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 701433603  32 SSEAGEPYRLLNGTEYIVGRKNCAILIQDDQSISRSHAVLTVSRPETTSSQSLSVPILTVRDTSKYGTFVNGSKL-CGSS 110
Cdd:cd22667    7 QDGAGTSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGEKLkGGSE 86

                         90       100
                 ....*....|....*....|..
gi 701433603 111 MSLKSGDRINFGVFESKFRVEY 132
Cdd:cd22667   87 VTLKDGDVITFGVLGSKFRVEY 108

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 701433603  722 KNFKTFRKVAYPGAGQLPYIIGGSDLIAHHAKKNSELEDWLRQEMEEQNRHAREESLADDLF 783
Cdd:pfam08599   1 KNFKKFRKVAYPGAGGLPHIIGGSDLLVHNRGKNSELEEWLKQAMEEESQSAREESLADDLF 62

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 701433603  32 SSEAGEPYRLLNGTEYIVGRKNCAILIQDDQSISRSHAVLTVSRPETTSSQSLSVPILTVRDTSKYGTFVNGSKL-CGSS 110
Cdd:cd22667    7 QDGAGTSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGEKLkGGSE 86

                         90       100
                 ....*....|....*....|..
gi 701433603 111 MSLKSGDRINFGVFESKFRVEY 132
Cdd:cd22667   87 VTLKDGDVITFGVLGSKFRVEY 108

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 701433603  722 KNFKTFRKVAYPGAGQLPYIIGGSDLIAHHAKKNSELEDWLRQEMEEQNRHAREESLADDLF 783
Cdd:pfam08599   1 KNFKKFRKVAYPGAGGLPHIIGGSDLLVHNRGKNSELEEWLKQAMEEESQSAREESLADDLF 62

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701433603  33 SEAGEPYRLlNGTEYIVGR-KNCAILIqDDQSISRSHAVLTVSRPEttssqslsvpiLTVRDT-SKYGTFVNGSKLcGSS 110
Cdd:COG1716   10 PLAGRRFPL-DGGPLTIGRaPDNDIVL-DDPTVSRRHARIRRDGGG-----------WVLEDLgSTNGTFVNGQRV-TEP 75

                         90       100
                 ....*....|....*....|.
gi 701433603 111 MSLKSGDRINFGVFESKFRVE 131
Cdd:COG1716   76 APLRDGDVIRLGKTELRFRLS 96

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701433603  135 LVVCSSCLDVAQKTALNQAIQQLGGLVVNEWTEECTHLVMvsVKVTVKTICALICGRPIIKPEFFVELI 203
Cdd:pfam00533   9 KTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75

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 701433603  32 SSEAGEPYRLLNGTEYIVGRKNCAILIQDDQSISRSHAVLTVSRPETTSSQSLSVPILTVRDTSKYGTFVNGSKL-CGSS 110
Cdd:cd22667    7 QDGAGTSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGEKLkGGSE 86

                         90       100
                 ....*....|....*....|..
gi 701433603 111 MSLKSGDRINFGVFESKFRVEY 132
Cdd:cd22667   87 VTLKDGDVITFGVLGSKFRVEY 108

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 701433603  722 KNFKTFRKVAYPGAGQLPYIIGGSDLIAHHAKKNSELEDWLRQEMEEQNRHAREESLADDLF 783
Cdd:pfam08599   1 KNFKKFRKVAYPGAGGLPHIIGGSDLLVHNRGKNSELEEWLKQAMEEESQSAREESLADDLF 62

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 701433603 135 LVVCSSCLDVAQKTALNQAIQQLGGLVVNEWTEECTHLVMVSVKVTVKTICALICGRPIIKPEFFVE 201
Cdd:cd00027    1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLD 67

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 701433603  42 LNGTEYIVGR-KNCAILIqDDQSISRSHAVLTVSRPEttssqslsvpiLTVRDT-SKYGTFVNGSKLcGSSMSLKSGDRI 119
Cdd:cd00060   16 LTKGVVTIGRsPDCDIVL-DDPSVSRRHARIEVDGGG-----------VYLEDLgSTNGTFVNGKRI-TPPVPLQDGDVI 82

                         90
                 ....*....|..
gi 701433603 120 NFGVFEskFRVE 131
Cdd:cd00060   83 RLGDTT--FRFE 92

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701433603 136 VVCSSCLDVAQKTALNQAIQQLGGLVVNEwTEECTHLVMVSVKVTVKTICALICGRPIIKPE 197
Cdd:cd17712    3 RVLFTGFDPVQVRKLTKKVTILGGEVVES-PQECTHLVAPKVSRTVKFLTAISVCKHIVTPE 63

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 701433603 135 LVVCSSCLDVAQKTALNQAIQQLGGLVVNEWTEECTHLVMVSVKV-----TVKTICALICGRPIIKPE 197
Cdd:cd17734    1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADERgvcprTMKYLMGILAGKWIVSFE 68

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 701433603  31 LSSEAGEPYRLLNGtEYIVGRKNCAILIQDDQSISRSHAVLTVSRPEttssqslsvpiLTVRDT-SKYGTFVNGSKLcgS 109
Cdd:cd22698    8 KGSEEGKDYELDQD-EFTIGRSSNNDIRLNDHSVSRHHARIVRQGDK-----------CNLTDLgSTNGTFLNGIRV--G 73

