gi 15233429  401 EGMDEMEFTEAESNMNDLVAEYQQYQDATVG 431
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATAD 431
 
Name Accession Description Interval E-value
PLN00220 PLN00220
tubulin beta chain; Provisional
1-431 0e+00

tubulin beta chain; Provisional


Pssm-ID: 215107  Cd Length: 447  Bit Score: 980.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    1 MREILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGP 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   81 FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  161 DRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTCCL 240
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGK 320
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  321 MSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|.
gi 15233429  401 EGMDEMEFTEAESNMNDLVAEYQQYQDATVG 431
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATAD 431
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: 877.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   2 REILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGPF 81
Cdd:cd02187   1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  82 GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPD 161
Cdd:cd02187  81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 162 RMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTCCLR 241
Cdd:cd02187 161 RIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLR 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 242 FPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGKM 321
Cdd:cd02187 241 FPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRI 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 322 STKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGE 401
Cdd:cd02187 321 STKEVDEQMSKVQNKNSSYFVEWIPNNVKTSVCDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGE 400
                       410       420
                ....*....|....*....|....*
gi 15233429 402 GMDEMEFTEAESNMNDLVAEYQQYQ 426
Cdd:cd02187 401 GMDEMEFTEAESNLNDLISEYQQYQ 425
COG5023 COG5023
Tubulin [Cytoskeleton];
1-430 0e+00

Tubulin [Cytoskeleton];


Pssm-ID: 227356  Cd Length: 443  Bit Score: 689.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   1 MREILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGP 80
Cdd:COG5023   1 MREIITLQVGQCGNQIGNAFWETLCLEHGIGPDGTLLDSSDEGDERFDVFFYEASDGKFVPRAILVDLEPGVIDQVRNGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  81 FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:COG5023  81 YGSLFHPENIIFGKEGAGNNWARGHYTVGKEIIDDVMDMIRREADGCDGLQGFLLLHSLGGGTGSGLGSLLLERLREEYP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 161 DRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTCCL 240
Cdd:COG5023 161 KKIKLTFSVFPAPKVSDVVVEPYNSVLTLHRLLENSDCTFVVDNEALYDICRRNLRIQNPSYDDLNQLISTVMSSVTTSL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGK 320
Cdd:COG5023 241 RFPGYLNVDLRSIQTNLVPYPRLHFPLVSYTPFTSDGSAAHEKNSVSEVTNQLFDPKNQMVSCDPRKGRYMAVCLLFRGD 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 321 MSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAP---TGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHW 397
Cdd:COG5023 321 VDPRDVSRAVTRVQSKRTIQFVEWCPTGFKVAICKRPPsepAEVDVSGCMLSNTTSIAEAFKRIDDQFDLMFKKRAFLHW 400
                       410       420       430
                ....*....|....*....|....*....|...
gi 15233429 398 YTGEGMDEMEFTEAESNMNDLVAEYQQYQDATV 430
Cdd:COG5023 401 YVGEGMEEGEFSEAREDVADLEEEYEAAEQDSY 433
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
3-211 5.42e-63

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: 205.14  E-value: 5.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429     3 EILHIQGGQCGNQIGAKFWEVICGEHGIDqtgqscgdtdlqleRINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGPFg 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCKEHGID--------------SLNVFFSESGSVEFIPRSIAIDTDPQALNEIKAGSL- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    83 qifrPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDR 162
Cdd:pfam00091  66 ----PNKIFLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGA 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 15233429   163 MMMTFSVFPSpKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDIC 211
Cdd:pfam00091 142 LTVAVVTFPF-GFSEGVVRPYNAILGLKELREHSDSVIVIDNDALLDIC 189
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
47-244 3.66e-58

