NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24585862|ref|NP_724420|]
View 

Fission, mitochondrial 1, isoform D [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1-64 3.30e-22

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 cd12212:

Pssm-ID: 451380 [Multi-domain]  Cd Length: 115  Bit Score: 82.99  E-value: 3.30e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24585862   1 MILEELARTHPDGRRDYIYYLAFGNARIKEYTSGLKYCRAFLDIE-SNDQVRSLEEYIKKEIDKE 64
Cdd:cd12212  49 ELLEELYRDGPERRRECLYYLALGHYKLGEYSEARRYVDALLEIEpDNRQALALKELIEDKITKE 113
 
Name Accession Description Interval E-value
Fis1 cd12212
Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an ...
1-64 3.30e-22

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: 82.99  E-value: 3.30e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24585862   1 MILEELARTHPDGRRDYIYYLAFGNARIKEYTSGLKYCRAFLDIE-SNDQVRSLEEYIKKEIDKE 64
Cdd:cd12212  49 ELLEELYRDGPERRRECLYYLALGHYKLGEYSEARRYVDALLEIEpDNRQALALKELIEDKITKE 113
Fis1_TPR_C pfam14853
Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of ...
15-64 9.18e-16

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: 64.85  E-value: 9.18e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24585862   15 RDYIYYLAFGNARIKEYTSGLKYCRAFLDIE-SNDQVRSLEEYIKKEIDKE 64
Cdd:pfam14853  1 RECLYYLAVGHYKLGEYSEARRYVDALLEIEpDNRQALALKELIEDKITKE 51
 
Name Accession Description Interval E-value
Fis1 cd12212
Mitochondrial Fission Protein Fis1, cytosolic domain; Fis1, along with Dnm1 and Mdv1, is an ...
1-64 3.30e-22

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: 82.99  E-value: 3.30e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24585862   1 MILEELARTHPDGRRDYIYYLAFGNARIKEYTSGLKYCRAFLDIE-SNDQVRSLEEYIKKEIDKE 64
Cdd:cd12212  49 ELLEELYRDGPERRRECLYYLALGHYKLGEYSEARRYVDALLEIEpDNRQALALKELIEDKITKE 113
Fis1_TPR_C pfam14853
Fis1 C-terminal tetratricopeptide repeat; The mitochondrial fission protein Fis1 consists of ...
15-64 9.18e-16

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: 64.85  E-value: 9.18e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24585862   15 RDYIYYLAFGNARIKEYTSGLKYCRAFLDIE-SNDQVRSLEEYIKKEIDKE 64
Cdd:pfam14853  1 RECLYYLAVGHYKLGEYSEARRYVDALLEIEpDNRQALALKELIEDKITKE 51
 
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