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 33356172   2 WKLLPAAGPAGgEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEE 81
Cdd:cd22667   1 WWLLSEQDGAG-TSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGE 79

                        90       100
                ....*....|....*....|....*....
gi 33356172  82 KMQNGFSRTLKSGDGITFGVFGSKFRIEY 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 33356172   683 KNFKKFKKVTYPGAGKLPHIIGGSDLIAHHARKNTELEEWLRQEMEVQNQHAKEESLADDLF 744
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 33356172   2 WKLLPAAGPAGgEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEE 81
Cdd:cd22667   1 WWLLSEQDGAG-TSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGE 79

                        90       100
                ....*....|....*....|....*....
gi 33356172  82 KMQNGFSRTLKSGDGITFGVFGSKFRIEY 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 33356172   683 KNFKKFKKVTYPGAGKLPHIIGGSDLIAHHARKNTELEEWLRQEMEVQNQHAKEESLADDLF 744
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 33356172   1 MWKLLPAAGPAGGEPYRLlTGVEYVVGR-KNCAILIeNDQSISRNHAVLTA---NFSVTNLsqtdeipvltlkdNSKYGT 76
Cdd:COG1716   1 MARLVVLEGPLAGRRFPL-DGGPLTIGRaPDNDIVL-DDPTVSRRHARIRRdggGWVLEDL-------------GSTNGT 65

                        90       100       110
                ....*....|....*....|....*....|....*
gi 33356172  77 FVNEEKMQNgfSRTLKSGDGITFGvfGSKFRIEYE 111
Cdd:COG1716  66 FVNGQRVTE--PAPLRDGDVIRLG--KTELRFRLS 96

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33356172     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 33356172   2 WKLLPAAGPAGgEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEE 81
Cdd:cd22667   1 WWLLSEQDGAG-TSYYLLPGGEYTVGRKDCDIIIVDDSSISRKHATLTVLHPEANLSDPDTRPELTLKDLSKYGTFVNGE 79

                        90       100
                ....*....|....*....|....*....
gi 33356172  82 KMQNGFSRTLKSGDGITFGVFGSKFRIEY 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 33356172   683 KNFKKFKKVTYPGAGKLPHIIGGSDLIAHHARKNTELEEWLRQEMEVQNQHAKEESLADDLF 744
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 33356172   1 MWKLLPAAGPAGGEPYRLlTGVEYVVGR-KNCAILIeNDQSISRNHAVLTA---NFSVTNLsqtdeipvltlkdNSKYGT 76
Cdd:COG1716   1 MARLVVLEGPLAGRRFPL-DGGPLTIGRaPDNDIVL-DDPTVSRRHARIRRdggGWVLEDL-------------GSTNGT 65

                        90       100       110
                ....*....|....*....|....*....|....*
gi 33356172  77 FVNEEKMQNgfSRTLKSGDGITFGvfGSKFRIEYE 111
Cdd:COG1716  66 FVNGQRVTE--PAPLRDGDVIRLG--KTELRFRLS 96

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 33356172   3 KLLPAAGPAGGEPYRLlTGVEYVVGR-KNCAILIeNDQSISRNHAVLTAN---FSVTNLSqtdeipvltlkdnSKYGTFV 78
Cdd:cd00060   1 RLIVLDGDGGGREFPL-TKGVVTIGRsPDCDIVL-DDPSVSRRHARIEVDgggVYLEDLG-------------STNGTFV 65

                        90       100       110
                ....*....|....*....|....*....|.
gi 33356172  79 NEEKMQNgfSRTLKSGDGITFGvfGSKFRIE 109
Cdd:cd00060  66 NGKRITP--PVPLQDGDVIRLG--DTTFRFE 92

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33356172    24 YVVGR-KNCAILIeNDQSISRNHAVLTANFSvtnlsqtdeiPVLTLKD-NSKYGTFVNEEKMQNgFSRTLKSGDGITF 99
Cdd:pfam00498   1 VTIGRsPDCDIVL-DDPSVSRRHAEIRYDGG----------GRFYLEDlGSTNGTFVNGQRLGP-EPVRLKDGDVIRL 66

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 33356172  14 EPYRLLTGVEYVVGRK-NCAILIeNDQSISRNHAVLtanFSVtnlsQTDE--IPVLTLKDNSKYGTFVNEEKMQNGFSRT 90
Cdd:cd22670  14 IVLPIYKNQVITIGRSpSCDIVI-NDPFVSRTHCRI---YSV----QFDEssAPLVYVEDLSSNGTYLNGKLIGRNNTVL 85