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: 192.32  E-value: 3.66e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429     47 INVYFNEasgGKYVPRAVLMDLEPGTMDSLRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYT-----EGAELIDSVLDVVR 121
Cdd:smart00864   1 KIKVFGV---GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    122 KEAENCDclqGFQVCHslgggtgsgmgtlLISKIREEYPDRmMMTFSVFpsPKVSDTVVEPYNATLSVHQLVENADECMV 201
Cdd:smart00864  78 EELEGAD---GVFITAgmgggt-gtgaapVIAEIAKEYGIL-TVAVVTK--PFSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 15233429    202 LDNEALYDICFRTLKLaNPTFGDLNHLISATMSGVTCCLRFPG 244
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
 
Name Accession Description Interval E-value
PLN00220 PLN00220
tubulin beta chain; Provisional
1-431 0e+00

tubulin beta chain; Provisional


Pssm-ID: 215107  Cd Length: 447  Bit Score: 980.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    1 MREILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGP 80
Cdd:PLN00220   1 MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   81 FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:PLN00220  81 YGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  161 DRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTCCL 240
Cdd:PLN00220 161 DRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGK 320
Cdd:PLN00220 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  321 MSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
Cdd:PLN00220 321 MSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|.
gi 15233429  401 EGMDEMEFTEAESNMNDLVAEYQQYQDATVG 431
Cdd:PLN00220 401 EGMDEMEFTEAESNMNDLVSEYQQYQDATAD 431
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-430 0e+00

tubulin beta chain; Provisional


Pssm-ID: 240228  Cd Length: 445  Bit Score: 914.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    1 MREILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGP 80
Cdd:PTZ00010   1 MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSVRAGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   81 FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:PTZ00010  81 YGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  161 DRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTCCL 240
Cdd:PTZ00010 161 DRIMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGK 320
Cdd:PTZ00010 241 RFPGQLNSDLRKLAVNLVPFPRLHFFMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  321 MSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
Cdd:PTZ00010 321 MSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSVCDIPPKGLKMSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTG 400
                        410       420       430
                 ....*....|....*....|....*....|
gi 15233429  401 EGMDEMEFTEAESNMNDLVAEYQQYQDATV 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: 877.28  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   2 REILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGPF 81
Cdd:cd02187   1 REIIHIQIGQCGNQIGAKFWETISKEHGIDPDGTYKGDSDLQLERINVYFNEASGGKYVPRAVLVDLEPGTIDSVRSGPY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  82 GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPD 161
Cdd:cd02187  81 GQLFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 162 RMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTCCLR 241
Cdd:cd02187 161 RIMSTFSVLPSPKVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLR 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 242 FPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGKM 321
Cdd:cd02187 241 FPGQLNSDLRKLATNLVPFPRLHFLTPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRI 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 322 STKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGE 401
Cdd:cd02187 321 STKEVDEQMSKVQNKNSSYFVEWIPNNVKTSVCDIPPRGLKMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGE 400
                       410       420
                ....*....|....*....|....*
gi 15233429 402 GMDEMEFTEAESNMNDLVAEYQQYQ 426
Cdd:cd02187 401 GMDEMEFTEAESNLNDLISEYQQYQ 425
COG5023 COG5023
Tubulin [Cytoskeleton];
1-430 0e+00

Tubulin [Cytoskeleton];


