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Conserved domains on  [gi|1039737294|ref|XP_017170055|]
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BAH and coiled-coil domain-containing protein 1 isoform X2 [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. ...
 2516-2679 2.06e-58

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: 197.62  E-value: 2.06e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2516 KETLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMVVKVKWFYHPEETKLGKRQSDGKvrcgqvrwgpspcpgslgew 2595
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGE-------------------- 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2596 alslgvacfcrgrprhcmcslarqNALYQSCHEDENDVQTISHKCQVVGREQYEQMMRGR-KYQDQQDLYYLAGTYDPTT 2674
Cdd:cd04714     61 ------------------------KELFASDHQDENSVQTIEHKCYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDT 116


                   ....*
gi 1039737294 2675 GRLVT 2679
Cdd:cd04714    117 GMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1974-2041 1.18e-39

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: 141.87  E-value: 1.18e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 1974 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASSDEED--LDSVLVEFDDGDTGHIAVSNIRLLPPDFK 2041
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. ...
 2516-2679 2.06e-58

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: 197.62  E-value: 2.06e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2516 KETLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMVVKVKWFYHPEETKLGKRQSDGKvrcgqvrwgpspcpgslgew 2595
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGE-------------------- 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2596 alslgvacfcrgrprhcmcslarqNALYQSCHEDENDVQTISHKCQVVGREQYEQMMRGR-KYQDQQDLYYLAGTYDPTT 2674
Cdd:cd04714     61 ------------------------KELFASDHQDENSVQTIEHKCYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDT 116


                   ....*
gi 1039737294 2675 GRLVT 2679
Cdd:cd04714    117 GMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1974-2041 1.18e-39

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: 141.87  E-value: 1.18e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 1974 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASSDEED--LDSVLVEFDDGDTGHIAVSNIRLLPPDFK 2041
Cdd:cd20470      1 PQSSRQLPPGTRVCAYWSQKSRCLYPGNVVRGSSGIDEEddEDSVMVEFDDGDRGRISVSNIRLLPPDYK 70
BAH smart00439
Bromo adjacent homology domain;
2518-2678 7.03e-13

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 67.32  E-value: 7.03e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294  2518 TLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSN--MVVKVKWFYHPEETKLGKRqsdgkvrcgqvrwgpspcpgslgew 2595
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKA------------------------- 55

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294  2596 alslgvACFCRgrprhcmcslarqNALYQSCHEDENDVQTISHKCQVVGREQYEQmMRGRKYQDQQDLYYLAGTYDPTTG 2675
Cdd:smart00439   56 ------ALFDK-------------NEVFLSDEYDTVPLSDIIGKCNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKG 115


                    ...
gi 1039737294  2676 RLV 2678
Cdd:smart00439  116 SFK 118
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 2517-2678 4.82e-10

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: 59.24  E-value: 4.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2517 ETLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMV-VKVKWFYHPEETklgkrqsdgkvrcgqvrwgpspcPGSLGEW 2595
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEET-----------------------VHRAGKA 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2596 ALSlgvacfcrgrprhcmcslarqNALYQSCHEDENDVQTISHKCQVVGREQYEqmmRGR-KYQDQQDLYYLAGTYDPTT 2674
Cdd:pfam01426   58 FNK---------------------DELFLSDEEDDVPLSAIIGKCSVLHKSDLE---SLDpYKIKEPDDFFCELLYDPKT 113


                   ....
gi 1039737294 2675 GRLV 2678
Cdd:pfam01426  114 KSFK 117
Tudor_3 pfam18115
DNA repair protein Crb2 Tudor domain; This is the tudor domain found in DNA repair protein ...
 1984-2036 5.94e-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: 5.94e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039737294 1984 TRVCAYWSQKSRCLYPGNVVRGASSDEEDLdsvLVEFDDGDTGHIAVSNIRLL 2036
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. ...
 2516-2679 2.06e-58

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: 197.62  E-value: 2.06e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2516 KETLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMVVKVKWFYHPEETKLGKRQSDGKvrcgqvrwgpspcpgslgew 2595
Cdd:cd04714      1 KEIIRVGDCVLFKSPGRPSLPYVARIESLWEDPEGNMVVRVKWYYRPEETKGGRKPNHGE-------------------- 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2596 alslgvacfcrgrprhcmcslarqNALYQSCHEDENDVQTISHKCQVVGREQYEQMMRGR-KYQDQQDLYYLAGTYDPTT 2674
Cdd:cd04714     61 ------------------------KELFASDHQDENSVQTIEHKCYVLTFAEYERLARVKkKPQDGVDFYYCAGTYNPDT 116


                   ....*
gi 1039737294 2675 GRLVT 2679
Cdd:cd04714    117 GMLKC 121
Tudor_BAHCC1 cd20470
Tudor domain found in BAH and coiled-coil domain-containing protein 1 (BAHCC1) and similar ...
 1974-2041 1.18e-39

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: 141.87  E-value: 1.18e-39
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 1974 PQSSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASSDEED--LDSVLVEFDDGDTGHIAVSNIRLLPPDFK 2041
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 ...
 1976-2041 1.17e-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: 1.17e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039737294 1976 SSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASSDEE-DLDSVLVEFDDGDTGHIAVSNIRLLPPDFK 2041
Cdd:cd20397      1 SVEYLPPGTRVCAYWSQQYRCLYPGTVISGEPDSEDsQEGKVPVEFDDGDSGKIPLSDIRLLPPDYP 67
Tudor_TNRC18 cd20469
Tudor domain found in trinucleotide repeat-containing gene 18 protein (TNRC18) and similar ...
 1976-2042 9.12e-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: 9.12e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039737294 1976 SSRYLPPGTRVCAYWSQKSRCLYPGNVVRGASSDEEDLDSVLVEFDDGDTGHIAVSNIRLLPPDFKI 2042
Cdd:cd20469      1 SVRFLPEGTRVCAYWSQQYRCLYPGTVVKGSPDPEEDDDLITVEFDDGDSGRIPLDHIRLLPPDYPI 67
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 2516-2678 1.49e-22

