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Conserved domains on  [gi|910751310|pdb|5C7E|E]
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Chain E, ASPR2 protein

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
34-92 9.68e-12

C-terminal to LisH motif; Alpha-helical motif of unknown function.


:

Pssm-ID: 128914  Cd Length: 58  Bit Score: 57.97  E-value: 9.68e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
5C7E_E          34 FFFNMKYFEEKVHAGEWDEVEKYLSGFTKVDDNRYSmKIFFEIRKQKYLEALDRHDRAK 92
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNS-KLEFELRKQKFLELVRQGKLEE 58
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
4-34 8.15e-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: 38.57  E-value: 8.15e-05
                           10        20        30
                   ....*....|....*....|....*....|.
5C7E_E           4 LSRELVFLILQFLDEEKFKETVHKLEQESGF 34
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
 
Name Accession Description Interval E-value
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
34-92 9.68e-12

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 57.97  E-value: 9.68e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
5C7E_E          34 FFFNMKYFEEKVHAGEWDEVEKYLSGFTKVDDNRYSmKIFFEIRKQKYLEALDRHDRAK 92
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNS-KLEFELRKQKFLELVRQGKLEE 58
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
4-34 8.15e-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: 38.57  E-value: 8.15e-05
                           10        20        30
                   ....*....|....*....|....*....|.
5C7E_E           4 LSRELVFLILQFLDEEKFKETVHKLEQESGF 34
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
5-33 1.40e-04

LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif.


Pssm-ID: 375350  Cd Length: 30  Bit Score: 37.76  E-value: 1.40e-04
                          10        20
                  ....*....|....*....|....*....
5C7E_E          5 SRELVFLILQFLDEEKFKETVHKLEQESG 33
Cdd:pfam17814   1 SQDVVRLILQFLKENGLHRTLQALQTESG 29
 
Name Accession Description Interval E-value
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
34-92 9.68e-12

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 57.97  E-value: 9.68e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
5C7E_E          34 FFFNMKYFEEKVHAGEWDEVEKYLSGFTKVDDNRYSmKIFFEIRKQKYLEALDRHDRAK 92
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNS-KLEFELRKQKFLELVRQGKLEE 58
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
4-34 8.15e-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: 38.57  E-value: 8.15e-05
                           10        20        30
                   ....*....|....*....|....*....|.
5C7E_E           4 LSRELVFLILQFLDEEKFKETVHKLEQESGF 34
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
5-33 1.40e-04

LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif.


Pssm-ID: 375350  Cd Length: 30  Bit Score: 37.76  E-value: 1.40e-04
                          10        20
                  ....*....|....*....|....*....
5C7E_E          5 SRELVFLILQFLDEEKFKETVHKLEQESG 33
Cdd:pfam17814   1 SQDVVRLILQFLKENGLHRTLQALQTESG 29
 
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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