NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|123779929|sp|Q2YDW2|]
View 

RecName: Full=Protein misato homolog 1

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
6-550 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: 606.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929   6 REVLTLQLGHFAGFVGAHWWNQQDAALGRMAEDEESPGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLNTLKEEGNL 85
Cdd:cd06060    1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPDHDVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929  86 YRDR-QLEAAVAWQGKLSTHREDAHPKNPNLQGLLSAEGV----RSSDGAWRAKLIQNIqngkENSIKVWSDFLRVHLHP 160
Cdd:cd06060   81 YEEPdDDSSESQWWGDVETHVQEPIEKNEFQQDLEEEETYqvelESQSTAEDGDKVYLL----EESVRVWSDYLRVYYHP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 161 RSICVIHKYHHDGETGRLEAFGQGESVLKEPRYLEELEDRLHFYVEECDYLQGFQLLCDLHDGFSGVGAKTAELLQDEYA 240
Cdd:cd06060  157 RSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEECDSLQGFQILVDTDDGFGGVAAKLLENLRDEYG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 241 GRGVLTWGLLPGPYSLGEPQKNIYRLLNTAFGLVHLTGYSSFVCPLSLGGNLGLRPKPPVNFPSLHYDatLPFHCSAILA 320
Cdd:cd06060  237 KKSILTPGLSPASPPDPDSQRRIKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPGWPRTFPHLDYS--SPYHTSAVLA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 321 TALDTVTVPYRLRSSMVTMAHLADVLSFSGKKVVTAEAIIPFPLVRGQSLPDILTQLGEATpwtsLSACGDSAGHRCFAQ 400
Cdd:cd06060  315 AALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDLLGDL----SLTPSCQNETDVFAQ 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 401 SVVLRGIDRASHTSKLNPgtplPSALHACASGEEVLAQYLQQQHPRVLSSSHLLLTPCKVAPPYPHFFSSF--SQKGLAM 478
Cdd:cd06060  391 SVVLRGIPESRLKSPLQP----RSPASRCSSVEEVLEGYLQCTFPGSSSAVTTLPQPLPVPTPFPSIFSPSlgRKGFLLD 466
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123779929 479 DSTPKGAAVQSIPVFGALRSTSSLHRTLGDLAEELSRLDLRRWASFMDAG-VEQDDMEEMLHELHRLAQCYQE 550
Cdd:cd06060  467 DSRPASLDVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGGgLERDEFKESLEELLSLADCYGD 539
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
6-550 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: 606.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929   6 REVLTLQLGHFAGFVGAHWWNQQDAALGRMAEDEESPGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLNTLKEEGNL 85
Cdd:cd06060    1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPDHDVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929  86 YRDR-QLEAAVAWQGKLSTHREDAHPKNPNLQGLLSAEGV----RSSDGAWRAKLIQNIqngkENSIKVWSDFLRVHLHP 160
Cdd:cd06060   81 YEEPdDDSSESQWWGDVETHVQEPIEKNEFQQDLEEEETYqvelESQSTAEDGDKVYLL----EESVRVWSDYLRVYYHP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 161 RSICVIHKYHHDGETGRLEAFGQGESVLKEPRYLEELEDRLHFYVEECDYLQGFQLLCDLHDGFSGVGAKTAELLQDEYA 240
Cdd:cd06060  157 RSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEECDSLQGFQILVDTDDGFGGVAAKLLENLRDEYG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 241 GRGVLTWGLLPGPYSLGEPQKNIYRLLNTAFGLVHLTGYSSFVCPLSLGGNLGLRPKPPVNFPSLHYDatLPFHCSAILA 320
Cdd:cd06060  237 KKSILTPGLSPASPPDPDSQRRIKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPGWPRTFPHLDYS--SPYHTSAVLA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 321 TALDTVTVPYRLRSSMVTMAHLADVLSFSGKKVVTAEAIIPFPLVRGQSLPDILTQLGEATpwtsLSACGDSAGHRCFAQ 400
Cdd:cd06060  315 AALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDLLGDL----SLTPSCQNETDVFAQ 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 401 SVVLRGIDRASHTSKLNPgtplPSALHACASGEEVLAQYLQQQHPRVLSSSHLLLTPCKVAPPYPHFFSSF--SQKGLAM 478
Cdd:cd06060  391 SVVLRGIPESRLKSPLQP----RSPASRCSSVEEVLEGYLQCTFPGSSSAVTTLPQPLPVPTPFPSIFSPSlgRKGFLLD 466
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123779929 479 DSTPKGAAVQSIPVFGALRSTSSLHRTLGDLAEELSRLDLRRWASFMDAG-VEQDDMEEMLHELHRLAQCYQE 550
Cdd:cd06060  467 DSRPASLDVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGGgLERDEFKESLEELLSLADCYGD 539
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
6-118 3.26e-39