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: 95.15  E-value: 1.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2516 KETLRIGDCAVFLSAG--RPNLPYIGRIESLWESWGSNMVVKVKWFYHPEETKLGKRQSdgkvrcgqvrwgpspcpgslg 2593
Cdd:cd04370      1 GITYEVGDSVYVEPDDsiKSDPPYIARIEELWEDTNGSKQVKVRWFYRPEETPKGLSPF--------------------- 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2594 ewalslgvacfcrgrprhcmcslARQNALYQSCHEDENDVQTISHKCQVVGREQYEQMMRgRKYQDQQDLYYLAGTYDPT 2673
Cdd:cd04370     60 -----------------------ALRRELFLSDHLDEIPVESIIGKCKVLFVSEFEGLKQ-RPNKIDTDDFFCRLAYDPT 115


                   ....*
gi 1039737294 2674 TGRLV 2678
Cdd:cd04370    116 TKEFK 120
BAH smart00439
Bromo adjacent homology domain;
2518-2678 7.03e-13

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 67.32  E-value: 7.03e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294  2518 TLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSN--MVVKVKWFYHPEETKLGKRqsdgkvrcgqvrwgpspcpgslgew 2595
Cdd:smart00439    1 TISVGDFVLVEPDDADEPYYIGRIEEIFETKKNSesKMVRVRWFYRPEETVLEKA------------------------- 55

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294  2596 alslgvACFCRgrprhcmcslarqNALYQSCHEDENDVQTISHKCQVVGREQYEQmMRGRKYQDQQDLYYLAGTYDPTTG 2675
Cdd:smart00439   56 ------ALFDK-------------NEVFLSDEYDTVPLSDIIGKCNVLYKSDYPG-LRPEGSIGEPDVFFCESAYDPEKG 115


                    ...
gi 1039737294  2676 RLV 2678
Cdd:smart00439  116 SFK 118
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 2517-2678 4.82e-10

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: 59.24  E-value: 4.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2517 ETLRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMV-VKVKWFYHPEETklgkrqsdgkvrcgqvrwgpspcPGSLGEW 2595
Cdd:pfam01426    1 ETYSVGDFVLVEPDDADEPYYVARIEELFEDTKNGKKmVRVQWFYRPEET-----------------------VHRAGKA 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2596 ALSlgvacfcrgrprhcmcslarqNALYQSCHEDENDVQTISHKCQVVGREQYEqmmRGR-KYQDQQDLYYLAGTYDPTT 2674
Cdd:pfam01426   58 FNK---------------------DELFLSDEEDDVPLSAIIGKCSVLHKSDLE---SLDpYKIKEPDDFFCELLYDPKT 113


                   ....
gi 1039737294 2675 GRLV 2678
Cdd:pfam01426  114 KSFK 117
BAH_polybromo cd04717
BAH, or Bromo Adjacent Homology domain, as present in polybromo and yeast RSC1/2. The human ...
 2519-2565 4.08e-06

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: 47.96  E-value: 4.08e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1039737294 2519 LRIGDCAVFLSAGRPNLPYIGRIESLWESWGSNMVVKVKWFYHPEET 2565
Cdd:cd04717      4 YRVGDCVYVANPEDPSKPIIFRIERLWKDEDGEKFFFGCWFYRPEET 50
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 1982-2033 3.85e-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: 3.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039737294 1982 PGTRVCAYWSQKSRcLYPGNVVRgassDEEDlDSVLVEFDDGDTGHIAVSNI 2033
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 ...
 1984-2036 5.94e-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: 5.94e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039737294 1984 TRVCAYWSQKSRCLYPGNVVRGASSDEEDLdsvLVEFDDGDTGHIAVSNIRLL 2036
Cdd:pfam18115    1 NRVFALWKGKDRAYYPATCLGTSGSGSQRY---LVRFDDGTPTEVDSGQVRRL 50
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 2501-2642 1.16e-04

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: 44.76  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039737294 2501 KGKARKLFYKAIVRGKETLRIGDCAVFLSA-GRPnlPYIGRIESLWESWGSNMVVKVKWFYHPEETKLGKrqsdgkvrcg 2579
Cdd:cd04713      3 KGKKKKCHYTSFEKDGNKYRLEDCVLLVPEdDQK--PYIAIIKDIYKQEEGSLKLEVQWLYRPEEIEKKK---------- 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039737294 2580 qvrwgpspcpgsLGEWalslgvacfCRGRPRHcmcslarqnaLYQSCHEDENDVQTISHKCQV 2642
Cdd:cd04713     71 ------------GGNW---------KAEDPRE----------LFYSFHRDEVPAESVLHPCKV 102
Tudor_SpCrb2-like_rpt1 cd20395
first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and ...
 1983-2036 2.73e-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: 2.73e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039737294 1983 GTRVCAYWSqKSRCLYPGNVVRGASSDeedldSVLVEFDDGDTGHIAVSNIRLL 2036
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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