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Conserved domains on  [gi|17737379|ref|NP_523435|]
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misato, isoform A [Drosophila melanogaster]

Protein Classification

misato family protein( domain architecture ID 10149475)

misato family protein similar to human protein misato homolog 1 that regulates mitochondrial distribution and morphology, and is required for mitochondrial fusion and mitochondrial network formation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
5-570 0e+00

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: 571.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379   5 REILTFQFGTYANYVGTHFWNQQEANFRYGDESEQVAEEqlPNNDILYREGRNDLNRTTYTPRLLSVDLSGTLGHLPVTG 84
Cdd:cd06060   1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPDH--DVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379  85 ELYGNFVQrdeellplstgeeleqvrkraEESGVCSPEQLEVQEQSKASISEYQRDLL------------KNAVVPEKNY 152
Cdd:cd06060  79 ALYEEPDD---------------------DSSESQWWGDVETHVQEPIEKNEFQQDLEeeetyqvelesqSTAEDGDKVY 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 153 QLAATANSWVDFLYARYHPRTLNVLPGLIRDPTAQALGTYSAGTEMWQEVSFNEEFCDRIRLYVEECDGLQGFHVLFDID 232
Cdd:cd06060 138 LLEESVRVWSDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEECDSLQGFQILVDTD 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 233 DGFGGLAGKCLEHLNDEYSRASFALPLHYPRITSYPQADTRlshSIRVVNNVLGYHQLSEQALMFTPLSTLETIWRNNNl 312
Cdd:cd06060 218 DGFGGVAAKLLENLRDEYGKKSILTPGLSPASPPDPDSQRR---IKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPG- 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 313 KSRSLPGLQWetDNLYQTSALLAAFFDTATLSYRLRQTPESLLRFCECVTPAGRKMTAAGLALPFGLREGQDLIEFLDQS 392
Cdd:cd06060 294 WPRTFPHLDY--SSPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDL 371
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 393 GDHallTQLTPGCEPGTSYVVQSVTARGIPAERLKRPrelagDQLRMAAYSCDSISHMLQLYYQCTYHGSVTNAAATPLP 472
Cdd:cd06060 372 LGD---LSLTPSCQNETDVFAQSVVLRGIPESRLKSP-----LQPRSPASRCSSVEEVLEGYLQCTFPGSSSAVTTLPQP 443
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 473 LKTQLPFPYEMFAAgISRDGYRLPEGAERETgsRVDSAPMLAAVQNSTKLGEHLDNVHAQSHRVQLAKLQAYSNSG-LER 551
Cdd:cd06060 444 LPVPTPFPSIFSPS-LGRKGFLLDDSRPASL--DVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGGgLER 520
                       570
                ....*....|....*....
gi 17737379 552 DEYDTALDQLLEFRDLYAD 570
Cdd:cd06060 521 DEFKESLEELLSLADCYGD 539
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
5-570 0e+00

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: 571.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379   5 REILTFQFGTYANYVGTHFWNQQEANFRYGDESEQVAEEqlPNNDILYREGRNDLNRTTYTPRLLSVDLSGTLGHLPVTG 84
Cdd:cd06060   1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPDH--DVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379  85 ELYGNFVQrdeellplstgeeleqvrkraEESGVCSPEQLEVQEQSKASISEYQRDLL------------KNAVVPEKNY 152
Cdd:cd06060  79 ALYEEPDD---------------------DSSESQWWGDVETHVQEPIEKNEFQQDLEeeetyqvelesqSTAEDGDKVY 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 153 QLAATANSWVDFLYARYHPRTLNVLPGLIRDPTAQALGTYSAGTEMWQEVSFNEEFCDRIRLYVEECDGLQGFHVLFDID 232
Cdd:cd06060 138 LLEESVRVWSDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEECDSLQGFQILVDTD 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 233 DGFGGLAGKCLEHLNDEYSRASFALPLHYPRITSYPQADTRlshSIRVVNNVLGYHQLSEQALMFTPLSTLETIWRNNNl 312
Cdd:cd06060 218 DGFGGVAAKLLENLRDEYGKKSILTPGLSPASPPDPDSQRR---IKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPG- 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 313 KSRSLPGLQWetDNLYQTSALLAAFFDTATLSYRLRQTPESLLRFCECVTPAGRKMTAAGLALPFGLREGQDLIEFLDQS 392
Cdd:cd06060 294 WPRTFPHLDY--SSPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDL 371
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 393 GDHallTQLTPGCEPGTSYVVQSVTARGIPAERLKRPrelagDQLRMAAYSCDSISHMLQLYYQCTYHGSVTNAAATPLP 472
Cdd:cd06060 372 LGD---LSLTPSCQNETDVFAQSVVLRGIPESRLKSP-----LQPRSPASRCSSVEEVLEGYLQCTFPGSSSAVTTLPQP 443
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 473 LKTQLPFPYEMFAAgISRDGYRLPEGAERETgsRVDSAPMLAAVQNSTKLGEHLDNVHAQSHRVQLAKLQAYSNSG-LER 551
Cdd:cd06060 444 LPVPTPFPSIFSPS-LGRKGFLLDDSRPASL--DVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGGgLER 520
                       570
                ....*....|....*....
gi 17737379 552 DEYDTALDQLLEFRDLYAD 570
Cdd:cd06060 521 DEFKESLEELLSLADCYGD 539
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
5-143 5.04e-44

