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Conserved domains on  [gi|1953275762|ref|XP_038535483|]
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ataxin-10 isoform X3 [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Atx10homo_assoc super family cl19985
Spinocerebellar ataxia type 10 protein domain; This is the conserved C-terminal 100 residues ...
 370-395 9.55e-07

Spinocerebellar ataxia type 10 protein domain; This is the conserved C-terminal 100 residues of Ataxin-10. Ataxin-10 belongs to the family of armadillo repeat proteins and in solution it tends to form homotrimeric complexes, which associate via a tip-to-tip association in a horseshoe-shaped contact with the concave sides of the molecules facing each other. This domain may represent the homo-association site since that is located near the C-terminus of Ataxin-10. The protein does not contain a signal sequence for secretion or any subcellular compartment confirming its cytoplasmic localization, specifically to the olivocerebellar region.


The actual alignment was detected with superfamily member pfam09759:

Pssm-ID: 462885 [Multi-domain]  Cd Length: 99  Bit Score: 46.69  E-value: 9.55e-07
                          10        20
                  ....*....|....*....|....*.
gi 1953275762 370 FKSHLIRLIGNLCYKNKDNQDKMKTL 395
Cdd:pfam09759   1 FKRDLIRLIGNLCYKNKEVQDEVREL 26
 
Name Accession Description Interval E-value
Atx10homo_assoc pfam09759
Spinocerebellar ataxia type 10 protein domain; This is the conserved C-terminal 100 residues ...
 370-395 9.55e-07

Spinocerebellar ataxia type 10 protein domain; This is the conserved C-terminal 100 residues of Ataxin-10. Ataxin-10 belongs to the family of armadillo repeat proteins and in solution it tends to form homotrimeric complexes, which associate via a tip-to-tip association in a horseshoe-shaped contact with the concave sides of the molecules facing each other. This domain may represent the homo-association site since that is located near the C-terminus of Ataxin-10. The protein does not contain a signal sequence for secretion or any subcellular compartment confirming its cytoplasmic localization, specifically to the olivocerebellar region.


Pssm-ID: 462885 [Multi-domain]  Cd Length: 99  Bit Score: 46.69  E-value: 9.55e-07
                          10        20
                  ....*....|....*....|....*.
gi 1953275762 370 FKSHLIRLIGNLCYKNKDNQDKMKTL 395
Cdd:pfam09759   1 FKRDLIRLIGNLCYKNKEVQDEVREL 26
 
Name Accession Description Interval E-value
Atx10homo_assoc pfam09759
Spinocerebellar ataxia type 10 protein domain; This is the conserved C-terminal 100 residues ...
 370-395 9.55e-07

Spinocerebellar ataxia type 10 protein domain; This is the conserved C-terminal 100 residues of Ataxin-10. Ataxin-10 belongs to the family of armadillo repeat proteins and in solution it tends to form homotrimeric complexes, which associate via a tip-to-tip association in a horseshoe-shaped contact with the concave sides of the molecules facing each other. This domain may represent the homo-association site since that is located near the C-terminus of Ataxin-10. The protein does not contain a signal sequence for secretion or any subcellular compartment confirming its cytoplasmic localization, specifically to the olivocerebellar region.


Pssm-ID: 462885 [Multi-domain]  Cd Length: 99  Bit Score: 46.69  E-value: 9.55e-07
                          10        20
                  ....*....|....*....|....*.
gi 1953275762 370 FKSHLIRLIGNLCYKNKDNQDKMKTL 395
Cdd:pfam09759   1 FKRDLIRLIGNLCYKNKEVQDEVREL 26
 
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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