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Conserved domains on  [gi|2015696289|ref|NP_001380829|]
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26S proteasome complex subunit SEM1 isoform b [Homo sapiens]

Protein Classification

DSS1_Sem1 domain-containing protein( domain architecture ID 10194942)

DSS1_Sem1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DSS1_Sem1 cd13768
proteasome complex subunit DSS1/Sem1; The evolutionarily conserved deleted in split hand/split ...
23-58 1.86e-13

proteasome complex subunit DSS1/Sem1; The evolutionarily conserved deleted in split hand/split foot protein 1 (DSS1)/Sem1 is a subunit of the regulatory particle (RP) of the proteasome. It is implicated in ubiquitin-mediated proteolysis, is required for the maintenance of genomic stability, and functions in DNA damage response. DSS1/Sem1 also displays RP-independent functions; it serves as a functional component of the nuclear pore associated TREX-2 transcription-export complex and is required for proper nuclear export of mRNA. In mammalian cells, DSS1 binds and stabilizes the tumor suppressor BRCA2, and contributes to its function in mediating homologous recombinational repair. In yeast, Sem1 also complexes with the COP9 signalosome, which is involved in de-neddylation. DSS1/Sem1 may be a versatile protein which contributes to the functional integrity of multiple protein complexes involved in various biological processes.


:

Pssm-ID: 259841  Cd Length: 61  Bit Score: 58.94  E-value: 1.86e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 2015696289 23 PAEDWAGLDED-----EDAHVWEDNWDDDNVEDDFSNQLRA 58
Cdd:cd13768   16 PVEDWTDEETEensaeEDEHLWEDNWDDDDVEDDFSKQLRA 56
 
Name Accession Description Interval E-value
DSS1_Sem1 cd13768
proteasome complex subunit DSS1/Sem1; The evolutionarily conserved deleted in split hand/split ...
23-58 1.86e-13

proteasome complex subunit DSS1/Sem1; The evolutionarily conserved deleted in split hand/split foot protein 1 (DSS1)/Sem1 is a subunit of the regulatory particle (RP) of the proteasome. It is implicated in ubiquitin-mediated proteolysis, is required for the maintenance of genomic stability, and functions in DNA damage response. DSS1/Sem1 also displays RP-independent functions; it serves as a functional component of the nuclear pore associated TREX-2 transcription-export complex and is required for proper nuclear export of mRNA. In mammalian cells, DSS1 binds and stabilizes the tumor suppressor BRCA2, and contributes to its function in mediating homologous recombinational repair. In yeast, Sem1 also complexes with the COP9 signalosome, which is involved in de-neddylation. DSS1/Sem1 may be a versatile protein which contributes to the functional integrity of multiple protein complexes involved in various biological processes.


Pssm-ID: 259841  Cd Length: 61  Bit Score: 58.94  E-value: 1.86e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 2015696289 23 PAEDWAGLDED-----EDAHVWEDNWDDDNVEDDFSNQLRA 58
Cdd:cd13768   16 PVEDWTDEETEensaeEDEHLWEDNWDDDDVEDDFSKQLRA 56
DSS1_SEM1 pfam05160
DSS1/SEM1 family; This family contains the breast cancer tumour suppressor BRCA2-interacting ...
23-58 7.45e-13

DSS1/SEM1 family; This family contains the breast cancer tumour suppressor BRCA2-interacting protein DSS1 and its homolog SEM1, both of which are short acidic proteins. DSS1 has been shown to be a conserved component of the Rae1 mediated mRNA export pathway in Schizosaccharomyces pombe.


Pssm-ID: 461563  Cd Length: 59  Bit Score: 57.20  E-value: 7.45e-13
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 2015696289 23 PAEDWAGLDEDED-AHVWEDNWDDDNVEDDFSNQLRA 58
Cdd:pfam05160 19 PVEDWDEEEEEADnAHLWEEDWDDDDVEDDFSKQLRA 55
 
Name Accession Description Interval E-value
DSS1_Sem1 cd13768
proteasome complex subunit DSS1/Sem1; The evolutionarily conserved deleted in split hand/split ...
23-58 1.86e-13

proteasome complex subunit DSS1/Sem1; The evolutionarily conserved deleted in split hand/split foot protein 1 (DSS1)/Sem1 is a subunit of the regulatory particle (RP) of the proteasome. It is implicated in ubiquitin-mediated proteolysis, is required for the maintenance of genomic stability, and functions in DNA damage response. DSS1/Sem1 also displays RP-independent functions; it serves as a functional component of the nuclear pore associated TREX-2 transcription-export complex and is required for proper nuclear export of mRNA. In mammalian cells, DSS1 binds and stabilizes the tumor suppressor BRCA2, and contributes to its function in mediating homologous recombinational repair. In yeast, Sem1 also complexes with the COP9 signalosome, which is involved in de-neddylation. DSS1/Sem1 may be a versatile protein which contributes to the functional integrity of multiple protein complexes involved in various biological processes.


Pssm-ID: 259841  Cd Length: 61  Bit Score: 58.94  E-value: 1.86e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 2015696289 23 PAEDWAGLDED-----EDAHVWEDNWDDDNVEDDFSNQLRA 58
Cdd:cd13768   16 PVEDWTDEETEensaeEDEHLWEDNWDDDDVEDDFSKQLRA 56
DSS1_SEM1 pfam05160
DSS1/SEM1 family; This family contains the breast cancer tumour suppressor BRCA2-interacting ...
23-58 7.45e-13

DSS1/SEM1 family; This family contains the breast cancer tumour suppressor BRCA2-interacting protein DSS1 and its homolog SEM1, both of which are short acidic proteins. DSS1 has been shown to be a conserved component of the Rae1 mediated mRNA export pathway in Schizosaccharomyces pombe.


Pssm-ID: 461563  Cd Length: 59  Bit Score: 57.20  E-value: 7.45e-13
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 2015696289 23 PAEDWAGLDEDED-AHVWEDNWDDDNVEDDFSNQLRA 58
Cdd:pfam05160 19 PVEDWDEEEEEADnAHLWEEDWDDDDVEDDFSKQLRA 55
 
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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