                        90       100
                ....*....|....*....|..
gi 33356172  91 LKSGDGITfgvFGSKFRIEYEP 112
Cdd:cd22670  86 LSDGDVIE---IAHSATFVYVH 104

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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33356172  26 VGRKNCAILIENdQSISRNHAVLtanfsvtNLSQTDEIPVLtlKD-NSKYGTFVNEEKMQNGFSRtLKSGDGITFGVFGS 104
Cdd:cd22700  20 IGREGCDLVLQS-PGVEEQHAVI-------EYSEQENCFVL--QDlNTAQGTYVNDCRIQNAAVR-LAPGDVLRFGFGGL 88

                ....*..
gi 33356172 105 KFRIEYE 111
Cdd:cd22700  89 PYELVVD 95

seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the seventh BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33356172 118 SCLDVSGKTALNQAILQLGGFTVN--NWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKA 183
Cdd:cd17738   7 SGFSEDEKKELISIIEKLGGKVLDsdEFDPKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKA 74

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 33356172 113 LVACSSCLDVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKV-----TIKTICALICGRPIVKPEYFTEFLKA 183
Cdd:cd17734   1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADERgvcprTMKYLMGILAGKWIVSFEWVEACLKA 76

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 33356172  24 YVVGR--KNCAILIENdQSISRNHAVLtaNF-SVTNLSQTDEIPVLT--LKD-NSKYGTFVNEEKMQNGFSRTLKSGDGI 97
Cdd:cd22676  23 YLIGRdrRVADIPLDH-PSCSKQHAVI--QFrEVEKRNEGDVIENIRpyIIDlGSTNGTFLNGEKIEPRRYYELREKDVL 99

                ...
gi 33356172  98 TFG 100
Cdd:cd22676 100 KFG 102

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 33356172  14 EPYRLLTGVEYVVGR-KNCAILIENdQSISRNHAVLtaNFSVTNLSQTDEIPVLTLkdNSKYGTFVNEEKMQNGFSRTLK 92
Cdd:cd22677  14 ETLDLNGKSFYVFGRlPGCDVVLEH-PSISRYHAVL--QYRGDADDHDGGFYLYDL--GSTHGTFLNKQRIPPKQYYRLR 88

                ....*...
gi 33356172  93 SGDGITFG 100
Cdd:cd22677  89 VGHVLKFG 96

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 33356172  11 AGGEPYRLLTGVEYVvGRKNCAILIENdQSISRNHAVLtaNFSvtnlSQTDEIPVLTLkdNSKYGTFVNEEKMQNGFSRT 90
Cdd:cd22724  11 SGGTRHRLPREMIFV-GRDDCELMLQS-RSVDKQHAVI--NYD----ASTDEHKVKDL--GSLNGTFVNDVRIPEQTYIT 80

                        90
                ....*....|
gi 33356172  91 LKSGDGITFG 100
Cdd:cd22724  81 LKLDDKLRFG 90

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 33356172  12 GGEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTanfsvtnlSQTDEipvLTLKD-NSKYGTFVNEEKMQngfSRT 90
Cdd:cd22694   6 PGGELRFDPGSSVRIGRDPDADVRLDDPRVSRRHALLE--------FDGDG---WVYTDlGSRNGTYLNGRRVQ---QVK 71

                        90
                ....*....|
gi 33356172  91 LKSGDGITFG 100
Cdd:cd22694  72 LSDGTRVRLG 81

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 33356172   2 WKLLPAAGPAGGEPYRLLtGVEYVVGR-KNCAILIENDQSISRNHAVLtanfsvtnlsQTDEIPVLTLKDNSKYGTFVNE 80
Cdd:cd22672   2 WGQLVRLTEESSPPILLR-KDEFTIGRaKDCDLSFPGNKLVSGDHCKI----------IRDEKGQVWLEDTSTNGTLVNK 70

                        90
                ....*....|....*....
gi 33356172  81 EKMQNGFSRTLKSGDGITF 99
Cdd:cd22672  71 VKVVKGQKVELKHGDVIYL 89

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33356172  41 ISRNHAVLTAnfsvTNLSqtdeipvLTLKD-NSKYGTFVNEEKMQNGFS----RTLKSGDGITFGV 101
Cdd:cd22679  49 LSRNHALLWY----DDGK-------FYLQDtKSSNGTFVNNQRLSKGSEesepRELHSGDIVQFGV 103