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Conserved domains on  [gi|1039737296|ref|XP_017170056|]
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BAH and coiled-coil domain-containing protein 1 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 2517-2636 7.92e-66

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: 218.81  E-value: 7.92e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2517 KETLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMVVKVKWFYHPEETKLGKRQSDGKNALYQSCHEDENDVQTISHK 2596
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1039737296 2597 CQVVGREQYEQMMRGR-KYQDQQDLYYLAGTYDPTTGRLVT 2636
Cdd:cd04714     81 CYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1975-2042 9.94e-40

Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar proteins; BAHCC1, also called Bromo adjacent homology domain-containing protein 2 (BAHD2), or BAH domain-containing protein 2, may function as a transcriptional regulator. BAHCC1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410541  Cd Length: 70  Bit Score: 142.25  E-value: 9.94e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 1975 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASSDEED--LDSVLVEFDDGDTGHIAVSNIRLLPPDFK 2042
Cdd:cd20470      1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRGSSGIDEEddEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 2517-2636 7.92e-66

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: 218.81  E-value: 7.92e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2517 KETLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMVVKVKWFYHPEETKLGKRQSDGKNALYQSCHEDENDVQTISHK 2596
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1039737296 2597 CQVVGREQYEQMMRGR-KYQDQQDLYYLAGTYDPTTGRLVT 2636
Cdd:cd04714     81 CYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1975-2042 9.94e-40

Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar proteins; BAHCC1, also called Bromo adjacent homology domain-containing protein 2 (BAHD2), or BAH domain-containing protein 2, may function as a transcriptional regulator. BAHCC1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410541  Cd Length: 70  Bit Score: 142.25  E-value: 9.94e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 1975 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASSDEED--LDSVLVEFDDGDTGHIAVSNIRLLPPDFK 2042
Cdd:cd20470      1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRGSSGIDEEddEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
BAH smart00439
Bromo adjacent homology domain;
2519-2635 3.53e-20

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 88.12  E-value: 3.53e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296  2519 TLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSN--MVVKVKWFYHPEETKLGKRQSDGKNALYQSCHEDENDVQTISHK 2596
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1039737296  2597 CQVVGREQYEQmMRGRKYQDQQDLYYLAGTYDPTTGRLV 2635
Cdd:smart00439   81 CNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKGSFK 118
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 2518-2635 2.91e-16

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: 76.96  E-value: 2.91e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2518 ETLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMV-VKVKWFYHPEETKLGKRQSDGKNALYQSCHEDENDVQTISHK 2596
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1039737296 2597 CQVVGREQYEqmmRGR-KYQDQQDLYYLAGTYDPTTGRLV 2635
Cdd:pfam01426   81 CSVLHKSDLE---SLDpYKIKEPDDFFCELLYDPKTKSFK 117
Tudor_3 pfam18115
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ...
 1985-2037 5.85e-05

DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein crb2. Structural and functional studies of Crb2 and its mammalian homolog 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it also binds to H4K20me1. Furthermore, despite low amino acid sequence similarity, Crb2 is structurally related to 53BP1 in having two tudor domains and a conserved dimethyllysine-binding pocket, and that, like 53BP1, it directly binds H4-K20me2.


Pssm-ID: 436284  Cd Length: 50  Bit Score: 42.55  E-value: 5.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039737296 1985 TRVCAYWSQKSRCLYPGNVVRGASSDEEDLdsvLVEFDDGDTGHIAVSNIRLL 2037
Cdd:pfam18115    1 NRVFALWKGKDRAYYPATCLGTSGSGSQRY---LVRFDDGTPTEVDSGQVRRL 50
 
Name Accession Description Interval E-value
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 2517-2636 7.92e-66

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: 218.81  E-value: 7.92e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2517 KETLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMVVKVKWFYHPEETKLGKRQSDGKNALYQSCHEDENDVQTISHK 2596
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1039737296 2597 CQVVGREQYEQMMRGR-KYQDQQDLYYLAGTYDPTTGRLVT 2636
Cdd:cd04714     81 CYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDTGMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1975-2042 9.94e-40

Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar proteins; BAHCC1, also called Bromo adjacent homology domain-containing protein 2 (BAHD2), or BAH domain-containing protein 2, may function as a transcriptional regulator. BAHCC1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410541  Cd Length: 70  Bit Score: 142.25  E-value: 9.94e-40
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 1975 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASSDEED--LDSVLVEFDDGDTGHIAVSNIRLLPPDFK 2042
Cdd:cd20470      1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRGSSGIDEEddEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
Tudor_BAHCC1-like cd20397
Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The ...
 1977-2042 1.06e-32

