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Conserved domains on  [gi|6320423|ref|NP_010503|]
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chromatin-binding protein RAD9 [Saccharomyces cerevisiae S288C]

Protein Classification

BRCT domain-containing protein( domain architecture ID 13755487)

BRCT (BRCA1 C-terminus) domain-containing protein may interact with DNA, and participate in DNA-damage checkpoint or DNA-repair pathways

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rad9_Rad53_bind pfam08605
Fungal Rad9-like Rad53-binding; In Saccharomyces cerevisiae the Rad9 a key adaptor protein in ...
 772-900 2.83e-62

Fungal Rad9-like Rad53-binding; In Saccharomyces cerevisiae the Rad9 a key adaptor protein in DNA damage checkpoint pathways. DNA damage induces Rad9 phosphorylation, and Rad53 specifically associates with this region of Rad9, when phosphorylated, via Rad53 pfam00498 domains. This region is structurally composed of a pair of TUDOR domains.


:

Pssm-ID: 369994  Cd Length: 129  Bit Score: 208.03  E-value: 2.83e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320423     772 DNSFLSKDDIIFGNAVWCQYTwNYKFYPGILLEVDTNQDGCWIYFETGRSLTKDEDIYYLDIRIGDAVTFDGNEYVVVGL 851
Cdd:pfam08605    1 DLSVLTKKDIIFMNAVWYYFD-KLNFYPGKILSVGTSQDGCIVLFEEGAYEVKNGDVYYLDLRIGDAVKCDMNTYVVVGL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 6320423     852 ECR-SHDLNIIRCIRGYDTVHLKKKNASGLLGKRTLIKALSSISLDLSEW 900
Cdd:pfam08605   80 ECKiSADDKVIRCIRGYDTVHLKQVSRSGKLGPENLIKPLSDIYLDLSQW 129
BRCT_p53bp1_rpt1 cd17745
first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ...
 998-1113 1.65e-23

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: 96.23  E-value: 1.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320423   998 VFDKCIFVLTSLFE-----NREELRQTIESQGGTVIESGFSTLFNFTHPLakslvnkgntdnirelalklawKPHSLFAD 1072
Cdd:cd17745    1 IFSGCAFLLTGAEEtdkpfDKERLESQIEANGGTVLEDFDEELFNDGRSS----------------------TRKSRSKD 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 6320423  1073 CRFACLITKRHLRSLKYLETLALGWPTLHWKFISACIEKKR 1113
Cdd:cd17745   59 LRFVFLIADSPSRTPKYLQALALGIPCVSHKWILDCIEAGK 99
 
Name Accession Description Interval E-value
Rad9_Rad53_bind pfam08605
Fungal Rad9-like Rad53-binding; In Saccharomyces cerevisiae the Rad9 a key adaptor protein in ...
 772-900 2.83e-62

Fungal Rad9-like Rad53-binding; In Saccharomyces cerevisiae the Rad9 a key adaptor protein in DNA damage checkpoint pathways. DNA damage induces Rad9 phosphorylation, and Rad53 specifically associates with this region of Rad9, when phosphorylated, via Rad53 pfam00498 domains. This region is structurally composed of a pair of TUDOR domains.


Pssm-ID: 369994  Cd Length: 129  Bit Score: 208.03  E-value: 2.83e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320423     772 DNSFLSKDDIIFGNAVWCQYTwNYKFYPGILLEVDTNQDGCWIYFETGRSLTKDEDIYYLDIRIGDAVTFDGNEYVVVGL 851
Cdd:pfam08605    1 DLSVLTKKDIIFMNAVWYYFD-KLNFYPGKILSVGTSQDGCIVLFEEGAYEVKNGDVYYLDLRIGDAVKCDMNTYVVVGL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 6320423     852 ECR-SHDLNIIRCIRGYDTVHLKKKNASGLLGKRTLIKALSSISLDLSEW 900
Cdd:pfam08605   80 ECKiSADDKVIRCIRGYDTVHLKQVSRSGKLGPENLIKPLSDIYLDLSQW 129
BRCT_p53bp1_rpt1 cd17745
first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ...
 998-1113 1.65e-23

