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Conserved domains on  [gi|1034654797|ref|XP_016867425|]
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membrane protein BRI3 isoform X4 [Homo sapiens]

Protein Classification

BRI3 family protein( domain architecture ID 8734)

BRI3 (brain protein I3) family protein is a DUF2367 domain-containing protein; similar to human brain protein I3 that participates in tumor necrosis factor-alpha (TNF)-induced cell death

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRI3 super family cl10861
Brain protein I3; This is a highly conserved family of proteins which contains three pairs of ...
 29-81 5.31e-08

Brain protein I3; This is a highly conserved family of proteins which contains three pairs of cysteine residues within a length of 42 amino acids and is rich in proline residues towards the N-terminus. It includes a membrane protein that has been found to be highly expressed in the mouse brain and consequently, several members have been assigned as brain protein I3 (Bri3). Their function is unknown but they appear to play a role in TNF-induced cell death.


The actual alignment was detected with superfamily member pfam10164:

Pssm-ID: 431102  Cd Length: 104  Bit Score: 46.82  E-value: 5.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654797  29 GYGAIPAAPPPPPYPYLVTGIPTHHPRV--------YNIHSRTVTRYPANSIVVVGGCPVC 81
Cdd:pfam10164   1 GYGAIPTAPPQYLITYVVTQAPPPYQYPdgpavsqqPQQTTYTIVVQPTQSVVVVGGCPAC 61
 
Name Accession Description Interval E-value
BRI3 pfam10164
Brain protein I3; This is a highly conserved family of proteins which contains three pairs of ...
 29-81 5.31e-08

Brain protein I3; This is a highly conserved family of proteins which contains three pairs of cysteine residues within a length of 42 amino acids and is rich in proline residues towards the N-terminus. It includes a membrane protein that has been found to be highly expressed in the mouse brain and consequently, several members have been assigned as brain protein I3 (Bri3). Their function is unknown but they appear to play a role in TNF-induced cell death.


Pssm-ID: 431102  Cd Length: 104  Bit Score: 46.82  E-value: 5.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654797  29 GYGAIPAAPPPPPYPYLVTGIPTHHPRV--------YNIHSRTVTRYPANSIVVVGGCPVC 81
Cdd:pfam10164   1 GYGAIPTAPPQYLITYVVTQAPPPYQYPdgpavsqqPQQTTYTIVVQPTQSVVVVGGCPAC 61
 
Name Accession Description Interval E-value
BRI3 pfam10164
Brain protein I3; This is a highly conserved family of proteins which contains three pairs of ...
 29-81 5.31e-08

Brain protein I3; This is a highly conserved family of proteins which contains three pairs of cysteine residues within a length of 42 amino acids and is rich in proline residues towards the N-terminus. It includes a membrane protein that has been found to be highly expressed in the mouse brain and consequently, several members have been assigned as brain protein I3 (Bri3). Their function is unknown but they appear to play a role in TNF-induced cell death.


Pssm-ID: 431102  Cd Length: 104  Bit Score: 46.82  E-value: 5.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654797  29 GYGAIPAAPPPPPYPYLVTGIPTHHPRV--------YNIHSRTVTRYPANSIVVVGGCPVC 81
Cdd:pfam10164   1 GYGAIPTAPPQYLITYVVTQAPPPYQYPdgpavsqqPQQTTYTIVVQPTQSVVVVGGCPAC 61
 
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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