NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958657349|ref|XP_038941484|]
View 

tubulin delta chain isoform X3 [Rattus norvegicus]

Protein Classification

tubulin family protein( domain architecture ID 10115139)

tubulin family protein similar to tubulin delta chain that acts as a positive regulator of hedgehog signaling and regulates ciliary function

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
1-333 1.06e-162

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: 460.96  E-value: 1.06e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSD 80
Cdd:cd02189   111 LEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEYPKAYLLNTVVWPYSSGEVPVQNYNTLLTLSHLQESSD 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  81 ALLIHENDVVHKICAKRMNIKQI-SFRDLNRVLAHQLGSVFQPTHSEDSSFHYCRNPLGDLMEHLVPHPEFKMLGVRNIP 159
Cdd:cd02189   191 GILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVLLPSSSPTSPSPLRRCPLGDLLEHLCPHPAYKLLTLRSLP 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 160 QMSAESLAYSTFTWAGLLKHLRQMLISRAKMEEGIDWQvrpplsglppigKASAHKEPHFNTSLANLVILRG---REVHS 236
Cdd:cd02189   271 QMPEPSRAFSTYTWPSLLKRLRQMLITGAKLEEGIDWQ------------LLDTSGSHNPNKSLAALLVLRGkdaMKVHS 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 237 ADVGGFRDAALYTSWlePADAFSVWKTPRPFDKYEKSAALVSNSQLLVKPLDMVVGKAWNMFSSKAYIHQYTKFGMEEED 316
Cdd:cd02189   339 ADLSAFKDPVLYSPW--VPNPFNVSVSPRPFNGYEKSVTLLSNSQNIVGPLDSLLEKAWQMFKAGAYLHQYEKYGVEEED 416
                         330
                  ....*....|....*..
gi 1958657349 317 FLDSFTLLEQVVASYGS 333
Cdd:cd02189   417 FLDAFATLEQIIAAYKS 433
 
Name Accession Description Interval E-value
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
1-333 1.06e-162

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: 460.96  E-value: 1.06e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSD 80
Cdd:cd02189   111 LEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEYPKAYLLNTVVWPYSSGEVPVQNYNTLLTLSHLQESSD 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  81 ALLIHENDVVHKICAKRMNIKQI-SFRDLNRVLAHQLGSVFQPTHSEDSSFHYCRNPLGDLMEHLVPHPEFKMLGVRNIP 159
Cdd:cd02189   191 GILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVLLPSSSPTSPSPLRRCPLGDLLEHLCPHPAYKLLTLRSLP 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 160 QMSAESLAYSTFTWAGLLKHLRQMLISRAKMEEGIDWQvrpplsglppigKASAHKEPHFNTSLANLVILRG---REVHS 236
Cdd:cd02189   271 QMPEPSRAFSTYTWPSLLKRLRQMLITGAKLEEGIDWQ------------LLDTSGSHNPNKSLAALLVLRGkdaMKVHS 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 237 ADVGGFRDAALYTSWlePADAFSVWKTPRPFDKYEKSAALVSNSQLLVKPLDMVVGKAWNMFSSKAYIHQYTKFGMEEED 316
Cdd:cd02189   339 ADLSAFKDPVLYSPW--VPNPFNVSVSPRPFNGYEKSVTLLSNSQNIVGPLDSLLEKAWQMFKAGAYLHQYEKYGVEEED 416
                         330
                  ....*....|....*..
gi 1958657349 317 FLDSFTLLEQVVASYGS 333
Cdd:cd02189   417 FLDAFATLEQIIAAYKS 433
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
1-94 7.50e-33

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: 120.40  E-value: 7.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSD 80
Cdd:pfam00091  96 LEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGALTVAVVTFPFGFSEGVVRPYNAILGLKELIEHSD 175
                          90
                  ....*....|....
gi 1958657349  81 ALLIHENDVVHKIC 94
Cdd:pfam00091 176 SVIVIDNDALYDIC 189
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
1-119 6.39e-25

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


Pssm-ID: 214867 [Multi-domain]  Cd Length: 192  Bit Score: 99.48  E-value: 6.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349    1 MNLIQTEVEKCDslsGFFIIMSMAGGTGSGLGAFITQKLQDQysSSLKMNQIIWPyGTGEVIVQNYNSILTLSHLYRSSD 80
Cdd:smart00864  73 LDEIREELEGAD---GVFITAGMGGGTGTGAAPVIAEIAKEY--GILTVAVVTKP-FSFEGVVRPYNAELGLEELREHVD 146
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958657349   81 ALLIHENDVVHKICAKRmNIKQISFRDLNRVLAHQLGSV 119
Cdd:smart00864 147 SLIVIDNDALLDICGRK-LPLRPAFKDANDLLAQAVSGI 184
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-317 1.66e-24

