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Conserved domains on  [gi|30697711|ref|NP_177025|]
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Agenet and 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_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 144-271 1.49e-70

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: 224.63  E-value: 1.49e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697711 144 YLRNGVRISVNDFVYVLAEQHKRLVAYIEDLYEDSKGKKMVVVRWFHKTEEVGSVLSDD-DNDREIFFSLNRQDISIECI 222
Cdd:cd04721   1 FCRNGVTISVHDFVYVLSEEEDRYVAYIEDLYEDKKGSKMVKVRWFHTTDEVGAALSPDsVNPREIFLSPNLQVISVECI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 30697711 223 DYLATVLSPQHYEKFLKVPMHV-QTVAFFCQKLYGDDGLKPYDITQLEGY 271
Cdd:cd04721  81 DGLATVLTREHYEKFQSVPKNSsELQAYFCYRQIDNNKVKPFDITQLRGY 130
Tudor_Agenet_AtDUF_rpt1_3 cd20405
first and third Tudor-like Agenet domains found in a family of Arabidopsis thaliana DUF724 ...
 363-421 6.09e-14

first and third Tudor-like Agenet domains found in a family of Arabidopsis thaliana DUF724 domain-containing proteins (AtDUFs); The family includes a group of AtDUFs (AtDUF1-3 and AtDUF6-8) that may be involved in the polar growth of plant cells via transportation of RNAs. Members of this family have four Tudor-like Agenet domains, except for AtDUF8, which contains only two copies of the Tudor-like Agenet domain. AtDUF4 and AtDUF5 are not included here due to the lack of a Tudor-like Agenet domain. The model corresponds to the first and third Tudor-like Agenet domains in AtDUF1-3 and AtDUF6-7, as well as the first Tudor-like Agenet domain in AtDUF8. 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: 410476  Cd Length: 65  Bit Score: 66.90  E-value: 6.09e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30697711 363 IKKGSLIEVLSEDSGIRGCWFKALVLKKH--KDKVKVQYQDIQDaDDESKKLEEWILTSRV 421
Cdd:cd20405   1 FSKGTEVEVSSEEEGFRGSWYRAIVVKEPegEKKFLVKYDELLL-DDGSEPLEETVDLRRV 60
Tudor_Agenet_FMRP-like_rpt2 cd20403
second Tudor-like Agenet domain found in the fragile X mental retardation protein (FMRP) ...
 455-500 6.07e-09

second Tudor-like Agenet domain found in the fragile X mental retardation protein (FMRP) family; The FMRP family includes synaptic functional regulator FMR1, fragile X mental retardation syndrome-related protein 1 (FXR1) and 2 (FXR2). FMR1, also called fragile X mental retardation protein 1 (FMRP), is a multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs. FXR1 and FXR2 are RNA-binding proteins that shuttle between the nucleus and cytoplasm and associate with polyribosomes, predominantly with the 60S ribosomal subunit. Members of this family contain two copies of the Tudor-like Agenet domain. The model corresponds to the second 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: 410474  Cd Length: 50  Bit Score: 52.32  E-value: 6.07e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 30697711 455 VGMPVDVWWC--DGWWEGiVVQEVSEEKFEVYLPG--EKKMSAFHRNDLR 500
Cdd:cd20403   1 EGDEVEVYSRapDGWWEG-VVKMVKGEFYVVEFPGfdETYTEIVELERLR 49
 
Name Accession Description Interval E-value
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 144-271 1.49e-70

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: 224.63  E-value: 1.49e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697711 144 YLRNGVRISVNDFVYVLAEQHKRLVAYIEDLYEDSKGKKMVVVRWFHKTEEVGSVLSDD-DNDREIFFSLNRQDISIECI 222
Cdd:cd04721   1 FCRNGVTISVHDFVYVLSEEEDRYVAYIEDLYEDKKGSKMVKVRWFHTTDEVGAALSPDsVNPREIFLSPNLQVISVECI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 30697711 223 DYLATVLSPQHYEKFLKVPMHV-QTVAFFCQKLYGDDGLKPYDITQLEGY 271
Cdd:cd04721  81 DGLATVLTREHYEKFQSVPKNSsELQAYFCYRQIDNNKVKPFDITQLRGY 130
Tudor_Agenet_AtDUF_rpt1_3 cd20405
first and third Tudor-like Agenet domains found in a family of Arabidopsis thaliana DUF724 ...
 363-421 6.09e-14

