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Conserved domains on  [gi|313465675|gb|ADR51609|]
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beta-tubulin 1, partial [Puccinia gansensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00220 super family cl30499
tubulin beta chain; Provisional
 1-181 1.52e-129

tubulin beta chain; Provisional


The actual alignment was detected with superfamily member PLN00220:

Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 370.69  E-value: 1.52e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:PLN00220 187 LSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFF 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWIP 160
Cdd:PLN00220 267 MVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIP 346

                        170       180
                 ....*....|....*....|.
gi 313465675 161 NNVQTAHCDIAPRGHKMSVTF 181
Cdd:PLN00220 347 NNVKSSVCDIPPKGLKMASTF 367
 
Name Accession Description Interval E-value
PLN00220 PLN00220
tubulin beta chain; Provisional
 1-181 1.52e-129

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 370.69  E-value: 1.52e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:PLN00220 187 LSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFF 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWIP 160
Cdd:PLN00220 267 MVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIP 346

                        170       180
                 ....*....|....*....|.
gi 313465675 161 NNVQTAHCDIAPRGHKMSVTF 181
Cdd:PLN00220 347 NNVKSSVCDIPPKGLKMASTF 367
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 1-181 3.00e-128

The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.


Pssm-ID: 276956 [Multi-domain]  Cd Length: 425  Bit Score: 366.51  E-value: 3.00e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:cd02187  186 LSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLATNLVPFPRLHFL 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWIP 160
Cdd:cd02187  266 TPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRISTKEVDEQMSKVQNKNSSYFVEWIP 345

                        170       180
                 ....*....|....*....|.
gi 313465675 161 NNVQTAHCDIAPRGHKMSVTF 181
Cdd:cd02187  346 NNVKTSVCDIPPRGLKMSATF 366
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
 75-178 3.32e-51

Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules. (The FtsZ GTPases have been split into their won family).


Pssm-ID: 397858 [Multi-domain]  Cd Length: 125  Bit Score: 160.47  E-value: 3.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   75 PRLHFFMVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNY 154
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80

                          90       100
                  ....*....|....*....|....
gi 313465675  155 FVEWIPNNVQTAHCDIAPRGHKMS 178
Cdd:pfam03953  81 FVEWCPTGIKVAICSQSPYVVPGS 104
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
 60-166 5.34e-26

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


Pssm-ID: 214868 [Multi-domain]  Cd Length: 120  Bit Score: 96.08  E-value: 5.34e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675    60 LNSDLRKLAVNMVPFPrlhFFMVGFAPLTArgsqQYRAITVPELT--SQMFDAKNMMAASDPRHgrYLTVAAyfrgKVSM 137
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASG----ENRALEAAELAisSPLLEDSNIMGAKGVLV--NITGGP----DLTL 67

                           90       100       110
                   ....*....|....*....|....*....|
gi 313465675   138 KEVEENMLSVQSKNS-NYFVEWIPNNVQTA 166
Cdd:smart00865  68 KEVNEAMERIREKADpDAFIIWGPVIDEEL 97
 
Name Accession Description Interval E-value
PLN00220 PLN00220
tubulin beta chain; Provisional
 1-181 1.52e-129

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 370.69  E-value: 1.52e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:PLN00220 187 LSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFF 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWIP 160
Cdd:PLN00220 267 MVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIP 346

                        170       180
                 ....*....|....*....|.
gi 313465675 161 NNVQTAHCDIAPRGHKMSVTF 181
Cdd:PLN00220 347 NNVKSSVCDIPPKGLKMASTF 367
PTZ00010 PTZ00010
tubulin beta chain; Provisional
 1-181 1.98e-129

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 370.26  E-value: 1.98e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:PTZ00010 187 LSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPFPRLHFF 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWIP 160
Cdd:PTZ00010 267 MMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSYFVEWIP 346

                        170       180
                 ....*....|....*....|.
gi 313465675 161 NNVQTAHCDIAPRGHKMSVTF 181
Cdd:PTZ00010 347 NNIKSSVCDIPPKGLKMSVTF 367
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 1-181 3.00e-128

The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.


