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Conserved domains on  [gi|530425624|ref|XP_005260725|]
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barrier-to-autointegration factor-like protein isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAF super family cl03803
Barrier to autointegration factor; The BAF protein has a SAM-domain-like bundle of ...
 3-89 7.86e-49

Barrier to autointegration factor; The BAF protein has a SAM-domain-like bundle of orthogonally packed alpha-hairpins - one classic and one pseudo helix-hairpin-helix motif. The protein is involved in the prevention of retroviral DNA integration.


The actual alignment was detected with superfamily member smart01023:

Pssm-ID: 470880  Cd Length: 87  Bit Score: 149.42  E-value: 7.86e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425624    3 NMSPRLRAFLSEPIGEKDVCWVDGISHELAINLVTKGINKAYILLGQFLLMHKNEAEFQRWLICCFGATECEAQQTSHCL 82
Cdd:smart01023  1 TTSQKHRNFVGEPMGEKPVTALAGIGEVLGGRLETKGFDKAYVVLGQFLLLKKDEELFKEWLKDTCGANAKQARDCYNCL 80


                  ....*..
gi 530425624   83 KEWCACF 89
Cdd:smart01023 81 REWCDSF 87
 
Name Accession Description Interval E-value
BAF smart01023
Barrier to autointegration factor; Barrier-to-autointegration factor (BAF) is an essential ...
 3-89 7.86e-49

Barrier to autointegration factor; Barrier-to-autointegration factor (BAF) is an essential protein that is highly conserved in metazoan evolution, and which may act as a DNA-bridging protein. BAF binds directly to double-stranded DNA, to transcription activators, and to inner nuclear membrane proteins, including lamin A filament proteins that anchor nuclear-pore complexes in place, and nuclear LEM-domain proteins that bind to laminins filaments and chromatin. New findings suggest that BAF has structural roles in nuclear assembly and chromatin organization, represses gene expression and might interlink chromatin structure, nuclear architecture and gene regulation in metazoans. BAF can be exploited by retroviruses to act as a host component of pre-integration complexes, which promote the integration of the retroviral DNA into the host chromosome by preventing autointegration of retroviral DNA. BAF might contribute to the assembly or activity of retroviral pre-integration complexes through direct binding to the retroviral proteins p55 Gag and matrix, as well as to DNA.


Pssm-ID: 198091  Cd Length: 87  Bit Score: 149.42  E-value: 7.86e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425624    3 NMSPRLRAFLSEPIGEKDVCWVDGISHELAINLVTKGINKAYILLGQFLLMHKNEAEFQRWLICCFGATECEAQQTSHCL 82
Cdd:smart01023  1 TTSQKHRNFVGEPMGEKPVTALAGIGEVLGGRLETKGFDKAYVVLGQFLLLKKDEELFKEWLKDTCGANAKQARDCYNCL 80


                  ....*..
gi 530425624   83 KEWCACF 89
Cdd:smart01023 81 REWCDSF 87
BAF pfam02961
Barrier to autointegration factor; The BAF protein has a SAM-domain-like bundle of ...
 4-89 1.29e-45

Barrier to autointegration factor; The BAF protein has a SAM-domain-like bundle of orthogonally packed alpha-hairpins - one classic and one pseudo helix-hairpin-helix motif. The protein is involved in the prevention of retroviral DNA integration.


Pssm-ID: 460766  Cd Length: 88  Bit Score: 141.18  E-value: 1.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425624   4 MSPRLRAFLSEPIGEKDVCWVDGISHELAINLVTKGINKAYILLGQFLLMHKNEAEFQRWLICCFGATECEAQQTSHCLK 83
Cdd:pfam02961  3 TSQKHRNFVSEPMGDKPVTALAGIGEVLGGRLEDKGFDKAYVVLGQFLLLKKDEELFQDWLKDTCGANSKQAGDCYNCLK 82


                 ....*.
gi 530425624  84 EWCACF 89
Cdd:pfam02961 83 EWCDAF 88
 
Name Accession Description Interval E-value
BAF smart01023
Barrier to autointegration factor; Barrier-to-autointegration factor (BAF) is an essential ...
 3-89 7.86e-49

Barrier to autointegration factor; Barrier-to-autointegration factor (BAF) is an essential protein that is highly conserved in metazoan evolution, and which may act as a DNA-bridging protein. BAF binds directly to double-stranded DNA, to transcription activators, and to inner nuclear membrane proteins, including lamin A filament proteins that anchor nuclear-pore complexes in place, and nuclear LEM-domain proteins that bind to laminins filaments and chromatin. New findings suggest that BAF has structural roles in nuclear assembly and chromatin organization, represses gene expression and might interlink chromatin structure, nuclear architecture and gene regulation in metazoans. BAF can be exploited by retroviruses to act as a host component of pre-integration complexes, which promote the integration of the retroviral DNA into the host chromosome by preventing autointegration of retroviral DNA. BAF might contribute to the assembly or activity of retroviral pre-integration complexes through direct binding to the retroviral proteins p55 Gag and matrix, as well as to DNA.


Pssm-ID: 198091  Cd Length: 87  Bit Score: 149.42  E-value: 7.86e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425624    3 NMSPRLRAFLSEPIGEKDVCWVDGISHELAINLVTKGINKAYILLGQFLLMHKNEAEFQRWLICCFGATECEAQQTSHCL 82
Cdd:smart01023  1 TTSQKHRNFVGEPMGEKPVTALAGIGEVLGGRLETKGFDKAYVVLGQFLLLKKDEELFKEWLKDTCGANAKQARDCYNCL 80


                  ....*..
gi 530425624   83 KEWCACF 89
Cdd:smart01023 81 REWCDSF 87
BAF pfam02961
Barrier to autointegration factor; The BAF protein has a SAM-domain-like bundle of ...
 4-89 1.29e-45

Barrier to autointegration factor; The BAF protein has a SAM-domain-like bundle of orthogonally packed alpha-hairpins - one classic and one pseudo helix-hairpin-helix motif. The protein is involved in the prevention of retroviral DNA integration.


Pssm-ID: 460766  Cd Length: 88  Bit Score: 141.18  E-value: 1.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425624   4 MSPRLRAFLSEPIGEKDVCWVDGISHELAINLVTKGINKAYILLGQFLLMHKNEAEFQRWLICCFGATECEAQQTSHCLK 83
Cdd:pfam02961  3 TSQKHRNFVSEPMGDKPVTALAGIGEVLGGRLEDKGFDKAYVVLGQFLLLKKDEELFQDWLKDTCGANSKQAGDCYNCLK 82


                 ....*.
gi 530425624  84 EWCACF 89
Cdd:pfam02961 83 EWCDAF 88
 
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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