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Conserved domains on  [gi|89271931|emb|CAJ81694|]
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nibrin, partial [Xenopus tropicalis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
 2-108 1.89e-41

forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.


:

Pssm-ID: 438719 [Multi-domain]  Cd Length: 108  Bit Score: 145.16  E-value: 1.89e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   2 WRLVAE-RAGGDTYYILTGTDYVVGRKNCAILIPDDQSISRCHATLSVSYPSASLSQTNAVSVLTIKDSSKYGTTVSGER 80
Cdd:cd22667   1 WWLLSEqDGAGTSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGEK 80

                        90       100
                ....*....|....*....|....*...
gi 89271931  81 MQPAVPRSLKPSDEVIFGCFHSKYRVEY 108
Cdd:cd22667  81 LKGGSEVTLKDGDVITFGVLGSKFRVEY 108
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 109-182 3.69e-38

BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage syndrome protein 1 (NBS1), or cell cycle regulatory protein p95, is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The BRCT (Breast Cancer Suppressor Protein BRCA1, carboxy-terminal) domain is found within many DNA damage repair and cell cycle checkpoint proteins. The unique diversity of this domain superfamily allows BRCT modules to interact forming homo/hetero BRCT multimers, BRCT-non-BRCT interactions, and interactions within DNA strand breaks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is absent in this group.


:

Pssm-ID: 349372 [Multi-domain]  Cd Length: 74  Bit Score: 135.04  E-value: 3.69e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89271931 109 EPLVVCSSCLDNTEKNSLKQNLIHLGGHMLNNWTEKCTHLVMTSIKVTIKTICALICCKPIIKPDYFRELINAI 182
Cdd:cd17741   1 EPLVVCSSCLDSEEKKKLKQIIAKLGGKVVNEWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYLDALLEAI 74
NIBRIN_BRCT_II pfam16508
Second BRCT domain on Nijmegen syndrome breakage protein;
215-321 1.25e-23

Second BRCT domain on Nijmegen syndrome breakage protein;


:

Pssm-ID: 465151  Cd Length: 118  Bit Score: 96.21  E-value: 1.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   215 KRKSIFKDKVFLFLNTKQYMKLSPAVLLGGGKAHLLESLT---------------DTSVLENSTTCVIDVAMTETQLSEt 279
Cdd:pfam16508   2 ERKTLFEGKTFVFLDQKQFERLSPPITNGGGKALLYEVEPgettpddfvryvknvGSELLTGKGVVVVRFRPKKSSNEE- 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 89271931   280 qstqpWISCTLDLLHSK-GLRAIPEAEIGLAVINVSTEIYCNP 321
Cdd:pfam16508  81 -----WIASFENELALRlGQRVIEQSEFLDAILHCSASKLCNP 118
 
Name Accession Description Interval E-value
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
 2-108 1.89e-41

forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438719 [Multi-domain]  Cd Length: 108  Bit Score: 145.16  E-value: 1.89e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   2 WRLVAE-RAGGDTYYILTGTDYVVGRKNCAILIPDDQSISRCHATLSVSYPSASLSQTNAVSVLTIKDSSKYGTTVSGER 80
Cdd:cd22667   1 WWLLSEqDGAGTSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGEK 80

                        90       100
                ....*....|....*....|....*...
gi 89271931  81 MQPAVPRSLKPSDEVIFGCFHSKYRVEY 108
Cdd:cd22667  81 LKGGSEVTLKDGDVITFGVLGSKFRVEY 108
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 109-182 3.69e-38

BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage syndrome protein 1 (NBS1), or cell cycle regulatory protein p95, is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The BRCT (Breast Cancer Suppressor Protein BRCA1, carboxy-terminal) domain is found within many DNA damage repair and cell cycle checkpoint proteins. The unique diversity of this domain superfamily allows BRCT modules to interact forming homo/hetero BRCT multimers, BRCT-non-BRCT interactions, and interactions within DNA strand breaks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is absent in this group.


