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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   20 IPVFTVLKNGAILKNIFVVNSRDFSsperngstvsdddgEVEEILVVGRHPDCDILLTHPSISRFHLEIRSISSRQKLFV 99
Cdd:cd22691    1 IPVLTVLKNGSVLKNIFLHGKFSKS--------------EEEDILVVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITL 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 18399229  100 TDLSSVHGTWVRDLRIEPHGCVEVEEGDTIRIGGSTRIYRLHWIPLS 146
Cdd:cd22691   67 TDLSSVHGTWVNGQRIEPGVPVELEEGDTVRLGASTRVYRLHWIPVS 113

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   20 IPVFTVLKNGAILKNIFVVNSRDFSsperngstvsdddgEVEEILVVGRHPDCDILLTHPSISRFHLEIRSISSRQKLFV 99
Cdd:cd22691    1 IPVLTVLKNGSVLKNIFLHGKFSKS--------------EEEDILVVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITL 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 18399229  100 TDLSSVHGTWVRDLRIEPHGCVEVEEGDTIRIGGSTRIYRLHWIPLS 146
Cdd:cd22691   67 TDLSSVHGTWVNGQRIEPGVPVELEEGDTVRLGASTRVYRLHWIPVS 113

PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   1239 IVLDTSSLLDKesrkpLQLLQGL-KGTHLVVPRTVLRELNEVKRSRSFLFRRRTEIASSALDWIEECKVNSKWWIQVQSP 1317
Cdd:pfam13638    1 YVLDTNVLLHD-----PDALFNFgEENDVVIPITVLEELDGLKKGSDESGRELARLARQANRWLDELLENNGGRLRGQTL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   1318 TEEtkaiaptppvtpqsngssafpfslhwnnyAPEIDSPTSEDQVLECALLYRNRNRDEKLVLLSNDVTLKIKAMAEGVI 1397
Cdd:pfam13638   76 DER-----------------------------LPPDPFDKNDNRILAVALYLKEELPDRPVILVSKDINLRIKADALGIP 126

                   ....*
gi 18399229   1398 CETPH 1402
Cdd:pfam13638  127 AEDYE 131

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18399229     65 VVGRHPDCDILLTHPSISRFHLEIRSISSRQkLFVTDLSSVHGTWVRDLRIEPHgCVEVEEGDTIRI 131
Cdd:pfam00498    2 TIGRSPDCDIVLDDPSVSRRHAEIRYDGGGR-FYLEDLGSTNGTFVNGQRLGPE-PVRLKDGDVIRL 66

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   20 IPVFTVLKNGAILKNIFVVNSRDFSsperngstvsdddgEVEEILVVGRHPDCDILLTHPSISRFHLEIRSISSRQKLFV 99
Cdd:cd22691    1 IPVLTVLKNGSVLKNIFLHGKFSKS--------------EEEDILVVGRHPDCDIVLDHPSISRFHLEIRIIPSRRKITL 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 18399229  100 TDLSSVHGTWVRDLRIEPHGCVEVEEGDTIRIGGSTRIYRLHWIPLS 146
Cdd:cd22691   67 TDLSSVHGTWVNGQRIEPGVPVELEEGDTVRLGASTRVYRLHWIPVS 113

PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   1239 IVLDTSSLLDKesrkpLQLLQGL-KGTHLVVPRTVLRELNEVKRSRSFLFRRRTEIASSALDWIEECKVNSKWWIQVQSP 1317
Cdd:pfam13638    1 YVLDTNVLLHD-----PDALFNFgEENDVVIPITVLEELDGLKKGSDESGRELARLARQANRWLDELLENNGGRLRGQTL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   1318 TEEtkaiaptppvtpqsngssafpfslhwnnyAPEIDSPTSEDQVLECALLYRNRNRDEKLVLLSNDVTLKIKAMAEGVI 1397
Cdd:pfam13638   76 DER-----------------------------LPPDPFDKNDNRILAVALYLKEELPDRPVILVSKDINLRIKADALGIP 126

                   ....*
gi 18399229   1398 CETPH 1402
Cdd:pfam13638  127 AEDYE 131

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   61 EEILVVGRHPDCDILLTHPSISRFHLEIRSISSRqkLFVTDLSSVHGTWVRDLRIEphGCVEVEEGDTIRIGGSTRIYRL 140
Cdd:COG1716   20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGG--WVLEDLGSTNGTFVNGQRVT--EPAPLRDGDVIRLGKTELRFRL 95

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 18399229   52 TVSDDDGEVEEI------LVVGRHPDCDILLTHPSISRFHLEIRSISSRqkLFVTDLSSVHGTWVRDLRIEPHgcVEVEE 125
Cdd:cd00060    3 IVLDGDGGGREFpltkgvVTIGRSPDCDIVLDDPSVSRRHARIEVDGGG--VYLEDLGSTNGTFVNGKRITPP--VPLQD 78

