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Conserved domains on  [gi|51247856]
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Chain B, PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB ALPHA SUBUNIT

Protein Classification

LisH domain-containing protein( domain architecture ID 10553536)

LIS1 homology (LisH) domain-containing protein similar to Saccharomyces cerevisiae transcription activator MSS11 that regulates pseudohyphal differentiation, invasive growth, floculation, adhesion and starch metabolism in response to nutrient availability

CATH:  1.20.960.30
Gene Ontology:  GO:0005515
SCOP:  3001444

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 12-36 4.77e-06

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: 39.22  E-value: 4.77e-06
                         10        20
                 ....*....|....*....|....*
gi 51247856   12 ELNRAIADYLRSNGYEEAYSVFKKE 36
Cdd:pfam08513  1 ELNRLIYDYLVKEGYEETAEAFEKE 25
 
Name Accession Description Interval E-value
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 12-36 4.77e-06

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: 39.22  E-value: 4.77e-06
                         10        20
                 ....*....|....*....|....*
gi 51247856   12 ELNRAIADYLRSNGYEEAYSVFKKE 36
Cdd:pfam08513  1 ELNRLIYDYLVKEGYEETAEAFEKE 25
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 9-40 8.94e-06

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: 38.57  E-value: 8.94e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 51247856     9 QRDELNRAIADYLRSNGYEEAYSVFKKEAELD 40
Cdd:smart00667  2 SRSELNRLILEYLLRNGYEETAETLQKESGLS 33
 
Name Accession Description Interval E-value
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 12-36 4.77e-06

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: 39.22  E-value: 4.77e-06
                         10        20
                 ....*....|....*....|....*
gi 51247856   12 ELNRAIADYLRSNGYEEAYSVFKKE 36
Cdd:pfam08513  1 ELNRLIYDYLVKEGYEETAEAFEKE 25
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 9-40 8.94e-06

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: 38.57  E-value: 8.94e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 51247856     9 QRDELNRAIADYLRSNGYEEAYSVFKKEAELD 40
Cdd:smart00667  2 SRSELNRLILEYLLRNGYEETAETLQKESGLS 33
LisH_2 pfam16045
LisH;
13-36 3.84e-03

LisH;


Pssm-ID: 464992  Cd Length: 28  Bit Score: 32.05  E-value: 3.84e-03
                         10        20
                 ....*....|....*....|....
gi 51247856   13 LNRAIADYLRSNGYEEAYSVFKKE 36
Cdd:pfam16045  1 LNSLIAEYLQSQGYNYTLSVFLPE 24
 
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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