Pssm-ID: 349372 [Multi-domain]  Cd Length: 74  Bit Score: 135.04  E-value: 3.69e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89271931 109 EPLVVCSSCLDNTEKNSLKQNLIHLGGHMLNNWTEKCTHLVMTSIKVTIKTICALICCKPIIKPDYFRELINAI 182
Cdd:cd17741   1 EPLVVCSSCLDSEEKKKLKQIIAKLGGKVVNEWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYLDALLEAI 74
NIBRIN_BRCT_II pfam16508
Second BRCT domain on Nijmegen syndrome breakage protein;
215-321 1.25e-23

Second BRCT domain on Nijmegen syndrome breakage protein;


Pssm-ID: 465151  Cd Length: 118  Bit Score: 96.21  E-value: 1.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   215 KRKSIFKDKVFLFLNTKQYMKLSPAVLLGGGKAHLLESLT---------------DTSVLENSTTCVIDVAMTETQLSEt 279
Cdd:pfam16508   2 ERKTLFEGKTFVFLDQKQFERLSPPITNGGGKALLYEVEPgettpddfvryvknvGSELLTGKGVVVVRFRPKKSSNEE- 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 89271931   280 qstqpWISCTLDLLHSK-GLRAIPEAEIGLAVINVSTEIYCNP 321
Cdd:pfam16508  81 -----WIASFENELALRlGQRVIEQSEFLDAILHCSASKLCNP 118
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
1-107 6.21e-08

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 50.73  E-value: 6.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   1 MWRL-VAERAGGDTYYILTGTDYVVGR-KNCAILIPDDqSISRCHATLSVSYPSaslsqtnavsvLTIKD-SSKYGTTVS 77
Cdd:COG1716   1 MARLvVLEGPLAGRRFPLDGGPLTIGRaPDNDIVLDDP-TVSRRHARIRRDGGG-----------WVLEDlGSTNGTFVN 68

                        90       100       110
                ....*....|....*....|....*....|
gi 89271931  78 GERMQpaVPRSLKPSDEVIFGCFHSKYRVE 107
Cdd:COG1716  69 GQRVT--EPAPLRDGDVIRLGKTELRFRLS 96
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 22-97 2.31e-06

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 45.26  E-value: 2.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89271931    22 YVVGR-KNCAILIpDDQSISRCHATLSVsypsaslsqtNAVSVLTIKD-SSKYGTTVSGERMQPaVPRSLKPSDEVIF 97
Cdd:pfam00498   1 VTIGRsPDCDIVL-DDPSVSRRHAEIRY----------DGGGRFYLEDlGSTNGTFVNGQRLGP-EPVRLKDGDVIRL 66
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 111-179 7.86e-06

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: 43.82  E-value: 7.86e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89271931   111 LVVCSSCLDNTEKNSLKQNLIHLGGHMLNNWTEKCTHLVMtsIKVTIKTICALICCKPIIKPDYFRELI 179
Cdd:pfam00533   9 KTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
 
Name Accession Description Interval E-value
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
 2-108 1.89e-41

forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438719 [Multi-domain]  Cd Length: 108  Bit Score: 145.16  E-value: 1.89e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   2 WRLVAE-RAGGDTYYILTGTDYVVGRKNCAILIPDDQSISRCHATLSVSYPSASLSQTNAVSVLTIKDSSKYGTTVSGER 80
Cdd:cd22667   1 WWLLSEqDGAGTSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGEK 80

                        90       100
                ....*....|....*....|....*...
gi 89271931  81 MQPAVPRSLKPSDEVIFGCFHSKYRVEY 108
Cdd:cd22667  81 LKGGSEVTLKDGDVITFGVLGSKFRVEY 108
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 109-182 3.69e-38

BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage syndrome protein 1 (NBS1), or cell cycle regulatory protein p95, is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The BRCT (Breast Cancer Suppressor Protein BRCA1, carboxy-terminal) domain is found within many DNA damage repair and cell cycle checkpoint proteins. The unique diversity of this domain superfamily allows BRCT modules to interact forming homo/hetero BRCT multimers, BRCT-non-BRCT interactions, and interactions within DNA strand breaks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is absent in this group.