Pssm-ID: 227356  Cd Length: 443  Bit Score: 689.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   1 MREILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGP 80
Cdd:COG5023   1 MREIITLQVGQCGNQIGNAFWETLCLEHGIGPDGTLLDSSDEGDERFDVFFYEASDGKFVPRAILVDLEPGVIDQVRNGP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  81 FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:COG5023  81 YGSLFHPENIIFGKEGAGNNWARGHYTVGKEIIDDVMDMIRREADGCDGLQGFLLLHSLGGGTGSGLGSLLLERLREEYP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 161 DRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTCCL 240
Cdd:COG5023 161 KKIKLTFSVFPAPKVSDVVVEPYNSVLTLHRLLENSDCTFVVDNEALYDICRRNLRIQNPSYDDLNQLISTVMSSVTTSL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGK 320
Cdd:COG5023 241 RFPGYLNVDLRSIQTNLVPYPRLHFPLVSYTPFTSDGSAAHEKNSVSEVTNQLFDPKNQMVSCDPRKGRYMAVCLLFRGD 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 321 MSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAP---TGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHW 397
Cdd:COG5023 321 VDPRDVSRAVTRVQSKRTIQFVEWCPTGFKVAICKRPPsepAEVDVSGCMLSNTTSIAEAFKRIDDQFDLMFKKRAFLHW 400
                       410       420       430
                ....*....|....*....|....*....|...
gi 15233429 398 YTGEGMDEMEFTEAESNMNDLVAEYQQYQDATV 430
Cdd:COG5023 401 YVGEGMEEGEFSEAREDVADLEEEYEAAEQDSY 433
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
2-424 9.41e-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: 465.09  E-value: 9.41e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   2 REILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINV--YFNEASGGKYVPRAVLMDLEPGTMDSLRSG 79
Cdd:cd02186   1 REIISIHVGQAGVQIGNACWELFCLEHGIQPDGQMPSDKTIGGDDDNFntFFSETGSGKYVPRAVFVDLEPTVIDEIRTG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  80 PFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEY 159
Cdd:cd02186  81 PYRQLFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 160 PDRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTCC 239
Cdd:cd02186 161 GKKSKLEFSIYPSPQVSTSVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTAS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 240 LRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRG 319
Cdd:cd02186 241 LRFDGALNVDLNEFQTNLVPYPRIHFPLVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRG 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 320 KMSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAPT---GLKMASTF-----IGNSTSIQEMFRRVSEQFTAMFRR 391
Cdd:cd02186 321 DVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTvvpGSDLAKVDrsvcmLANSTAIAEAFQRLDHKFDLLYSK 400
                       410       420       430
                ....*....|....*....|....*....|...
gi 15233429 392 KAFLHWYTGEGMDEMEFTEAESNMNDLVAEYQQ 424
Cdd:cd02186 401 RAFVHWYVGEGMEEGEFSEAREDLAALEKDYEE 433
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
3-424 2.79e-160

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: 462.06  E-value: 2.79e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   3 EILHIQGGQCGNQIGAKFWEVIcgehgidqtgqscgdtdlqlerinvyfneasggkyvpRAVLMDLEPGTMDSLRSGPFG 82
Cdd:cd06059   1 EIITIQVGQCGNQIGDRFWELA-------------------------------------RAVLVDMEEGVINEVLKGPLG 43
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  83 QIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDR 162
Cdd:cd06059  44 QLFDPNQFVTGVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYPKV 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 163 MMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFR---TLKLANPTFGDLNHLISATMSGVTCC 239
Cdd:cd06059 124 YRFTFSVFPSPDDDNVITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLTSS 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 240 LRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRG 319
Cdd:cd06059 204 LRFEGSLNVDLNEITTNLVPFPRLHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDNQLVGCDPRHGTYLACALLLRG 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 320 KMST-KEVDEQMMNVQNKNSsyFVEWIPNNVKSSVCDIAPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWY 398
Cdd:cd06059 284 KVFSlSDVRRNIDRIKPKLK--FISWNPDGFKVGLCSVPPVGQKYSLLFLSNNTSIASTFERLIERFDKLYKRKAFLHHY 361
                       410       420
                ....*....|....*....|....*.
gi 15233429 399 TGEGMDEMEFTEAESNMNDLVAEYQQ 424
Cdd:cd06059 362 TGEGMEEGDFSEARESLANLIQEYQE 387
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-428 1.19e-139