Tudor domain found in the BAH and coiled-coil domain-containing protein 1 (BAHCC1) family; The family of BAHCC1 includes BAHCC1 and trinucleotide repeat-containing gene 18 protein (TNRC18). BAHCC1 may function as a transcriptional regulator. The biological function of TNRC18 remains unclear. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410468  Cd Length: 67  Bit Score: 122.05  E-value: 1.06e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039737296 1977 SSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASSDEE-DLDSVLVEFDDGDTGHIAVSNIRLLPPDFK 2042
Cdd:cd20397      1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDSEDsQEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
Tudor_TNRC18 cd20469
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ...
 1977-2043 8.97e-32

Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar proteins; TNRC18, also called long CAG trinucleotide repeat-containing gene 79 protein (CAGL79), is a protein that in humans is encoded by the TNRC18 gene. Its biological function remains unclear. TNRC18 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410540  Cd Length: 67  Bit Score: 119.45  E-value: 8.97e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039737296 1977 SSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASSDEEDLDSVLVEFDDGDTGHIAVSNIRLLPPDFKI 2043
Cdd:cd20469      1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 2517-2635 7.82e-30

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: 115.95  E-value: 7.82e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2517 KETLRIGDCAVFLSAG--RPNLPYIGRIESLWESWGSNMVVKVKWFYHPEETKLGKRQSDGKNALYQSCHEDENDVQTIS 2594
Cdd:cd04370      1 GITYEVGDSVYVEPDDsiKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFALRRELFLSDHLDEIPVESII 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1039737296 2595 HKCQVVGREQYEQMMRgRKYQDQQDLYYLAGTYDPTTGRLV 2635
Cdd:cd04370     81 GKCKVLFVSEFEGLKQ-RPNKIDTDDFFCRLAYDPTTKEFK 120
BAH smart00439
Bromo adjacent homology domain;
2519-2635 3.53e-20

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 88.12  E-value: 3.53e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296  2519 TLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSN--MVVKVKWFYHPEETKLGKRQSDGKNALYQSCHEDENDVQTISHK 2596
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKNEVFLSDEYDTVPLSDIIGK 80

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1039737296  2597 CQVVGREQYEQmMRGRKYQDQQDLYYLAGTYDPTTGRLV 2635
Cdd:smart00439   81 CNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKGSFK 118
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 2518-2635 2.91e-16

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: 76.96  E-value: 2.91e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2518 ETLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMV-VKVKWFYHPEETKLGKRQSDGKNALYQSCHEDENDVQTISHK 2596
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGK 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1039737296 2597 CQVVGREQYEqmmRGR-KYQDQQDLYYLAGTYDPTTGRLV 2635
Cdd:pfam01426   81 CSVLHKSDLE---SLDpYKIKEPDDFFCELLYDPKTKSFK 117
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 2502-2599 2.76e-10

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: 60.94  E-value: 2.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2502 KGKARKLFYKAIVRGKETLRIGDCAVFLSA-GRPnlPYIGRIESLWESWGSNMVVKVKWFYHPEETKL---GKRQSDGKN 2577
Cdd:cd04713      3 KGKKKKCHYTSFEKDGNKYRLEDCVLLVPEdDQK--PYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEKkkgGNWKAEDPR 80

                           90       100
                   ....*....|....*....|..
gi 1039737296 2578 ALYQSCHEDENDVQTISHKCQV 2599
Cdd:cd04713     81 ELFYSFHRDEVPAESVLHPCKV 102
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 2520-2612 7.38e-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: 50.28  E-value: 7.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2520 LRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMVVKVKWFYHPEETK--LGKRQSdgKNALYQSCHEDENDVQTISHKC 2597
Cdd:cd04717      4 YRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEETFhePTRKFY--KNEVFKSPLYETVPVEEIVGKC 81

                           90
                   ....*....|....*
gi 1039737296 2598 QVVGREQYeqmMRGR 2612
Cdd:cd04717     82 AVMDVKDY---IKGR 93
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 1983-2034 3.79e-05

Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; 53BP1, also called p53-binding protein 1 (p53BP1), is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics, and class-switch recombination (CSR) during antibody genesis. It plays a key role in the repair of DSBs in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1. It is recruited to DSB sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSB sites. 53BP1 contains one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410454  Cd Length: 52  Bit Score: 43.02  E-value: 3.79e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039737296 1983 PGTRVCAYWSQKSRcLYPGNVVRgassDEEDlDSVLVEFDDGDTGHIAVSNI 2034
Cdd:cd20383      1 VGTRVFAKWSSDGY-YYPGIITR----VLGD-GKYKVLFDDGYERDVKGKDI 46
Tudor_3 pfam18115
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ...
 1985-2037 5.85e-05

DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein crb2. Structural and functional studies of Crb2 and its mammalian homolog 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it also binds to H4K20me1. Furthermore, despite low amino acid sequence similarity, Crb2 is structurally related to 53BP1 in having two tudor domains and a conserved dimethyllysine-binding pocket, and that, like 53BP1, it directly binds H4-K20me2.


