plasma membrane, autoregulation-binding site, misato segment II, myosin-like, tubulin/FtsZ protein [Arabidopsis thaliana]
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
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 ... |
2-498 | 6.77e-167 | ||||||||
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: 482.97 E-value: 6.77e-167
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| Name | Accession | Description | Interval | E-value | ||||||||
| misato | cd06060 | Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ... |
2-498 | 6.77e-167 | ||||||||
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: 482.97 E-value: 6.77e-167
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| Tubulin_3 | pfam14881 | Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the ... |
101-280 | 1.23e-25 | ||||||||
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: 103.61 E-value: 1.23e-25
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| Name | Accession | Description | Interval | E-value | ||||||||
| misato | cd06060 | Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ... |
2-498 | 6.77e-167 | ||||||||
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: 482.97 E-value: 6.77e-167
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| Tubulin_3 | pfam14881 | Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the ... |
101-280 | 1.23e-25 | ||||||||
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: 103.61 E-value: 1.23e-25
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| Misat_Tub_SegII | pfam10644 | Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ... |
1-77 | 7.14e-25 | ||||||||
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: 99.25 E-value: 7.14e-25
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| Tubulin_FtsZ_Cetz-like | cd00286 | Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ... |
113-203 | 1.96e-09 | ||||||||
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: 58.96 E-value: 1.96e-09
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| Tubulin | cd06059 | The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ... |
113-212 | 9.90e-07 | ||||||||
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: 51.05 E-value: 9.90e-07
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| alpha_tubulin | cd02186 | The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ... |
111-212 | 7.51e-05 | ||||||||
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: 45.22 E-value: 7.51e-05
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