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 103.25  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPY-GTGEVIVQNYNSILTLSHLYRSS 79
Cdd:PTZ00335  119 LDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSpQVSTAVVEPYNSVLSTHSLLEHT 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  80 DALLIHENDVVHKICAKRMNIKQISFRDLNRVLAHQLGSVFQPTHSEDSSFhycrNPLGDLMEHLVPHPEFKMLGVRNIP 159
Cdd:PTZ00335  199 DVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALN----VDLTEFQTNLVPYPRIHFMLSSYAP 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 160 QMSAESLAYSTFTWAGllkhlrqmlISRAKMEEgidwqvrpplsglppiGKASAHKEPHFNTSLANLVILRGrEVHSADV 239
Cdd:PTZ00335  275 IISAEKAYHEQLSVAE---------ITNSAFEP----------------ANMMAKCDPRHGKYMACCLMYRG-DVVPKDV 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 240 GGfrdaalytswlepadAFSVWKTPRP---------------------------FDKYEKSAALVSNSQLLVKPLDMVVG 292
Cdd:PTZ00335  329 NA---------------AIATIKTKRTiqfvdwcptgfkcginyqpptvvpggdLAKVQRAVCMISNSTAIAEVFSRIDH 393
                         330       340
                  ....*....|....*....|....*
gi 1958657349 293 KAWNMFSSKAYIHQYTKFGMEEEDF 317
Cdd:PTZ00335  394 KFDLMYAKRAFVHWYVGEGMEEGEF 418
 
Name Accession Description Interval E-value
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
1-333 1.06e-162

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: 460.96  E-value: 1.06e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSD 80
Cdd:cd02189   111 LEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEYPKAYLLNTVVWPYSSGEVPVQNYNTLLTLSHLQESSD 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  81 ALLIHENDVVHKICAKRMNIKQI-SFRDLNRVLAHQLGSVFQPTHSEDSSFHYCRNPLGDLMEHLVPHPEFKMLGVRNIP 159
Cdd:cd02189   191 GILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVLLPSSSPTSPSPLRRCPLGDLLEHLCPHPAYKLLTLRSLP 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 160 QMSAESLAYSTFTWAGLLKHLRQMLISRAKMEEGIDWQvrpplsglppigKASAHKEPHFNTSLANLVILRG---REVHS 236
Cdd:cd02189   271 QMPEPSRAFSTYTWPSLLKRLRQMLITGAKLEEGIDWQ------------LLDTSGSHNPNKSLAALLVLRGkdaMKVHS 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 237 ADVGGFRDAALYTSWlePADAFSVWKTPRPFDKYEKSAALVSNSQLLVKPLDMVVGKAWNMFSSKAYIHQYTKFGMEEED 316
Cdd:cd02189   339 ADLSAFKDPVLYSPW--VPNPFNVSVSPRPFNGYEKSVTLLSNSQNIVGPLDSLLEKAWQMFKAGAYLHQYEKYGVEEED 416
                         330
                  ....*....|....*..
gi 1958657349 317 FLDSFTLLEQVVASYGS 333
Cdd:cd02189   417 FLDAFATLEQIIAAYKS 433
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
1-280 5.46e-80

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: 246.94  E-value: 5.46e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSD 80
Cdd:cd00286    78 LDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDEYPNRLVVTFSILPGPDEGVIVYPYNAALTLKTLTEHAD 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  81 ALLIHENDVVHKICAKRMNIKQISFRDLNRVLAHQLGSVFQPTHSEDSSFHYcrnpLGDLMEHLVPHPEFKMLGVRNIPQ 160
Cdd:cd00286   158 CLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTEALRFEGSLNVD----LRELAENLVPLPRGHFLMLGYAPL 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 161 MSAESLaystFTWAGLLKHLRQMLISRAKMEEGIDwqvrpplsglppigkasahkePHFNTSLANLVILRGR-EVHSADV 239
Cdd:cd00286   234 DSATSA----TPRSLRVKELTRRAFLPANLLVGCD---------------------PDHGEAIAALLVIRGPpDLSSKEV 288
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958657349 240 GGFRDAALYTSWLEPADAFSVWKT---PRPFDKYEKSAALVSNS 280
Cdd:cd00286   289 ERAIARVKETLGHLFSWSPAGVKTgisPKPPAEGEVSVLALLNS 332
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
1-331 1.61e-72

