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Conserved domains on  [gi|1184725737|ref|NP_001337703|]
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protein misato homolog 1 isoform 6 [Homo sapiens]

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 ...
 6-428 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: 537.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737   6 REVLTLQLGHFAGFVGAHWWNQQDAALGRATDSKEPPGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLSSLKEEGGL 85
Cdd:cd06060     1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPDHDVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEGAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737  86 YRDKQLDAAIAWQ-GKLTTHKEELYPKNPYLQDFLSAEGVLSSDgvwrvksipngkgsSPLPTATTPKPLIPTEASIRVW 164
Cdd:cd06060    81 YEEPDDDSSESQWwGDVETHVQEPIEKNEFQQDLEEEETYQVEL--------------ESQSTAEDGDKVYLLEESVRVW 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 165 SDFLRVHLHPRSICMIQKYNHDGEAGRLEAFGQGESVLKEPKYQEELEDRLHFYVEECDYLQGFQILCDLHDGFSGVGAK 244
Cdd:cd06060   147 SDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEECDSLQGFQILVDTDDGFGGVAAK 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 245 AAELLQDEYSGRGIITWGLLPGPYHRGEAQRNIYRLLNTAFGLVHLTAHSSLVCPLSLGGSLGLRPEPPVSFPYLHYDat 324
Cdd:cd06060   227 LLENLRDEYGKKSILTPGLSPASPPDPDSQRRIKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPGWPRTFPHLDYS-- 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 325 LPFHCSAILATALDTVTVPYRLCSSPVSMVHLADMLSFCGKKVVTAGAIIPFPLAPGQSLPDSLMQFGGATPWTPlsacG 404
Cdd:cd06060   305 SPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDLLGDLSLTP----S 380

                         410       420
                  ....*....|....*....|....
gi 1184725737 405 EPSGTRCFAQSVVLRGIDRACHTS 428
Cdd:cd06060   381 CQNETDVFAQSVVLRGIPESRLKS 404
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
 6-428 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: 537.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737   6 REVLTLQLGHFAGFVGAHWWNQQDAALGRATDSKEPPGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLSSLKEEGGL 85
Cdd:cd06060     1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPDHDVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEGAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737  86 YRDKQLDAAIAWQ-GKLTTHKEELYPKNPYLQDFLSAEGVLSSDgvwrvksipngkgsSPLPTATTPKPLIPTEASIRVW 164
Cdd:cd06060    81 YEEPDDDSSESQWwGDVETHVQEPIEKNEFQQDLEEEETYQVEL--------------ESQSTAEDGDKVYLLEESVRVW 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 165 SDFLRVHLHPRSICMIQKYNHDGEAGRLEAFGQGESVLKEPKYQEELEDRLHFYVEECDYLQGFQILCDLHDGFSGVGAK 244
Cdd:cd06060   147 SDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEECDSLQGFQILVDTDDGFGGVAAK 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 245 AAELLQDEYSGRGIITWGLLPGPYHRGEAQRNIYRLLNTAFGLVHLTAHSSLVCPLSLGGSLGLRPEPPVSFPYLHYDat 324
Cdd:cd06060   227 LLENLRDEYGKKSILTPGLSPASPPDPDSQRRIKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPGWPRTFPHLDYS-- 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 325 LPFHCSAILATALDTVTVPYRLCSSPVSMVHLADMLSFCGKKVVTAGAIIPFPLAPGQSLPDSLMQFGGATPWTPlsacG 404
Cdd:cd06060   305 SPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDLLGDLSLTP----S 380

                         410       420
                  ....*....|....*....|....
gi 1184725737 405 EPSGTRCFAQSVVLRGIDRACHTS 428
Cdd:cd06060   381 CQNETDVFAQSVVLRGIPESRLKS 404
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
 6-117 9.10e-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: 151.25  E-value: 9.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737   6 REVLTLQLGHFAGFVGAHWWNQQDAALgrATDSKEPPGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLSSLKEEGGL 85
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWNTQESYF--TYDPNEEPSEVDHDVLFREGETLDGQVTYTPRLLIYDLKGSFGSLRKEGAL 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1184725737  86 Y--RDKQLDAAIAWQGKLTTHKEELYPKNPYLQD 117
Cdd:pfam10644  79 YelNESAGSNAATWDGKVVVQRQPPIEKSEYQQS 112
PTZ00387 PTZ00387
epsilon tubulin; Provisional
 205-301 2.17e-05

