uncharacterized protein Dmel_CG14853, isoform A [Drosophila melanogaster]
List of domain hits
Name | Accession | Description | Interval | E-value | ||
Fis1 super family | cl21750 | Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an ... |
119-153 | 9.40e-05 | ||
Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an essential protein in mediating mitochondrial fission. Dnm1 and Fis1 are highly conserved, with a common mechanism in disparate species. In mutants of these proteins, mitochondrial fission is impaired, resulting in networks of undivided mitochondria. The Fis1 N-terminus is cytosolic and tethered to the mitochondrial outer membrane via a C-terminal transmembrane domain. Fis1 appears to act via the recruitment of division complexes to the mitochondrial outer membrane, via interactions with Mdv1 or Caf4. Fis1 has tandem Tetratricopeptide repeat (TPR) motifs which are known to mediate protein-protein interactions. The actual alignment was detected with superfamily member pfam14853: Pssm-ID: 451380 [Multi-domain] Cd Length: 53 Bit Score: 39.81 E-value: 9.40e-05
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Name | Accession | Description | Interval | E-value | ||
Fis1_TPR_C | pfam14853 | Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of ... |
119-153 | 9.40e-05 | ||
Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of two tetratricopeptide repeats. This domain is the C-terminal tetratricopeptide repeat Pssm-ID: 434269 [Multi-domain] Cd Length: 53 Bit Score: 39.81 E-value: 9.40e-05
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Fis1 | cd12212 | Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an ... |
119-154 | 3.11e-04 | ||
Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an essential protein in mediating mitochondrial fission. Dnm1 and Fis1 are highly conserved, with a common mechanism in disparate species. In mutants of these proteins, mitochondrial fission is impaired, resulting in networks of undivided mitochondria. The Fis1 N-terminus is cytosolic and tethered to the mitochondrial outer membrane via a C-terminal transmembrane domain. Fis1 appears to act via the recruitment of division complexes to the mitochondrial outer membrane, via interactions with Mdv1 or Caf4. Fis1 has tandem Tetratricopeptide repeat (TPR) motifs which are known to mediate protein-protein interactions. Pssm-ID: 276936 [Multi-domain] Cd Length: 115 Bit Score: 39.84 E-value: 3.11e-04
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Name | Accession | Description | Interval | E-value | ||
Fis1_TPR_C | pfam14853 | Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of ... |
119-153 | 9.40e-05 | ||
Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of two tetratricopeptide repeats. This domain is the C-terminal tetratricopeptide repeat Pssm-ID: 434269 [Multi-domain] Cd Length: 53 Bit Score: 39.81 E-value: 9.40e-05
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Fis1 | cd12212 | Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an ... |
119-154 | 3.11e-04 | ||
Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an essential protein in mediating mitochondrial fission. Dnm1 and Fis1 are highly conserved, with a common mechanism in disparate species. In mutants of these proteins, mitochondrial fission is impaired, resulting in networks of undivided mitochondria. The Fis1 N-terminus is cytosolic and tethered to the mitochondrial outer membrane via a C-terminal transmembrane domain. Fis1 appears to act via the recruitment of division complexes to the mitochondrial outer membrane, via interactions with Mdv1 or Caf4. Fis1 has tandem Tetratricopeptide repeat (TPR) motifs which are known to mediate protein-protein interactions. Pssm-ID: 276936 [Multi-domain] Cd Length: 115 Bit Score: 39.84 E-value: 3.11e-04
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Blast search parameters | ||||
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