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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020   2 WKLLPAAGPAGgEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEE 81
Cdd:cd22667    1 WWLLSEQDGAG-TSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGE 79

                         90       100
                 ....*....|....*....|....*....
gi 767953020  82 KMQNGFSRTLKSGDGITFGVFGSKFRIEY 110
Cdd:cd22667   80 KLKGGSEVTLKDGDVITFGVLGSKFRVEY 108

Second BRCT domain on Nijmegen syndrome breakage protein;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020  217 ERKQIFKGKTFIFLNAKQHKKLSSAVVFGGGEARL-------------ITEENEEEHNFFLAPGTCVVDTGITnsqtliP 283
Cdd:pfam16508   2 ERKTLFEGKTFVFLDQKQFERLSPPITNGGGKALLyevepgettpddfVRYVKNVGSELLTGKGVVVVRFRPK------K 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767953020  284 DCQKKWIQSIMDMLQRQ-GLRPIPEAEIGLAVIFMTTKNYCDP 325
Cdd:pfam16508  76 SSNEEWIASFENELALRlGQRVIEQSEFLDAILHCSASKLCNP 118

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020   2 WKLLPAAGPAGgEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEE 81
Cdd:cd22667    1 WWLLSEQDGAG-TSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGE 79

                         90       100
                 ....*....|....*....|....*....
gi 767953020  82 KMQNGFSRTLKSGDGITFGVFGSKFRIEY 110
Cdd:cd22667   80 KLKGGSEVTLKDGDVITFGVLGSKFRVEY 108

Second BRCT domain on Nijmegen syndrome breakage protein;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020  217 ERKQIFKGKTFIFLNAKQHKKLSSAVVFGGGEARL-------------ITEENEEEHNFFLAPGTCVVDTGITnsqtliP 283
Cdd:pfam16508   2 ERKTLFEGKTFVFLDQKQFERLSPPITNGGGKALLyevepgettpddfVRYVKNVGSELLTGKGVVVVRFRPK------K 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767953020  284 DCQKKWIQSIMDMLQRQ-GLRPIPEAEIGLAVIFMTTKNYCDP 325
Cdd:pfam16508  76 SSNEEWIASFENELALRlGQRVIEQSEFLDAILHCSASKLCNP 118

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953020   24 YVVGR-KNCAILIeNDQSISRNHAVLTANFSvtnlsqtdeiPVLTLKD-NSKYGTFVNEEKMQNgFSRTLKSGDGITF 99
Cdd:pfam00498   1 VTIGRsPDCDIVL-DDPSVSRRHAEIRYDGG----------GRFYLEDlGSTNGTFVNGQRLGP-EPVRLKDGDVIRL 66

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020  109 EYEPLVACSSCLDVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKavESKK 188
Cdd:pfam16770   6 PYDIRAVLTGCERWIDKEDLDKKKLRLLGIKIVQDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLK--EGKL 83

                  ....
gi 767953020  189 QPPQ 192
Cdd:pfam16770  84 PDEE 87

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020   2 WKLLPAAGPAGgEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEE 81
Cdd:cd22667    1 WWLLSEQDGAG-TSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGE 79

                         90       100
                 ....*....|....*....|....*....
gi 767953020  82 KMQNGFSRTLKSGDGITFGVFGSKFRIEY 110
Cdd:cd22667   80 KLKGGSEVTLKDGDVITFGVLGSKFRVEY 108

Second BRCT domain on Nijmegen syndrome breakage protein;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020  217 ERKQIFKGKTFIFLNAKQHKKLSSAVVFGGGEARL-------------ITEENEEEHNFFLAPGTCVVDTGITnsqtliP 283
Cdd:pfam16508   2 ERKTLFEGKTFVFLDQKQFERLSPPITNGGGKALLyevepgettpddfVRYVKNVGSELLTGKGVVVVRFRPK------K 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767953020  284 DCQKKWIQSIMDMLQRQ-GLRPIPEAEIGLAVIFMTTKNYCDP 325
Cdd:pfam16508  76 SSNEEWIASFENELALRlGQRVIEQSEFLDAILHCSASKLCNP 118

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767953020 113 LVACSSCLDVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTE 179
Cdd:cd00027    1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLD 67

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020   1 MWKLLPAAG-PAGGEPYRLLTG-VEYVVGRKN--CAILIENDQS---ISRNHAVLtanfSVTNlSQTDEIPVLtLKDNSK 73
Cdd:cd22685    5 LLRIGLSASrSEPRDLYTFRPDlCEYRIGRNPevCDVFLCSSQHpnlISREHAEI----HAER-DGNGNWKVL-IEDRST 78

                         90       100
                 ....*....|....*....|....*..
gi 767953020  74 YGTFVNEEKMQNGFSRTLKSGDGITFG 100
Cdd:cd22685   79 NGTYVNDVRLQDGQRRELSDGDTITFG 105