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: 229.40  E-value: 1.61e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPYGTGE-VIVQNYNSILTLSHLYRSS 79
Cdd:cd06059    78 LDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYPKVYRFTFSVFPSPDDDnVITSPYNSVLALNHLTEHA 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  80 DALLIHENDVVHKICAK---RMNIKQISFRDLNRVLAHQLGSVFQPTHSEDSSfhycRNPLGDLMEHLVPHPEFKMLgvr 156
Cdd:cd06059   158 DCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLTSSLRFEGSL----NVDLNEITTNLVPFPRLHFL--- 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 157 nIPQMSAESLAYSTFTWAGLLKHLRQMLISRAKMEEGIDwqvrpplsglppigkasahkePHFNTSLANLVILRGREVHS 236
Cdd:cd06059   231 -LPSLSPLTSANDVTLEPLTLDQLFSDLFSKDNQLVGCD---------------------PRHGTYLACALLLRGKVFSL 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 237 ADVGGFRDAALYTSWLEPAdAFSVWKTPR---PFDKYEKSAALVSNSQLLVKPLDMVVGKAWNMFSSKAYIHQYTKFGME 313
Cdd:cd06059   289 SDVRRNIDRIKPKLKFISW-NPDGFKVGLcsvPPVGQKYSLLFLSNNTSIASTFERLIERFDKLYKRKAFLHHYTGEGME 367
                         330
                  ....*....|....*...
gi 1958657349 314 EEDFLDSFTLLEQVVASY 331
Cdd:cd06059   368 EGDFSEARESLANLIQEY 385
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
1-94 7.50e-33

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: 120.40  E-value: 7.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSD 80
Cdd:pfam00091  96 LEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGALTVAVVTFPFGFSEGVVRPYNAILGLKELIEHSD 175
                          90
                  ....*....|....
gi 1958657349  81 ALLIHENDVVHKIC 94
Cdd:pfam00091 176 SVIVIDNDALYDIC 189
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-326 1.11e-32

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: 125.73  E-value: 1.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPYG-TGEVIVQNYNSILTLSHLYRSS 79
Cdd:cd02186   118 LDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDYGKKSKLEFSIYPSPqVSTSVVEPYNSVLTTHSLLEHS 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  80 DALLIHENDVVHKICAKRMNIKQISFRDLNRVLAHQLGSVFQPTHSEDSSFHycrnPLGDLMEHLVPHPEFKMLGVRNIP 159
Cdd:cd02186   198 DCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNV----DLNEFQTNLVPYPRIHFPLVSYAP 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 160 QMSAESLAYSTFTwaglLKHLRQMLISRAKMeegidwqvrpplsglppigkaSAHKEPHFNTSLANLVILRGrevhsaDV 239
Cdd:cd02186   274 IISAEKANHEQLS----VQEITNSCFEPANQ---------------------MVKCDPRHGKYMACCLLYRG------DV 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 240 ggfrdaalytSWLEPADAFSVWKTPR---------------------------PFDKYEKSAALVSNSQLLVKPLDMVVG 292
Cdd:cd02186   323 ----------VPKDVNAAIATIKTKRtiqfvdwcptgfkvginyqpptvvpgsDLAKVDRSVCMLANSTAIAEAFQRLDH 392
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1958657349 293 KAWNMFSSKAYIHQYTKFGMEEEDF---LDSFTLLEQ 326
Cdd:cd02186   393 KFDLLYSKRAFVHWYVGEGMEEGEFseaREDLAALEK 429
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
1-334 7.99e-27

