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Conserved domains on  [gi|1907140190|ref|XP_036018159|]
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TP53-binding protein 1 isoform X5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
53-BP1_Tudor pfam09038
Tumour suppressor p53-binding protein-1 Tudor; Members of this family consist of ten ...
 1451-1568 4.07e-82

Tumour suppressor p53-binding protein-1 Tudor; Members of this family consist of ten beta-strands and a carboxy-terminal alpha-helix. The amino-terminal five beta-strands and the C-terminal five beta-strands adopt folds that are identical to each other. This domain is essential for the recruitment of proteins to double stranded breaks in DNA, which is mediated by interaction with methylated Lys 79 of histone H3.


:

Pssm-ID: 430382  Cd Length: 118  Bit Score: 264.97  E-value: 4.07e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190 1451 SFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKE 1530
Cdd:pfam09038    1 SFVGLRVVAKWSSNGYFYSGKIMKDAGAGKFKLLFDDGYECDVAGKDILLCDPIPLDTEVTALLEDEYFSAGVVKGHKKE 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907140190 1531 SGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGL 1568
Cdd:pfam09038   81 GGELFYSIEKDGQRKWYKRKAVILSLEQGNKLREQHGL 118
BRCT_3 pfam18428
BRCA1 C Terminus (BRCT) domain; Brca1 C-terminal (BRCT) domains are a common protein-protein ...
 1831-1934 1.09e-48

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.


:

Pssm-ID: 465764  Cd Length: 100  Bit Score: 168.64  E-value: 1.09e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190 1831 NPFQNLKVLLVSDQQqNFLELWSEILMTGGAASVKQHHSsahNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEW 1910
Cdd:pfam18428    1 NPFKDLRILLVSEQK-NFVDFWSQILKLAGATVVKQHKS---DKAIPEGKFDVVVTDRSCPEEVLKKATQLGIPLVSTEW 76

                           90       100
                   ....*....|....*....|....
gi 1907140190 1911 VIQCLIVGERIGFKQHPKYKHDYV 1934
Cdd:pfam18428   77 VIQCLIHGELLPYDSHPKYRYDYT 100
BRCT_p53bp1_rpt1 cd17745
first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ...
 1692-1803 6.30e-28

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.


:

Pssm-ID: 349376 [Multi-domain]  Cd Length: 99  Bit Score: 109.32  E-value: 6.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190 1692 LFLGYAFLLTMATTSDklasrsklldgptgsseeeeefleiPPFNKQYTECQLRAGAGYILEDFNEAQC----------- 1760
Cdd:cd17745      1 IFSGCAFLLTGAEETD-------------------------KPFDKERLESQIEANGGTVLEDFDEELFndgrsstrksr 55

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907140190 1761 -NTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQ 1803
Cdd:cd17745     56 sKDLRFVFLIADSPSRTPKYLQALALGIPCVSHKWILDCIEAGK 99
 
Name Accession Description Interval E-value
53-BP1_Tudor pfam09038
Tumour suppressor p53-binding protein-1 Tudor; Members of this family consist of ten ...
 1451-1568 4.07e-82

Tumour suppressor p53-binding protein-1 Tudor; Members of this family consist of ten beta-strands and a carboxy-terminal alpha-helix. The amino-terminal five beta-strands and the C-terminal five beta-strands adopt folds that are identical to each other. This domain is essential for the recruitment of proteins to double stranded breaks in DNA, which is mediated by interaction with methylated Lys 79 of histone H3.


Pssm-ID: 430382  Cd Length: 118  Bit Score: 264.97  E-value: 4.07e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190 1451 SFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKE 1530
Cdd:pfam09038    1 SFVGLRVVAKWSSNGYFYSGKIMKDAGAGKFKLLFDDGYECDVAGKDILLCDPIPLDTEVTALLEDEYFSAGVVKGHKKE 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907140190 1531 SGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGL 1568
Cdd:pfam09038   81 GGELFYSIEKDGQRKWYKRKAVILSLEQGNKLREQHGL 118
BRCT_3 pfam18428
BRCA1 C Terminus (BRCT) domain; Brca1 C-terminal (BRCT) domains are a common protein-protein ...
 1831-1934 1.09e-48

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.


Pssm-ID: 465764  Cd Length: 100  Bit Score: 168.64  E-value: 1.09e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190 1831 NPFQNLKVLLVSDQQqNFLELWSEILMTGGAASVKQHHSsahNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEW 1910
Cdd:pfam18428    1 NPFKDLRILLVSEQK-NFVDFWSQILKLAGATVVKQHKS---DKAIPEGKFDVVVTDRSCPEEVLKKATQLGIPLVSTEW 76

                           90       100
                   ....*....|....*....|....
gi 1907140190 1911 VIQCLIVGERIGFKQHPKYKHDYV 1934
Cdd:pfam18428   77 VIQCLIHGELLPYDSHPKYRYDYT 100
BRCT_p53bp1_rpt2 cd17724
Second (C-terminal) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ...
 1832-1918 9.97e-34

Second (C-terminal) 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 corresponds to the second BRCT domain.