tubulin alpha chain; Provisional


Pssm-ID: 185562  Cd Length: 448  Bit Score: 411.79  E-value: 1.19e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    1 MREILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLE--RINVYFNEASGGKYVPRAVLMDLEPGTMDSLRS 78
Cdd:PTZ00335   1 MREVISIHIGQAGIQVGNACWELFCLEHGIQPDGQMPSDKNIGVEddAFNTFFSETGAGKHVPRCVFLDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   79 GPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREE 158
Cdd:PTZ00335  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  159 YPDRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTC 238
Cdd:PTZ00335 161 YGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  239 CLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFR 318
Cdd:PTZ00335 241 SLRFDGALNVDLTEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  319 GKMSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAPT---GLKMAST-----FIGNSTSIQEMFRRVSEQFTAMFR 390
Cdd:PTZ00335 321 GDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKCGINYQPPTvvpGGDLAKVqravcMISNSTAIAEVFSRIDHKFDLMYA 400
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15233429  391 RKAFLHWYTGEGMDEMEFTEAEsnmNDLVAEYQQYQDA 428
Cdd:PTZ00335 401 KRAFVHWYVGEGMEEGEFSEAR---EDLAALEKDYEEV 435
PLN00221 PLN00221
tubulin alpha chain; Provisional
1-424 1.73e-133

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 396.10  E-value: 1.73e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    1 MREILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQL--ERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRS 78
Cdd:PLN00221   1 MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGgdDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   79 GPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREE 158
Cdd:PLN00221  81 GTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  159 YPDRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTC 238
Cdd:PLN00221 161 YGKKSKLGFTVYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  239 CLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFR 318
Cdd:PLN00221 241 SLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  319 GKMSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAPT--------GLKMASTFIGNSTSIQEMFRRVSEQFTAMFR 390
Cdd:PLN00221 321 GDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTvvpggdlaKVQRAVCMISNSTAVAEVFSRIDHKFDLMYA 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 15233429  391 RKAFLHWYTGEGMDEMEFTEAESNMNDLVAEYQQ 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 9.45e-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: 377.13  E-value: 9.45e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   3 EILHIQGGQCGNQIGAKFWEVicgehgidqtgqscgdtdlqlerinvyfneasggkyvprAVLMDLEPGTMDSLRSGPFG 82
Cdd:cd00286   1 EIVTIQVGQCGNQIGAAFWEQ---------------------------------------AVLVDLEPAVLDELLSGPLR 41
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  83 QIFRPDNFVFGQS--GAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYP 160
Cdd:cd00286  42 QLFHPENIILIQKyhGAGNNWAKGHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDEYP 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 161 DRMMMTFSVFPSPKVSdTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTCCL 240
Cdd:cd00286 122 NRLVVTFSILPGPDEG-VIVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTEAL 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 241 RFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGK 320
Cdd:cd00286 201 RFEGSLNVDLRELAENLVPLPRGHFLMLGYAPLDSATSATPRSLRVKELTRRAFLPANLLVGCDPDHGEAIAALLVIRGP 280
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 15233429 321 --MSTKEVDEQMMNVQNKNSSYFvEWIPNNVKSSVCDIAPTGLKMASTFIGNS 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 1.25e-127

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: 380.35  E-value: 1.25e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   2 REILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGPF 81
Cdd:cd02188   1 REIITLQVGQCGNQIGSEFWKQLCSEHGISPDGSLEDFATDGNDRKDVFFYQADDEHYIPRAILLDLEPRVINSIQNSPY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  82 GQIFRPDNFVFGQ--SGAGNNWAKGhYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEY 159
Cdd:cd02188  81 KNLFNPENIYLSKegGGAGNNWASG-YSQGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 160 PDRMMMTFSVFPSPK-VSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTC 238
Cdd:cd02188 160 PKKLIQTYSVFPNQEeSSDVVVQPYNSILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTS 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 239 CLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTS-RGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVF 317
Cdd:cd02188 240 TLRFPGYMNNDLVSLISSLIPTPRLHFLMTSYTPLTSdQVASSVRKTTVLDVMRRLLQPKNRMVSTSTKNGCYISILNII 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 318 RGKMSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAPTgLKMASTFIG----NSTSIQEMFRRVSEQFTAMFRRKA 393
Cdd:cd02188 320 QGEVDPTQVHKSLQRIRERKLANFIPWGPASIQVALSKKSPY-VQTAHRVSGlmlaNHTSISSLFEKILSQYDKLRKRNA 398
                       410       420       430
                ....*....|....*....|....*....|..
gi 15233429 394 FLHWYTGEGMDE---MEFTEAESNMNDLVAEY 422
Cdd:cd02188 399 FLENYRKEDMFQdnlEEFDESREVVQSLIDEY 430
PLN00222 PLN00222
tubulin gamma chain; Provisional
2-423 3.66e-103