first and third Tudor-like Agenet domains found in a family of Arabidopsis thaliana DUF724 domain-containing proteins (AtDUFs); The family includes a group of AtDUFs (AtDUF1-3 and AtDUF6-8) that may be involved in the polar growth of plant cells via transportation of RNAs. Members of this family have four Tudor-like Agenet domains, except for AtDUF8, which contains only two copies of the Tudor-like Agenet domain. AtDUF4 and AtDUF5 are not included here due to the lack of a Tudor-like Agenet domain. The model corresponds to the first and third Tudor-like Agenet domains in AtDUF1-3 and AtDUF6-7, as well as the first Tudor-like Agenet domain in AtDUF8. 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: 410476  Cd Length: 65  Bit Score: 66.90  E-value: 6.09e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30697711 363 IKKGSLIEVLSEDSGIRGCWFKALVLKKH--KDKVKVQYQDIQDaDDESKKLEEWILTSRV 421
Cdd:cd20405   1 FSKGTEVEVSSEEEGFRGSWYRAIVVKEPegEKKFLVKYDELLL-DDGSEPLEETVDLRRV 60
Agenet pfam05641
Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the ...
 366-421 2.22e-13

Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the agenet domain is unknown. This family now matches both the two Agenet domains in the FMR proteins.


Pssm-ID: 461700  Cd Length: 61  Bit Score: 65.03  E-value: 2.22e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30697711   366 GSLIEVLSEDSGIRGCWFKALVLKKH-KDKVKVQYQDIQDaDDESKKLEEWILTSRV 421
Cdd:pfam05641   1 GDKVEVLSDEEGFRGAWFRAKVIKVLkGDKYLVEYDDLLD-EDGGGPLEEWVPASDI 56
Tudor_Agenet_FMRP-like_rpt2 cd20403
second Tudor-like Agenet domain found in the fragile X mental retardation protein (FMRP) ...
 455-500 6.07e-09

second Tudor-like Agenet domain found in the fragile X mental retardation protein (FMRP) family; The FMRP family includes synaptic functional regulator FMR1, fragile X mental retardation syndrome-related protein 1 (FXR1) and 2 (FXR2). FMR1, also called fragile X mental retardation protein 1 (FMRP), is a multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs. FXR1 and FXR2 are RNA-binding proteins that shuttle between the nucleus and cytoplasm and associate with polyribosomes, predominantly with the 60S ribosomal subunit. Members of this family contain two copies of the Tudor-like Agenet domain. The model corresponds to the second 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: 410474  Cd Length: 50  Bit Score: 52.32  E-value: 6.07e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 30697711 455 VGMPVDVWWC--DGWWEGiVVQEVSEEKFEVYLPG--EKKMSAFHRNDLR 500
Cdd:cd20403   1 EGDEVEVYSRapDGWWEG-VVKMVKGEFYVVEFPGfdETYTEIVELERLR 49
Agenet smart00743
Tudor-like domain present in plant sequences; Domain in plant sequences with possible ...
 455-507 2.00e-08

Tudor-like domain present in plant sequences; Domain in plant sequences with possible chromatin-associated functions.


Pssm-ID: 214798  Cd Length: 59  Bit Score: 50.79  E-value: 2.00e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 30697711    455 VGMPVDVWWCDGWWEGIVVQEVSEEKFEVYLPG--EKKMSAFHRNDLRQSREWLD 507
Cdd:smart00743   5 EGDRVEVFSEDSWWEAVVTKVLGDGKYLVEYKGesEPLELTVDWSDLRPHPPWVD 59
BAH smart00439
Bromo adjacent homology domain;
150-255 4.81e-08

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 51.91  E-value: 4.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697711    150 RISVNDFVYVLAEQHKRL--VAYIEDLYEDSKGK--KMVVVRWFHKTEEVGSVLSDDDNDREIFFSLNRQDISIECI--- 222
Cdd:smart00439   1 TISVGDFVLVEPDDADEPyyIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKNEVFLSDEYDTVPLSDIigk 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 30697711    223 ---DYLATVLSPQHYEKFLKVPMhvqtvaFFCQKLY 255
Cdd:smart00439  81 cnvLYKSDYPGLRPEGSIGEPDV------FFCESAY 110
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 151-255 1.16e-06

