BRCA1 C Terminus (BRCT) domain; Brca1 C-terminal (BRCT) domains are a common protein-protein interaction regions in proteins involved in the DNA damage response and DNA repair. For example 53BP1 which plays multiple roles in mammalian DNA damage repair, has a C-terminal tandem BRCT domain (BRCT2), which in its orthologs, Saccharomyces cerevisiae Rad9p and Schizosaccharomyces pombe Crb2, mediates binding to the equivalents of gammaH2AX. Structural and functional studies indicate that the 53BP1-BRCT2 domain is a competent binding module for phosphorylated peptides with a clear specificity for the DNA-damage marker gammaH2AX, and in isolation from other parts of 53BP1 is sufficient for localization to sites of DNA damage in cells associated with gammaH2AX.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039760892 1774 NPFQNLKVLLVSDQQqNFLELWSEILMTGGAASVKQHHSsahNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEW 1853
Cdd:pfam18428    1 NPFKDLRILLVSEQK-NFVDFWSQILKLAGATVVKQHKS---DKAIPEGKFDVVVTDRSCPEEVLKKATQLGIPLVSTEW 76

                           90       100
                   ....*....|....*....|....
gi 1039760892 1854 VIQCLIVGERIGFKQHPKYKHDYV 1877
Cdd:pfam18428   77 VIQCLIHGELLPYDSHPKYRYDYT 100

BRCA1 C Terminus (BRCT) domain; Brca1 C-terminal (BRCT) domains are a common protein-protein interaction regions in proteins involved in the DNA damage response and DNA repair. For example 53BP1 which plays multiple roles in mammalian DNA damage repair, has a C-terminal tandem BRCT domain (BRCT2), which in its orthologs, Saccharomyces cerevisiae Rad9p and Schizosaccharomyces pombe Crb2, mediates binding to the equivalents of gammaH2AX. Structural and functional studies indicate that the 53BP1-BRCT2 domain is a competent binding module for phosphorylated peptides with a clear specificity for the DNA-damage marker gammaH2AX, and in isolation from other parts of 53BP1 is sufficient for localization to sites of DNA damage in cells associated with gammaH2AX.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039760892 1774 NPFQNLKVLLVSDQQqNFLELWSEILMTGGAASVKQHHSsahNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEW 1853
Cdd:pfam18428    1 NPFKDLRILLVSEQK-NFVDFWSQILKLAGATVVKQHKS---DKAIPEGKFDVVVTDRSCPEEVLKKATQLGIPLVSTEW 76

                           90       100
                   ....*....|....*....|....
gi 1039760892 1854 VIQCLIVGERIGFKQHPKYKHDYV 1877
Cdd:pfam18428   77 VIQCLIHGELLPYDSHPKYRYDYT 100

first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, also termed 53BP1, or TP53-binding protein 1 (TP53BP1) , is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis. TP53BP1 contains two tandem BRCT repeats. This family also includes Schizosaccharomyces pombe Crb2, which is a checkpoint mediator required for the cellular response to DNA damage. This model corresponds to the first BRCT domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039760892 1635 LFLGYAFLLTMATTSDklasrsklldgptgsseeeeefleiPPFNKQYTECQLRAGAGYILEDFNEAQC----------- 1703
Cdd:cd17745      1 IFSGCAFLLTGAEETD-------------------------KPFDKERLESQIEANGGTVLEDFDEELFndgrsstrksr 55

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039760892 1704 -NTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQ 1746
Cdd:cd17745     56 sKDLRFVFLIADSPSRTPKYLQALALGIPCVSHKWILDCIEAGK 99

breast cancer carboxy-terminal domain;

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039760892  1773 ENPFQNLKVLLVSDQQQNFLELWSE-ILMTGGAASVKQHHSSahnkdialgVFDVVVTDPSCPASVLKCAEALQLPVVSQ 1851
Cdd:smart00292    1 PKLFKGKTFYITGSFDKEERDELKElIEALGGKVTSSLSSKT---------TTHVIVGSPEGGKLELLKAIALGIPIVKE 71

