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Conserved domains on  [gi|22328317|ref|NP_192335|]
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Bromo-adjacent homology (BAH) domain-containing protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAH super family cl02608
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 1-104 2.64e-51

BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions.


The actual alignment was detected with superfamily member cd04714:

Pssm-ID: 470629  Cd Length: 121  Bit Score: 161.03  E-value: 2.64e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328317   1 MRPSDAGKAPYVARVEKIEADARNNVKVHCRWYYCPEESHGGRRQLHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYTR 80
Cdd:cd04714  12 FKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYER 91

                        90       100       110
                ....*....|....*....|....*....|
gi 22328317  81 LENV------GVEDYYCIFDYKAATGAFTP 104
Cdd:cd04714  92 LARVkkkpqdGVDFYYCAGTYNPDTGMLKC 121
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 113-155 6.73e-03

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


:

Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 33.34  E-value: 6.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 22328317    113 CEMPYNSDELMELLLCHYRVHLACVGVTIEEAKKLEHFVCVEC 155
Cdd:smart00249   5 CGKPDDGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 1-104 2.64e-51

BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240065  Cd Length: 121  Bit Score: 161.03  E-value: 2.64e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328317   1 MRPSDAGKAPYVARVEKIEADARNNVKVHCRWYYCPEESHGGRRQLHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYTR 80
Cdd:cd04714  12 FKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYER 91

                        90       100       110
                ....*....|....*....|....*....|
gi 22328317  81 LENV------GVEDYYCIFDYKAATGAFTP 104
Cdd:cd04714  92 LARVkkkpqdGVDFYYCAGTYNPDTGMLKC 121
BAH smart00439
Bromo adjacent homology domain;
1-106 3.18e-28

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 101.99  E-value: 3.18e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328317      1 MRPSDAGKAPYVARVEKIEADARNN--VKVHCRWYYCPEESHGGRRQLHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNY 78
Cdd:smart00439  10 VEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKNEVFLSDEYDTVPLSDIIGKCNVLYKSDY 89

                           90       100       110
                   ....*....|....*....|....*....|..
gi 22328317     79 TRLENVGVE----DYYCIFDYKAATGAFTPDR 106
Cdd:smart00439  90 PGLRPEGSIgepdVFFCESAYDPEKGSFKKLP 121
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 1-106 7.47e-20

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 80.43  E-value: 7.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328317     1 MRPSDAGKAPYVARVEKI-EADARNNVKVHCRWYYCPEESHGGRRQLHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYT 79
Cdd:pfam01426  11 VEPDDADEPYYVARIEELfEDTKNGKKMVRVQWFYRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGKCSVLHKSDLE 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 22328317    80 RLENVGV---EDYYCIFDYKAATGAFTPDR 106
Cdd:pfam01426  91 SLDPYKIkepDDFFCELLYDPKTKSFKKLP 120
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 113-155 6.73e-03

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 33.34  E-value: 6.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 22328317    113 CEMPYNSDELMELLLCHYRVHLACVGVTIEEAKKLEHFVCVEC 155
Cdd:smart00249   5 CGKPDDGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 1-104 2.64e-51

BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240065  Cd Length: 121  Bit Score: 161.03  E-value: 2.64e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328317   1 MRPSDAGKAPYVARVEKIEADARNNVKVHCRWYYCPEESHGGRRQLHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYTR 80
Cdd:cd04714  12 FKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHKCYVLTFAEYER 91

                        90       100       110
                ....*....|....*....|....*....|
gi 22328317  81 LENV------GVEDYYCIFDYKAATGAFTP 104
Cdd:cd04714  92 LARVkkkpqdGVDFYYCAGTYNPDTGMLKC 121
BAH smart00439
Bromo adjacent homology domain;
1-106 3.18e-28

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 101.99  E-value: 3.18e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328317      1 MRPSDAGKAPYVARVEKIEADARNN--VKVHCRWYYCPEESHGGRRQLHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNY 78
Cdd:smart00439  10 VEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKNEVFLSDEYDTVPLSDIIGKCNVLYKSDY 89

                           90       100       110
                   ....*....|....*....|....*....|..
gi 22328317     79 TRLENVGVE----DYYCIFDYKAATGAFTPDR 106
Cdd:smart00439  90 PGLRPEGSIgepdVFFCESAYDPEKGSFKKLP 121
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 1-106 7.47e-20

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 80.43  E-value: 7.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328317     1 MRPSDAGKAPYVARVEKI-EADARNNVKVHCRWYYCPEESHGGRRQLHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYT 79
Cdd:pfam01426  11 VEPDDADEPYYVARIEELfEDTKNGKKMVRVQWFYRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGKCSVLHKSDLE 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 22328317    80 RLENVGV---EDYYCIFDYKAATGAFTPDR 106
Cdd:pfam01426  91 SLDPYKIkepDDFFCELLYDPKTKSFKKLP 120
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 4-93 1.39e-13

BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions.