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: 138.92  E-value: 3.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929    6 REVLTLQLGHFAGFVGAHWWNQQDAALgrMAEDEESPGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLNTLKEEGNL 85
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWNTQESYF--TYDPNEEPSEVDHDVLFREGETLDGQVTYTPRLLIYDLKGSFGSLRKEGAL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 123779929   86 Y--RDRQLEAAVAWQGKLSTHREDAHPKNPNLQGL 118
Cdd:pfam10644  79 YelNESAGSNAATWDGKVVVQRQPPIEKSEYQQSL 113
PTZ00387 PTZ00387
epsilon tubulin; Provisional
191-239 1.03e-03

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 41.63  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 123779929 191 PRYLEELEDRLHFYVEECDYLQGFQLLCDLHDGF-SGVGAKTAELLQDEY 239
Cdd:PTZ00387 111 DKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTgSGLGTRILGMLEDEF 160
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
6-550 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: 606.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929   6 REVLTLQLGHFAGFVGAHWWNQQDAALGRMAEDEESPGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLNTLKEEGNL 85
Cdd:cd06060    1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPDHDVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929  86 YRDR-QLEAAVAWQGKLSTHREDAHPKNPNLQGLLSAEGV----RSSDGAWRAKLIQNIqngkENSIKVWSDFLRVHLHP 160
Cdd:cd06060   81 YEEPdDDSSESQWWGDVETHVQEPIEKNEFQQDLEEEETYqvelESQSTAEDGDKVYLL----EESVRVWSDYLRVYYHP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 161 RSICVIHKYHHDGETGRLEAFGQGESVLKEPRYLEELEDRLHFYVEECDYLQGFQLLCDLHDGFSGVGAKTAELLQDEYA 240
Cdd:cd06060  157 RSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEECDSLQGFQILVDTDDGFGGVAAKLLENLRDEYG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 241 GRGVLTWGLLPGPYSLGEPQKNIYRLLNTAFGLVHLTGYSSFVCPLSLGGNLGLRPKPPVNFPSLHYDatLPFHCSAILA 320
Cdd:cd06060  237 KKSILTPGLSPASPPDPDSQRRIKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPGWPRTFPHLDYS--SPYHTSAVLA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 321 TALDTVTVPYRLRSSMVTMAHLADVLSFSGKKVVTAEAIIPFPLVRGQSLPDILTQLGEATpwtsLSACGDSAGHRCFAQ 400
Cdd:cd06060  315 AALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDLLGDL----SLTPSCQNETDVFAQ 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 401 SVVLRGIDRASHTSKLNPgtplPSALHACASGEEVLAQYLQQQHPRVLSSSHLLLTPCKVAPPYPHFFSSF--SQKGLAM 478
Cdd:cd06060  391 SVVLRGIPESRLKSPLQP----RSPASRCSSVEEVLEGYLQCTFPGSSSAVTTLPQPLPVPTPFPSIFSPSlgRKGFLLD 466
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123779929 479 DSTPKGAAVQSIPVFGALRSTSSLHRTLGDLAEELSRLDLRRWASFMDAG-VEQDDMEEMLHELHRLAQCYQE 550
Cdd:cd06060  467 DSRPASLDVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGGgLERDEFKESLEELLSLADCYGD 539
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
154-499 3.64e-75

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: 241.54  E-value: 3.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 154 LRVHLHPRSICVIHKYHhdgetGRLEAFGQGESVLkEPRYLEELEDRLHFYVEECDYLQGFQLLCDLHDG-FSGVGAKTA 232
Cdd:cd00286   40 LRQLFHPENIILIQKYH-----GAGNNWAKGHSVA-GEEYQEEILDAIRKEVEECDELQGFFITHSLGGGtGSGLGPLLA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 233 ELLQDEYAGRGVLTWGLLPGPYslgepQKNIYRLLNTAFGLVHLTGYSSFVCPLSLGGNLGLRPKPpvnfpsLHYDATLP 312
Cdd:cd00286  114 ERLKDEYPNRLVVTFSILPGPD-----EGVIVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRP------LHIDAPAY 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 313 FHCSAILATALDTVTVPYRLRSSMVTMAHLAdvlsfsgkkvvtaeAIIPFPLVRGQSLPDILTQLGEATPWTSLSACGDS 392
Cdd:cd00286  183 DHINELVAQRLGSLTEALRFEGSLNVDLREL--------------AENLVPLPRGHFLMLGYAPLDSATSATPRSLRVKE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 393 AGHRCFAQSVVLRGidrashtsklnpgtplpsalHACASGEEVLAQYLQQQhPRVLSSSHLLLTPCKVAPPYPHFFsSFS 472
Cdd:cd00286  249 LTRRAFLPANLLVG--------------------CDPDHGEAIAALLVIRG-PPDLSSKEVERAIARVKETLGHLF-SWS 306
                        330       340
                 ....*....|....*....|....*..
gi 123779929 473 QKGLAMDSTPKGAAvQSIPVFGALRST 499
Cdd:cd00286  307 PAGVKTGISPKPPA-EGEVSVLALLNS 332
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
154-550 5.32e-67