Pssm-ID: 276956 [Multi-domain]  Cd Length: 425  Bit Score: 366.51  E-value: 3.00e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:cd02187  186 LSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLATNLVPFPRLHFL 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWIP 160
Cdd:cd02187  266 TPGFAPLTSRGSQQYRKLTVPELTQQLFDAKNMMAACDPRHGRYLTAAAIFRGRISTKEVDEQMSKVQNKNSSYFVEWIP 345

                        170       180
                 ....*....|....*....|.
gi 313465675 161 NNVQTAHCDIAPRGHKMSVTF 181
Cdd:cd02187  346 NNVKTSVCDIPPRGLKMSATF 366
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
 1-181 1.98e-67

Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, gamma-, delta-, epsilon, and zeta-tubulins as well as FtsZ and CetZ, all of which are involved in polymer formation. Tubulin is the major component of microtubules, but also exists as a heterodimer and as a curved oligomer. Microtubules exist in all eukaryotic cells and are responsible for many functions, including cellular transport, cell motility, and mitosis. FtsZ forms a ring-shaped septum at the site of bacterial cell division, which is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria, archaea, and chloroplasts. A recent study found that CetZ proteins, formerly annotated FtsZ type 2, are not required for cell division, whereas FtsZ proteins play an important role. Instead, CetZ proteins are shown to be involved in controlling archaeal cell shape dynamics. The results from inactivation studies of CetZ proteins in Haloferax volcanii suggest that CetZ1 is essential for normal swimming motility and rod-cell development.


Pssm-ID: 276954 [Multi-domain]  Cd Length: 332  Bit Score: 208.80  E-value: 1.98e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:cd00286  147 LTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTEALRFEGSLNVDLRELAENLVPLPRGHFL 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKV--SMKEVEENMLSVQSKNSNYFvEW 158
Cdd:cd00286  227 MLGYAPLDSATSATPRSLRVKELTRRAFLPANLLVGCDPDHGEAIAALLVIRGPPdlSSKEVERAIARVKETLGHLF-SW 305

                        170       180
                 ....*....|....*....|...
gi 313465675 159 IPNNVQTAHCDIAPRGHKMSVTF 181
Cdd:cd00286  306 SPAGVKTGISPKPPAEGEVSVLA 328
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 1-172 8.94e-59

The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.


Pssm-ID: 276955 [Multi-domain]  Cd Length: 434  Bit Score: 189.29  E-value: 8.94e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:cd02186  188 LTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNVDLNEFQTNLVPYPRIHFP 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWIP 160
Cdd:cd02186  268 LVSYAPIISAEKANHEQLSVQEITNSCFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCP 347

                        170
                 ....*....|..
gi 313465675 161 NNVQTAHCDIAP 172
Cdd:cd02186  348 TGFKVGINYQPP 359
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
 1-181 2.88e-58

The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins. Also included in this group is the mitochondrial Misato/DML1 protein family, involved in mitochondrial fusion and in mitochondrial distribution and morphology.


Pssm-ID: 276963 [Multi-domain]  Cd Length: 387  Bit Score: 186.64  E-value: 2.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFR---TLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRL 77
Cdd:cd06059  148 LALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLTSSLRFEGSLNVDLNEITTNLVPFPRL 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  78 HFFMVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKV-SMKEVEENMLSVQSKNSnyFV 156
Cdd:cd06059  228 HFLLPSLSPLTSANDVTLEPLTLDQLFSDLFSKDNQLVGCDPRHGTYLACALLLRGKVfSLSDVRRNIDRIKPKLK--FI 305

                        170       180
                 ....*....|....*....|....*
gi 313465675 157 EWIPNNVQTAHCDIAPRGHKMSVTF 181
Cdd:cd06059  306 SWNPDGFKVGLCSVPPVGQKYSLLF 330
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
 75-178 3.32e-51

Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins are GTPases. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules. (The FtsZ GTPases have been split into their won family).


