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Conserved domains on  [gi|34304368|ref|NP_898861|]
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dysbindin isoform b [Homo sapiens]

Protein Classification

Dysbindin domain-containing protein( domain architecture ID 10517140)

Dysbindin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dysbindin pfam04440
Dysbindin (Dystrobrevin binding protein 1); Dysbindin is an evolutionary conserved 40-kDa ...
 175-271 5.26e-61

Dysbindin (Dystrobrevin binding protein 1); Dysbindin is an evolutionary conserved 40-kDa coiled-coil-containing protein that binds to alpha- and beta-dystrobrevin in muscle and brain. Dystrophin and alpha-dystrobrevin are co-immunoprecipitated with dysbindin, indicating that dysbindin is DPC-associated in muscle. Dysbindin co-localizes with alpha-dystrobrevin at the sarcolemma and is up-regulated in dystrophin-deficient muscle. In the brain, dysbindin is found primarily in axon bundles and especially in certain axon terminals, notably mossy fibre synaptic terminals in the cerebellum and hippocampus. Dysbindin may have implications for the molecular pathology of Duchenne muscular dystrophy and may provide an alternative route for anchoring dystrobrevin and the DPC to the muscle membrane. Genetic variation in the human dysbindin gene is also thought to be associated with Schizophrenia.


:

Pssm-ID: 461312  Cd Length: 143  Bit Score: 190.46  E-value: 5.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304368   175 AEHAQKVLEMEHTQQMKLKERQKFFEEAFQQDMEQYLSTGYLQIAERREPIGSMSSMEVNVDMLEQMDLMDISDQEALDV 254
Cdd:pfam04440   1 AEHAQKVLEMEHTQQLKLKERQKFFEEAFQQDMEQYLSTGYLQITERRQPLGSVSSMEVNVDLLDQMELTDMSDQEALDV 80

                          90
                  ....*....|....*..
gi 34304368   255 FLNSGGEENTVLSPALG 271
Cdd:pfam04440  81 FADSDGEENALESPAGL 97
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
60-213 5.63e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304368   60 AALHRRAKDCASAGELVDSEVVMLSAHWEkkktsLVELQEQLQQLPALIADLESMTANLTHLEASFEEVENNLLHLEDLC 139
Cdd:COG4913  641 DALQERREALQRLAEYSWDEIDVASAERE-----IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI 715

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304368  140 GQCE--LERCKHMQSQ---QLENYKKNKRKEL-----ETFKAELDAEHAQKVLEMEHTQQMKLKERQKFFEEAFQQDMEQ 209
Cdd:COG4913  716 GRLEkeLEQAEEELDElqdRLEAAEDLARLELralleERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795


                 ....
gi 34304368  210 YLST 213
Cdd:COG4913  796 FNRE 799
 
Name Accession Description Interval E-value
Dysbindin pfam04440
Dysbindin (Dystrobrevin binding protein 1); Dysbindin is an evolutionary conserved 40-kDa ...
 175-271 5.26e-61

Dysbindin (Dystrobrevin binding protein 1); Dysbindin is an evolutionary conserved 40-kDa coiled-coil-containing protein that binds to alpha- and beta-dystrobrevin in muscle and brain. Dystrophin and alpha-dystrobrevin are co-immunoprecipitated with dysbindin, indicating that dysbindin is DPC-associated in muscle. Dysbindin co-localizes with alpha-dystrobrevin at the sarcolemma and is up-regulated in dystrophin-deficient muscle. In the brain, dysbindin is found primarily in axon bundles and especially in certain axon terminals, notably mossy fibre synaptic terminals in the cerebellum and hippocampus. Dysbindin may have implications for the molecular pathology of Duchenne muscular dystrophy and may provide an alternative route for anchoring dystrobrevin and the DPC to the muscle membrane. Genetic variation in the human dysbindin gene is also thought to be associated with Schizophrenia.