Pssm-ID: 349372 [Multi-domain]  Cd Length: 74  Bit Score: 135.04  E-value: 3.69e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89271931 109 EPLVVCSSCLDNTEKNSLKQNLIHLGGHMLNNWTEKCTHLVMTSIKVTIKTICALICCKPIIKPDYFRELINAI 182
Cdd:cd17741   1 EPLVVCSSCLDSEEKKKLKQIIAKLGGKVVNEWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYLDALLEAI 74
NIBRIN_BRCT_II pfam16508
Second BRCT domain on Nijmegen syndrome breakage protein;
215-321 1.25e-23

Second BRCT domain on Nijmegen syndrome breakage protein;


Pssm-ID: 465151  Cd Length: 118  Bit Score: 96.21  E-value: 1.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   215 KRKSIFKDKVFLFLNTKQYMKLSPAVLLGGGKAHLLESLT---------------DTSVLENSTTCVIDVAMTETQLSEt 279
Cdd:pfam16508   2 ERKTLFEGKTFVFLDQKQFERLSPPITNGGGKALLYEVEPgettpddfvryvknvGSELLTGKGVVVVRFRPKKSSNEE- 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 89271931   280 qstqpWISCTLDLLHSK-GLRAIPEAEIGLAVINVSTEIYCNP 321
Cdd:pfam16508  81 -----WIASFENELALRlGQRVIEQSEFLDAILHCSASKLCNP 118
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 111-177 3.88e-10

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: 55.83  E-value: 3.88e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89271931 111 LVVCSSCLDNTEKNSLKQNLIHLGGHMLNNWTEKCTHLVMTSIKVTIKTICALICCKPIIKPDYFRE 177
Cdd:cd00027   1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLD 67
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 15-107 9.10e-09

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 52.66  E-value: 9.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931  15 YILTGTDYVVGRKNCAILIPDDQSISRCHATLSVSYpsaslsqtnavSVLTIKD-SSKYGTTVSGERMQPAVPrsLKPSD 93
Cdd:cd00060  14 FPLTKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDG-----------GGVYLEDlGSTNGTFVNGKRITPPVP--LQDGD 80

                        90
                ....*....|....
gi 89271931  94 EVIFGcfHSKYRVE 107
Cdd:cd00060  81 VIRLG--DTTFRFE 92
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
1-107 6.21e-08

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 50.73  E-value: 6.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   1 MWRL-VAERAGGDTYYILTGTDYVVGR-KNCAILIPDDqSISRCHATLSVSYPSaslsqtnavsvLTIKD-SSKYGTTVS 77
Cdd:COG1716   1 MARLvVLEGPLAGRRFPLDGGPLTIGRaPDNDIVLDDP-TVSRRHARIRRDGGG-----------WVLEDlGSTNGTFVN 68

                        90       100       110
                ....*....|....*....|....*....|
gi 89271931  78 GERMQpaVPRSLKPSDEVIFGCFHSKYRVE 107
Cdd:COG1716  69 GQRVT--EPAPLRDGDVIRLGKTELRFRLS 96
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
 112-181 2.72e-07

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: 48.00  E-value: 2.72e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931 112 VVCSSCLDNTEKnsLKQNLIHLGGHMLNNWTEkCTHLVMTSIKVTIKTICALICCKPIIKPDYFRELINA 181
Cdd:cd17744   2 RVLFTGVSDKEE--GEKIIKKLGGSVVDSVED-CTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKA 68
BRCT_PAXIP1_rpt5 cd17712
fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 112-177 8.59e-07

fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the fifth BRCT domain.