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: 47.69  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697711   151 ISVNDFVYVLAEQH--KRLVAYIEDLYEDSK-GKKMVVVRWFHKTEEVGSVLSDDDNDREIFFSLNRQDISIECIDYLAT 227
Cdd:pfam01426   3 YSVGDFVLVEPDDAdePYYVARIEELFEDTKnGKKMVRVQWFYRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGKCS 82

                          90       100
                  ....*....|....*....|....*...
gi 30697711   228 VLSPQHYEKFLKVPMHVQTVaFFCQKLY 255
Cdd:pfam01426  83 VLHKSDLESLDPYKIKEPDD-FFCELLY 109
Agenet smart00743
Tudor-like domain present in plant sequences; Domain in plant sequences with possible ...
 361-427 5.09e-06

Tudor-like domain present in plant sequences; Domain in plant sequences with possible chromatin-associated functions.


Pssm-ID: 214798  Cd Length: 59  Bit Score: 44.24  E-value: 5.09e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30697711    361 HHIKKGSLIEVLSEDsgirgCWFKALVLKKHKD-KVKVQYQDiqdaDDESKKLEEWILTSRVAAGDHL 427
Cdd:smart00743   1 SDFKEGDRVEVFSED-----SWWEAVVTKVLGDgKYLVEYKG----ESEPLELTVDWSDLRPHPPWVD 59
 
Name Accession Description Interval E-value
BAH_plant_1 cd04721
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 144-271 1.49e-70

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: 224.63  E-value: 1.49e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697711 144 YLRNGVRISVNDFVYVLAEQHKRLVAYIEDLYEDSKGKKMVVVRWFHKTEEVGSVLSDD-DNDREIFFSLNRQDISIECI 222
Cdd:cd04721   1 FCRNGVTISVHDFVYVLSEEEDRYVAYIEDLYEDKKGSKMVKVRWFHTTDEVGAALSPDsVNPREIFLSPNLQVISVECI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 30697711 223 DYLATVLSPQHYEKFLKVPMHV-QTVAFFCQKLYGDDGLKPYDITQLEGY 271
Cdd:cd04721  81 DGLATVLTREHYEKFQSVPKNSsELQAYFCYRQIDNNKVKPFDITQLRGY 130
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 148-264 6.65e-16

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: 74.35  E-value: 6.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697711 148 GVRISVNDFVYVLAEQHKRL----VAYIEDLYEDSKGKKMVVVRWFHKTEEVGSVLSDDDNDREIFFSLNRQDISIECID 223
Cdd:cd04370   1 GITYEVGDSVYVEPDDSIKSdppyIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPFALRRELFLSDHLDEIPVESII 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 30697711 224 YLATVLSPQHYEKFLKVPMHVQTVAFFCQKLY--GDDGLKPYD 264
Cdd:cd04370  81 GKCKVLFVSEFEGLKQRPNKIDTDDFFCRLAYdpTTKEFKALE 123
Tudor_Agenet_AtDUF_rpt1_3 cd20405
first and third Tudor-like Agenet domains found in a family of Arabidopsis thaliana DUF724 ...
 363-421 6.09e-14

first and third Tudor-like Agenet domains found in a family of Arabidopsis thaliana DUF724 domain-containing proteins (AtDUFs); The family includes a group of AtDUFs (AtDUF1-3 and AtDUF6-8) that may be involved in the polar growth of plant cells via transportation of RNAs. Members of this family have four Tudor-like Agenet domains, except for AtDUF8, which contains only two copies of the Tudor-like Agenet domain. AtDUF4 and AtDUF5 are not included here due to the lack of a Tudor-like Agenet domain. The model corresponds to the first and third Tudor-like Agenet domains in AtDUF1-3 and AtDUF6-7, as well as the first Tudor-like Agenet domain in AtDUF8. 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: 410476  Cd Length: 65  Bit Score: 66.90  E-value: 6.09e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30697711 363 IKKGSLIEVLSEDSGIRGCWFKALVLKKH--KDKVKVQYQDIQDaDDESKKLEEWILTSRV 421
Cdd:cd20405   1 FSKGTEVEVSSEEEGFRGSWYRAIVVKEPegEKKFLVKYDELLL-DDGSEPLEETVDLRRV 60
Agenet pfam05641
Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the ...
 366-421 2.22e-13

Agenet domain; This domain is related to the TUDOR domain pfam00567. The function of the agenet domain is unknown. This family now matches both the two Agenet domains in the FMR proteins.