Pssm-ID: 397858 [Multi-domain]  Cd Length: 125  Bit Score: 160.47  E-value: 3.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   75 PRLHFFMVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNY 154
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANKASHEKTSVLDVTRRLFDPKNQMVSCDPRNGKYMACALLYRGDVSPKDVHRAIQRIKEKRSAQ 80

                          90       100
                  ....*....|....*....|....
gi 313465675  155 FVEWIPNNVQTAHCDIAPRGHKMS 178
Cdd:pfam03953  81 FVEWCPTGIKVAICSQSPYVVPGS 104
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
 1-160 1.80e-50

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 167.96  E-value: 1.80e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:PTZ00335 189 LSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDLTEFQTNLVPYPRIHFM 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWIP 160
Cdd:PTZ00335 269 LSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAIATIKTKRTIQFVDWCP 348
PLN00221 PLN00221
tubulin alpha chain; Provisional
 1-160 9.75e-50

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 166.14  E-value: 9.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:PLN00221 189 LSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTASLRFDGALNVDITEFQTNLVPYPRIHFM 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWIP 160
Cdd:PLN00221 269 LSSYAPVISAEKAYHEQLSVAEITNSAFEPASMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCP 348
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
 1-167 1.51e-37

The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of tubulin superfamily. Gamma is a low abundance protein present within the cells in both various types of microtubule-organizing centers and cytoplasmic protein complexes. Gamma-tubulin recruits the alpha/beta-tubulin dimers that form the minus ends of microtubules and is thought to be involved in microtubule nucleation and capping.


Pssm-ID: 276957 [Multi-domain]  Cd Length: 430  Bit Score: 133.82  E-value: 1.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:cd02188  188 LTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTSTLRFPGYMNNDLVSLISSLIPTPRLHFL 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPLT-ARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNYFVEWI 159
Cdd:cd02188  268 MTSYTPLTsDQVASSVRKTTVLDVMRRLLQPKNRMVSTSTKNGCYISILNIIQGEVDPTQVHKSLQRIRERKLANFIPWG 347


                 ....*...
gi 313465675 160 PNNVQTAH 167
Cdd:cd02188  348 PASIQVAL 355
PLN00222 PLN00222
tubulin gamma chain; Provisional
 1-166 4.00e-31

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 116.87  E-value: 4.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPTYGDLNHLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFF 80
Cdd:PLN00222 190 LTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTTTLRYPGYMNNDLVGLLASLIPTPRCHFL 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  81 MVGFAPL-TARGSQQYRAITVPELTSQMFDAKNMMAASDPR-----HGRYLTVAAYFRGKVSMKEVEENMLSVQSKNSNY 154
Cdd:PLN00222 270 MTGYTPLtVERQANVIRKTTVLDVMRRLLQTKNIMVSSYARtkeasQAKYISILNIIQGEVDPTQVHKSLQRIRERKLAN 349

                        170
                 ....*....|..
gi 313465675 155 FVEWIPNNVQTA 166
Cdd:PLN00222 350 FIEWGPASIQVA 361
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
 1-179 1.18e-30

The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The epsilon-tubulins which are widespread but not ubiquitous among eukaryotes play a role in basal body/centriole morphogenesis.