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: 222.08  E-value: 5.32e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 154 LRVHLHPRSICVihkyhhdGETGRLEAFGQGESVLKePRYLEELEDRLHFYVEECDYLQGFQLLCDLHDG-FSGVGAKTA 232
Cdd:cd06059   42 LGQLFDPNQFVT-------GVSGAGNNWAVGYYVYG-PKYIESILDRIRKQVEKCDSLQGFFILHSLGGGtGSGLGSYLL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 233 ELLQDEYAGRGVLTWGLLPGPYSLGepqkNIYRLLNTAFGLVHLTGYSSFVCPLSLGGNLGLRPKPPVNfpsLHYDATLP 312
Cdd:cd06059  114 ELLEDEYPKVYRFTFSVFPSPDDDN----VITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRQPAT---LDIDFPPF 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 313 FHCSAILATALDTVTVPYRLRSSMvtMAHLADVLSfsgkkvvtaeAIIPFPlvRGQSLPDILTQLGEATPWTSLSACGDS 392
Cdd:cd06059  187 DDMNNLVAQLLSSLTSSLRFEGSL--NVDLNEITT----------NLVPFP--RLHFLLPSLSPLTSANDVTLEPLTLDQ 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 393 AGHRCFAQSVVLRGIDrashtsklnPGTPLPsalHACAsgeevlaqYLQQQhpRVLSSSHLLLTPCKVAPPYPhfFSSFS 472
Cdd:cd06059  253 LFSDLFSKDNQLVGCD---------PRHGTY---LACA--------LLLRG--KVFSLSDVRRNIDRIKPKLK--FISWN 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 473 QKGLAMDSTPKgAAVQSIPVFGALRSTSSLHRTLGDLAEELSRLDLRRWASFMDAGV--EQDDMEEMLHELHRLAQCYQE 550
Cdd:cd06059  309 PDGFKVGLCSV-PPVGQKYSLLFLSNNTSIASTFERLIERFDKLYKRKAFLHHYTGEgmEEGDFSEARESLANLIQEYQE 387
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
6-118 3.26e-39

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: 138.92  E-value: 3.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929    6 REVLTLQLGHFAGFVGAHWWNQQDAALgrMAEDEESPGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLNTLKEEGNL 85
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWNTQESYF--TYDPNEEPSEVDHDVLFREGETLDGQVTYTPRLLIYDLKGSFGSLRKEGAL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 123779929   86 Y--RDRQLEAAVAWQGKLSTHREDAHPKNPNLQGL 118
Cdd:pfam10644  79 YelNESAGSNAATWDGKVVVQRQPPIEKSEYQQSL 113
Tubulin_3 pfam14881
Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the ...
146-332 1.77e-24

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: 100.53  E-value: 1.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929  146 SIKVWSDFLRVHLHPRSICVIHKYHHDGETGRLEAFGQGESVLKEPRYLEELEDR-LHFYVEECDYLQGFQLLCDLHDGF 224
Cdd:pfam14881   8 TVRYWSDFNRVFYHPRSIVQLNEYELNSQLMPFEDWSVGEELFRELDKEHDLLDRdLRPFAEECDQLQGLQVFTGSDDAW 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929  225 SGVGAKTAELLQDEYAGRGVL-TWGL-LPGPYSLGEPQKNIYRLLNTAFGLVHLTGYSSFVCPLSLggnlglrpkppvnf 302
Cdd:pfam14881  88 GGFAARYLERLRDEYGKKSIIwVWALqDPLKRIRRTKRERRLRLANKARSLQSLSPQASLYVPIAT-------------- 153
                         170       180       190
                  ....*....|....*....|....*....|
gi 123779929  303 PSlhyDATLPFHCSAILATALDTVTVPYRL 332
Cdd:pfam14881 154 LS---DGQSEWHTSALLSSAIESATLPSRL 180
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
191-418 8.42e-07

