forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938604  47 GKPPPGLHLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIR 126
Cdd:cd22674     1 GKPPPGLHLDVVKDGKLIEKLMIDEKKYYLFGRNSDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIR 80

                          90       100
                  ....*....|....*....|....*...
gi 1243938604 127 LEPHKPQQIPIDSTVSFGASTRAYTLRE 154
Cdd:cd22674    81 LEPHKPQQLPIDSTLRFGASTRRYILRE 108

forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938604  47 GKPPPGLHLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIR 126
Cdd:cd22674     1 GKPPPGLHLDVVKDGKLIEKLMIDEKKYYLFGRNSDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIR 80

                          90       100
                  ....*....|....*....|....*...
gi 1243938604 127 LEPHKPQQIPIDSTVSFGASTRAYTLRE 154
Cdd:cd22674    81 LEPHKPQQLPIDSTLRFGASTRRYILRE 108

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1243938604   75 YLFGRNPDLCDFTIDHQSCSRVHAALVYHKHlKRVFLIDLNSTHGTFLGHIRL 127
Cdd:smart00240   1 VTIGRSSEDCDIQLDGPSISRRHAVIVYDGG-GRFYLIDLGSTNGTFVNGKRI 52

forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938604  47 GKPPPGLHLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIR 126
Cdd:cd22674     1 GKPPPGLHLDVVKDGKLIEKLMIDEKKYYLFGRNSDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIR 80

                          90       100
                  ....*....|....*....|....*...
gi 1243938604 127 LEPHKPQQIPIDSTVSFGASTRAYTLRE 154
Cdd:cd22674    81 LEPHKPQQLPIDSTLRFGASTRRYILRE 108

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 1243938604  54 HLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLK----------RVFLIDLNSTHGTFLG 123
Cdd:cd22676     2 RLYVFKGGEQLETIDIHRQSAYLIGRDRRVADIPLDHPSCSKQHAVIQFREVEKrnegdvieniRPYIIDLGSTNGTFLN 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1243938604 124 HIRLEPHKPQQIPIDSTVSFGASTRAYTLR 153
Cdd:cd22676    82 GEKIEPRRYYELREKDVLKFGLSTREYVLL 111

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 1243938604  54 HLDVVKGDKLIEKLII-------DEKKYYLFGRNPDlCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIR 126
Cdd:cd22691     3 VLTVLKNGSVLKNIFLhgkfsksEEEDILVVGRHPD-CDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQR 81

                          90       100
                  ....*....|....*....|....*.
gi 1243938604 127 LEPHKPQQIPIDSTVSFGASTRAYTL 152
Cdd:cd22691    82 IEPGVPVELEEGDTVRLGASTRVYRL 107

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938604  46 AGKPPPGLHLDVVKGDKLI-EKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLK-----------RVFLID 113
Cdd:cd22719     9 ARKPSKRWRLYVFKDGEPLnEPLHIHRQSCYLFGRERKVADIPTDHPSCSKQHAVIQYRLTEKeggdgmmgkavRPYIMD 88

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1243938604 114 LNSTHGTFLGHIRLEPHKPQQIPIDSTVSFGASTRAYTL 152
Cdd:cd22719    89 LGSTNGTFLNGERIEPQRYYELLEKDTIKFGNSSREYVL 127

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1243938604  75 YLFGRNPDlCDFTIDHQSCSRVHAALVYHKHLkRVFLIDLNSTHGTFLGHIRLEPhKPQQIPIDSTVSF 143
Cdd:pfam00498   1 VTIGRSPD-CDIVLDDPSVSRRHAEIRYDGGG-RFYLEDLGSTNGTFVNGQRLGP-EPVRLKDGDVIRL 66

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938604  53 LHLDVVKGDKLIEKLIIDEKKYyLFGRNPDlCDFTIDHQSCSRVHAALVYHKHlkRVFLIDLNSTHGTFLGHIRLEphKP 132
Cdd:COG1716     2 ARLVVLEGPLAGRRFPLDGGPL-TIGRAPD-NDIVLDDPTVSRRHARIRRDGG--GWVLEDLGSTNGTFVNGQRVT--EP 75

                          90
                  ....*....|....*
gi 1243938604 133 QQIPIDSTVSFGAST 147
Cdd:COG1716    76 APLRDGDVIRLGKTE 90

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 1243938604  74 YYLFGRNPDLCDFTIDHQSC----SRVHAALvyhkHLKRV------FLIDLNSTHGTFLGHIRLEPHKPQQIPIDSTVSF 143
Cdd:cd22685    29 EYRIGRNPEVCDVFLCSSQHpnliSREHAEI----HAERDgngnwkVLIEDRSTNGTYVNDVRLQDGQRRELSDGDTITF 104

                          90
                  ....*....|....*..
gi 1243938604 144 GASTRAYTLREKPQTLP 160
Cdd:cd22685   105 GHKNGRRVKQWPYQKSS 121

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 1243938604  75 YLFGRNPdlCDFTIDH-QSCSRVHAALV---------YHKHLKRVFLIDLnSTHGTFLGHIRLEPHKPQQIPIDSTVSFG 144
Cdd:cd22667    22 YTVGRKD--CDIIIVDdSSISRKHATLTvlhpeanlsDPDTRPELTLKDL-SKYGTFVNGEKLKGGSEVTLKDGDVITFG 98

                  .
gi 1243938604 145 A 145
Cdd:cd22667    99 V 99

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243938604  84 CDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRLEPHKPQQIPIDSTVSFGASTRAYTLREKPQTLP 160
Cdd:cd22725    30 CELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYITLKLNDVIRFGYDSNMYVLERSQHKVP 106

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 1243938604  76 LFGRnpDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRLephkPQQIPID----STVSFGASTRAYT 151
Cdd:cd22704    20 FVGR--EDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRI----PEQTYITlklgDSIRFGYDTNVYR 93

                  ....*..
gi 1243938604 152 LREKPQT 158
Cdd:cd22704    94 FEQLSLT 100

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1243938604  72 KKYYLFGRNPDlCDFTIDHQSCSRVHAALVYHKHlKRVFLIDLNSTHGTFL 122
Cdd:cd22673    20 KKSCTFGRDLS-CDIRIQLPGVSREHCRIEVDEN-GKAYLENLSTTNPTLV 68

forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938604  53 LHLDVVKGDklIEKLIID----EKKYYLFGRNPDlCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRLE 128
Cdd:cd22678     1 LKLEVVAGP--CEGLRFDlqpgTRLPLTIGRIQR-GDIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESIS 77

                          90       100
                  ....*....|....*....|
gi 1243938604 129 P-HKPQQIPIDSTVSFGAST 147
Cdd:cd22678    78 PnGRPVVLSSGDVITLGSET 97