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Conserved domains on  [gi|18150219|gb|AAL61559|]
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dystrophin, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 1-59 3.78e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member pfam00435:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 105  Bit Score: 40.38  E-value: 3.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18150219     1 GYMMDLTAHQGRVGNILQLGSKLIGTGKlseDEETEVQEQMNLLNSRWECLRVASMEKQ 59
Cdd:pfam00435  45 ALEAELAAHQDRVEALNELAEKLIDEGH---YASEEIQERLEELNERWEQLLELAAERK 100
 
Name Accession Description Interval E-value
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 1-59 3.78e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.38  E-value: 3.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18150219     1 GYMMDLTAHQGRVGNILQLGSKLIGTGKlseDEETEVQEQMNLLNSRWECLRVASMEKQ 59
Cdd:pfam00435  45 ALEAELAAHQDRVEALNELAEKLIDEGH---YASEEIQERLEELNERWEQLLELAAERK 100
SPEC smart00150
Spectrin repeats;
3-59 6.57e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 36.92  E-value: 6.57e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18150219      3 MMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEVQEQMNLLNSRWECLRVASMEKQ 59
Cdd:smart00150  44 EAELEAHEERVEALNELGEQLI---EEGHPDAEEIEERLEELNERWEELKELAEERR 97
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2-59 2.21e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 33.96  E-value: 2.21e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18150219   2 YMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEVQEQMNLLNSRWECLRVASMEKQ 59
Cdd:cd00176  45 LEAELAAHEERVEALNELGEQLI---EEGHPDAEEIQERLEELNQRWEELRELAEERR 99
 
Name Accession Description Interval E-value
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
 1-59 3.78e-06

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 40.38  E-value: 3.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18150219     1 GYMMDLTAHQGRVGNILQLGSKLIGTGKlseDEETEVQEQMNLLNSRWECLRVASMEKQ 59
Cdd:pfam00435  45 ALEAELAAHQDRVEALNELAEKLIDEGH---YASEEIQERLEELNERWEQLLELAAERK 100
SPEC smart00150
Spectrin repeats;
3-59 6.57e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 36.92  E-value: 6.57e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18150219      3 MMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEVQEQMNLLNSRWECLRVASMEKQ 59
Cdd:smart00150  44 EAELEAHEERVEALNELGEQLI---EEGHPDAEEIEERLEELNERWEELKELAEERR 97
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 2-59 2.21e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 33.96  E-value: 2.21e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18150219   2 YMMDLTAHQGRVGNILQLGSKLIgtgKLSEDEETEVQEQMNLLNSRWECLRVASMEKQ 59
Cdd:cd00176  45 LEAELAAHEERVEALNELGEQLI---EEGHPDAEEIQERLEELNQRWEELRELAEERR 99
 
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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