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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720408986 111 EPLVVCSSCLDVSGKTVLNQAILQLGGLTANNWTEECTHLVMSAVKVTIKTICALICGRPIIKPEYFSEFLKAV 184
Cdd:cd17741     1 EPLVVCSSCLDSEEKKKLKQIIAKLGGKVVNEWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYLDALLEAI 74

DNA damage repair protein Nbs1; This C terminal region of the DNA damage repair protein Nbs1 has been identified to be necessary for the binding of Mre11 and Tel1.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720408986 681 KNFKKFKKATFPGAGKLPHIIGGSDLVGHHARKNTELEEWLKQEMEVSRKggpHTRDCTLA 741
Cdd:pfam08599   1 KNFKKFRKVAYPGAGGLPHIIGGSDLLVHNRGKNSELEEWLKQAMEEESQ---SAREESLA 58

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720408986 111 EPLVVCSSCLDVSGKTVLNQAILQLGGLTANNWTEECTHLVMSAVKVTIKTICALICGRPIIKPEYFSEFLKAV 184
Cdd:cd17741     1 EPLVVCSSCLDSEEKKKLKQIIAKLGGKVVNEWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYLDALLEAI 74

DNA damage repair protein Nbs1; This C terminal region of the DNA damage repair protein Nbs1 has been identified to be necessary for the binding of Mre11 and Tel1.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720408986 681 KNFKKFKKATFPGAGKLPHIIGGSDLVGHHARKNTELEEWLKQEMEVSRKggpHTRDCTLA 741
Cdd:pfam08599   1 KNFKKFRKVAYPGAGGLPHIIGGSDLLVHNRGKNSELEEWLKQAMEEESQ---SAREESLA 58

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720408986  24 YVVGR-KNCGILIeNDQSISRNHAVLTVNFPvtslsqtdeiPTLTIKD-NSKYGTFVNEEKMQTGlSCTLKTGDRVTF 99
Cdd:pfam00498   1 VTIGRsPDCDIVL-DDPSVSRRHAEIRYDGG----------GRFYLEDlGSTNGTFVNGQRLGPE-PVRLKDGDVIRL 66

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720408986   24 YVVGR--KNCGILIEnDQSISRNHAVLTVnfpvtslsqtDEIPTLTIKDN-SKYGTFVNEEKM 83
Cdd:smart00240   1 VTIGRssEDCDIQLD-GPSISRRHAVIVY----------DGGGRFYLIDLgSTNGTFVNGKRI 52

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720408986 111 EPLVVCSSCLDVSGKTVLNQAILQLGGLTANNWTEECTHLVMSAVKVTIKTICALICGRPIIKPEYFSEFLKAV 184
Cdd:cd17741     1 EPLVVCSSCLDSEEKKKLKQIIAKLGGKVVNEWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYLDALLEAI 74

DNA damage repair protein Nbs1; This C terminal region of the DNA damage repair protein Nbs1 has been identified to be necessary for the binding of Mre11 and Tel1.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720408986 681 KNFKKFKKATFPGAGKLPHIIGGSDLVGHHARKNTELEEWLKQEMEVSRKggpHTRDCTLA 741
Cdd:pfam08599   1 KNFKKFRKVAYPGAGGLPHIIGGSDLLVHNRGKNSELEEWLKQAMEEESQ---SAREESLA 58

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408986   3 KLLPAAGAAPGEPYRLLAGVeYVVGR-KNCGILIeNDQSISRNHAVLTVNFPVtslsqtdeiptLTIKD-NSKYGTFVNE 80
Cdd:cd00060     1 RLIVLDGDGGGREFPLTKGV-VTIGRsPDCDIVL-DDPSVSRRHARIEVDGGG-----------VYLEDlGSTNGTFVNG 67

                          90       100
                  ....*....|....*....|....*....
gi 1720408986  81 EKMQTglSCTLKTGDRVTFGVFEskFRVE 109
Cdd:cd00060    68 KRITP--PVPLQDGDVIRLGDTT--FRFE 92