                         90       100
                 ....*....|....*....|..
gi 701433603 110 SMSLKSGDRINFGvfESKFRVE 131
Cdd:cd22698   74 THELKHGDRIQLG--ETIFRFI 93

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 701433603  41 LLNGTEYIVGRKNCAILIQDDQSISRSHAVLTVSrpettssQSLsvpiLTVRD-TSKYGTFVNGSKLCGSSMSLKSGDRI 119
Cdd:cd22683   17 ITNRNVTTIGRSRSCDLVLSDPSISRFHAELRLE-------QNG----INVIDnNSANGTFINGKRIKGKTYILKNGDII 85

                 ...
gi 701433603 120 NFG 122
Cdd:cd22683   86 VFG 88

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 701433603  41 LLNGTEYIVGR-KNCAILIQDDQsISRSHAVLTVSRPETtssqslSVPILTVRDTSKYGTFVNGSKL-CGSSMSLKSGDR 118
Cdd:cd22690   15 ELTQNTTFIGRsKDCDEEITDPR-ISKHHCIITRKRSGK------GLDDVYVTDTSTNGTFINNNRLgKGSQSLLQDGDE 87

                 .
gi 701433603 119 I 119
Cdd:cd22690   88 I 88

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 701433603  30 GLSSEAGEPYRLLNGTeYIVGRKNCAILIQDdQSISRSHAVLTVSrpetTSSQSLSVPILTvrdtSKYGTFVNGSKLCGS 109
Cdd:cd22704    3 CLVSSDGTRHRLPRSM-LFVGREDCDLILQS-RSVDKQHAVITYD----QIDNEFKIKDLG----SLNGTFVNDSRIPEQ 72

                         90       100
                 ....*....|....*....|...
gi 701433603 110 S-MSLKSGDRINFGVFESKFRVE 131
Cdd:cd22704   73 TyITLKLGDSIRFGYDTNVYRFE 95

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 701433603   42 LNGTEYIVGR-KNCAILIQDDqSISRSHAVLTVsRPEttssqslSVPILTVRDTSkyGTFVNGSKLCGSSMSLKSGDRIN 120
Cdd:pfam16697  14 LEGGRYRIGSdPDCDIVLSDK-EVSRVHLKLEV-DDE-------GWRLDDLGSGN--GTLVNGQRVTELGIALRPGDRIE 82

                          90
                  ....*....|.
gi 701433603  121 FGVFESKFRVE 131
Cdd:pfam16697  83 LGQTEFCLVPA 93

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701433603  129 RVEYEPLVVCSSCLDVAQKTALNQAI-QQLGGLVVNEwTEECTHLVMVSVKVTVKTICALICGRPIIKPEFFVELIKAI 206
Cdd:pfam16770   4 LPPYDIRAVLTGCERWIDKEDLDKKKlRLLGIKIVQD-PSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEG 81

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 701433603  34 EAGEPYRLLNGTEYIVGR--KNCAILIqDDQSISRSHAVL----TVSRPETTSSQSLSVPILTVrdTSKYGTFVNGSKL- 106
Cdd:cd22676   10 EQLETIDIHRQSAYLIGRdrRVADIPL-DHPSCSKQHAVIqfreVEKRNEGDVIENIRPYIIDL--GSTNGTFLNGEKIe 86

                         90       100
                 ....*....|....*....|..
gi 701433603 107 CGSSMSLKSGDRINFGVFESKF 128
Cdd:cd22676   87 PRRYYELREKDVLKFGLSTREY 108

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701433603  46 EYIVGRKNCAILIQDDQSISRSHAVLTVSRPEttssqslsvpiLTVRDT-SKYGTFVNGSKLC-GSSMSLKSGDRINFGV 123
Cdd:cd22682   21 TIVIGRSVESQVQIDDDSVSRYHAKLAVNPSA-----------VSIIDLgSTNGTIVNGKKIPkLASCDLQNGDQIKIGN 89

                 ....*..
gi 701433603 124 FESKFRV 130
Cdd:cd22682   90 TIFKFHE 96

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 701433603  42 LNGTEYIVGRKNCAILIQDDQSISRSHAVLTVsrpettSSQSLSVPILtvrdTSKYGTFVNGSKLCGSSMSLKSGDRINF 121
Cdd:cd22680   18 FDFSSVSIGRDPENVIVIPDPFVSRNHARITV------DSNEIYIEDL----GSTNGTFVNDFKRIKGPAKLHPNDIIKL 87

                 .
gi 701433603 122 G 122
Cdd:cd22680   88 G 88

second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; 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 second BRCT domain.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701433603 135 LVVCSSCLDVAQKTALNQAIQQLGGLVVNEWTEECTHLVmVSVKVTVKTICALICGR-PIIKPEFFVELIKA 205
Cdd:cd17731    6 LVICVTGFDSEERKEIQQLVEQNGGSYSPDLSKNCTHLI-AGSPSGQKYEFARKWNSiHIVTPEWLYDSIEA 76

first BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; 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 first BRCT domain.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 701433603 135 LVVCSSCLDVAQKTALNQAIQQLGGLVVNEWTEECTHLVMVSVKvTVKTICALICGRPIIKPE 197
Cdd:cd17737    2 VTISCTSLEKEEREEVHKYVQLMGGRVSRDLTVSVTHLIAGEVG-SKKYLVAASLKKPIMLPS 63