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 1059100239   2 WKLLPVAGPAGgEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEE 81
Cdd:cd22667     1 WWLLSEQDGAG-TSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGE 79

                          90       100
                  ....*....|....*....|....*....
gi 1059100239  82 KMQNGSSRTLKSGDSITFGVFESKFRVEY 110
Cdd:cd22667    80 KLKGGSEVTLKDGDVITFGVLGSKFRVEY 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 1059100239 682 NNFKKFKKVTYPGAGKLPHIIGGSDLIPHHARKNTELEEWLRQEMEVQNQHAKEESLADDLF 743
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 1059100239   2 WKLLPVAGPAGgEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEE 81
Cdd:cd22667     1 WWLLSEQDGAG-TSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGE 79

                          90       100
                  ....*....|....*....|....*....
gi 1059100239  82 KMQNGSSRTLKSGDSITFGVFESKFRVEY 110
Cdd:cd22667    80 KLKGGSEVTLKDGDVITFGVLGSKFRVEY 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 1059100239 682 NNFKKFKKVTYPGAGKLPHIIGGSDLIPHHARKNTELEEWLRQEMEVQNQHAKEESLADDLF 743
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 1059100239   1 MWKLLPVAGPAGGEPYRLlTGVEYVVGR-KNCAILIeNDQSISRNHAVLTA---NFSVTNLsqtdeipvltlkdNSKYGT 76
Cdd:COG1716     1 MARLVVLEGPLAGRRFPL-DGGPLTIGRaPDNDIVL-DDPTVSRRHARIRRdggGWVLEDL-------------GSTNGT 65

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1059100239  77 FVNEEKMQngSSRTLKSGDSITFGVFESKFRVE 109
Cdd:COG1716    66 FVNGQRVT--EPAPLRDGDVIRLGKTELRFRLS 96

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1059100239   24 YVVGR--KNCAILIEnDQSISRNHAVLTAnfsvtnlsqtDEIPVLTLKDN-SKYGTFVNEEKM 83
Cdd:smart00240   1 VTIGRssEDCDIQLD-GPSISRRHAVIVY----------DGGGRFYLIDLgSTNGTFVNGKRI 52

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 1059100239   2 WKLLPVAGPAGgEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEE 81
Cdd:cd22667     1 WWLLSEQDGAG-TSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGE 79

                          90       100
                  ....*....|....*....|....*....
gi 1059100239  82 KMQNGSSRTLKSGDSITFGVFESKFRVEY 110
Cdd:cd22667    80 KLKGGSEVTLKDGDVITFGVLGSKFRVEY 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 1059100239 682 NNFKKFKKVTYPGAGKLPHIIGGSDLIPHHARKNTELEEWLRQEMEVQNQHAKEESLADDLF 743
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 1059100239   1 MWKLLPVAGPAGGEPYRLlTGVEYVVGR-KNCAILIeNDQSISRNHAVLTA---NFSVTNLsqtdeipvltlkdNSKYGT 76
Cdd:COG1716     1 MARLVVLEGPLAGRRFPL-DGGPLTIGRaPDNDIVL-DDPTVSRRHARIRRdggGWVLEDL-------------GSTNGT 65

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1059100239  77 FVNEEKMQngSSRTLKSGDSITFGVFESKFRVE 109
Cdd:COG1716    66 FVNGQRVT--EPAPLRDGDVIRLGKTELRFRLS 96

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 1059100239 113 LVACSSCLDVSGKTALNQAVLQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTE 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 1059100239   9 GPAGGEPYRLLTG-VEYVVGRKN--CAILIENDQS---ISRNHAVLtanfSVTNlSQTDEIPVLtLKDNSKYGTFVNEEK 82
Cdd:cd22685    14 RSEPRDLYTFRPDlCEYRIGRNPevCDVFLCSSQHpnlISREHAEI----HAER-DGNGNWKVL-IEDRSTNGTYVNDVR 87

                          90
                  ....*....|....*...
gi 1059100239  83 MQNGSSRTLKSGDSITFG 100
Cdd:cd22685    88 LQDGQRRELSDGDTITFG 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 1059100239 132 VLQLGGFTVNNWtEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKA 183
Cdd:cd17744    18 IKKLGGSVVDSV-EDCTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKA 68

forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1059100239  26 VGRKNCAILIENdQSISRNHAVLtanfsvtNLSQTDEIPVLtlKD-NSKYGTFVNEEKMQNGSSRtLKSGDSITFG 100
Cdd:cd22700    20 IGREGCDLVLQS-PGVEEQHAVI-------EYSEQENCFVL--QDlNTAQGTYVNDCRIQNAAVR-LAPGDVLRFG 84

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 1059100239 120 LDVSGKTALNQAVLQLGGFTVNNwTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKA 183
Cdd:cd17712     9 FDPVQVRKLTKKVTILGGEVVES-PQECTHLVAPKVSRTVKFLTAISVCKHIVTPEWLEESFKQ 71

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 1059100239  21 GVEYVVGRK---NCAILIENDQSISRNHAVLtanfsvtnlsQTDEIPVLTLKDN-SKYGTFVNEEKMQNGSSRTLKSGDS 96
Cdd:cd22663    20 GKEVTVGRGlgvTYQLVSTCPLMISRNHCVL----------KKNDEGQWTIKDNkSLNGVWVNGERIEPLKPYPLNEGDL 89