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 1720408986   1 MWKLLPAAG-AAPGEPYRLLAG-VEYVVGRKN--CGILIENDQS---ISRNHAVLTVnfpvtsLSQTDEIPTLTIKDNSK 73
Cdd:cd22685     5 LLRIGLSASrSEPRDLYTFRPDlCEYRIGRNPevCDVFLCSSQHpnlISREHAEIHA------ERDGNGNWKVLIEDRST 78

                          90       100
                  ....*....|....*....|....*..
gi 1720408986  74 YGTFVNEEKMQTGLSCTLKTGDRVTFG 100
Cdd:cd22685    79 NGTYVNDVRLQDGQRRELSDGDTITFG 105

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 1720408986  17 RLLAGVEYVVGRK---NCGILIENDQSISRNHAVLtvnfpvtslsQTDEIPTLTIKDN-SKYGTFVNEEKMQTGLSCTLK 92
Cdd:cd22663    16 LLEDGKEVTVGRGlgvTYQLVSTCPLMISRNHCVL----------KKNDEGQWTIKDNkSLNGVWVNGERIEPLKPYPLN 85

                          90       100
                  ....*....|....*....|
gi 1720408986  93 TGDRVTFGV-FESKFRVEYE 111
Cdd:cd22663    86 EGDLIQLGVpPENKEPAEYV 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
                  ....*....|....*....|....*....|....*....|....*
gi 1720408986 132 ILQLGGLTANNWtEECTHLVMSAVKVTIKTICALICGRPIIKPEY 176
Cdd:cd17744    18 IKKLGGSVVDSV-EDCTHLVTDKVRRTVKFLCALARGIPIVSPDW 61

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720408986  25 VVGR-KNCGILIeNDQSISRNHAVLTVNFPVtslsqtDEIPTLTIKDNSKYGTFVNEEKMQTGLSCTLKTGDRVTF 99
Cdd:cd22690    22 FIGRsKDCDEEI-TDPRISKHHCIITRKRSG------KGLDDVYVTDTSTNGTFINNNRLGKGSQSLLQDGDEIVL 90

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408986   2 WKLLPAAGAAPGEPYRLLAGVEYVVGR--KNCGILIENdQSISRNHAVLtVNFPVTSLSQTDEIPTLT--IKD-NSKYGT 76
Cdd:cd22676     1 WRLYVFKGGEQLETIDIHRQSAYLIGRdrRVADIPLDH-PSCSKQHAVI-QFREVEKRNEGDVIENIRpyIIDlGSTNGT 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1720408986  77 FVNEEKMQTGLSCTLKTGDRVTFGVFESKF 106
Cdd:cd22676    79 FLNGEKIEPRRYYELREKDVLKFGLSTREY 108

forkhead associated (FHA) domain found in aprataxin, bifunctional polynucleotide phosphatase/kinase (PNKP), aprataxin and PNK-like factor (APLF), and similar proteins; The family includes aprataxin, PNKP, and APLF. Aprataxin (EC 3.6.1.71/EC 3.6.1.72), also called forkhead-associated domain histidine triad-like protein (FHA-HIT), is a DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair, and base excision repair. It catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. It can also hydrolyze adenosine 5'-monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity. Likewise, it catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA but has higher specific activity with 5'-linked adenosine (AppDNA). PNKP (EC 3.1.3.32/EC 2.7.1.78), also called DNA 5'-kinase/3'-phosphatase, or polynucleotide kinase-3'-phosphatase, plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNKP ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone. APLF, also called apurinic-apyrimidinic endonuclease APLF, PNK and APTX-like FHA domain-containing protein, or XRCC1-interacting protein 1 (XIP1), is a novel apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease with conserved zinc-finger-like motifs involved in single-strand and double-strand DNA break repair. It is recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions. It can introduce nicks at hydroxyuracil and other types of pyrimidine base damage. Together with PARP3, APLF promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ). Members of this family contain an FHA domain at their N-terminus. The FHA domain is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408986  13 GEPYRLLAGVEYVVGRKNC-GIlieNDQSISRNHAVLTVNfpvtslsqtDEIPTLTIKDNSKYGTFVN-----EEKMQTG 86
Cdd:cd22671    10 GPPIELKEGGPTVLGRGPLlGI---RDKRVSRKQAEITVD---------DDTGSVTVTQLGTNPSFVNradgeGKVLKKG 77