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767953020 132 ILQLGGFTVNNWtEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKA 183
Cdd:cd17744   18 IKKLGGSVVDSV-EDCTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKA 68

forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020  26 VGRKNCAILIENdQSISRNHAVLTANfsvtnlSQTDEipvLTLKD-NSKYGTFVNEEKMQNGFSRTLKSGDGITFGVFGS 104
Cdd:cd22704   21 VGREDCDLILQS-RSVDKQHAVITYD------QIDNE---FKIKDlGSLNGTFVNDSRIPEQTYITLKLGDSIRFGYDTN 90

                 ....*
gi 767953020 105 KFRIE 109
Cdd:cd22704   91 VYRFE 95

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953020 118 SCLDVSGKTALNQAILQLGGFTVN--NWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKA 183
Cdd:cd17738    7 SGFSEDEKKELISIIEKLGGKVLDsdEFDPKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKA 74

second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020  18 LLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLsqtdeiPVLTLKDNSKYGTFVNEEKMQNGFSRTLKSGDGI 97
Cdd:cd22690   15 ELTQNTTFIGRSKDCDEEITDPRISKHHCIITRKRSGKGL------DDVYVTDTSTNGTFINNNRLGKGSQSLLQDGDEI 88

                 ..
gi 767953020  98 TF 99
Cdd:cd22690   89 VL 90

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020  21 GVEYVVGRK---NCAILIENDQSISRNHAVLtanfsvtnlsQTDEIPVLTLKDN-SKYGTFVNEEKMQNGFSRTLKSGDG 96
Cdd:cd22663   20 GKEVTVGRGlgvTYQLVSTCPLMISRNHCVL----------KKNDEGQWTIKDNkSLNGVWVNGERIEPLKPYPLNEGDL 89

                 ....*
gi 767953020  97 ITFGV 101
Cdd:cd22663   90 IQLGV 94

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767953020 118 SCLDVSGKTALNQAILQLGGFTV-NNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKA 183
Cdd:cd17736    6 TSVHSEEQELLESVVKKLGGFRVeDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEA 72

forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020   9 GPAGGEPYRLLTGvEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDeipvltlkdnSKYGTFVNEEKMQngfS 88
Cdd:cd22698    9 GSEEGKDYELDQD-EFTIGRSSNNDIRLNDHSVSRHHARIVRQGDKCNLTDLG----------STNGTFLNGIRVG---T 74

                         90
                 ....*....|..
gi 767953020  89 RTLKSGDGITFG 100
Cdd:cd22698   75 HELKHGDRIQLG 86

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767953020  26 VGRKNCAILIENdQSISRNHAVLTANfsvtnlSQTDEIPVLTLkdNSKYGTFVNEEKMQNGFSRTLKSGDGITFG 100
Cdd:cd22725   25 VGREDCELMLQS-RSVDKQHAVINYD------QDTDEHWVKDL--GSLNGTFVNDVRIPDQKYITLKLNDVIRFG 90

forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020   2 WKLLPAAGPAGGEPYRLLtGVEYVVGR-KNCAILIENDQSISRNHAVLtanfsvtnlsQTDEIPVLTLKDNSKYGTFVNE 80
Cdd:cd22672    2 WGQLVRLTEESSPPILLR-KDEFTIGRaKDCDLSFPGNKLVSGDHCKI----------IRDEKGQVWLEDTSTNGTLVNK 70

                         90
                 ....*....|....*....
gi 767953020  81 EKMQNGFSRTLKSGDGITF 99
Cdd:cd22672   71 VKVVKGQKVELKHGDVIYL 89

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953020    24 YVVGR--KNCAILIEnDQSISRNHAVLTAnfsvtnlsqtDEIPVLTLKDN-SKYGTFVNEEKM 83
Cdd:smart00240   1 VTIGRssEDCDIQLD-GPSISRRHAVIVY----------DGGGRFYLIDLgSTNGTFVNGKRI 52

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020  109 EYEPLVACSSCLDVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKavESKK 188
Cdd:pfam16770   6 PYDIRAVLTGCERWIDKEDLDKKKLRLLGIKIVQDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLK--EGKL 83

                  ....
gi 767953020  189 QPPQ 192
Cdd:pfam16770  84 PDEE 87

forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953020  23 EYVVGR-KNCAILIEnDQSISRNHAVLTANFSVTNLsqtdeipvltLKDNSKYGTFVNEEKMQnGFSRTLKSGDGITFGV 101
Cdd:cd22683   22 VTTIGRsRSCDLVLS-DPSISRFHAELRLEQNGINV----------IDNNSANGTFINGKRIK-GKTYILKNGDIIVFGK 89

                 ....*....
gi 767953020 102 FgsKFRIEY 110
Cdd:cd22683   90 C--SFLIKY 96