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 47.03  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 205 PKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEYSGRGIITWGLLPG--------PYhrgeaqr 275
Cdd:PTZ00387  111 DKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTgSGLGTRILGMLEDEFPHVFRFCPVVFPSavddvitsPY------- 183

                          90       100
                  ....*....|....*....|....*.
gi 1184725737 276 niyrllNTAFGLVHLTAHSSLVCPLS 301
Cdd:PTZ00387  184 ------NSFFALRELIEHADCVLPLD 203
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
 6-428 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: 537.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737   6 REVLTLQLGHFAGFVGAHWWNQQDAALGRATDSKEPPGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLSSLKEEGGL 85
Cdd:cd06060     1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPDHDVHDVLFREGETLQGEETYTPRLLLVDLKGSLGSLRKEGAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737  86 YRDKQLDAAIAWQ-GKLTTHKEELYPKNPYLQDFLSAEGVLSSDgvwrvksipngkgsSPLPTATTPKPLIPTEASIRVW 164
Cdd:cd06060    81 YEEPDDDSSESQWwGDVETHVQEPIEKNEFQQDLEEEETYQVEL--------------ESQSTAEDGDKVYLLEESVRVW 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 165 SDFLRVHLHPRSICMIQKYNHDGEAGRLEAFGQGESVLKEPKYQEELEDRLHFYVEECDYLQGFQILCDLHDGFSGVGAK 244
Cdd:cd06060   147 SDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEECDSLQGFQILVDTDDGFGGVAAK 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 245 AAELLQDEYSGRGIITWGLLPGPYHRGEAQRNIYRLLNTAFGLVHLTAHSSLVCPLSLGGSLGLRPEPPVSFPYLHYDat 324
Cdd:cd06060   227 LLENLRDEYGKKSILTPGLSPASPPDPDSQRRIKRLLNDALSLSSLSEHSSLFVPLSLPSLLWRKPGWPRTFPHLDYS-- 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 325 LPFHCSAILATALDTVTVPYRLCSSPVSMVHLADMLSFCGKKVVTAGAIIPFPLAPGQSLPDSLMQFGGATPWTPlsacG 404
Cdd:cd06060   305 SPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSLLDSLQDLLGDLSLTP----S 380

                         410       420
                  ....*....|....*....|....
gi 1184725737 405 EPSGTRCFAQSVVLRGIDRACHTS 428
Cdd:cd06060   381 CQNETDVFAQSVVLRGIPESRLKS 404
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
 154-436 1.14e-82

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: 261.19  E-value: 1.14e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 154 LIPTEAS--IRVWSDFLRVHLHPRSICMIQKYnhdgeAGRLEAFGQGESVLkEPKYQEELEDRLHFYVEECDYLQGFQIL 231
Cdd:cd00286    24 LVDLEPAvlDELLSGPLRQLFHPENIILIQKY-----HGAGNNWAKGHSVA-GEEYQEEILDAIRKEVEECDELQGFFIT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 232 CDLHDG-FSGVGAKAAELLQDEYSGRGIITWGLLPGPYHrgeaqRNIYRLLNTAFGLVHLTAHSSLVCPLSLGGSLGLRP 310
Cdd:cd00286    98 HSLGGGtGSGLGPLLAERLKDEYPNRLVVTFSILPGPDE-----GVIVYPYNAALTLKTLTEHADCLLLVDNEALYDICP 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 311 EPpvsfpyLHYDATLPFHCSAILATALDTVTVPYRLCSSPVSMVHLadmlsfcgkkvvtaGAIIPFPLAPGQSLPDSLMQ 390
Cdd:cd00286   173 RP------LHIDAPAYDHINELVAQRLGSLTEALRFEGSLNVDLRE--------------LAENLVPLPRGHFLMLGYAP 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1184725737 391 FGGATPWTPLSACGEPSGTRCFAQSVVLRGIDRACHTSHRLMVVLA 436
Cdd:cd00286   233 LDSATSATPRSLRVKELTRRAFLPANLLVGCDPDHGEAIAALLVIR 278
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
 168-422 2.51e-61