Pssm-ID: 276959 [Multi-domain]  Cd Length: 449  Bit Score: 115.41  E-value: 1.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATPT----------------------YGDLNHLVSIVMSGITTCLRFPG 58
Cdd:cd02190  192 LALRELTEHADCVLPVENQALMDIVNKIKSSKDKGktgvlaainssgggqkkgkkkpFDDMNNIVANLLLNLTSSMRFEG 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  59 QLNSDLRKLAVNMVPFPRLHFFMVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMK 138
Cdd:cd02190  272 SLNVDLNEITTNLVPFPRLHFLLSSLSPLYALADVRLPPRRLDQMFSDAFSRDHQLLKADPKHGLYLACALLVRGNVSIS 351

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 313465675 139 EVEENMLSVQSKNSnyFVEWIPNNVQTAHCDIAPRGHKMSV 179
Cdd:cd02190  352 DLRRNIDRLKRQLK--FVSWNQDGWKIGLCSVPPVGQPYSL 390
PTZ00387 PTZ00387
epsilon tubulin; Provisional
 1-179 2.37e-29

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 112.12  E-value: 2.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKL---------------------ATPT------YGDLNHLVSIVMSGITTC 53
Cdd:PTZ00387 187 FALRELIEHADCVLPLDNDALANIADSALSRkkkklakgnikrgpqphkysvAKPTetkklpYDKMNNIVAQLLSNLTSS 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  54 LRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTARGSQQYRAITVPELTSQMFDAKNMMAASDPRHGRYLTVAAYFRG 133
Cdd:PTZ00387 267 MRFEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGPRRLDQMFKDCLDPDHQMVAATPEAGKYLATALIVRG 346

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 313465675 134 KVSMKEVEENMLSVqsKNSNYFVEWIPNNVQTAHCDIAPRGHKMSV 179
Cdd:PTZ00387 347 PQNVSDVTRNILRL--KEQLNMIYWNEDGFKTGLCNVSPLGQPYSL 390
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
 60-166 5.34e-26

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


Pssm-ID: 214868 [Multi-domain]  Cd Length: 120  Bit Score: 96.08  E-value: 5.34e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675    60 LNSDLRKLAVNMVPFPrlhFFMVGFAPLTArgsqQYRAITVPELT--SQMFDAKNMMAASDPRHgrYLTVAAyfrgKVSM 137
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASG----ENRALEAAELAisSPLLEDSNIMGAKGVLV--NITGGP----DLTL 67

                           90       100       110
                   ....*....|....*....|....*....|
gi 313465675   138 KEVEENMLSVQSKNS-NYFVEWIPNNVQTA 166
Cdd:smart00865  68 KEVNEAMERIREKADpDAFIIWGPVIDEEL 97
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
 1-180 1.67e-08

The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. Delta-tubulin plays an essential role in forming the triplet microtubules of centrioles and basal bodies.


Pssm-ID: 276958 [Multi-domain]  Cd Length: 433  Bit Score: 53.04  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675   1 LSVHQLDENSDETFCIDNEALYDICFRTLKLATP-TYGDLN-----HLVSIVMSGITTCLRFPGQLNSdLRKLAVNMVPF 74
Cdd:cd02189  180 LTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINrviarQLAGVLLPSSSPTSPSPLRRCP-LGDLLEHLCPH 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313465675  75 PRLHFFMVGFAPLTARGSQQYRAITVPEL---TSQMF----------DAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVE 141
Cdd:cd02189  259 PAYKLLTLRSLPQMPEPSRAFSTYTWPSLlkrLRQMLitgakleegiDWQLLDTSGSHNPNKSLAALLVLRGKDAMKVHS 338

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 313465675 142 ENMLSVqsKNSNYFVEWIPNNVQTAHCDIAPRGHKMSVT 180
Cdd:cd02189  339 ADLSAF--KDPVLYSPWVPNPFNVSVSPRPFNGYEKSVT 375
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
 1-25 4.48e-04

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


Pssm-ID: 459669 [Multi-domain]  Cd Length: 190  Bit Score: 39.12  E-value: 4.48e-04
                          10        20
                  ....*....|....*....|....*
gi 313465675    1 LSVHQLDENSDETFCIDNEALYDIC 25
Cdd:pfam00091 165 LGLKELIEHSDSVIVIDNDALYDIC 189
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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