Pssm-ID: 461312  Cd Length: 143  Bit Score: 190.46  E-value: 5.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304368   175 AEHAQKVLEMEHTQQMKLKERQKFFEEAFQQDMEQYLSTGYLQIAERREPIGSMSSMEVNVDMLEQMDLMDISDQEALDV 254
Cdd:pfam04440   1 AEHAQKVLEMEHTQQLKLKERQKFFEEAFQQDMEQYLSTGYLQITERRQPLGSVSSMEVNVDLLDQMELTDMSDQEALDV 80

                          90
                  ....*....|....*..
gi 34304368   255 FLNSGGEENTVLSPALG 271
Cdd:pfam04440  81 FADSDGEENALESPAGL 97
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
60-213 5.63e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304368   60 AALHRRAKDCASAGELVDSEVVMLSAHWEkkktsLVELQEQLQQLPALIADLESMTANLTHLEASFEEVENNLLHLEDLC 139
Cdd:COG4913  641 DALQERREALQRLAEYSWDEIDVASAERE-----IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI 715

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304368  140 GQCE--LERCKHMQSQ---QLENYKKNKRKEL-----ETFKAELDAEHAQKVLEMEHTQQMKLKERQKFFEEAFQQDMEQ 209
Cdd:COG4913  716 GRLEkeLEQAEEELDElqdRLEAAEDLARLELralleERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795


                 ....
gi 34304368  210 YLST 213
Cdd:COG4913  796 FNRE 799
 
Name Accession Description Interval E-value
Dysbindin pfam04440
Dysbindin (Dystrobrevin binding protein 1); Dysbindin is an evolutionary conserved 40-kDa ...
 175-271 5.26e-61

Dysbindin (Dystrobrevin binding protein 1); Dysbindin is an evolutionary conserved 40-kDa coiled-coil-containing protein that binds to alpha- and beta-dystrobrevin in muscle and brain. Dystrophin and alpha-dystrobrevin are co-immunoprecipitated with dysbindin, indicating that dysbindin is DPC-associated in muscle. Dysbindin co-localizes with alpha-dystrobrevin at the sarcolemma and is up-regulated in dystrophin-deficient muscle. In the brain, dysbindin is found primarily in axon bundles and especially in certain axon terminals, notably mossy fibre synaptic terminals in the cerebellum and hippocampus. Dysbindin may have implications for the molecular pathology of Duchenne muscular dystrophy and may provide an alternative route for anchoring dystrobrevin and the DPC to the muscle membrane. Genetic variation in the human dysbindin gene is also thought to be associated with Schizophrenia.


Pssm-ID: 461312  Cd Length: 143  Bit Score: 190.46  E-value: 5.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304368   175 AEHAQKVLEMEHTQQMKLKERQKFFEEAFQQDMEQYLSTGYLQIAERREPIGSMSSMEVNVDMLEQMDLMDISDQEALDV 254
Cdd:pfam04440   1 AEHAQKVLEMEHTQQLKLKERQKFFEEAFQQDMEQYLSTGYLQITERRQPLGSVSSMEVNVDLLDQMELTDMSDQEALDV 80

                          90
                  ....*....|....*..
gi 34304368   255 FLNSGGEENTVLSPALG 271
Cdd:pfam04440  81 FADSDGEENALESPAGL 97
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
60-213 5.63e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304368   60 AALHRRAKDCASAGELVDSEVVMLSAHWEkkktsLVELQEQLQQLPALIADLESMTANLTHLEASFEEVENNLLHLEDLC 139
Cdd:COG4913  641 DALQERREALQRLAEYSWDEIDVASAERE-----IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI 715

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34304368  140 GQCE--LERCKHMQSQ---QLENYKKNKRKEL-----ETFKAELDAEHAQKVLEMEHTQQMKLKERQKFFEEAFQQDMEQ 209
Cdd:COG4913  716 GRLEkeLEQAEEELDElqdRLEAAEDLARLELralleERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795


                 ....
gi 34304368  210 YLST 213
Cdd:COG4913  796 FNRE 799
 
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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