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: 109.64  E-value: 7.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSD 80
Cdd:cd02190   123 LEKLRRAAEKCDSLQSFFLLHSLGGGTGSGLGSYILELLEDEFPDVYRFVTSVFPSGDDDVITSPYNSVLALRELTEHAD 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  81 ALLIHENDVVHKICAK----------------------RMNIKQISFRDLNRVLAHQLGSVfqpTHSedSSFHycrNPLG 138
Cdd:cd02190   203 CVLPVENQALMDIVNKiksskdkgktgvlaainssgggQKKGKKKPFDDMNNIVANLLLNL---TSS--MRFE---GSLN 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 139 -DLME---HLVPHPEFKMLgvrnipqMSAESLAYSTFTWAGLLKHLRQM---LISRakmeegiDWQvrppLSGLPPigKA 211
Cdd:cd02190   275 vDLNEittNLVPFPRLHFL-------LSSLSPLYALADVRLPPRRLDQMfsdAFSR-------DHQ----LLKADP--KH 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 212 SahkephfnTSLANLVILRGrEVHSAD----VGGFRDAALYTSWLEpaDAF-----SVWKTPRPFdkyekSAALVSNSQL 282
Cdd:cd02190   335 G--------LYLACALLVRG-NVSISDlrrnIDRLKRQLKFVSWNQ--DGWkiglcSVPPVGQPY-----SLLCLANNTC 398
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958657349 283 LVKPLDMVVGKAWNMFSSKAYIHQYTKfGMEEEDFLDSFTLLEQVVASYGSL 334
Cdd:cd02190   399 IKPTFTEMHERFDKLYKRKAHLHHYTQ-YMEQDDFDEALESLLDLIEEYKDL 449
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
1-109 1.83e-26

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: 108.40  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWP--YGTGEVIVQNYNSILTLSHLYRS 78
Cdd:cd02188   117 LDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRYPKKLIQTYSVFPnqEESSDVVVQPYNSILTLKRLTLN 196
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958657349  79 SDALLIHENDVVHKICAKRMNIKQISFRDLN 109
Cdd:cd02188   197 ADCVVVLDNTALNRIATDRLKIDNPSFSQIN 227
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-331 2.71e-25

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: 104.96  E-value: 2.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPYG-TGEVIVQNYNSILTLSHLYRSS 79
Cdd:cd02187   116 LDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPDRIMSTFSVLPSPkVSDTVVEPYNAVLSLHQLVENA 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  80 DALLIHENDVVHKICAKRMNIKQISFRDLNRVLAhqlgsvfQPTHSEDSSFhycRNPlGDLME-------HLVPHPEFKM 152
Cdd:cd02187   196 DETFCIDNEALYNICQRTLKLTQPTYDDLNHLIS-------QVMSGITSSL---RFP-GQLNSdlrklatNLVPFPRLHF 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 153 LGVRNIPQMSAESLAYSTFTwaglLKHLRQMLISRAKMEEGIDWqvrpplsglppigkasahKEPHFntsLANLVILRGR 232
Cdd:cd02187   265 LTPGFAPLTSRGSQQYRKLT----VPELTQQLFDAKNMMAACDP------------------RHGRY---LTAAAIFRGR 319
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 233 eVHSADV----GGFRD--AALYTSWLepADAFSVWKTPRPFDKYEKSAALVSNS----QLLVKpldmvVGKAWN-MFSSK 301
Cdd:cd02187   320 -ISTKEVdeqmSKVQNknSSYFVEWI--PNNVKTSVCDIPPRGLKMSATFIGNStaiqELFKR-----LSEQFTaMFRRK 391
                         330       340       350
                  ....*....|....*....|....*....|
gi 1958657349 302 AYIHQYTKFGMEEEDFLDSFTLLEQVVASY 331
Cdd:cd02187   392 AFLHWYTGEGMDEMEFTEAESNLNDLISEY 421
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
1-119 6.39e-25

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


Pssm-ID: 214867 [Multi-domain]  Cd Length: 192  Bit Score: 99.48  E-value: 6.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349    1 MNLIQTEVEKCDslsGFFIIMSMAGGTGSGLGAFITQKLQDQysSSLKMNQIIWPyGTGEVIVQNYNSILTLSHLYRSSD 80
Cdd:smart00864  73 LDEIREELEGAD---GVFITAGMGGGTGTGAAPVIAEIAKEY--GILTVAVVTKP-FSFEGVVRPYNAELGLEELREHVD 146
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958657349   81 ALLIHENDVVHKICAKRmNIKQISFRDLNRVLAHQLGSV 119
Cdd:smart00864 147 SLIVIDNDALLDICGRK-LPLRPAFKDANDLLAQAVSGI 184
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
1-317 1.66e-24

