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 148222109 201 PNFELSGALLEDTNTFRGVVIKYSEPAEARIPKKRWRLYPFKNDEALPVMYVHRQSAYLMGRQRRIADIPIDHPSCSKQH 280
Cdd:cd22718    1 PNFGLSGALAEDTNTFRGVVIKYSEPPEARKPKKRWRLYPFKGDEALPVLYIHRQSAYLLGRDRKIADIPIDHPSCSKQH 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148222109 281 AVLQYRMVEFTRANGTSGRRVRPYIIDLGSGNGTYLNNQRIEPQRYYELKEKDVLKFGFSSREYVVLHE 349
Cdd:cd22718   81 AVLQYRLVEYTRPDGTKGRRVRPYIIDLESANGTFLNNKKIEPQRYYELKEKDVLKFGFSSREYVLLHE 149

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 148222109 201 PNFELSGALLEDTNTFRGVVIKYSEPAEARIPKKRWRLYPFKNDEALPVMYVHRQSAYLMGRQRRIADIPIDHPSCSKQH 280
Cdd:cd22718    1 PNFGLSGALAEDTNTFRGVVIKYSEPPEARKPKKRWRLYPFKGDEALPVLYIHRQSAYLLGRDRKIADIPIDHPSCSKQH 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148222109 281 AVLQYRMVEFTRANGTSGRRVRPYIIDLGSGNGTYLNNQRIEPQRYYELKEKDVLKFGFSSREYVVLHE 349
Cdd:cd22718   81 AVLQYRLVEYTRPDGTKGRRVRPYIIDLESANGTFLNNKKIEPQRYYELKEKDVLKFGFSSREYVLLHE 149

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148222109 254 RQSAYLMGRQRRiADIPIDHPSCSKQHAVLQYRmveftrangtsGRRVrpYIIDLGSGNGTYLNNQRIepQRYYELKEKD 333
Cdd:COG1716   19 DGGPLTIGRAPD-NDIVLDDPTVSRRHARIRRD-----------GGGW--VLEDLGSTNGTFVNGQRV--TEPAPLRDGD 82

                 ....*
gi 148222109 334 VLKFG 338
Cdd:COG1716   83 VIRLG 87

transcription termination factor Rho; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148222109   6 DKRRKRRAHSPVAVTIKQGRISPARQHRTRRTPSPRSSDGGSPHRHQGRRRSRSPSERKNKSSFKRSKSPKNKRHRSDSR 85
Cdd:PRK12678  79 RAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARA 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148222109  86 SPPPlevKIKQEKVEHSQRPHQEKPRKERGQEDHRRNRDRDQAEQDRYKHPRSRDKDRDRNREEQNLRAQREERQ 160
Cdd:PRK12678 159 DAAE---RTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRR 230

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 148222109 201 PNFELSGALLEDTNTFRGVVIKYSEPAEARIPKKRWRLYPFKNDEALPVMYVHRQSAYLMGRQRRIADIPIDHPSCSKQH 280
Cdd:cd22718    1 PNFGLSGALAEDTNTFRGVVIKYSEPPEARKPKKRWRLYPFKGDEALPVLYIHRQSAYLLGRDRKIADIPIDHPSCSKQH 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148222109 281 AVLQYRMVEFTRANGTSGRRVRPYIIDLGSGNGTYLNNQRIEPQRYYELKEKDVLKFGFSSREYVVLHE 349
Cdd:cd22718   81 AVLQYRLVEYTRPDGTKGRRVRPYIIDLESANGTFLNNKKIEPQRYYELKEKDVLKFGFSSREYVLLHE 149

