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Conserved domains on  [gi|398365755|ref|NP_011632|]
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uncharacterized protein YGR117C [Saccharomyces cerevisiae S288C]

Protein Classification

LisH domain-containing protein( domain architecture ID 10652832)

LIS1 homology (LisH) domain-containing protein similar to Homo sapiens LisH domain-containing protein ARMC9 that is required for appropriate acetylation and polyglutamylation of ciliary microtubules, and regulation of cilium length

CATH:  1.20.960.40
Gene Ontology:  GO:0005515
SCOP:  3001444

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
12-39 6.06e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


:

Pssm-ID: 128913  Cd Length: 34  Bit Score: 40.11  E-value: 6.06e-05
                           10        20
                   ....*....|....*....|....*...
gi 398365755    12 NLLIANYLKHNGLEDTLAAFIRETALPL 39
Cdd:smart00667   7 NRLILEYLLRNGYEETAETLQKESGLSL 34
 
Name Accession Description Interval E-value
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
12-39 6.06e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 40.11  E-value: 6.06e-05
                           10        20
                   ....*....|....*....|....*...
gi 398365755    12 NLLIANYLKHNGLEDTLAAFIRETALPL 39
Cdd:smart00667   7 NRLILEYLLRNGYEETAETLQKESGLSL 34
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
12-34 8.47e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 33.83  E-value: 8.47e-03
                          10        20
                  ....*....|....*....|...
gi 398365755   12 NLLIANYLKHNGLEDTLAAFIRE 34
Cdd:pfam08513   3 NRLIYDYLVKEGYEETAEAFEKE 25
 
Name Accession Description Interval E-value
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
12-39 6.06e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 40.11  E-value: 6.06e-05
                           10        20
                   ....*....|....*....|....*...
gi 398365755    12 NLLIANYLKHNGLEDTLAAFIRETALPL 39
Cdd:smart00667   7 NRLILEYLLRNGYEETAETLQKESGLSL 34
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
12-34 8.47e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 33.83  E-value: 8.47e-03
                          10        20
                  ....*....|....*....|...
gi 398365755   12 NLLIANYLKHNGLEDTLAAFIRE 34
Cdd:pfam08513   3 NRLIYDYLVKEGYEETAEAFEKE 25
 
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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