Misato segment II myosin-like domain
Misat_Myo_SegII | |||||||||
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Identifiers | |||||||||
Symbol | Misat_Myo_SegII | ||||||||
Pfam | PF10644 | ||||||||
Pfam clan | CL0442 | ||||||||
InterPro | IPR019605 | ||||||||
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The Misato segment II myosin-like domain is an evolutionary conserved protein domain.
The misato protein contains three distinct, conserved domains, segments I, II and III and is involved in the regulation of mitochondrial distribution and morphology.[1] This entry represents misato segment II.
Segments I and III are common to tubulins (INTERPRO), but segment II aligns with myosin heavy chain sequences from Drosophila melanogaster (Fruit fly, SWISSPROT), rabbit (SWISSPROT), and human.
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 organisms. 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 characteristic of the myosin tail alpha-helical coiled-coils.[2]
References[]
- ^ Kimura M, Okano Y (April 2007). "Human Misato regulates mitochondrial distribution and morphology". Exp. Cell Res. 313 (7): 1393–404. doi:10.1016/j.yexcr.2007.02.004. PMID 17349998.
- ^ Miklos GL, Yamamoto M, Burns RG, Maleszka R (May 1997). "An essential cell division gene of Drosophila, absent from Saccharomyces, encodes an unusual protein with tubulin-like and myosin-like peptide motifs". Proc. Natl. Acad. Sci. U.S.A. 94 (10): 5189–94. Bibcode:1997PNAS...94.5189M. doi:10.1073/pnas.94.10.5189. PMC 24654. PMID 9144213.
- Protein domains