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 103.25  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPY-GTGEVIVQNYNSILTLSHLYRSS 79
Cdd:PTZ00335  119 LDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSpQVSTAVVEPYNSVLSTHSLLEHT 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  80 DALLIHENDVVHKICAKRMNIKQISFRDLNRVLAHQLGSVFQPTHSEDSSFhycrNPLGDLMEHLVPHPEFKMLGVRNIP 159
Cdd:PTZ00335  199 DVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALN----VDLTEFQTNLVPYPRIHFMLSSYAP 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 160 QMSAESLAYSTFTWAGllkhlrqmlISRAKMEEgidwqvrpplsglppiGKASAHKEPHFNTSLANLVILRGrEVHSADV 239
Cdd:PTZ00335  275 IISAEKAYHEQLSVAE---------ITNSAFEP----------------ANMMAKCDPRHGKYMACCLMYRG-DVVPKDV 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 240 GGfrdaalytswlepadAFSVWKTPRP---------------------------FDKYEKSAALVSNSQLLVKPLDMVVG 292
Cdd:PTZ00335  329 NA---------------AIATIKTKRTiqfvdwcptgfkcginyqpptvvpggdLAKVQRAVCMISNSTAIAEVFSRIDH 393
                         330       340
                  ....*....|....*....|....*
gi 1958657349 293 KAWNMFSSKAYIHQYTKFGMEEEDF 317
Cdd:PTZ00335  394 KFDLMYAKRAFVHWYVGEGMEEGEF 418
PLN00222 PLN00222
tubulin gamma chain; Provisional
1-165 1.07e-21

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 95.30  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWP--YGTGEVIVQNYNSILTLSHLYRS 78
Cdd:PLN00222  119 MDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRYSKKLVQTYSVFPnqMETSDVVVQPYNSLLTLKRLTLN 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  79 SDALLIHENDVVHKICAKRMNIKQISFRDLNRVLAhqlgSVFQPTHSEDSSFHYCRNPLGDLMEHLVPHPE--FKMLGVR 156
Cdd:PLN00222  199 ADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVS----TVMSASTTTLRYPGYMNNDLVGLLASLIPTPRchFLMTGYT 274

                  ....*....
gi 1958657349 157 NIPQMSAES 165
Cdd:PLN00222  275 PLTVERQAN 283
PTZ00010 PTZ00010
tubulin beta chain; Provisional
1-331 4.48e-21

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 93.30  E-value: 4.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPY-GTGEVIVQNYNSILTLSHLYRSS 79
Cdd:PTZ00010  117 LDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSpKVSDTVVEPYNATLSVHQLVENA 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  80 DALLIHENDVVHKICAKRMNIKQISFRDLNRVLAHQLGSV-----FQPTHSEDssfhycrnpLGDLMEHLVPHPEFKMLG 154
Cdd:PTZ00010  197 DESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVtcclrFPGQLNSD---------LRKLAVNLVPFPRLHFFM 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 155 VRNIPQMSAESLAYSTFTWAGLLKhlrQMLISRAKMeegidwqvrpplsglppigkasAHKEPHFNTSLANLVILRGReV 234
Cdd:PTZ00010  268 MGFAPLTSRGSQQYRGLSVPELTQ---QMFDAKNMM----------------------CAADPRHGRYLTASALFRGR-M 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 235 HSADVG------GFRDAALYTSWLEPADAFSVWKTPRPFDKyeKSAALVSNSQLLVKPLDMVVGKAWNMFSSKAYIHQYT 308
Cdd:PTZ00010  322 STKEVDeqmlnvQNKNSSYFVEWIPNNIKSSVCDIPPKGLK--MSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYT 399
                         330       340
                  ....*....|....*....|...
gi 1958657349 309 KFGMEEEDFLDSFTLLEQVVASY 331
Cdd:PTZ00010  400 GEGMDEMEFTEAESNMNDLVSEY 422
PTZ00387 PTZ00387
epsilon tubulin; Provisional
2-334 1.92e-19

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 88.63  E-value: 1.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   2 NLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSDA 81
Cdd:PTZ00387  119 ESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEFPHVFRFCPVVFPSAVDDVITSPYNSFFALRELIEHADC 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  82 LLIHENDVVHKIC--AKRMNIKQISFRDLNRVLAHQLGSVFQPTHSEDSSFHYCRN-----------------PLG-DLM 141
Cdd:PTZ00387  199 VLPLDNDALANIAdsALSRKKKKLAKGNIKRGPQPHKYSVAKPTETKKLPYDKMNNivaqllsnltssmrfegSLNvDIN 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 142 E---HLVPHPEFKML---------------GVRNIPQMsaeslaystftWAGLLKHLRQMLISrakmeegidwqvrppls 203
Cdd:PTZ00387  279 EittNLVPYPRLHFLtssiaplvslkdvavGPRRLDQM-----------FKDCLDPDHQMVAA----------------- 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 204 glppigkasahkEPHFNTSLANLVILRGREVHS---ADVGGFRDAALYTSWLEpaDAFSVWKTPRPFDKYEKSAALVSNS 280
Cdd:PTZ00387  331 ------------TPEAGKYLATALIVRGPQNVSdvtRNILRLKEQLNMIYWNE--DGFKTGLCNVSPLGQPYSLLCLANN 396
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958657349 281 QLLVKPLDMVVGKAWNMFSSKAYIHQYTKFgMEEEDFLDSFTLLEQVVASYGSL 334
Cdd:PTZ00387  397 CCIRNKFESMLERFNKLYKRKSHVHHYTEY-LEQAYFDETLETIQNLIDDYAYL 449
PLN00220 PLN00220
tubulin beta chain; Provisional
1-331 2.70e-18