Pssm-ID: 349344  Cd Length: 75  Bit Score: 46.85  E-value: 8.59e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89271931 112 VVCSSCLDNTEKNSLKQNLIHLGGHMLNNwTEKCTHLVMTSIKVTIKTICALICCKPIIKPDYFRE 177
Cdd:cd17712   3 RVLFTGFDPVQVRKLTKKVTILGGEVVES-PQECTHLVAPKVSRTVKFLTAISVCKHIVTPEWLEE 67
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 116-181 9.56e-07

seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the seventh BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349370 [Multi-domain]  Cd Length: 75  Bit Score: 46.41  E-value: 9.56e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89271931 116 SCLDNTEKNSLKQNLIHLGGHMLN--NWTEKCTHLVMTSIKVTIKTICALICCKPIIKPDYFRELINA 181
Cdd:cd17738   7 SGFSEDEKKELISIIEKLGGKVLDsdEFDPKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKA 74
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
 23-111 1.02e-06

forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438743 [Multi-domain]  Cd Length: 113  Bit Score: 47.80  E-value: 1.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931  23 VVGR-KNCAILIpDDQSISRCHATLSvsypSASLSQTnavsvLTIKD-SSKYGTTVSGERMQPAVPRSLKPSDEVIFGCF 100
Cdd:cd22691  32 VVGRhPDCDIVL-DHPSISRFHLEIR----IIPSRRK-----ITLTDlSSVHGTWVNGQRIEPGVPVELEEGDTVRLGAS 101

                        90
                ....*....|.
gi 89271931 101 HSKYRVEYEPL 111
Cdd:cd22691 102 TRVYRLHWIPV 112
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 22-97 2.31e-06

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 45.26  E-value: 2.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89271931    22 YVVGR-KNCAILIpDDQSISRCHATLSVsypsaslsqtNAVSVLTIKD-SSKYGTTVSGERMQPaVPRSLKPSDEVIF 97
Cdd:pfam00498   1 VTIGRsPDCDIVL-DDPSVSRRHAEIRY----------DGGGRFYLEDlGSTNGTFVNGQRLGP-EPVRLKDGDVIRL 66
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 111-179 7.86e-06

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: 43.82  E-value: 7.86e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89271931   111 LVVCSSCLDNTEKNSLKQNLIHLGGHMLNNWTEKCTHLVMtsIKVTIKTICALICCKPIIKPDYFRELI 179
Cdd:pfam00533   9 KTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
 2-98 1.16e-05

forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438715 [Multi-domain]  Cd Length: 110  Bit Score: 44.66  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   2 WRLVAERAGGDTYYIL--TGTDYVVGRK---NCAILIPDDQSISRCHATLsvsypsaslsQTNAVSVLTIKD-SSKYGTT 75
Cdd:cd22663   1 WCLRRVGHGIDPLVLLleDGKEVTVGRGlgvTYQLVSTCPLMISRNHCVL----------KKNDEGQWTIKDnKSLNGVW 70

                        90       100
                ....*....|....*....|...
gi 89271931  76 VSGERMQPAVPRSLKPSDEVIFG 98
Cdd:cd22663  71 VNGERIEPLKPYPLNEGDLIQLG 93
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
 22-98 7.45e-05

forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.


Pssm-ID: 438737 [Multi-domain]  Cd Length: 130  Bit Score: 42.79  E-value: 7.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931  22 YVVGRKN--CAILIPDDQS---ISRCHATLSVSypsaslSQTNAVSVLTIKDSSKYGTTVSGERMQPAVPRSLKPSDEVI 96
Cdd:cd22685  30 YRIGRNPevCDVFLCSSQHpnlISREHAEIHAE------RDGNGNWKVLIEDRSTNGTYVNDVRLQDGQRRELSDGDTIT 103