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: 96.23  E-value: 1.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320423   998 VFDKCIFVLTSLFE-----NREELRQTIESQGGTVIESGFSTLFNFTHPLakslvnkgntdnirelalklawKPHSLFAD 1072
Cdd:cd17745    1 IFSGCAFLLTGAEEtdkpfDKERLESQIEANGGTVLEDFDEELFNDGRSS----------------------TRKSRSKD 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 6320423  1073 CRFACLITKRHLRSLKYLETLALGWPTLHWKFISACIEKKR 1113
Cdd:cd17745   59 LRFVFLIADSPSRTPKYLQALALGIPCVSHKWILDCIEAGK 99
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 997-1109 4.43e-04

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 39.97  E-value: 4.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320423     997 NVFDKCIFVLTSLFE-NREELRQTIESQGGTVIESgfstlfnfthplakslVNKGNTdnirelalklawkphslfadcrf 1075
Cdd:pfam00533    4 KLFSGKTFVITGLDGlERDELKELIEKLGGKVTDS----------------LSKKTT----------------------- 44

                           90       100       110
                   ....*....|....*....|....*....|....
gi 6320423    1076 aCLITKRhlRSLKYLETLALGWPTLHWKFISACI 1109
Cdd:pfam00533   45 -HVIVEA--RTKKYLKAKELGIPIVTEEWLLDCI 75
 
Name Accession Description Interval E-value
Rad9_Rad53_bind pfam08605
Fungal Rad9-like Rad53-binding; In Saccharomyces cerevisiae the Rad9 a key adaptor protein in ...
 772-900 2.83e-62

Fungal Rad9-like Rad53-binding; In Saccharomyces cerevisiae the Rad9 a key adaptor protein in DNA damage checkpoint pathways. DNA damage induces Rad9 phosphorylation, and Rad53 specifically associates with this region of Rad9, when phosphorylated, via Rad53 pfam00498 domains. This region is structurally composed of a pair of TUDOR domains.


Pssm-ID: 369994  Cd Length: 129  Bit Score: 208.03  E-value: 2.83e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320423     772 DNSFLSKDDIIFGNAVWCQYTwNYKFYPGILLEVDTNQDGCWIYFETGRSLTKDEDIYYLDIRIGDAVTFDGNEYVVVGL 851
Cdd:pfam08605    1 DLSVLTKKDIIFMNAVWYYFD-KLNFYPGKILSVGTSQDGCIVLFEEGAYEVKNGDVYYLDLRIGDAVKCDMNTYVVVGL 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 6320423     852 ECR-SHDLNIIRCIRGYDTVHLKKKNASGLLGKRTLIKALSSISLDLSEW 900
Cdd:pfam08605   80 ECKiSADDKVIRCIRGYDTVHLKQVSRSGKLGPENLIKPLSDIYLDLSQW 129
BRCT_p53bp1_rpt1 cd17745
first (central) BRCT domain in p53-binding protein 1 (p53BP1) and similar proteins; p53BP1, ...
 998-1113 1.65e-23

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: 96.23  E-value: 1.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320423   998 VFDKCIFVLTSLFE-----NREELRQTIESQGGTVIESGFSTLFNFTHPLakslvnkgntdnirelalklawKPHSLFAD 1072
Cdd:cd17745    1 IFSGCAFLLTGAEEtdkpfDKERLESQIEANGGTVLEDFDEELFNDGRSS----------------------TRKSRSKD 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 6320423  1073 CRFACLITKRHLRSLKYLETLALGWPTLHWKFISACIEKKR 1113
Cdd:cd17745   59 LRFVFLIADSPSRTPKYLQALALGIPCVSHKWILDCIEAGK 99
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 997-1109 4.43e-04

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 39.97  E-value: 4.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320423     997 NVFDKCIFVLTSLFE-NREELRQTIESQGGTVIESgfstlfnfthplakslVNKGNTdnirelalklawkphslfadcrf 1075
Cdd:pfam00533    4 KLFSGKTFVITGLDGlERDELKELIEKLGGKVTDS----------------LSKKTT----------------------- 44

                           90       100       110
                   ....*....|....*....|....*....|....
gi 6320423    1076 aCLITKRhlRSLKYLETLALGWPTLHWKFISACI 1109
Cdd:pfam00533   45 -HVIVEA--RTKKYLKAKELGIPIVTEEWLLDCI 75
 
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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