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: 207.05  E-value: 2.51e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 168 LRVHLHPRSICMIQKynhdgeaGRLEAFGQGESVLKePKYQEELEDRLHFYVEECDYLQGFQILCDLHDG-FSGVGAKAA 246
Cdd:cd06059    42 LGQLFDPNQFVTGVS-------GAGNNWAVGYYVYG-PKYIESILDRIRKQVEKCDSLQGFFILHSLGGGtGSGLGSYLL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 247 ELLQDEYSGRGIITWGLLPGPYHRGeaqrNIYRLLNTAFGLVHLTAHSSLVCPLSLGGSLGLRPEPPvsfPYLHYDATLP 326
Cdd:cd06059   114 ELLEDEYPKVYRFTFSVFPSPDDDN----VITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRQP---ATLDIDFPPF 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 327 FHCSAILATALDTVTVPYRLCSSpvSMVHLADMLSfcgkkvvtagAIIPFPLapGQSLPDSLMQFGGATPWTPLSACGEP 406
Cdd:cd06059   187 DDMNNLVAQLLSSLTSSLRFEGS--LNVDLNEITT----------NLVPFPR--LHFLLPSLSPLTSANDVTLEPLTLDQ 252

                         250
                  ....*....|....*.
gi 1184725737 407 SGTRCFAQSVVLRGID 422
Cdd:cd06059   253 LFSDLFSKDNQLVGCD 268
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
 6-117 9.10e-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: 151.25  E-value: 9.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737   6 REVLTLQLGHFAGFVGAHWWNQQDAALgrATDSKEPPGELCPDVLYRTGRTLHGQETYTPRLILMDLKGSLSSLKEEGGL 85
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWNTQESYF--TYDPNEEPSEVDHDVLFREGETLDGQVTYTPRLLIYDLKGSFGSLRKEGAL 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1184725737  86 Y--RDKQLDAAIAWQGKLTTHKEELYPKNPYLQD 117
Cdd:pfam10644  79 YelNESAGSNAATWDGKVVVQRQPPIEKSEYQQS 112
Tubulin_3 pfam14881
Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the ...
 156-346 2.94e-27

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: 108.23  E-value: 2.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 156 PTEASIRVWSDFLRVHLHPRSICMIQKYNHDGEAGRLEAFGQGESVLKEPKYQEELEDR-LHFYVEECDYLQGFQILCDL 234
Cdd:pfam14881   4 LTTSTVRYWSDFNRVFYHPRSIVQLNEYELNSQLMPFEDWSVGEELFRELDKEHDLLDRdLRPFAEECDQLQGLQVFTGS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 235 HDGFSGVGAKAAELLQDEYSGRGII-TWGL-LPGPYHRGEAQRNIYRLLNTAFGLVHLTAHSSLVCPLSLggslglrpeP 312
Cdd:pfam14881  84 DDAWGGFAARYLERLRDEYGKKSIIwVWALqDPLKRIRRTKRERRLRLANKARSLQSLSPQASLYVPIAT---------L 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1184725737 313 PvsfpylhyDATLPFHCSAILATALDTVTVPYRL 346
Cdd:pfam14881 155 S--------DGQSEWHTSALLSSAIESATLPSRL 180
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
 205-301 1.16e-08

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: 57.63  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 205 PKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEYSGRGIITWGLLP--------GPYhrgeaqr 275
Cdd:cd02190   116 PQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTgSGLGSYILELLEDEFPDVYRFVTSVFPsgdddvitSPY------- 188

                          90       100
                  ....*....|....*....|....*.
gi 1184725737 276 niyrllNTAFGLVHLTAHSSLVCPLS 301
Cdd:cd02190   189 ------NSVLALRELTEHADCVLPVE 208
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
 166-297 5.33e-07