Pssm-ID: 349356  Cd Length: 87  Bit Score: 125.18  E-value: 9.97e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190 1832 PFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWV 1911
Cdd:cd17724      1 LFKGLKILVVSKKKKPFRETWSFILKAAGATSVKKLPSTSAASSSDIGKIDVVVTDGSCPSTVLKKARQLGIPVVSTEWV 80


                   ....*..
gi 1907140190 1912 IQCLIVG 1918
Cdd:cd17724     81 IQCLING 87
BRCT_p53bp1_rpt1 cd17745
first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ...
 1692-1803 6.30e-28

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.


Pssm-ID: 349376 [Multi-domain]  Cd Length: 99  Bit Score: 109.32  E-value: 6.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190 1692 LFLGYAFLLTMATTSDklasrsklldgptgsseeeeefleiPPFNKQYTECQLRAGAGYILEDFNEAQC----------- 1760
Cdd:cd17745      1 IFSGCAFLLTGAEETD-------------------------KPFDKERLESQIEANGGTVLEDFDEELFndgrsstrksr 55

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907140190 1761 -NTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQ 1803
Cdd:cd17745     56 sKDLRFVFLIADSPSRTPKYLQALALGIPCVSHKWILDCIEAGK 99
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 1453-1504 5.30e-22

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: 90.79  E-value: 5.30e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907140190 1453 VGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPI 1504
Cdd:cd20383      1 VGTRVFAKWSSDGYYYPGIITRVLGDGKYKVLFDDGYERDVKGKDIILCEPL 52
BRCT smart00292
breast cancer carboxy-terminal domain;
1830-1915 1.30e-06

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 47.76  E-value: 1.30e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190  1830 ENPFQNLKVLLVSDQQQNFLELWSE-ILMTGGAASVKQHHSSahnkdialgVFDVVVTDPSCPASVLKCAEALQLPVVSQ 1908
Cdd:smart00292    1 PKLFKGKTFYITGSFDKEERDELKElIEALGGKVTSSLSSKT---------TTHVIVGSPEGGKLELLKAIALGIPIVKE 71


                    ....*..
gi 1907140190  1909 EWVIQCL 1915
Cdd:smart00292   72 EWLLDCL 78
 
Name Accession Description Interval E-value
53-BP1_Tudor pfam09038
Tumour suppressor p53-binding protein-1 Tudor; Members of this family consist of ten ...
 1451-1568 4.07e-82

Tumour suppressor p53-binding protein-1 Tudor; Members of this family consist of ten beta-strands and a carboxy-terminal alpha-helix. The amino-terminal five beta-strands and the C-terminal five beta-strands adopt folds that are identical to each other. This domain is essential for the recruitment of proteins to double stranded breaks in DNA, which is mediated by interaction with methylated Lys 79 of histone H3.


Pssm-ID: 430382  Cd Length: 118  Bit Score: 264.97  E-value: 4.07e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190 1451 SFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKE 1530
Cdd:pfam09038    1 SFVGLRVVAKWSSNGYFYSGKIMKDAGAGKFKLLFDDGYECDVAGKDILLCDPIPLDTEVTALLEDEYFSAGVVKGHKKE 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907140190 1531 SGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGL 1568
Cdd:pfam09038   81 GGELFYSIEKDGQRKWYKRKAVILSLEQGNKLREQHGL 118
BRCT_3 pfam18428
BRCA1 C Terminus (BRCT) domain; Brca1 C-terminal (BRCT) domains are a common protein-protein ...
 1831-1934 1.09e-48

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.


Pssm-ID: 465764  Cd Length: 100  Bit Score: 168.64  E-value: 1.09e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190 1831 NPFQNLKVLLVSDQQqNFLELWSEILMTGGAASVKQHHSsahNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEW 1910
Cdd:pfam18428    1 NPFKDLRILLVSEQK-NFVDFWSQILKLAGATVVKQHKS---DKAIPEGKFDVVVTDRSCPEEVLKKATQLGIPLVSTEW 76

                           90       100
                   ....*....|....*....|....
gi 1907140190 1911 VIQCLIVGERIGFKQHPKYKHDYV 1934
Cdd:pfam18428   77 VIQCLIHGELLPYDSHPKYRYDYT 100
BRCT_p53bp1_rpt2 cd17724
Second (C-terminal) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ...
 1832-1918 9.97e-34

Second (C-terminal) 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 corresponds to the second BRCT domain.


Pssm-ID: 349356  Cd Length: 87  Bit Score: 125.18  E-value: 9.97e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190 1832 PFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWV 1911
Cdd:cd17724      1 LFKGLKILVVSKKKKPFRETWSFILKAAGATSVKKLPSTSAASSSDIGKIDVVVTDGSCPSTVLKKARQLGIPVVSTEWV 80


                   ....*..
gi 1907140190 1912 IQCLIVG 1918
Cdd:cd17724     81 IQCLING 87
BRCT_p53bp1_rpt1 cd17745
first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ...
 1692-1803 6.30e-28

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.