                          90       100
                  ....*....|....*....|...
gi 1720408986  87 LSCTLKTGDRVTFGVFESKFRVE 109
Cdd:cd22671    78 ESVELKDGDVISLLPGKYPFRVE 100

forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408986  19 LAGVEYVVGRK-NCGILIEnDQSISRNHAVLTVnfpvtslsqtdEIPTLTIKD-NSKYGTFVNEEKMQTGlSCTLKTGDR 96
Cdd:cd22680    18 FDFSSVSIGRDpENVIVIP-DPFVSRNHARITV-----------DSNEIYIEDlGSTNGTFVNDFKRIKG-PAKLHPNDI 84

                  ....
gi 1720408986  97 VTFG 100
Cdd:cd22680    85 IKLG 88

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408986  19 LAGVEYVVGR-KNCGILIeNDQSISRNHAVLTVNFPVTSLSQTDeiptltikdnSKYGTFVNEEKmQTGLSCTLKTGDRV 97
Cdd:pfam16697  14 LEGGRYRIGSdPDCDIVL-SDKEVSRVHLKLEVDDEGWRLDDLG----------SGNGTLVNGQR-VTELGIALRPGDRI 81

                          90
                  ....*....|..
gi 1720408986  98 TFGVFESKFRVE 109
Cdd:pfam16697  82 ELGQTEFCLVPA 93

first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408986  12 PGEPYRLLAGVEYVVGRK-NCGILIENDQsISRNHAVLTvnfpvtslSQTDEiptLTIKD-NSKYGTFVNEEKMQTGLsc 89
Cdd:cd22694     6 PGGELRFDPGSSVRIGRDpDADVRLDDPR-VSRRHALLE--------FDGDG---WVYTDlGSRNGTYLNGRRVQQVK-- 71

                          90
                  ....*....|.
gi 1720408986  90 tLKTGDRVTFG 100
Cdd:cd22694    72 -LSDGTRVRLG 81

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408986   2 WKLLPAAGAAPGEPYRLLagveyVVGRKNCGILIENdQSISRNHAVLTVNfpvtslSQTDEiptLTIKD-NSKYGTFVNE 80
Cdd:cd22725     6 WFLVSSSGTRHRLPREMI-----FVGREDCELMLQS-RSVDKQHAVINYD------QDTDE---HWVKDlGSLNGTFVND 70

                          90       100
                  ....*....|....*....|
gi 1720408986  81 EKMQTGLSCTLKTGDRVTFG 100
Cdd:cd22725    71 VRIPDQKYITLKLNDVIRFG 90

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 1720408986  23 EYVVGR-KNCGILIEnDQSISRNHAVLTVnfpvtslsqtdEIPTLTIKD-NSKYGTFVNEEKMQtGLSCTLKTGDRVTFG 100
Cdd:cd22683    22 VTTIGRsRSCDLVLS-DPSISRFHAELRL-----------EQNGINVIDnNSANGTFINGKRIK-GKTYILKNGDIIVFG 88

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 1720408986 107 RVEYEPLVVCSSCLDVSGKTVLNQAILQLGGLTANNWTEECTHLVMSAVKVTIKTICALICGRPIIKPeyfsEFLKAVES 186
Cdd:pfam16770   4 LPPYDIRAVLTGCERWIDKEDLDKKKLRLLGIKIVQDPSKCNHLIAPKILRTEKFLCALAFAPYILSP----DFITDCLK 79

                          90
                  ....*....|
gi 1720408986 187 KKQPPDIESF 196
Cdd:pfam16770  80 EGKLPDEEDY 89

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720408986 114 VVCSScLDVSGKTVLNQAILQLGGLT-ANNWTEECTHLVMSAVKVTIKTICALICGRPIIKPEYFSEFLKA 183
Cdd:cd17736     3 LVMTS-VHSEEQELLESVVKKLGGFRvEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEA 72