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 organizms. 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 characteriztic 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: 431412 [Multi-domain]  Cd Length: 115  Bit Score: 152.02  E-value: 5.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379     5 REILTFQFGTYANYVGTHFWNQQEANFRYGDESEqvaEEQLpNNDILYREGRNDLNRTTYTPRLLSVDLSGTLGHLPVTG 84
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWNTQESYFTYDPNEE---PSEV-DHDVLFREGETLDGQVTYTPRLLIYDLKGSFGSLRKEG 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379    85 ELYGnfvqrdeellplstgeeleqvRKRAEESGVCSPE-QLEVQEQSKASISEYQRDLLK 143
Cdd:pfam10644  77 ALYE---------------------LNESAGSNAATWDgKVVVQRQPPIEKSEYQQSLDK 115
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
188-297 5.77e-06

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 48.94  E-value: 5.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379  188 ALGTYSAGTEMWqevsfneEFC-DRIRLYVEECDGLQGFHVLFDIDDGFG-GLAGKCLEHLNDEY---SRASFALplhYP 262
Cdd:PTZ00335 104 ARGHYTIGKEIV-------DLClDRIRKLADNCTGLQGFLVFHAVGGGTGsGLGSLLLERLSVDYgkkSKLGFTI---YP 173
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 17737379  263 ritsYPQADTRLshsIRVVNNVLGYHQLSEQ---ALMF 297
Cdd:PTZ00335 174 ----SPQVSTAV---VEPYNSVLSTHSLLEHtdvAVML 204
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
5-570 0e+00

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: 571.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379   5 REILTFQFGTYANYVGTHFWNQQEANFRYGDESEQVAEEqlPNNDILYREGRNDLNRTTYTPRLLSVDLSGTLGHLPVTG 84
Cdd:cd06060   1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPDH--DVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379  85 ELYGNFVQrdeellplstgeeleqvrkraEESGVCSPEQLEVQEQSKASISEYQRDLL------------KNAVVPEKNY 152
Cdd:cd06060  79 ALYEEPDD---------------------DSSESQWWGDVETHVQEPIEKNEFQQDLEeeetyqvelesqSTAEDGDKVY 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 153 QLAATANSWVDFLYARYHPRTLNVLPGLIRDPTAQALGTYSAGTEMWQEVSFNEEFCDRIRLYVEECDGLQGFHVLFDID 232
Cdd:cd06060 138 LLEESVRVWSDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEECDSLQGFQILVDTD 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 233 DGFGGLAGKCLEHLNDEYSRASFALPLHYPRITSYPQADTRlshSIRVVNNVLGYHQLSEQALMFTPLSTLETIWRNNNl 312
Cdd:cd06060 218 DGFGGVAAKLLENLRDEYGKKSILTPGLSPASPPDPDSQRR---IKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPG- 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 313 KSRSLPGLQWetDNLYQTSALLAAFFDTATLSYRLRQTPESLLRFCECVTPAGRKMTAAGLALPFGLREGQDLIEFLDQS 392
Cdd:cd06060 294 WPRTFPHLDY--SSPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDL 371
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 393 GDHallTQLTPGCEPGTSYVVQSVTARGIPAERLKRPrelagDQLRMAAYSCDSISHMLQLYYQCTYHGSVTNAAATPLP 472
Cdd:cd06060 372 LGD---LSLTPSCQNETDVFAQSVVLRGIPESRLKSP-----LQPRSPASRCSSVEEVLEGYLQCTFPGSSSAVTTLPQP 443
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 473 LKTQLPFPYEMFAAgISRDGYRLPEGAERETgsRVDSAPMLAAVQNSTKLGEHLDNVHAQSHRVQLAKLQAYSNSG-LER 551
Cdd:cd06060 444 LPVPTPFPSIFSPS-LGRKGFLLDDSRPASL--DVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGGgLER 520
                       570
                ....*....|....*....
gi 17737379 552 DEYDTALDQLLEFRDLYAD 570
Cdd:cd06060 521 DEFKESLEELLSLADCYGD 539
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
5-143 5.04e-44

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 organizms. 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 characteriztic 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: 431412 [Multi-domain]  Cd Length: 115  Bit Score: 152.02  E-value: 5.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379     5 REILTFQFGTYANYVGTHFWNQQEANFRYGDESEqvaEEQLpNNDILYREGRNDLNRTTYTPRLLSVDLSGTLGHLPVTG 84
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWNTQESYFTYDPNEE---PSEV-DHDVLFREGETLDGQVTYTPRLLIYDLKGSFGSLRKEG 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379    85 ELYGnfvqrdeellplstgeeleqvRKRAEESGVCSPE-QLEVQEQSKASISEYQRDLLK 143
Cdd:pfam10644  77 ALYE---------------------LNESAGSNAATWDgKVVVQRQPPIEKSEYQQSLDK 115
Tubulin_3 pfam14881
Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the ...
161-347 3.40e-19

Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Misato from Drosophila and Dml1p from fungi are descendants of an ancestral tubulin-like protein, and exhibit regions with similarity to members of a GTPase family that includes eukaryotic tubulin and prokaryotic FtsZ. Dml1p and Misato have been co-opted into a role in mtDNA inheritance in yeast, and into a cell division-related mechanism in flies, respectively. Dml1p might additionally function in the partitioning of the mitochondrial organelle itself, or in the segregation of chromosomes, thereby explaining its essential requirement. This domain subject to extensive post-translational modifications.


Pssm-ID: 434281 [Multi-domain]  Cd Length: 180  Bit Score: 85.51  E-value: 3.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379   161 WVDFLYARYHPRTLNVLPGLIRDPTAQALGTYSAGTEMWQEVSFNEEFCDR-IRLYVEECDGLQGFHVLFDIDDGFGGLA 239
Cdd:pfam14881  12 WSDFNRVFYHPRSIVQLNEYELNSQLMPFEDWSVGEELFRELDKEHDLLDRdLRPFAEECDQLQGLQVFTGSDDAWGGFA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379   240 GKCLEHLNDEYSRAS--FALPLHYPRITsypQADTRLSHSIRVVNNVLGYHQLSEQALMFTPLSTLetiwrnnnlksrSL 317
Cdd:pfam14881  92 ARYLERLRDEYGKKSiiWVWALQDPLKR---IRRTKRERRLRLANKARSLQSLSPQASLYVPIATL------------SD 156
                         170       180       190
                  ....*....|....*....|....*....|
gi 17737379   318 PGLQWetdnlyQTSALLAAFFDTATLSYRL 347
Cdd:pfam14881 157 GQSEW------HTSALLSSAIESATLPSRL 180
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
210-294 3.13e-09

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: 59.14  E-value: 3.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 210 DRIRLYVEECDGLQGFHVLFDIDDGFG-GLAGKCLEHLNDEYSRAsfalplhyPRITS--YPQADtrlsHSIRVV---NN 283
Cdd:cd06059  79 DRIRKQVEKCDSLQGFFILHSLGGGTGsGLGSYLLELLEDEYPKV--------YRFTFsvFPSPD----DDNVITspyNS 146
                        90
                ....*....|.
gi 17737379 284 VLGYHQLSEQA 294
Cdd:cd06059 147 VLALNHLTEHA 157
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
188-294 1.24e-07

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: 53.95  E-value: 1.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 188 ALGTYSAGTEmwqevsFNEEFCDRIRLYVEECDGLQGFHVLFDIDDGFG-GLAGKCLEHLNDEYSRAsfalpLHYPRITs 266
Cdd:cd00286  63 AKGHSVAGEE------YQEEILDAIRKEVEECDELQGFFITHSLGGGTGsGLGPLLAERLKDEYPNR-----LVVTFSI- 130
                        90       100
                ....*....|....*....|....*...
gi 17737379 267 YPQADTRLshSIRVVNNVLGYHQLSEQA 294
Cdd:cd00286 131 LPGPDEGV--IVYPYNAALTLKTLTEHA 156
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
5-294 3.60e-06

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: 49.49  E-value: 3.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379   5 REILTFQFGTYANYVGTHFWNQ--QEANFRYGDESEQVAEEQLPNNDILYREGRNDlnrtTYTPRLLSVDLS-GTLGhlP 81
Cdd:cd02187   1 REIIHIQIGQCGNQIGAKFWETisKEHGIDPDGTYKGDSDLQLERINVYFNEASGG----KYVPRAVLVDLEpGTID--S 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379  82 VTGELYGNFVQRDeellPLSTGeeleqvrkraeesgvcspeqlevqeQSKASiseyqrdllknavvpeknyqlaataNSW 161
Cdd:cd02187  75 VRSGPYGQLFRPD----NFVFG-------------------------QSGAG-------------------------NNW 100
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 162 vdflyaryhprtlnvlpglirdptaqALGTYSAGTEMWQEVSfneefcDRIRLYVEECDGLQGFHVLFDIDDGFG-GLAG 240
Cdd:cd02187 101 --------------------------AKGHYTEGAELIDSVL------DVVRKEAESCDCLQGFQLTHSLGGGTGsGLGT 148
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17737379 241 KCLEHLNDEYSRasfalplhypRITS----YPQADTrlshSIRVV---NNVLGYHQLSEQA 294
Cdd:cd02187 149 LLLSKLREEYPD----------RIMStfsvLPSPKV----SDTVVepyNAVLSLHQLVENA 195
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
188-292 5.39e-06

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: 49.07  E-value: 5.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 188 ALGTYSAGtemwQEVSfnEEFCDRIRLYVEECDGLQGFHVLFDIDDGFG-GLAGKCLEHLNDEY---SRASFALplhYPr 263
Cdd:cd02186 103 ARGYYTIG----KEII--DPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGsGLTSLLLERLSVDYgkkSKLEFSI---YP- 172
                        90       100       110
                ....*....|....*....|....*....|..
gi 17737379 264 itsYPQadtrLSHSirVV---NNVLGYHQLSE 292
Cdd:cd02186 173 ---SPQ----VSTS--VVepyNSVLTTHSLLE 195
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
188-297 5.77e-06

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 48.94  E-value: 5.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379  188 ALGTYSAGTEMWqevsfneEFC-DRIRLYVEECDGLQGFHVLFDIDDGFG-GLAGKCLEHLNDEY---SRASFALplhYP 262
Cdd:PTZ00335 104 ARGHYTIGKEIV-------DLClDRIRKLADNCTGLQGFLVFHAVGGGTGsGLGSLLLERLSVDYgkkSKLGFTI---YP 173
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 17737379  263 ritsYPQADTRLshsIRVVNNVLGYHQLSEQ---ALMF 297
Cdd:PTZ00335 174 ----SPQVSTAV---VEPYNSVLSTHSLLEHtdvAVML 204
PLN00221 PLN00221
tubulin alpha chain; Provisional
188-292 3.29e-04

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 43.26  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379  188 ALGTYSAGTEMwqevsfnEEFC-DRIRLYVEECDGLQGFHVLFDIDDGFG-GLAGKCLEHLNDEYSRAS---FALplhYP 262
Cdd:PLN00221 104 ARGHYTIGKEI-------VDLClDRIRKLADNCTGLQGFLVFNAVGGGTGsGLGSLLLERLSVDYGKKSklgFTV---YP 173
                         90       100       110
                 ....*....|....*....|....*....|
gi 17737379  263 RitsyPQADTRLshsIRVVNNVLGYHQLSE 292
Cdd:PLN00221 174 S----PQVSTAV---VEPYNSVLSTHSLLE 196
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
210-294 8.91e-04

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: 41.84  E-value: 8.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17737379 210 DRIRLYVEECDGLQGFHVLFDIDDGFG-GLAGKCLEHLNDEYsrasfalPLHYpRITS--YPQADTrlshsiRVV----N 282
Cdd:cd02190 124 EKLRRAAEKCDSLQSFFLLHSLGGGTGsGLGSYILELLEDEF-------PDVY-RFVTsvFPSGDD------DVItspyN 189
                        90
                ....*....|..
gi 17737379 283 NVLGYHQLSEQA 294
Cdd:cd02190 190 SVLALRELTEHA 201
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
206-253 3.76e-03

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: 39.94  E-value: 3.76e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17737379 206 EEFCDRIRLYVEECDGLQGFHVLFDIDDGFG-GLAGKCLEHLNDEYSRA 253
Cdd:cd02189 108 EDILEALRREAERCDRLSGFLVLHSLAGGTGsGLGSRVTELLRDEYPKA 156
 
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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