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: 50.29  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 166 DFLRVHLHPRSICMIQKynhdgEAGRLEAFGQGEsvlKEPKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAK 244
Cdd:pfam00091  58 NEIKAGFNPNKILLGKE-----GTGGNGAGGYPE---IGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTgSGAAPV 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184725737 245 AAELLQDEYSGR---GIITWgllpgPYHRGEAQRNIYrllNTAFGLVHLTAHSSLV 297
Cdd:pfam00091 130 IAEILKELYPGAltvAVVTF-----PFGFSEGVVRPY---NAILGLKELIEHSDSV 177
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
 195-423 4.64e-06

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: 49.19  E-value: 4.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 195 FGQGESVLkepkyqEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEYSGRGIIT---WgllpgPYHR 270
Cdd:cd02189   100 YVHGPSLL------EDILEALRREAERCDRLSGFLVLHSLAGGTgSGLGSRVTELLRDEYPKAYLLNtvvW-----PYSS 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 271 GEA--QrNiyrlLNTAFGLVHLTAHSSLVCPLS-------LGGSLGLRpePPVSFPYL-HYDATLpfhcsaiLATAL--- 337
Cdd:cd02189   169 GEVpvQ-N----YNTLLTLSHLQESSDGILLFEnddlhkiCSKLLGLK--NPVSFSDInRVIARQ-------LAGVLlps 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 338 DTVTVPYRLCSSPVSMV--HLADMLSFcgkKVVT-------AGAIIPFPLAPGQSLPDSLMQF-------GGATPWTPLS 401
Cdd:cd02189   235 SSPTSPSPLRRCPLGDLleHLCPHPAY---KLLTlrslpqmPEPSRAFSTYTWPSLLKRLRQMlitgaklEEGIDWQLLD 311

                         250       260
                  ....*....|....*....|..
gi 1184725737 402 ACGEPSGTRCFAQSVVLRGIDR 423
Cdd:cd02189   312 TSGSHNPNKSLAALLVLRGKDA 333
PTZ00387 PTZ00387
epsilon tubulin; Provisional
 205-301 2.17e-05

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 47.03  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 205 PKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEYSGRGIITWGLLPG--------PYhrgeaqr 275
Cdd:PTZ00387  111 DKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTgSGLGTRILGMLEDEFPHVFRFCPVVFPSavddvitsPY------- 183

                          90       100
                  ....*....|....*....|....*.
gi 1184725737 276 niyrllNTAFGLVHLTAHSSLVCPLS 301
Cdd:PTZ00387  184 ------NSFFALRELIEHADCVLPLD 203
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 205-267 1.39e-04

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: 44.48  E-value: 1.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184725737 205 PKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEYSGRGIITWGLLPGP 267
Cdd:cd02187   109 AELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTgSGLGTLLLSKLREEYPDRIMSTFSVLPSP 172
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 206-267 5.30e-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: 42.53  E-value: 5.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184725737 206 KYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEYSGRGIITWGLLPGP 267
Cdd:cd02186   112 EIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTgSGLTSLLLERLSVDYGKKSKLEFSIYPSP 174
PTZ00010 PTZ00010
tubulin beta chain; Provisional
 205-267 3.20e-03

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 40.14  E-value: 3.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184725737 205 PKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEYSGRGIITWGLLPGP 267
Cdd:PTZ00010  110 AELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTgSGMGTLLISKLREEYPDRIMMTFSVFPSP 173
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
 172-265 6.94e-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: 39.06  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184725737 172 LHPRSICMIQK------YNHD--------GEAGRLEAFG--QGEsvlkepKYQEELEDRLHFYVEECDYLQGFQILcdlH 235
Cdd:cd02188    67 LEPRVINSIQNspyknlFNPEniylskegGGAGNNWASGysQGE------KVQEEILDIIDREAEGSDSLEGFVLC---H 137

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1184725737 236 D-----GfSGVGAKAAELLQDEYSGRGIITWGLLP 265
Cdd:cd02188   138 SiaggtG-SGMGSYLLERLSDRYPKKLIQTYSVFP 171
 
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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