Pssm-ID: 436284  Cd Length: 50  Bit Score: 42.55  E-value: 5.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039737296 1985 TRVCAYWSQKSRCLYPGNVVRGASSDEEDLdsvLVEFDDGDTGHIAVSNIRLL 2037
Cdd:pfam18115    1 NRVFALWKGKDRAYYPATCLGTSGSGSQRY---LVRFDDGTPTEVDSGQVRRL 50
BAH_fungalPHD cd04710
BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. ...
 2515-2633 2.41e-04

BAH, or Bromo Adjacent Homology domain, as present in fungal proteins containing PHD domains. 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: 240061  Cd Length: 135  Bit Score: 43.51  E-value: 2.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2515 RGKETLRIGDcAVFLSAGRPNLPY-IGRI------------ESLWESWGSNMVVKVKWFYHPEEtkLGKRQSDGKNALYQ 2581
Cdd:cd04710      7 KNGELLKVND-HIYMSSEPPGEPYyIGRImefvpkhefpsgIHARVFPASYFQVRLNWYYRPRD--ISRRVVADSRLLYA 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039737296 2582 SCHEDENDVQTISHKCQVVGREQYEQMmrgRKYQDQQDLYYLAGTYDPTTGR 2633
Cdd:cd04710     84 SMHSDICPIGSVRGKCTVRHRDQIPDL---EEYKKRPNHFYFDQLFDRYILR 132
BAH_MTA cd04709
BAH, or Bromo Adjacent Homology domain, as present in MTA1 and similar proteins. The ...
 2521-2604 6.47e-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: 42.76  E-value: 6.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2521 RIGDCAVFLSAgrPNLPY-IGRIESLWESWGSNMVVKVKWFYhpeetklgkRQSDGKNALYQSCHEDENDVQTISHKCQV 2599
Cdd:cd04709      5 RVGDYVYFESS--PNNPYlIRRIEELNKTARGHVEAKVVCYY---------RRRDIPDSLYQLADQHRRELEEKSDDLTP 73


                   ....*
gi 1039737296 2600 VGREQ 2604
Cdd:cd04709     74 KQRHQ 78
BAH_Orc1p_like cd04715
BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of ...
 2497-2600 1.62e-03

BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of Saccharomyces cerevisiae Orc1p and similar proteins. Orc1 is part of the Yeast Sir1-origin recognition complex, the Orc1p BAH doman functions in epigenetic silencing. 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: 240066  Cd Length: 159  Bit Score: 41.72  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2497 QRRGMKGKARKL-FYKAIVRGKETLRIGDCAVFLSAGRPnlPYIGRIESLWESWGSNM--VVKVKWFYHPEETKLGKRQS 2573
Cdd:cd04715      6 VKRGEGGKKKDGqFYRSFTYDGVEYRLYDDVYVHNGDSE--PYIGKIIKIYETAIDSGkkKVKVIWFFRPSEIRMELKGE 83

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1039737296 2574 DGK--NALYQSCHEDE-----NDVQTISHKCQVV 2600
Cdd:cd04715     84 PKRhiNEVFLACGRGEglaniNLLESIIGKCNVV 117
BAH_plant_2 cd04718
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 2523-2628 2.38e-03

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: 41.03  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737296 2523 GDCAVFLSAGRpnlpYIGRIESLWESWGSNMVvKVKWFYHPEETKLGKRQSDGKNALYQSCHEDENDVQTISHKCQVVGR 2602
Cdd:cd04718     43 SACEKLLSGDL----WLARIEKLWEENGTYWY-AARWYTLPEETHMGRQPHNLRRELYLTNDFADIEMECILRHCSVKCP 117

                           90       100
                   ....*....|....*....|....*.
gi 1039737296 2603 EQYEqmmrgRKYQDQQDLYYLAGTYD 2628
Cdd:cd04718    118 KEFR-----DASNDGDDVFLCEYEYD 138
Tudor_SpCrb2-like_rpt1 cd20395
first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and ...
 1984-2037 2.69e-03

first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and similar proteins; Crb2, also called RAD9 protein homolog, or checkpoint mediator protein crb2, is a DNA repair protein essential for cell cycle arrest at the G1 and G2 stages following DNA damage by X-, and UV-irradiation, or inactivation of DNA ligase. Crb2 contains two Tudor domains. The model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410466  Cd Length: 50  Bit Score: 38.11  E-value: 2.69e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039737296 1984 GTRVCAYWSqKSRCLYPGNVVRGASSDeedldSVLVEFDDGDTGHIAVSNIRLL 2037
Cdd:cd20395      1 PTRVLAFWK-GDGNYYPATIVGPVSSS-----AYKVQFDDGTSSSVPPTQIRRL 48
 
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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