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Conserved domains on  [gi|71994646|ref|NP_872162|]
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LisH domain-containing protein [Caenorhabditis elegans]

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 ...
 34-58 2.26e-04

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: 38.84  E-value: 2.26e-04
                          10        20
                  ....*....|....*....|....*
gi 71994646    34 RIDSLIYGYLRRNGMNQAADAMEQE 58
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
SF-CC1 super family cl36939
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 433-527 6.71e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


The actual alignment was detected with superfamily member TIGR01622:

Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 39.90  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994646   433 RSGGRSQSRSLRYGSSPQQSRpVEEQKRHRDTEKERERDHESDRESI------SSTSSRSNAPEKRERDAEKERKRKDKE 506
Cdd:TIGR01622   5 RERERLRDSSSAGDRDRRRDK-GRERSRDRSRDRERSRSRRRDRHRDrdyyrgRERRSRSRRPNRRYRPREKRRRRGDSY 83

                          90       100
                  ....*....|....*....|.
gi 71994646   507 HRRaleaDNNKYHAREKEKQK 527
Cdd:TIGR01622  84 RRR----RDDRRSRREKPRAR 100
 
Name Accession Description Interval E-value
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 34-58 2.26e-04

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: 38.84  E-value: 2.26e-04
                          10        20
                  ....*....|....*....|....*
gi 71994646    34 RIDSLIYGYLRRNGMNQAADAMEQE 58
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 32-59 4.26e-03

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: 35.49  E-value: 4.26e-03
                           10        20
                   ....*....|....*....|....*...
gi 71994646     32 HERIDSLIYGYLRRNGMNQAADAMEQES 59
Cdd:smart00667   3 RSELNRLILEYLLRNGYEETAETLQKES 30
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 433-527 6.71e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 39.90  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994646   433 RSGGRSQSRSLRYGSSPQQSRpVEEQKRHRDTEKERERDHESDRESI------SSTSSRSNAPEKRERDAEKERKRKDKE 506
Cdd:TIGR01622   5 RERERLRDSSSAGDRDRRRDK-GRERSRDRSRDRERSRSRRRDRHRDrdyyrgRERRSRSRRPNRRYRPREKRRRRGDSY 83

                          90       100
                  ....*....|....*....|.
gi 71994646   507 HRRaleaDNNKYHAREKEKQK 527
Cdd:TIGR01622  84 RRR----RDDRRSRREKPRAR 100
 
Name Accession Description Interval E-value
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 34-58 2.26e-04

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: 38.84  E-value: 2.26e-04
                          10        20
                  ....*....|....*....|....*
gi 71994646    34 RIDSLIYGYLRRNGMNQAADAMEQE 58
Cdd:pfam08513   1 ELNRLIYDYLVKEGYEETAEAFEKE 25
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 32-59 4.26e-03

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: 35.49  E-value: 4.26e-03
                           10        20
                   ....*....|....*....|....*...
gi 71994646     32 HERIDSLIYGYLRRNGMNQAADAMEQES 59
Cdd:smart00667   3 RSELNRLILEYLLRNGYEETAETLQKES 30
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 433-527 6.71e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 39.90  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994646   433 RSGGRSQSRSLRYGSSPQQSRpVEEQKRHRDTEKERERDHESDRESI------SSTSSRSNAPEKRERDAEKERKRKDKE 506
Cdd:TIGR01622   5 RERERLRDSSSAGDRDRRRDK-GRERSRDRSRDRERSRSRRRDRHRDrdyyrgRERRSRSRRPNRRYRPREKRRRRGDSY 83

                          90       100
                  ....*....|....*....|.
gi 71994646   507 HRRaleaDNNKYHAREKEKQK 527
Cdd:TIGR01622  84 RRR----RDDRRSRREKPRAR 100
 
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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