Pssm-ID: 461700  Cd Length: 61  Bit Score: 65.03  E-value: 2.22e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30697711   366 GSLIEVLSEDSGIRGCWFKALVLKKH-KDKVKVQYQDIQDaDDESKKLEEWILTSRV 421
Cdd:pfam05641   1 GDKVEVLSDEEGFRGAWFRAKVIKVLkGDKYLVEYDDLLD-EDGGGPLEEWVPASDI 56
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 136-255 7.28e-12

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: 63.64  E-value: 7.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697711 136 KRRKHYQSYLRNGVRISVNDFVYVLAEQH-KRLVAYIEDLYEDSKGKKMVVVRWFHKTEEV---GSVLSDDDNDREIFFS 211
Cdd:cd04713   6 KKKCHYTSFEKDGNKYRLEDCVLLVPEDDqKPYIAIIKDIYKQEEGSLKLEVQWLYRPEEIekkKGGNWKAEDPRELFYS 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 30697711 212 LNRQDISIECIDYLATV-LSPQHyekfLKVPMHVQTVAFFCQKLY 255
Cdd:cd04713  86 FHRDEVPAESVLHPCKVaFVPKG----KQIPLRKGHSGFIVRRVY 126
Tudor_Agenet_FMRP-like_rpt2 cd20403
second Tudor-like Agenet domain found in the fragile X mental retardation protein (FMRP) ...
 455-500 6.07e-09

second Tudor-like Agenet domain found in the fragile X mental retardation protein (FMRP) family; The FMRP family includes synaptic functional regulator FMR1, fragile X mental retardation syndrome-related protein 1 (FXR1) and 2 (FXR2). FMR1, also called fragile X mental retardation protein 1 (FMRP), is a multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of a subset of mRNAs. FXR1 and FXR2 are RNA-binding proteins that shuttle between the nucleus and cytoplasm and associate with polyribosomes, predominantly with the 60S ribosomal subunit. Members of this family contain two copies of the Tudor-like Agenet domain. The model corresponds to the second 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: 410474  Cd Length: 50  Bit Score: 52.32  E-value: 6.07e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 30697711 455 VGMPVDVWWC--DGWWEGiVVQEVSEEKFEVYLPG--EKKMSAFHRNDLR 500
Cdd:cd20403   1 EGDEVEVYSRapDGWWEG-VVKMVKGEFYVVEFPGfdETYTEIVELERLR 49
Agenet smart00743
Tudor-like domain present in plant sequences; Domain in plant sequences with possible ...
 455-507 2.00e-08

Tudor-like domain present in plant sequences; Domain in plant sequences with possible chromatin-associated functions.


Pssm-ID: 214798  Cd Length: 59  Bit Score: 50.79  E-value: 2.00e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 30697711    455 VGMPVDVWWCDGWWEGIVVQEVSEEKFEVYLPG--EKKMSAFHRNDLRQSREWLD 507
Cdd:smart00743   5 EGDRVEVFSEDSWWEAVVTKVLGDGKYLVEYKGesEPLELTVDWSDLRPHPPWVD 59
BAH smart00439
Bromo adjacent homology domain;
150-255 4.81e-08

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 51.91  E-value: 4.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697711    150 RISVNDFVYVLAEQHKRL--VAYIEDLYEDSKGK--KMVVVRWFHKTEEVGSVLSDDDNDREIFFSLNRQDISIECI--- 222
Cdd:smart00439   1 TISVGDFVLVEPDDADEPyyIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKAALFDKNEVFLSDEYDTVPLSDIigk 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 30697711    223 ---DYLATVLSPQHYEKFLKVPMhvqtvaFFCQKLY 255
Cdd:smart00439  81 cnvLYKSDYPGLRPEGSIGEPDV------FFCESAY 110
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 151-251 5.51e-08

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: 51.63  E-value: 5.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697711 151 ISVNDFVYVLAEQHKRL--VAYIEDLYEDSKGKKMVVVRWFHKTEEVGSVLSDDDNDREIFFSLNRQDISIECIDYLATV 228
Cdd:cd04714   4 IRVGDCVLFKSPGRPSLpyVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGEKELFASDHQDENSVQTIEHKCYV 83

                        90       100
                ....*....|....*....|...
gi 30697711 229 LSPQHYEKFLKVPMHVQTVAFFC 251
Cdd:cd04714  84 LTFAEYERLARVKKKPQDGVDFY 106
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 151-255 1.16e-06