tubulin gamma chain; Provisional


Pssm-ID: 215108  Cd Length: 454  Bit Score: 318.33  E-value: 3.66e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    2 REILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGPF 81
Cdd:PLN00222   3 REIITLQVGQCGNQIGMEFWKQLCLEHGISKDGILEDFATQGGDRKDVFFYQADDEHYIPRALLIDLEPRVINGIQNSEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   82 GQIFRPDNFVFGQSG--AGNNWAKGhYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEY 159
Cdd:PLN00222  83 RNLYNHENIFVSDHGggAGNNWASG-YHQGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  160 PDRMMMTFSVFPS-PKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTC 238
Cdd:PLN00222 162 SKKLVQTYSVFPNqMETSDVVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  239 CLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPL-TSRGSQQYSALSVPELTQQMWDAKNMMCAADPR-----HGRYLT 312
Cdd:PLN00222 242 TLRYPGYMNNDLVGLLASLIPTPRCHFLMTGYTPLtVERQANVIRKTTVLDVMRRLLQTKNIMVSSYARtkeasQAKYIS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  313 ASAVFRGKMSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAP---TGLKMASTFIGNSTSIQEMFRRVSEQFTAMF 389
Cdd:PLN00222 322 ILNIIQGEVDPTQVHKSLQRIRERKLANFIEWGPASIQVALSRKSPyvqTAHRVSGLMLANHTSIRHLFSKCLSQYDKLR 401
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15233429  390 RRKAFLHWYTGEGM----DEMEFTEAESNMNDLVAEYQ 423
Cdd:PLN00222 402 KKQAFLDNYRKFPMfadnDLSEFDESREIVESLVDEYK 439
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
2-425 7.65e-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: 306.86  E-value: 7.65e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   2 REILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGK-YVP------RAVLMDLEPGTMD 74
Cdd:cd02190   1 REIITVQVGQCGNQIGCRFWDLALREHAAYNKDGVYDDSMSSFFRNVDTRSGDPGDDgGSPikslkaRAVLIDMEEGVVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  75 SLRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISK 154
Cdd:cd02190  81 ELLKGPLGDLFDETQLVTDVSGAGNNWAHGYHEYGPQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSGLGSYILEL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 155 IREEYPDRMMMTFSVFPSpKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPT------------- 221
Cdd:cd02190 161 LEDEFPDVYRFVTSVFPS-GDDDVITSPYNSVLALRELTEHADCVLPVENQALMDIVNKIKSSKDKGktgvlaainssgg 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 222 ---------FGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQ 292
Cdd:cd02190 240 gqkkgkkkpFDDMNNIVANLLLNLTSSMRFEGSLNVDLNEITTNLVPFPRLHFLLSSLSPLYALADVRLPPRRLDQMFSD 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 293 MWDAKNMMCAADPRHGRYLTASAVFRGKMSTKEVDEqmmNVQN-KNSSYFVEWIPNNVKSSVCDIAPTGLKMASTFIGNS 371
Cdd:cd02190 320 AFSRDHQLLKADPKHGLYLACALLVRGNVSISDLRR---NIDRlKRQLKFVSWNQDGWKIGLCSVPPVGQPYSLLCLANN 396
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 15233429 372 TSIQEMFRRVSEQFTAMFRRKAFLHWYTgEGMDEMEFTEAESNMNDLVAEYQQY 425
Cdd:cd02190 397 TCIKPTFTEMHERFDKLYKRKAHLHHYT-QYMEQDDFDEALESLLDLIEEYKDL 449
PTZ00387 PTZ00387
epsilon tubulin; Provisional
1-428 1.47e-90