                ..
gi 89271931  97 FG 98
Cdd:cd22685 104 FG 105
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
 2-104 4.14e-04

forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438728 [Multi-domain]  Cd Length: 111  Bit Score: 39.97  E-value: 4.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   2 WRLVAERAG--GDTYYILTGTDYVVGR--KNCAILIpDDQSISRCHATLSVSYPSASLSQTNAVSVLT-IKD-SSKYGTT 75
Cdd:cd22676   1 WRLYVFKGGeqLETIDIHRQSAYLIGRdrRVADIPL-DHPSCSKQHAVIQFREVEKRNEGDVIENIRPyIIDlGSTNGTF 79

                        90       100
                ....*....|....*....|....*....
gi 89271931  76 VSGERMQPAVPRSLKPSDEVIFGCFHSKY 104
Cdd:cd22676  80 LNGEKIEPRRYYELREKDVLKFGLSTREY 108
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 105-190 4.93e-04

Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of regulator of Ty1 transposition protein 107 (RTT107). It is involved in binding phosphorylated histone H2A.


Pssm-ID: 465266  Cd Length: 91  Bit Score: 39.42  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   105 RVEYEPLVVCSSCLDNTEKNSL-KQNLIHLGGHMLNNwTEKCTHLVMTSIKVTIKTICALICCKPIIKPDYfreLINAIQ 183
Cdd:pfam16770   4 LPPYDIRAVLTGCERWIDKEDLdKKKLRLLGIKIVQD-PSKCNHLIAPKILRTEKFLCALAFAPYILSPDF---ITDCLK 79


                  ....*..
gi 89271931   184 QKRPLPE 190
Cdd:pfam16770  80 EGKLPDE 86
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
 22-98 2.37e-03

forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438726 [Multi-domain]  Cd Length: 108  Bit Score: 38.02  E-value: 2.37e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89271931  22 YVVGRKN--CAILIpDDQSISRCHATLsvsypsasLSQTNAVSVLTIKDSSKYGTTVSGERMQPAVPRSLKPSDEVIFG 98
Cdd:cd22674  29 YLFGRNSdvCDFVL-DHPSCSRVHAAL--------VYHKHLNRVFLIDLGSTHGTFVGGIRLEPHKPQQLPIDSTLRFG 98
BRCT_PAXIP1_rpt2 cd17710
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 111-190 3.31e-03

second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the second BRCT domain.


Pssm-ID: 349342 [Multi-domain]  Cd Length: 81  Bit Score: 36.83  E-value: 3.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931 111 LVVCSSCLDNTEKNSLKQNLIHLGGHMLNNWTEKCTHLVmTSIKVTIKTICALICCKP-IIKPDYfreLINAIQQKRPLP 189
Cdd:cd17710   5 VVVCPSQISAEDRLKLWAMVTFHGGKCQLNLDKKCTHLV-TGKASGAKYECALKHEGIkIVTPDW---VTDCIKAKTLLD 80


                .
gi 89271931 190 E 190
Cdd:cd17710  81 E 81
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
 4-98 3.63e-03

forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.


Pssm-ID: 438734 [Multi-domain]  Cd Length: 96  Bit Score: 37.12  E-value: 3.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89271931   4 LVAERAGGDTYYIlTGTDYVVGRK-NCAILIPDDqSISRCHATLSVSYPSASLsqtnavsvltIKDSSKYGTTVSGERMQ 82
Cdd:cd22682   5 IIGPPGVGKQFPI-TESTIVIGRSvESQVQIDDD-SVSRYHAKLAVNPSAVSI----------IDLGSTNGTIVNGKKIP 72

                        90
                ....*....|....*.
gi 89271931  83 PAVPRSLKPSDEVIFG 98
Cdd:cd22682  73 KLASCDLQNGDQIKIG 88
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 112-164 4.14e-03

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 36.41  E-value: 4.14e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 89271931 112 VVCSScLDNTEKNSLKQNLIHLGGH-MLNNWTEKCTHLVMTSIKVTIKTICALI 164
Cdd:cd17736   3 LVMTS-VHSEEQELLESVVKKLGGFrVEDSVTEKTTHVVVGSPRRTLNVLLGIA 55
 
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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