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: 47.69  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697711   151 ISVNDFVYVLAEQH--KRLVAYIEDLYEDSK-GKKMVVVRWFHKTEEVGSVLSDDDNDREIFFSLNRQDISIECIDYLAT 227
Cdd:pfam01426   3 YSVGDFVLVEPDDAdePYYVARIEELFEDTKnGKKMVRVQWFYRPEETVHRAGKAFNKDELFLSDEEDDVPLSAIIGKCS 82

                          90       100
                  ....*....|....*....|....*...
gi 30697711   228 VLSPQHYEKFLKVPMHVQTVaFFCQKLY 255
Cdd:pfam01426  83 VLHKSDLESLDPYKIKEPDD-FFCELLY 109
Agenet smart00743
Tudor-like domain present in plant sequences; Domain in plant sequences with possible ...
 361-427 5.09e-06

Tudor-like domain present in plant sequences; Domain in plant sequences with possible chromatin-associated functions.


Pssm-ID: 214798  Cd Length: 59  Bit Score: 44.24  E-value: 5.09e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30697711    361 HHIKKGSLIEVLSEDsgirgCWFKALVLKKHKD-KVKVQYQDiqdaDDESKKLEEWILTSRVAAGDHL 427
Cdd:smart00743   1 SDFKEGDRVEVFSED-----SWWEAVVTKVLGDgKYLVEYKG----ESEPLELTVDWSDLRPHPPWVD 59
Tudor_Agenet_AtDUF_rpt2_4 cd20406
second and fourth Tudor-like Agenet domains found in the family of Arabidopsis thaliana DUF724 ...
 459-500 2.52e-05

second and fourth Tudor-like Agenet domains found in the family of Arabidopsis thaliana DUF724 domain-containing proteins (AtDUFs); The family includes a group of AtDUFs (AtDUF1-3 and AtDUF6-8) that may be involved in the polar growth of plant cells via transportation of RNAs. Members of this family have four Tudor-like Agenet domains, except for AtDUF8, which contains only two copies of the Tudor-like Agenet domain. AtDUF4 and AtDUF5 are not included here due to the lack of a Tudor-like Agenet domain. The model corresponds to the second and fourth Tudor-like Agenet domains in AtDUF1-3 and AtDUF6-7, as well as the first Tudor-like Agenet domain in AtDUF8. 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: 410477  Cd Length: 47  Bit Score: 41.81  E-value: 2.52e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 30697711 459 VDVWWCDGWWEGIVVQEVSEEKFEVYLPGEKKMSAFHRNDLR 500
Cdd:cd20406   5 VDAFYNGGWWPGVVTKVLEDNRYLVYLDATKEELEFEHSDLR 46
BAH_Orc1p_animal cd04719
BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces ...
 151-222 2.13e-04

BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces cerevisiae Orc1p. Orc1 is part of the Yeast Sir1-origin recognition complex. The Orc1p BAH doman functions in epigenetic silencing. In vertebrates, a similar ORC protein complex exists, which has been shown essential for DNA replication in Xenopus laevis. 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: 240070  Cd Length: 128  Bit Score: 41.59  E-value: 2.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697711 151 ISVNDFVYVLAEQHKR-LVAYIEDLYEDSKGK---KMVVVRWFHKTEEVGSVLSDD----DNDREIFF---SLNRQDISI 219
Cdd:cd04719   4 IEVGDFVLIEGEDADGpDVARILHLYEDGNEDddpKRAIVQWFSRPSEVPKNKRKLlgrePHSQEVFFysrSSCDNDIDA 83


                ...
gi 30697711 220 ECI 222
Cdd:cd04719  84 ETI 86
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 148-222 6.41e-03

BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5)-methyltransferases (DCM) from plants. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. 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: 240067  Cd Length: 122  Bit Score: 37.04  E-value: 6.41e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30697711 148 GVRISVNDFVYVLAEQHKRL-VAYIEDLYEDSKGKKMVVVRWFHKTEE-VGSVLSDDDNDREIFFSLNRQDISIECI 222
Cdd:cd04716   1 GITYNLGDDAYVQGGEGEEPfICKITEFFEGTDGKTYFTAQWFYRAEDtVIERQATNHDKKRVFYSEIKNDNPLDCL 77
 
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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