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 85.26  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   1 MNLIQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPY-GTGEVIVQNYNSILTLSHLYRSS 79
Cdd:PLN00220  117 LDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSpKVSDTVVEPYNATLSVHQLVENA 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  80 DALLIHENDVVHKICAKRMNIKQISFRDLNRVLAHQLGSV-----FQPTHSEDssfhycrnpLGDLMEHLVPHPEFKMLG 154
Cdd:PLN00220  197 DECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVtcclrFPGQLNSD---------LRKLAVNLIPFPRLHFFM 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 155 VRNIPQMSAESLAYSTFTWAGLLKhlrQMLISRAKMeegidwqvrpplsglppigkasAHKEPHFNTSLANLVILRGR-- 232
Cdd:PLN00220  268 VGFAPLTSRGSQQYRALTVPELTQ---QMWDAKNMM----------------------CAADPRHGRYLTASAMFRGKms 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 233 --EVHSADVG-GFRDAALYTSWLEPADAFSVWKTPRPFDKYekSAALVSNSQLLVKPLDMVVGKAWNMFSSKAYIHQYTK 309
Cdd:PLN00220  323 tkEVDEQMINvQNKNSSYFVEWIPNNVKSSVCDIPPKGLKM--ASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTG 400
                         330       340
                  ....*....|....*....|..
gi 1958657349 310 FGMEEEDFLDSFTLLEQVVASY 331
Cdd:PLN00220  401 EGMDEMEFTEAESNMNDLVSEY 422
PLN00221 PLN00221
tubulin alpha chain; Provisional
4-317 2.36e-15

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 76.39  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   4 IQTEVEKCDSLSGFFIIMSMAGGTGSGLGAFITQKLQDQYSSSLKMNQIIWPY-GTGEVIVQNYNSILTLSHLYRSSDAL 82
Cdd:PLN00221  122 IRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSpQVSTAVVEPYNSVLSTHSLLEHTDVA 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349  83 LIHENDVVHKICAKRMNIKQISFRDLNRVLAHQLGSVfqpthSEDSSFHYCRN-PLGDLMEHLVPHPEFKMLGVRNIPQM 161
Cdd:PLN00221  202 VLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSL-----TASLRFDGALNvDITEFQTNLVPYPRIHFMLSSYAPVI 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 162 SAESLAYSTFTWAGllkhlrqmlISRAKMEegidwqvrpPLSGLppigkasAHKEPHFNTSLANLVILRGrEVHSADVgg 241
Cdd:PLN00221  277 SAEKAYHEQLSVAE---------ITNSAFE---------PASMM-------AKCDPRHGKYMACCLMYRG-DVVPKDV-- 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349 242 frDAALYTSWLEPADAFSVWkTPRPFD-----------------KYEKSAALVSNSQLLVKPLDMVVGKAWNMFSSKAYI 304
Cdd:PLN00221  329 --NAAVATIKTKRTIQFVDW-CPTGFKcginyqpptvvpggdlaKVQRAVCMISNSTAVAEVFSRIDHKFDLMYAKRAFV 405
                         330
                  ....*....|...
gi 1958657349 305 HQYTKFGMEEEDF 317
Cdd:PLN00221  406 HWYVGEGMEEGEF 418
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
8-80 1.16e-04

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


Pssm-ID: 276964 [Multi-domain]  Cd Length: 539  Bit Score: 43.85  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958657349   8 VEKCDSLSGFFIIMSMAGGtGSGLGAFITQKLQDQYSSSlkmnqIIWPYGTGEV----------IVQNYNSILTLSHLYR 77
Cdd:cd06060   201 VEECDSLQGFQILVDTDDG-FGGVAAKLLENLRDEYGKK-----SILTPGLSPAsppdpdsqrrIKRLLNDALSLSSLSE 274

                  ...
gi 1958657349  78 SSD 80
Cdd:cd06060   275 HSS 277
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH