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Conserved domains on  [gi|41054049|ref|NP_956181|]
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protein misato homolog 1 [Danio rerio]

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 ...
6-577 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: 622.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049   6 REVVTLQLGHYSNFIGTHWWNLQDAGLVYDADVPAG--ELQSDVLFREGLTLAGHVTYTPRLIAIDLKGSLQTLRKEGSL 83
Cdd:cd06060   1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPpdHDVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEGAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049  84 YDTENENSAFT-WDGQIMTHQESPPSKNRFLQELDNLDTGGVLAEPDfnhltssvdncsvpgasvavetinSSLERIQKS 162
Cdd:cd06060  81 YEEPDDDSSESqWWGDVETHVQEPIEKNEFQQDLEEEETYQVELESQ------------------------STAEDGDKV 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 163 YRLEGSVRVWSDFLRLHLHPRTISVINQYNHDGESERLEVFGQGEALLQGQV-LEDLEDRLHFFIEECDYLQGFQVLCDL 241
Cdd:cd06060 137 YLLEESVRVWSDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEeLEEFEDRLRFFVEECDSLQGFQILVDT 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 242 TDGFSGLGSKVTEYLQDSYGGRGILTWGVAPVNHPDTSSMKDLYHMMNCALGTLQMANHSSLFCPLTLRGGLCRRPPPPT 321
Cdd:cd06060 217 DDGFGGVAAKLLENLRDEYGKKSILTPGLSPASPPDPDSQRRIKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPGWPR 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 322 AFPLLNCDplLWYHSSSVLALALDALTVSYRMRHCSATMWQLSDALTTSGRKVVSAYGSVPFPMMLGGCLPDALDAFSna 401
Cdd:cd06060 297 TFPHLDYS--SPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDLL-- 372
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 402 vpwRSLSACPEISDRRFCFSQSVTLKGVDEQSLVSRLLPgmeaPSPLHYERSGEDVLSAYVRSHYPSSPLAVQLVSSGSK 481
Cdd:cd06060 373 ---GDLSLTPSCQNETDVFAQSVVLRGIPESRLKSPLQP----RSPASRCSSVEEVLEGYLQCTFPGSSSAVTTLPQPLP 445
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 482 VTPPFPQIFSPSLSAQGFLQSHSTPASpscPPVSCLPVLTSLQSSPAVGLQLSELQRACASLDLRRVAPSFLTHGPEHAE 561
Cdd:cd06060 446 VPTPFPSIFSPSLGRKGFLLDDSRPAS---LDVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGGGLERDE 522
                       570
                ....*....|....*.
gi 41054049 562 ISEYLEQLRNLAHCYR 577
Cdd:cd06060 523 FKESLEELLSLADCYG 538
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
6-577 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: 622.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049   6 REVVTLQLGHYSNFIGTHWWNLQDAGLVYDADVPAG--ELQSDVLFREGLTLAGHVTYTPRLIAIDLKGSLQTLRKEGSL 83
Cdd:cd06060   1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPpdHDVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEGAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049  84 YDTENENSAFT-WDGQIMTHQESPPSKNRFLQELDNLDTGGVLAEPDfnhltssvdncsvpgasvavetinSSLERIQKS 162
Cdd:cd06060  81 YEEPDDDSSESqWWGDVETHVQEPIEKNEFQQDLEEEETYQVELESQ------------------------STAEDGDKV 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 163 YRLEGSVRVWSDFLRLHLHPRTISVINQYNHDGESERLEVFGQGEALLQGQV-LEDLEDRLHFFIEECDYLQGFQVLCDL 241
Cdd:cd06060 137 YLLEESVRVWSDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEeLEEFEDRLRFFVEECDSLQGFQILVDT 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 242 TDGFSGLGSKVTEYLQDSYGGRGILTWGVAPVNHPDTSSMKDLYHMMNCALGTLQMANHSSLFCPLTLRGGLCRRPPPPT 321
Cdd:cd06060 217 DDGFGGVAAKLLENLRDEYGKKSILTPGLSPASPPDPDSQRRIKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPGWPR 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 322 AFPLLNCDplLWYHSSSVLALALDALTVSYRMRHCSATMWQLSDALTTSGRKVVSAYGSVPFPMMLGGCLPDALDAFSna 401
Cdd:cd06060 297 TFPHLDYS--SPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDLL-- 372
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 402 vpwRSLSACPEISDRRFCFSQSVTLKGVDEQSLVSRLLPgmeaPSPLHYERSGEDVLSAYVRSHYPSSPLAVQLVSSGSK 481
Cdd:cd06060 373 ---GDLSLTPSCQNETDVFAQSVVLRGIPESRLKSPLQP----RSPASRCSSVEEVLEGYLQCTFPGSSSAVTTLPQPLP 445
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 482 VTPPFPQIFSPSLSAQGFLQSHSTPASpscPPVSCLPVLTSLQSSPAVGLQLSELQRACASLDLRRVAPSFLTHGPEHAE 561
Cdd:cd06060 446 VPTPFPSIFSPSLGRKGFLLDDSRPAS---LDVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGGGLERDE 522
                       570
                ....*....|....*.
gi 41054049 562 ISEYLEQLRNLAHCYR 577
Cdd:cd06060 523 FKESLEELLSLADCYG 538
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
6-117 7.21e-55

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: 181.30  E-value: 7.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049     6 REVVTLQLGHYSNFIGTHWWNLQDAGLVYDADVPAGELQSDVLFREGLTLAGHVTYTPRLIAIDLKGSLQTLRKEGSLYD 85
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWNTQESYFTYDPNEEPSEVDHDVLFREGETLDGQVTYTPRLLIYDLKGSFGSLRKEGALYE 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 41054049    86 T--ENENSAFTWDGQIMTHQESPPSKNRFLQELD 117
Cdd:pfam10644  81 LneSAGSNAATWDGKVVVQRQPPIEKSEYQQSLD 114
PLN00222 PLN00222
tubulin gamma chain; Provisional
6-88 1.34e-03

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 41.37  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049    6 REVVTLQLGHYSNFIGTHWWN-------LQDAGLVYDADVPAGElQSDVLFREgltlAGHVTYTPRLIAIDLK----GSL 74
Cdd:PLN00222   3 REIITLQVGQCGNQIGMEFWKqlclehgISKDGILEDFATQGGD-RKDVFFYQ----ADDEHYIPRALLIDLEprviNGI 77
                         90
                 ....*....|....
gi 41054049   75 QTlRKEGSLYDTEN 88
Cdd:PLN00222  78 QN-SEYRNLYNHEN 90
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
6-577 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: 622.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049   6 REVVTLQLGHYSNFIGTHWWNLQDAGLVYDADVPAG--ELQSDVLFREGLTLAGHVTYTPRLIAIDLKGSLQTLRKEGSL 83
Cdd:cd06060   1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPpdHDVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEGAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049  84 YDTENENSAFT-WDGQIMTHQESPPSKNRFLQELDNLDTGGVLAEPDfnhltssvdncsvpgasvavetinSSLERIQKS 162
Cdd:cd06060  81 YEEPDDDSSESqWWGDVETHVQEPIEKNEFQQDLEEEETYQVELESQ------------------------STAEDGDKV 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 163 YRLEGSVRVWSDFLRLHLHPRTISVINQYNHDGESERLEVFGQGEALLQGQV-LEDLEDRLHFFIEECDYLQGFQVLCDL 241
Cdd:cd06060 137 YLLEESVRVWSDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEeLEEFEDRLRFFVEECDSLQGFQILVDT 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 242 TDGFSGLGSKVTEYLQDSYGGRGILTWGVAPVNHPDTSSMKDLYHMMNCALGTLQMANHSSLFCPLTLRGGLCRRPPPPT 321
Cdd:cd06060 217 DDGFGGVAAKLLENLRDEYGKKSILTPGLSPASPPDPDSQRRIKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPGWPR 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 322 AFPLLNCDplLWYHSSSVLALALDALTVSYRMRHCSATMWQLSDALTTSGRKVVSAYGSVPFPMMLGGCLPDALDAFSna 401
Cdd:cd06060 297 TFPHLDYS--SPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDLL-- 372
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 402 vpwRSLSACPEISDRRFCFSQSVTLKGVDEQSLVSRLLPgmeaPSPLHYERSGEDVLSAYVRSHYPSSPLAVQLVSSGSK 481
Cdd:cd06060 373 ---GDLSLTPSCQNETDVFAQSVVLRGIPESRLKSPLQP----RSPASRCSSVEEVLEGYLQCTFPGSSSAVTTLPQPLP 445
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 482 VTPPFPQIFSPSLSAQGFLQSHSTPASpscPPVSCLPVLTSLQSSPAVGLQLSELQRACASLDLRRVAPSFLTHGPEHAE 561
Cdd:cd06060 446 VPTPFPSIFSPSLGRKGFLLDDSRPAS---LDVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGGGLERDE 522
                       570
                ....*....|....*.
gi 41054049 562 ISEYLEQLRNLAHCYR 577
Cdd:cd06060 523 FKESLEELLSLADCYG 538
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
6-117 7.21e-55

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: 181.30  E-value: 7.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049     6 REVVTLQLGHYSNFIGTHWWNLQDAGLVYDADVPAGELQSDVLFREGLTLAGHVTYTPRLIAIDLKGSLQTLRKEGSLYD 85
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWNTQESYFTYDPNEEPSEVDHDVLFREGETLDGQVTYTPRLLIYDLKGSFGSLRKEGALYE 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 41054049    86 T--ENENSAFTWDGQIMTHQESPPSKNRFLQELD 117
Cdd:pfam10644  81 LneSAGSNAATWDGKVVVQRQPPIEKSEYQQSLD 114
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
165-430 5.74e-27

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: 111.73  E-value: 5.74e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 165 LEGSV--RVWSDFLRLHLHPRTISVINQYNHDGESerlevFGQGEALLQGQVLEDLEDRLHFFIEECDYLQGFQVLCDLT 242
Cdd:cd00286  27 LEPAVldELLSGPLRQLFHPENIILIQKYHGAGNN-----WAKGHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 243 DG-FSGLGSKVTEYLQDSYGGRGILTWGVAPvnHPDTSSmkdLYHMMNCALGTLQMANHSSLFCPLTLRG--GLCRRPPP 319
Cdd:cd00286 102 GGtGSGLGPLLAERLKDEYPNRLVVTFSILP--GPDEGV---IVYPYNAALTLKTLTEHADCLLLVDNEAlyDICPRPLH 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 320 PTAfpllncdpLLWYHSSSVLALALDALTVSYRmrhcsatmwqlSDALTTSGRKVVSAygsVPFPMMLGGCLPDALDAFS 399
Cdd:cd00286 177 IDA--------PAYDHINELVAQRLGSLTEALR-----------FEGSLNVDLRELAE---NLVPLPRGHFLMLGYAPLD 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 41054049 400 NAVPWRSLSACPEISDRRfCFSQSVTLKGVD 430
Cdd:cd00286 235 SATSATPRSLRVKELTRR-AFLPANLLVGCD 264
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
176-578 2.42e-21

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: 96.12  E-value: 2.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 176 LRLHLHPRTISVinqynhdGESERLEVFGQGEALLQGQVLEDLEDRLHFFIEECDYLQGFQVLCDLTDG-FSGLGSKVTE 254
Cdd:cd06059  42 LGQLFDPNQFVT-------GVSGAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGtGSGLGSYLLE 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 255 YLQDSYGGRGILTWGVAPVNHpDTSSMKDLYhmmNCALGTLQMANHSSLFCPLTLRG--GLCRRPPPPtafplLNCDPLL 332
Cdd:cd06059 115 LLEDEYPKVYRFTFSVFPSPD-DDNVITSPY---NSVLALNHLTEHADCVLPIDNEAlyDICNRQPAT-----LDIDFPP 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 333 WYHSSSVLALALDALTVSyrMRHCSATMWQLSDALTtsgrkvvsayGSVPFP---MMLGGCLPdalDAFSNAVPWRSLSA 409
Cdd:cd06059 186 FDDMNNLVAQLLSSLTSS--LRFEGSLNVDLNEITT----------NLVPFPrlhFLLPSLSP---LTSANDVTLEPLTL 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 410 CPEISDrrfCFSQSVTLKGVDeqslvsrllpgmeapsPLHYErsgedVLSA--YVRSHYPSSP---LAVQLVSSGSKVTP 484
Cdd:cd06059 251 DQLFSD---LFSKDNQLVGCD----------------PRHGT-----YLACalLLRGKVFSLSdvrRNIDRIKPKLKFIS 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 485 PFPQIFSPSLSAQgflqshstpaspscPPVSCLPVLTSLQSSPAVGLQLSELQRACASLDLRRvapSFLTH----GPEHA 560
Cdd:cd06059 307 WNPDGFKVGLCSV--------------PPVGQKYSLLFLSNNTSIASTFERLIERFDKLYKRK---AFLHHytgeGMEEG 369
                       410
                ....*....|....*...
gi 41054049 561 EISEYLEQLRNLAHCYRQ 578
Cdd:cd06059 370 DFSEARESLANLIQEYQE 387
Tubulin_3 pfam14881
Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the ...
168-353 1.80e-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: 86.28  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049   168 SVRVWSDFLRLHLHPRTISVINQYNHDGESERLEVFGQGEALLQgqVLE---DLEDR-LHFFIEECDYLQGFQVLCDLTD 243
Cdd:pfam14881   8 TVRYWSDFNRVFYHPRSIVQLNEYELNSQLMPFEDWSVGEELFR--ELDkehDLLDRdLRPFAEECDQLQGLQVFTGSDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049   244 GFSGLGSKVTEYLQDSYGGRGIL-TWGVAPVNHPDTSSMKDLY-HMMNCALGTLQMANHSSLFCPLTLrgglcrrppppt 321
Cdd:pfam14881  86 AWGGFAARYLERLRDEYGKKSIIwVWALQDPLKRIRRTKRERRlRLANKARSLQSLSPQASLYVPIAT------------ 153
                         170       180       190
                  ....*....|....*....|....*....|..
gi 41054049   322 afpLLNCDPlLWyHSSSVLALALDALTVSYRM 353
Cdd:pfam14881 154 ---LSDGQS-EW-HTSALLSSAIESATLPSRL 180
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
213-305 9.72e-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: 48.33  E-value: 9.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 213 QVLEDLEDRLHFFIEECDYLQGFQVLCDLTDGF-SGLGSKVTEYLQDSYGGRGILTWGVAPVnhPDTSSMK-DLYhmmNC 290
Cdd:cd02187 110 ELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTgSGLGTLLLSKLREEYPDRIMSTFSVLPS--PKVSDTVvEPY---NA 184
                        90
                ....*....|....*.
gi 41054049 291 ALGTLQMANHSSL-FC 305
Cdd:cd02187 185 VLSLHQLVENADEtFC 200
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
213-272 1.39e-05

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: 47.65  E-value: 1.39e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41054049 213 QVLEDLEDRLHFFIEECDYLQGFQVLCDLTDGF-SGLGSKVTEYLQDSYGGRGILTWGVAP 272
Cdd:cd02189 105 SLLEDILEALRREAERCDRLSGFLVLHSLAGGTgSGLGSRVTELLRDEYPKAYLLNTVVWP 165
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
213-279 1.07e-04

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: 44.84  E-value: 1.07e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41054049 213 QVLEDLEDRLHFFIEECDYLQGFQVLCDLTDGF-SGLGSKVTEYLQDSYGGRGILTWGVAPVNHPDTS 279
Cdd:cd02186 112 EIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTgSGLTSLLLERLSVDYGKKSKLEFSIYPSPQVSTS 179
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
226-301 2.59e-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: 42.21  E-value: 2.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41054049   226 IEECDYLQGFQVLCDLTDGF-SGLGSKVTEYLQDSYggRGILTwgVAPVNHPDTSSMKDLYhMMNCALGTLQMANHS 301
Cdd:pfam00091 103 VEGCDMLQGFFITASLGGGTgSGAAPVIAEILKELY--PGALT--VAVVTFPFGFSEGVVR-PYNAILGLKELIEHS 174
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
216-307 4.55e-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: 43.00  E-value: 4.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049 216 EDLEDRLHFFIEECDYLQGFQVLCDLTDGF-SGLGSKVTEYLQDSYGGRGILTWGVAPVNHPD--TSSmkdlYhmmNCAL 292
Cdd:cd02190 120 ESILEKLRRAAEKCDSLQSFFLLHSLGGGTgSGLGSYILELLEDEFPDVYRFVTSVFPSGDDDviTSP----Y---NSVL 192
                        90
                ....*....|....*
gi 41054049 293 GTLQMANHSSLFCPL 307
Cdd:cd02190 193 ALRELTEHADCVLPV 207
PLN00222 PLN00222
tubulin gamma chain; Provisional
6-88 1.34e-03

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 41.37  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049    6 REVVTLQLGHYSNFIGTHWWN-------LQDAGLVYDADVPAGElQSDVLFREgltlAGHVTYTPRLIAIDLK----GSL 74
Cdd:PLN00222   3 REIITLQVGQCGNQIGMEFWKqlclehgISKDGILEDFATQGGD-RKDVFFYQ----ADDEHYIPRALLIDLEprviNGI 77
                         90
                 ....*....|....
gi 41054049   75 QTlRKEGSLYDTEN 88
Cdd:PLN00222  78 QN-SEYRNLYNHEN 90
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
6-88 4.42e-03

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: 39.83  E-value: 4.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41054049   6 REVVTLQLGHYSNFIGTHWW-------NLQDAGLVYDADVPAGElQSDVLFREgltlAGHVTYTPRLIAIDLK----GSL 74
Cdd:cd02188   1 REIITLQVGQCGNQIGSEFWkqlcsehGISPDGSLEDFATDGND-RKDVFFYQ----ADDEHYIPRAILLDLEprviNSI 75
                        90
                ....*....|....
gi 41054049  75 QTlRKEGSLYDTEN 88
Cdd:cd02188  76 QN-SPYKNLFNPEN 88
 
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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