Pssm-ID: 239835 [Multi-domain]  Cd Length: 123  Bit Score: 64.34  E-value: 1.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328317   4 SDAGKAPYVARVEKIEADARNNVKVHCRWYYCPEESHGGRRQLHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYTRLEN 83
Cdd:cd04370  17 SIKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFALRRELFLSDHLDEIPVESIIGKCKVLFVSEFEGLKQ 96

                        90
                ....*....|
gi 22328317  84 VGVEDYYCIF 93
Cdd:cd04370  97 RPNKIDTDDF 106
BAH_plant_2 cd04718
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 31-102 3.72e-08

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240069  Cd Length: 148  Bit Score: 50.28  E-value: 3.72e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22328317  31 RWYYCPEESHGGRRQLHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYTRLENVGVEDYYCIFDYKAATGAF 102
Cdd:cd04718  73 RWYTLPEETHMGRQPHNLRRELYLTNDFADIEMECILRHCSVKCPKEFRDASNDGDDVFLCEYEYDVHWQSF 144
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 3-83 1.40e-07

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240064  Cd Length: 146  Bit Score: 48.62  E-value: 1.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328317   3 PSDAGKaPYVARVEKIEADARNNVKVHCRWYYCPEE---SHGGRRQLHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYT 79
Cdd:cd04713  31 PEDDQK-PYIAIIKDIYKQEEGSLKLEVQWLYRPEEiekKKGGNWKAEDPRELFYSFHRDEVPAESVLHPCKVAFVPKGK 109


                ....
gi 22328317  80 RLEN 83
Cdd:cd04713 110 QIPL 113
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 1-104 2.18e-07

BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human polybromo protein (BAF180) is a component of the SWI/SNF chromatin-remodeling complex PBAF. It is thought that polybromo participates in transcriptional regulation. Saccharomyces cerevisiae RSC1 and RSC2 are part of the 15-subunit nucleosome remodeling RSC complex. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240068  Cd Length: 121  Bit Score: 47.58  E-value: 2.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328317   1 MRPSDAGKAPYVARVEKIEADARNNVKVHCRWYYCPEESHggrrqlHGA------KELFLSDHFDVQSAHTIEGKCIVHT 74
Cdd:cd04717  12 VANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETF------HEPtrkfykNEVFKSPLYETVPVEEIVGKCAVMD 85

                        90       100       110
                ....*....|....*....|....*....|...
gi 22328317  75 FKNYTRLENVGVED---YYCIFDYKAATGAFTP 104
Cdd:cd04717  86 VKDYIKGRPTEISEedvYVCESRYNESAKSFKK 118
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 11-84 1.99e-05

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240072  Cd Length: 130  Bit Score: 42.43  E-value: 1.99e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22328317  11 YVARVEKIEADARNNVKVHCRWYYCPEESHG-GRRQLHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYTRLENV 84
Cdd:cd04721  24 YVAYIEDLYEDKKGSKMVKVRWFHTTDEVGAaLSPDSVNPREIFLSPNLQVISVECIDGLATVLTREHYEKFQSV 98
BAH_MTA cd04709
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ...
 5-76 1.22e-04

BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The Metastasis-associated protein MTA1 is part of the NURD (nucleosome remodeling and deacetylating) complex and plays a role in cellular transformation and metastasis. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240060  Cd Length: 164  Bit Score: 40.84  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22328317   5 DAGKAPYV-ARVEKIEADARNNVKVHCRWYY-----------------------CPEESHGGRRQLHGaKELFLSDHFDV 60
Cdd:cd04709  14 SSPNNPYLiRRIEELNKTARGHVEAKVVCYYrrrdipdslyqladqhrreleekSDDLTPKQRHQLRH-RELFLSRQVET 92

                        90
                ....*....|....*.
gi 22328317  61 QSAHTIEGKCIVHTFK 76
Cdd:cd04709  93 LPATHIRGKCSVTLLN 108
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 113-155 6.73e-03

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 33.34  E-value: 6.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 22328317    113 CEMPYNSDELMELLLCHYRVHLACVGVTIEEAKKLEHFVCVEC 155
Cdd:smart00249   5 CGKPDDGGELLQCDGCDRWYHQTCLGPPLLEEEPDGKWYCPKC 47
 
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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