epsilon tubulin; Provisional


Pssm-ID: 240395  Cd Length: 465  Bit Score: 285.85  E-value: 1.47e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    1 MREILHIQGGQCGNQIGAKFWEVICGEH-GIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSG 79
Cdd:PTZ00387   1 PREIVTVQVGQCGNQLGHRFWDVALKEHkKINANPQYDDARDSFFENVSENVNRPGKENLKARAVLVDMEEGVLNQILKS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   80 PFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEY 159
Cdd:PTZ00387  81 PLGDLFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  160 PDRMMMTFSVFPSpKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKL---------------------A 218
Cdd:PTZ00387 161 PHVFRFCPVVFPS-AVDDVITSPYNSFFALRELIEHADCVLPLDNDALANIADSALSRkkkklakgnikrgpqphkysvA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  219 NPT------FGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQ 292
Cdd:PTZ00387 240 KPTetkklpYDKMNNIVAQLLSNLTSSMRFEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGPRRLDQMFKD 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  293 MWDAKNMMCAADPRHGRYLTASAVFRGKMSTKEVDEQMMNVqnKNSSYFVEWIPNNVKSSVCDIAPTGLKMASTFIGNST 372
Cdd:PTZ00387 320 CLDPDHQMVAATPEAGKYLATALIVRGPQNVSDVTRNILRL--KEQLNMIYWNEDGFKTGLCNVSPLGQPYSLLCLANNC 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15233429  373 SIQEMFRRVSEQFTAMFRRKAFLHWYTgEGMDEMEFTEAESNMNDLVAEYQQYQDA 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 1.05e-72

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: 238.32  E-value: 1.05e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   4 ILHIQGGQCGNQIGAKFWEVICGEhgidqtGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGPFGQ 83
Cdd:cd02189   2 IVTVQVGQCGNQLGDELFDTLADE------ADSSASEGDQNSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRARSG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429  84 --IFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPD 161
Cdd:cd02189  76 awSYDPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEYPK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 162 RMMMTFSVFPSpKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANP-TFGDLNHLISATMSGV---- 236
Cdd:cd02189 156 AYLLNTVVWPY-SSGEVPVQNYNTLLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVllps 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 237 -TCCLRFPGQLNSdLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELtqqMWDAKNMMCAADP---------- 305
Cdd:cd02189 235 sSPTSPSPLRRCP-LGDLLEHLCPHPAYKLLTLRSLPQMPEPSRAFSTYTWPSL---LKRLRQMLITGAKleegidwqll 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429 306 ------RHGRYLTASAVFRGKMSTKEVDEQMMNVqnKNSSYFVEWIPNNVKSSVCDIAPTGLKMASTFIGNSTSIQEMFR 379
Cdd:cd02189 311 dtsgshNPNKSLAALLVLRGKDAMKVHSADLSAF--KDPVLYSPWVPNPFNVSVSPRPFNGYEKSVTLLSNSQNIVGPLD 388
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 15233429 380 RVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVAEYQQ 424
Cdd:cd02189 389 SLLEKAWQMFKAGAYLHQYEKYGVEEEDFLDAFATLEQIIAAYKS 433
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
3-211 5.42e-63

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: 205.14  E-value: 5.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429     3 EILHIQGGQCGNQIGAKFWEVICGEHGIDqtgqscgdtdlqleRINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGPFg 82
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCKEHGID--------------SLNVFFSESGSVEFIPRSIAIDTDPQALNEIKAGSL- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    83 qifrPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDR 162
Cdd:pfam00091  66 ----PNKIFLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGA 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 15233429   163 MMMTFSVFPSpKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDIC 211
Cdd:pfam00091 142 LTVAVVTFPF-GFSEGVVRPYNAILGLKELREHSDSVIVIDNDALLDIC 189
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
47-244 3.66e-58