Pssm-ID: 349376 [Multi-domain]  Cd Length: 99  Bit Score: 109.32  E-value: 6.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190 1692 LFLGYAFLLTMATTSDklasrsklldgptgsseeeeefleiPPFNKQYTECQLRAGAGYILEDFNEAQC----------- 1760
Cdd:cd17745      1 IFSGCAFLLTGAEETD-------------------------KPFDKERLESQIEANGGTVLEDFDEELFndgrsstrksr 55

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907140190 1761 -NTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQ 1803
Cdd:cd17745     56 sKDLRFVFLIADSPSRTPKYLQALALGIPCVSHKWILDCIEAGK 99
Tudor_53BP1 cd20383
Tudor domain found in tumor suppressor TP53-binding protein 1 (53BP1) and similar proteins; ...
 1453-1504 5.30e-22

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: 90.79  E-value: 5.30e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907140190 1453 VGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPI 1504
Cdd:cd20383      1 VGTRVFAKWSSDGYYYPGIITRVLGDGKYKVLFDDGYERDVKGKDIILCEPL 52
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
 1454-1498 7.56e-10

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.


Pssm-ID: 410449 [Multi-domain]  Cd Length: 47  Bit Score: 56.06  E-value: 7.56e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907140190 1454 GLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDI 1498
Cdd:cd04508      1 GDRVEAKWSDDGQWYPATVVAVNDDGKYTVLFDDGNEEEVSEDDI 45
Tudor_SpCrb2-like_rpt1 cd20395
first Tudor domain found in Schizosaccharomyces pombe Cut5-repeat binding protein 2 (Crb2) and ...
 1454-1502 1.83e-07

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: 49.28  E-value: 1.83e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907140190 1454 GLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCD 1502
Cdd:cd20395      1 PTRVLAFWKGDGNYYPATIVGPVSSSAYKVQFDDGTSSSVPPTQIRRLE 49
BRCT smart00292
breast cancer carboxy-terminal domain;
1830-1915 1.30e-06

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 47.76  E-value: 1.30e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907140190  1830 ENPFQNLKVLLVSDQQQNFLELWSE-ILMTGGAASVKQHHSSahnkdialgVFDVVVTDPSCPASVLKCAEALQLPVVSQ 1908
Cdd:smart00292    1 PKLFKGKTFYITGSFDKEERDELKElIEALGGKVTSSLSSKT---------TTHVIVGSPEGGKLELLKAIALGIPIVKE 71


                    ....*..
gi 1907140190  1909 EWVIQCL 1915
Cdd:smart00292   72 EWLLDCL 78
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
 1761-1802 6.04e-06

first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also termed nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The family corresponds to the first BRCT domain.


Pssm-ID: 349375 [Multi-domain]  Cd Length: 72  Bit Score: 45.69  E-value: 6.04e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1907140190 1761 NTAYQC-LLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHAN 1802
Cdd:cd17744     27 DSVEDCtHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKAN 69
Tudor_PHF20-like cd20386
Tudor domain found in PHD finger protein 20 (PHF20), PHF20-like protein 1 (PHF20L1), and ...
 1453-1489 6.67e-06

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.


Pssm-ID: 410457 [Multi-domain]  Cd Length: 50  Bit Score: 44.89  E-value: 6.67e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907140190 1453 VGLRVVAKWSSNgYFYSGKITRDVGAGKYKLLFDDGY 1489
Cdd:cd20386      3 VGEEVLARWSDC-KFYPAKILKVLDNGTYEVLFYDGF 38
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 1768-1798 5.80e-04

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 40.04  E-value: 5.80e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1907140190 1768 LIADQHCRTRKYFLCLASGIPCVSHVWVHDS 1798
Cdd:cd00027     38 LIAKSPSGEKYYLAALAWGIPIVSPEWLLDC 68
Tudor_Agenet_AtEML-like cd20404
Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and ...
 1453-1490 1.54e-03

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.


Pssm-ID: 410475 [Multi-domain]  Cd Length: 51  Bit Score: 38.41  E-value: 1.54e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1907140190 1453 VGLRVVAKWSSNGYFYSGKITR-DVGAGKYKLLFDDGYE 1490
Cdd:cd20404      1 VGRRVRVYWPEDGTWYEGVVVDyDPSTGKHRVEYDDGDE 39
Tudor_LBR cd20381
Tudor domain found in Lamin-B receptor (LBR) and similar proteins; LBR, also called integral ...
 1453-1498 2.20e-03

Tudor domain found in Lamin-B receptor (LBR) and similar proteins; LBR, also called integral nuclear envelope inner membrane (INM) protein or LMN2R, is a nuclear envelope protein that anchors the lamina and the heterochromatin to the inner nuclear membrane, in cellular senescence induced by excess thymidine. It is also important for cholesterol biosynthesis. LBR can interact with chromodomain proteins and DNA. It 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: 410452  Cd Length: 51  Bit Score: 37.67  E-value: 2.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907140190 1453 VGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDI 1498
Cdd:cd20381      4 VGETVMARWPGSRLYYEATVLNFDDSDEYTVKFKDGTELELKEKDV 49
 
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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