                    ....*..
gi 1039760892  1852 EWVIQCL 1858
Cdd:smart00292   72 EWLLDCL 78

BRCA1 C Terminus (BRCT) domain; Brca1 C-terminal (BRCT) domains are a common protein-protein interaction regions in proteins involved in the DNA damage response and DNA repair. For example 53BP1 which plays multiple roles in mammalian DNA damage repair, has a C-terminal tandem BRCT domain (BRCT2), which in its orthologs, Saccharomyces cerevisiae Rad9p and Schizosaccharomyces pombe Crb2, mediates binding to the equivalents of gammaH2AX. Structural and functional studies indicate that the 53BP1-BRCT2 domain is a competent binding module for phosphorylated peptides with a clear specificity for the DNA-damage marker gammaH2AX, and in isolation from other parts of 53BP1 is sufficient for localization to sites of DNA damage in cells associated with gammaH2AX.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039760892 1774 NPFQNLKVLLVSDQQqNFLELWSEILMTGGAASVKQHHSsahNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEW 1853
Cdd:pfam18428    1 NPFKDLRILLVSEQK-NFVDFWSQILKLAGATVVKQHKS---DKAIPEGKFDVVVTDRSCPEEVLKKATQLGIPLVSTEW 76

                           90       100
                   ....*....|....*....|....
gi 1039760892 1854 VIQCLIVGERIGFKQHPKYKHDYV 1877
Cdd:pfam18428   77 VIQCLIHGELLPYDSHPKYRYDYT 100

first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, also termed 53BP1, or TP53-binding protein 1 (TP53BP1) , is a double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis. TP53BP1 contains two tandem BRCT repeats. This family also includes Schizosaccharomyces pombe Crb2, which is a checkpoint mediator required for the cellular response to DNA damage. This model corresponds to the first BRCT domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039760892 1635 LFLGYAFLLTMATTSDklasrsklldgptgsseeeeefleiPPFNKQYTECQLRAGAGYILEDFNEAQC----------- 1703
Cdd:cd17745      1 IFSGCAFLLTGAEETD-------------------------KPFDKERLESQIEANGGTVLEDFDEELFndgrsstrksr 55

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039760892 1704 -NTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQ 1746
Cdd:cd17745     56 sKDLRFVFLIADSPSRTPKYLQALALGIPCVSHKWILDCIEAGK 99

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1039760892 1395 GLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDI 1439
Cdd:cd04508      1 GDRVEAKWSDDGQWYPATVVAVNDDGKYTVLFDDGNEEEVSEDDI 45

breast cancer carboxy-terminal domain;

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039760892  1773 ENPFQNLKVLLVSDQQQNFLELWSE-ILMTGGAASVKQHHSSahnkdialgVFDVVVTDPSCPASVLKCAEALQLPVVSQ 1851
Cdd:smart00292    1 PKLFKGKTFYITGSFDKEERDELKElIEALGGKVTSSLSSKT---------TTHVIVGSPEGGKLELLKAIALGIPIVKE 71

                    ....*..
gi 1039760892  1852 EWVIQCL 1858
Cdd:smart00292   72 EWLLDCL 78

Tudor domain found in PHD finger protein 20 (PHF20), PHF20-like protein 1 (PHF20L1), and similar proteins; PHF20, also called Glioma-expressed antigen 2, hepatocellular carcinoma-associated antigen 58, novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds to Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53-mediated signaling. PHF20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Both PHF20 and PHF20L1 contain an N-terminal malignant brain tumor (MBT) domain, a Tudor domain, a plant homeodomain (PHD) finger and putative DNA-binding domains AT hook and C2H2-type zinc finger. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1039760892 1394 VGLRVVAKWSSNgYFYSGKITRDVGAGKYKLLFDDGY 1430
Cdd:cd20386      3 VGEEVLARWSDC-KFYPAKILKVLDNGTYEVLFYDGF 38

Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and similar proteins; This family includes Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4), histone-lysine N-methyltransferase trithorax-like proteins ATX1-2 (AtATX1-2), histone-lysine N-methyltransferase ASHH3, DNA mismatch repair protein MSH6, and similar proteins. EMSY-like proteins contain an EMSY N-terminal domain, a central Tudor-like Agenet domain, and a C-terminal coiled-coil motif. AtEML1, AtEML2, and likely AtEML4, contribute to RPP7-mediated immunity. Besides this, AtEML1 and AtEML2 participate in a second EDM2-dependent function and affect floral transition. ATX-like proteins are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal Tudor-like Agenet domain, a PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. ASHR3, also called protein SET DOMAIN GROUP 7, functions as a histone-lysine N-methyltransferase (EC 2.1.1.43). It contains a SET domain and a Tudor-like Agenet domain. AtMSH6, also called MutS protein homolog 6, is a component of the post-replicative DNA mismatch repair system (MMR). It forms a heterodimer with MutS alpha (MSH2-MSH6 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. AtMSH6 contains a Tudor-like Agenet domain and a MutS 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.

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1039760892 1394 VGLRVVAKWSSNGYFYSGKITR-DVGAGKYKLLFDDGYE 1431
Cdd:cd20404      1 VGRRVRVYWPEDGTWYEGVVVDyDPSTGKHRVEYDDGDE 39