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: 192.32  E-value: 3.66e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429     47 INVYFNEasgGKYVPRAVLMDLEPGTMDSLRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYT-----EGAELIDSVLDVVR 121
Cdd:smart00864   1 KIKVFGV---GGGGPNAVNVDLEPGVIDGVRANTDAQALNPESLASGKIQAGNNWTRGLGAgadpeVGREAAEESLDEIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    122 KEAENCDclqGFQVCHslgggtgsgmgtlLISKIREEYPDRmMMTFSVFpsPKVSDTVVEPYNATLSVHQLVENADECMV 201
Cdd:smart00864  78 EELEGAD---GVFITAgmgggt-gtgaapVIAEIAKEYGIL-TVAVVTK--PFSFEGVVRPYNAELGLEELREHVDSLIV 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 15233429    202 LDNEALYDICFRTLKLaNPTFGDLNHLISATMSGVTCCLRFPG 244
Cdd:smart00864 151 IDNDALLDICGRKLPL-RPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
261-382 1.55e-53

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: 177.80  E-value: 1.55e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429   261 PRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGKMSTKEVDEQMMNVQNKNSSY 340
Cdd:pfam03953   1 PRLHFLLTSYAPLTSDNKASHEKTSVLEVTRQLFDPKNQMVSCDPRNGKYMACALLYRGDVDPKEVNKAIQRIKEKRSAQ 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 15233429   341 FVEWIPNNVKSSVCDIAPTGLKM---ASTFIGNSTSIQEMFRRVS 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 3.97e-23

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


Pssm-ID: 214868  Cd Length: 120  Bit Score: 94.92  E-value: 3.97e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429    246 LNSDLRKLAVNLIPFPrlhFFMVGFAPLTSrgsqQYSALSVPELTQ--QMWDAKNMMCAADPRHgrYLTASAvfrgKMST 323
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASG----ENRALEAAELAIssPLLEDSNIMGAKGVLV--NITGGP----DLTL 67
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233429    324 KEVDEQMMNVQNKNSS-YFVEWIPNNVKSsvcdiaptgLKMASTFIGN-STSIQEMFRRVSE 383
Cdd:smart00865  68 KEVNEAMERIREKADPdAFIIWGPVIDEE---------LGGDEIRVTViATGIGSLFKRLSE 120
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
2-78 1.37e-03

Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved domains, segments I, II and III. Segments I and III are common to Tubulins pfam00091, but segment II aligns with myosin heavy chain sequences from D. melanogaster (PIR C35815), rabbit (SP P04460), and human (PIR S12458). Segment II of misato is a major contributor to its greater length compared with the various tubulins. The most significant sequence similarities to this 54-amino acid region are from a motif found in the heavy chains of myosins from different organisms. A comparison of segment II with the vertebrate myosin heavy chains reveals that it is homologous to a myosin peptide in the hinge region linking the S2 and LMM domains. Segment II also contains heptad repeats which are characteristic of the myosin tail alpha-helical coiled-coils. This myosin-like homology may be due only to the fact that both myosin and Misato carry coiled-coils, which appear similar but are not necessarily homologous (Wood V, personal communication).


Pssm-ID: 313791  Cd Length: 115  Bit Score: 38.39  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233429     2 REILHIQGGQCGNQIGAKFWEVicgehgidQTGQSCGDTDLQLERIN--VYF--NEASGG--KYVPRAVLMDLePGTMDS 75
Cdd:pfam10644   1 REIVTLQLGNYANYVGTHFWNT--------QESYFTYDPNEEPSEVDhdVLFreGETLSGqiTYTPRLLIYDL-KGGLGS 71

                  ...
gi 15233429    76 LRS 78
Cdd:pfam10644  72 LRK 74
 
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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