                         90
                 ....*....|....*.
gi 18399229  126 GDTIRIGGSTriYRLH 141
Cdd:cd00060   79 GDVIRLGDTT--FRFE 92

forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   61 EEILVVGRHPDCDILLTHPSISRFHLEIRSI----SSRQKLFVTDLSSvHGTWVRDLRIEPHGCVEVEEGDTIRIGGSTR 136
Cdd:cd22670   21 NQVITIGRSPSCDIVINDPFVSRTHCRIYSVqfdeSSAPLVYVEDLSS-NGTYLNGKLIGRNNTVLLSDGDVIEIAHSAT 99

                 ....*
gi 18399229  137 IYRLH 141
Cdd:cd22670  100 FVYVH 104

VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; Saccharomyces cerevisiae mRNA-processing endoribonuclease Swt1p plays an important role in quality control of nuclear mRNPs in eukaryotes. Human transcriptional protein SWT1 (RNA endoribonuclease homolog, also known as HsSwt1, C1orf26, and chromosome 1 open reading frame 26) is an RNA endonuclease that participates in quality control of nuclear mRNPs and can associate with the nuclear pore complex (NPC). This subfamily belongs to the Smg5 and Smg6-like PIN domain family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229 1240 VLDTSSLLDKesrkpLQLLQGLKGTH--------LVVPRTVLRELNEVKRSRSFLFRRRteIASSALDWIEECKVNSKWW 1311
Cdd:cd18727    1 VLDTNVLISH-----LDLLKQLVEDVeklslpvvIVIPWVVLQELDGLKKSKRKSSLGW--LARRASTWLLEKLRSKHPR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229 1312 IQVQSPTEetkaiAPTPPVTPQSNGssafpfslhwnnyapeiDsptseDQVLECALLYRNRnRDEKLVLLSNDVTLKIKA 1391
Cdd:cd18727   74 VRGQALSE-----TLRASGDPGESN-----------------D-----DAILDCCLYFQEK-YGAPVVLLSNDKNLCNKA 125

                        170
                 ....*....|...
gi 18399229 1392 MAEGVICETPHEF 1404
Cdd:cd18727  126 LINGIPTISPEEG 138

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 18399229   65 VVGRhPDCDILLTH-PSISRFHLEIR---------SISSRQKLFVTDLSSvHGTWVRDLRIEPHGCVEVEEGDTIRIGGS 134
Cdd:cd22667   23 TVGR-KDCDIIIVDdSSISRKHATLTvlhpeanlsDPDTRPELTLKDLSK-YGTFVNGEKLKGGSEVTLKDGDVITFGVL 100

                 ....*...
gi 18399229  135 TRIYRLHW 142
Cdd:cd22667  101 GSKFRVEY 108

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18399229   64 LVVGRHPD--CDILLTHP-SISRFHLEIRSISSRQkLFVTDLSSVHGTWVRDLRIEPHGCVEVEEGDTIRIG 132
Cdd:cd22663   23 VTVGRGLGvtYQLVSTCPlMISRNHCVLKKNDEGQ-WTIKDNKSLNGVWVNGERIEPLKPYPLNEGDLIQLG 93

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

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 18399229      65 VVGRHP-DCDILLTHPSISRFHLEIRSISSRqKLFVTDLSSVHGTWVRDLRI 115
Cdd:smart00240    2 TIGRSSeDCDIQLDGPSISRRHAVIVYDGGG-RFYLIDLGSTNGTFVNGKRI 52

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18399229     61 EEILVVGRHPDCDILLTHPSISRFHLEIRSISSRqkLFVTDLSSVHGTWVRDLRIEPHGcVEVEEGDTIRIG 132
Cdd:pfam16697   16 GGRYRIGSDPDCDIVLSDKEVSRVHLKLEVDDEG--WRLDDLGSGNGTLVNGQRVTELG-IALRPGDRIELG 84

forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1) 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. The FHA domain is a small phosphopeptide recognition module.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   66 VGRHPD-CDILLTHPSISRFH--LEIR---------SISSRQKLFVTDLSSVHGTWVRDLRIEPHGCVEVEEGDTIRIGG 133
Cdd:cd22718   60 LGRDRKiADIPIDHPSCSKQHavLQYRlveytrpdgTKGRRVRPYIIDLESANGTFLNNKKIEPQRYYELKEKDVLKFGF 139

                 ....*..
gi 18399229  134 STRIYRL 140
Cdd:cd22718  140 SSREYVL 146

forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18399229   62 EILVVGRHPDCDILLTHPSISRFHLEIRSISSRQKlfVTDLSSVHGTWVRDLRIEPhgcVEVEEGDTIRIG 132
Cdd:cd22684   21 DVTTAGRHPESDIFLDDVTVSRRHAEFRRAEGGFV--VRDVGSLNGTYVNRERIDS---AVLRNGDEVQIG 86

forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called 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 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 FHA domain is a small phosphopeptide recognition module.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18399229   65 VVGRHPDCDILLTHPSISRFHLEIrSISSRQkLFVTDLSSVHGTWV-RDLRIEPHGCVEVEEGDTIRIG 132
Cdd:cd22665   24 VIGRDPSCSVVLPDKSVSKQHACI-EVDGGT-HLIEDLGSTNGTRIgNKVRLKPNVRYELIDGDLLLFG 90