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: 51.50  E-value: 8.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 191 PRYLEELEDRLHFYVEECDYLQGFQLLCDLHDGF-SGVGAKTAELLQDEYAGRGVLT---WgllpgPYSLGE-PQKNiyr 265
Cdd:cd02189  104 PSLLEDILEALRREAERCDRLSGFLVLHSLAGGTgSGLGSRVTELLRDEYPKAYLLNtvvW-----PYSSGEvPVQN--- 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 266 lLNTAFGLVHLTGYSSFVCPLS-------LGGNLGLrpKPPVNFPSL-HYDATLpfhcsaiLATAL---DTVTVPYRLRS 334
Cdd:cd02189  176 -YNTLLTLSHLQESSDGILLFEnddlhkiCSKLLGL--KNPVSFSDInRVIARQ-------LAGVLlpsSSPTSPSPLRR 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 335 SmvtmaHLADVLS----------FSGKKV-VTAEAIIPFPLVRGQSLPDILTQ-------LGEATPWTSLSACGDSAGHR 396
Cdd:cd02189  246 C-----PLGDLLEhlcphpayklLTLRSLpQMPEPSRAFSTYTWPSLLKRLRQmlitgakLEEGIDWQLLDTSGSHNPNK 320
                        250       260
                 ....*....|....*....|...
gi 123779929 397 CFAQSVVLRGIDRAS-HTSKLNP 418
Cdd:cd02189  321 SLAALLVLRGKDAMKvHSADLSA 343
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
191-287 2.74e-06

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: 49.93  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 191 PRYLEELEDRLHFYVEECDYLQGFQLLCDLHDGF-SGVGAKTAELLQDEYAGRGVLTWGLLP--------GPYslgepqk 261
Cdd:cd02190  116 PQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTgSGLGSYILELLEDEFPDVYRFVTSVFPsgdddvitSPY------- 188
                         90       100
                 ....*....|....*....|....*.
gi 123779929 262 niyrllNTAFGLVHLTGYSSFVCPLS 287
Cdd:cd02190  189 ------NSVLALRELTEHADCVLPVE 208
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
191-283 8.66e-06

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: 46.44  E-value: 8.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929  191 PRYLEELEDRLHFYVEECDYLQGFQLLCDLHDGF-SGVGAKTAELLQDEYAGR---GVLTWgllpgPYSLGEpqkNIYRL 266
Cdd:pfam00091  89 REAAEESLEEIRKEVEGCDMLQGFFITASLGGGTgSGAAPVIAEILKELYPGAltvAVVTF-----PFGFSE---GVVRP 160
                          90
                  ....*....|....*..
gi 123779929  267 LNTAFGLVHLTGYSSFV 283
Cdd:pfam00091 161 YNAILGLKELIEHSDSV 177
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
191-283 1.68e-05

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: 47.18  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123779929 191 PRYLEELEDRLHFYVEECDYLQGFQLLCDLHDGF-SGVGAKTAELLQDEYAGRGVLTWGLLPGPySLGEPQKNIYrllNT 269
Cdd:cd02187  109 AELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTgSGLGTLLLSKLREEYPDRIMSTFSVLPSP-KVSDTVVEPY---NA 184
                         90
                 ....*....|....
gi 123779929 270 AFGLVHLTGYSSFV 283
Cdd:cd02187  185 VLSLHQLVENADET 198
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
192-253 8.60e-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: 41.75  E-value: 8.60e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123779929 192 RYLEELEDRLHFYVEECDYLQGFQLLCDLHDGF-SGVGAKTAELLQDEYAGRGVLTWGLLPGP 253
Cdd:cd02186  112 EIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTgSGLTSLLLERLSVDYGKKSKLEFSIYPSP 174
PTZ00387 PTZ00387
epsilon tubulin; Provisional
191-239 1.03e-03

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 41.63  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 123779929 191 PRYLEELEDRLHFYVEECDYLQGFQLLCDLHDGF-SGVGAKTAELLQDEY 239
Cdd:PTZ00387 111 DKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTgSGLGTRILGMLEDEF 160
PTZ00010 PTZ00010
tubulin beta chain; Provisional
191-253 8.37e-03

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 38.99  E-value: 8.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123779929 191 PRYLEELEDRLHFYVEECDYLQGFQLLCDLHDGF-SGVGAKTAELLQDEYAGRGVLTWGLLPGP 253
Cdd:PTZ00010 110 AELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTgSGMGTLLISKLREEYPDRIMMTFSVFPSP 173
 
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