                          90
                  ....*....|....*.
gi 1059100239  97 ITFGV-FESKFRVEYE 111
Cdd:cd22663    90 IQLGVpPENKEPAEYV 105

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1059100239 113 LVACSSCLDVSGKTALNQAVLQLGGFTVNNWTEECTHLVMVSVKV-----TIKTICALICGRPIVKPEYFTEFLKAVQ 185
Cdd:cd17734     1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADERgvcprTMKYLMGILAGKWIVSFEWVEACLKAKK 78

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; 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). The FHA domain is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059100239  11 AGGEPYRLLTGVEYVvGRKNCAILIENdQSISRNHAVLtaNFSvtnlSQTDEIPVLTLkdNSKYGTFVNEEKMQNGSSRT 90
Cdd:cd22724    11 SGGTRHRLPREMIFV-GRDDCELMLQS-RSVDKQHAVI--NYD----ASTDEHKVKDL--GSLNGTFVNDVRIPEQTYIT 80

                          90
                  ....*....|....*....
gi 1059100239  91 LKSGDSITFGVFESKFRVE 109
Cdd:cd22724    81 LKLDDKLRFGYDTNLFTVV 99

forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059100239  14 EPYRLLTGVEYVVGR-KNCAILIENdQSISRNHAVLtaNFSVTNLSQTDEIPVLTLkdNSKYGTFVNEEKMQNGSSRTLK 92
Cdd:cd22677    14 ETLDLNGKSFYVFGRlPGCDVVLEH-PSISRYHAVL--QYRGDADDHDGGFYLYDL--GSTHGTFLNKQRIPPKQYYRLR 88

                  ....*...
gi 1059100239  93 SGDSITFG 100
Cdd:cd22677    89 VGHVLKFG 96

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 1059100239   9 GPAGGEPYRLLTGvEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDeipvltlkdnSKYGTFVNEEKMQngsS 88
Cdd:cd22698     9 GSEEGKDYELDQD-EFTIGRSSNNDIRLNDHSVSRHHARIVRQGDKCNLTDLG----------STNGTFLNGIRVG---T 74

                          90       100
                  ....*....|....*....|.
gi 1059100239  89 RTLKSGDSITFGvfESKFRVE 109
Cdd:cd22698    75 HELKHGDRIQLG--ETIFRFI 93

forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059100239  41 ISRNHAVLTAnfsvTNLSqtdeipvLTLKD-NSKYGTFVNEEKMQNGSS----RTLKSGDSITFGV--FESKFRVEYEPL 113
Cdd:cd22679    49 LSRNHALLWY----DDGK-------FYLQDtKSSNGTFVNNQRLSKGSEesepRELHSGDIVQFGVdvVENSRKVTHGCI 117

                  ....*.
gi 1059100239 114 VACSSC 119
Cdd:cd22679   118 VATVTL 123

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 1059100239   2 WKLLPVAGPAGGEPYRLLtGVEYVVGR-KNCAILIENDQSISRNHAVLtanfsvtnlsQTDEIPVLTLKDNSKYGTFVNE 80
Cdd:cd22672     2 WGQLVRLTEESSPPILLR-KDEFTIGRaKDCDLSFPGNKLVSGDHCKI----------IRDEKGQVWLEDTSTNGTLVNK 70

                          90
                  ....*....|....*....
gi 1059100239  81 EKMQNGSSRTLKSGDSITF 99
Cdd:cd22672    71 VKVVKGQKVELKHGDVIYL 89

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 1059100239  12 GGEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTanfsvtnlSQTDEipvLTLKD-NSKYGTFVNEEKMQngsSRT 90
Cdd:cd22694     6 PGGELRFDPGSSVRIGRDPDADVRLDDPRVSRRHALLE--------FDGDG---WVYTDlGSRNGTYLNGRRVQ---QVK 71

                          90
                  ....*....|
gi 1059100239  91 LKSGDSITFG 100
Cdd:cd22694    72 LSDGTRVRLG 81

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 1059100239   4 LLPVAGPAGGEPYRLLTGVEYVVGRK-NCAILIENDqSISRNHAVLTANfsvtnlsqtdeIPVLTLKD-NSKYGTFVNEE 81
Cdd:cd22682     2 LLMIIGPPGVGKQFPITESTIVIGRSvESQVQIDDD-SVSRYHAKLAVN-----------PSAVSIIDlGSTNGTIVNGK 69

                          90       100
                  ....*....|....*....|....*..
gi 1059100239  82 KMQNGSSRTLKSGDSITFGVFESKFRV 108
Cdd:cd22682    70 KIPKLASCDLQNGDQIKIGNTIFKFHE 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 1059100239  19 LTGVEYVVGRK-NCAILIEnDQSISRNHAVLTanfsVTNlsqtDEIPVLTLkdNSKYGTFVNEEKMQNGSSRtLKSGDSI 97
Cdd:cd22680    18 FDFSSVSIGRDpENVIVIP-DPFVSRNHARIT----VDS----NEIYIEDL--GSTNGTFVNDFKRIKGPAK-LHPNDII 85

                  ...
gi 1059100239  98 TFG 100
Cdd:cd22680    86 KLG 88