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 18399229   62 EILVVGRHpDCDILLTHPSISRFHLEIRSISSRQKLFVTDLSSVHGTWVRDLRIEPHGCVEVEEGDTIRIGGSTRIYRL- 140
Cdd:cd22725   21 EMIFVGRE-DCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYITLKLNDVIRFGYDSNMYVLe 99

                 ....*..
gi 18399229  141 ---HWIP 144
Cdd:cd22725  100 rsqHKVP 106

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 18399229   60 VEEILVVGRHPDCDILLTHPSISRFHLEI---RSISSRQKLFVTDlSSVHGTWVRDLRIEPHGCVEVEEGDTI 129
Cdd:cd22690   17 TQNTTFIGRSKDCDEEITDPRISKHHCIItrkRSGKGLDDVYVTD-TSTNGTFINNNRLGKGSQSLLQDGDEI 88

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18399229   66 VGRHPDCDILLTHPSISRFHLEIrsisSRQ--KLFVTDLSSVHGTWVRDLRIephGCVEVEEGDTIRIGgsTRIYR 139
Cdd:cd22698   25 IGRSSNNDIRLNDHSVSRHHARI----VRQgdKCNLTDLGSTNGTFLNGIRV---GTHELKHGDRIQLG--ETIFR 91

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18399229   62 EILVVGRHpDCDILLTHPSISRFHLEIRSISSRQKLFVTDLSSVHGTWVRDLRIEPHGCVEVEEGDTIRIGGSTRIY 138
Cdd:cd22724   21 EMIFVGRD-DCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIPEQTYITLKLDDKLRFGYDTNLF 96

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   37 VVNSRDFSSPERNGSTVSDDDGeveeilVVGRHPDCDILLTHPS--ISRFHLEIRSISSRqkLFVTDLSSvHGTWV--RD 112
Cdd:COG3456    7 IINSPDLESGSAASATFGRGGG------TIGRSADCDWVLPDPDrsVSRRHAEIRFRDGA--FCLTDLST-NGTFLngSD 77

                         90       100
                 ....*....|....*....|....*....
gi 18399229  113 LRIEPHGCVEVEEGDTIRIGGstriYRLH 141
Cdd:COG3456   78 HPLGPGRPVRLRDGDRLRIGD----YEIR 102

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 18399229   66 VGRHpDCDILLTHPSISRFHLEIRSISSRQKLFVTDLSSVHGTWVRDLRIEpHGCVEVEEGDTIRIGGSTRIYRL 140
Cdd:cd22700   20 IGRE-GCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRIQ-NAAVRLAPGDVLRFGFGGLPYEL 92

second 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 second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18399229   66 VGRHPDCDILLTHPSISRFHLEIRSISSRQKLfvTDLSSVHGTWVRDLRIEPhgcVEVEEGDTIRIG 132
Cdd:cd22737   25 IGRASDNDIVIPEGSVSRHHATLVPTPGGTQI--RDLRSTNGTFVNGLRVDA---ALLHDGDVVTIG 86

forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Chlamydia trachomatis Ct664 protein. Ct664 situates within the type III secretion system cluster that also encodes an STPK (CT673 in C. trachomatis), suggesting a role of CT664 in the chlamydial type III secretion system by mediating phosphorylation-dependent protein-protein interactions. The FHA domain is a small phosphopeptide recognition module.

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                 ....*....|....*....|....*....|....*....|....*....|...
gi 18399229   65 VVGRHPD-CDILLTHPSISRFHLEIrSISSRQKLFVTDLSSVHGTWVRDLRIE 116
Cdd:cd22696   24 FIGKDPTvCDIVLQDPSISRQHARL-SIDQDNRVFIEDLSSKNGVLVNGKPIE 75

forkhead associated (FHA) domain found in Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins; DDL, also called protein DAWDLE, is involved in 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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18399229   73 DILLTHPSISRFHLEIR-----------SISSRQKLFVTDLSSVHGTWVRDLRIEPHGCVEVEEGDTIRIGGSTRIYRL 140
Cdd:cd22719   49 DIPTDHPSCSKQHAVIQyrltekeggdgMMGKAVRPYIMDLGSTNGTFLNGERIEPQRYYELLEKDTIKFGNSSREYVL 127

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399229   59 EVEEILVVGRHPDCDIllTHPSISRFHLEIRSISSRQKLFVTDL----SSVHGTWVRDLRIEPHGCVEVEEGDTIRIGGS 134
Cdd:cd22671   16 KEGGPTVLGRGPLLGI--RDKRVSRKQAEITVDDDTGSVTVTQLgtnpSFVNRADGEGKVLKKGESVELKDGDVISLLPG 93

                 ....*..
gi 18399229  135 TRIYRLH 141
Cdd:cd22671   94 KYPFRVE 100