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 148222109 221 IKYSEPAEARIPKKRWRLYPFKNDEAL-PVMYVHRQSAYLMGRQRRIADIPIDHPSCSKQHAVLQYRMVEFTRANGTSGR 299
Cdd:cd22719    1 LLFVEPPEARKPSKRWRLYVFKDGEPLnEPLHIHRQSCYLFGRERKVADIPTDHPSCSKQHAVIQYRLTEKEGGDGMMGK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 148222109 300 RVRPYIIDLGSGNGTYLNNQRIEPQRYYELKEKDVLKFGFSSREYVVLHE 349
Cdd:cd22719   81 AVRPYIMDLGSTNGTFLNGERIEPQRYYELLEKDTIKFGNSSREYVLLHE 130

forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148222109 221 IKYSEPAEARIPKKRWRLYPFKNDEALPV--MYVHRQSAYLMGR------QRRIADIPIDHPSCSKQHAVLQYRMVEFtr 292
Cdd:cd22681    3 DNYFDYTGPERDRTLYKLVIYRNNSKGPIeeYELNSPSCYLIGRekgestEIVVADIGIPEETCSKQHCVIQFRNVKG-- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148222109 293 angtsgrRVRPYIIDLGSGNGTYLNNQRIEPQRYYELKEKDVLKFGFSSREYVV 346
Cdd:cd22681   81 -------ILKPYIMDLDSSNGTCLNDNVIPSSRYVELRSGDVITFSKSNDYELV 127

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148222109  258 YLMGRQRRiADIPIDHPSCSKQHAVLQYRmveftrangtSGRRVrpYIIDLGSGNGTYLNNQRIEPQrYYELKEKDVLKF 337
Cdd:pfam00498   1 VTIGRSPD-CDIVLDDPSVSRRHAEIRYD----------GGGRF--YLEDLGSTNGTFVNGQRLGPE-PVRLKDGDVIRL 66

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 148222109 237 RLYPFKNDEALPVMYVHRQSaYLMGRQRRiADIPIDHPSCSKQHAVLQYRmveftrangtsGRRVrpYIIDLGSGNGTYL 316
Cdd:cd00060    1 RLIVLDGDGGGREFPLTKGV-VTIGRSPD-CDIVLDDPSVSRRHARIEVD-----------GGGV--YLEDLGSTNGTFV 65

                         90       100
                 ....*....|....*....|..
gi 148222109 317 NNQRIEPQryYELKEKDVLKFG 338
Cdd:cd00060   66 NGKRITPP--VPLQDGDVIRLG 85

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148222109 254 RQSAYLMGRQRRiADIPIDHPSCSKQHAVLQYRmveftrangtsGRRVrpYIIDLGSGNGTYLNNQRIepQRYYELKEKD 333
Cdd:COG1716   19 DGGPLTIGRAPD-NDIVLDDPTVSRRHARIRRD-----------GGGW--VLEDLGSTNGTFVNGQRV--TEPAPLRDGD 82

                 ....*
gi 148222109 334 VLKFG 338
Cdd:COG1716   83 VIRLG 87

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148222109   261 GRQRRIADIPIDHPSCSKQHAVLQYRmveftrangtSGRRVrpYIIDLGSGNGTYLNNQRI 321
Cdd:smart00240   4 GRSSEDCDIQLDGPSISRRHAVIVYD----------GGGRF--YLIDLGSTNGTFVNGKRI 52

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 148222109 252 VHR--QSAYLMGRQRriADIPIDHPSCSKQHAVLQYRMV--EFtrangtsgrrvrpYIIDLGSGNGTYLNNQRIEPQRYY 327
Cdd:cd22704   11 RHRlpRSMLFVGRED--CDLILQSRSVDKQHAVITYDQIdnEF-------------KIKDLGSLNGTFVNDSRIPEQTYI 75

                         90
                 ....*....|....*....
gi 148222109 328 ELKEKDVLKFGFSSREYVV 346
Cdd:cd22704   76 TLKLGDSIRFGYDTNVYRF 94

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 148222109 249 VMYVHRQSAYLMGRQRriadipidhpSCSKQHAVLQYRmveftraNGTSGRRVRpyiiDLGSGNGTYLNNQRIEPQRYYE 328
Cdd:cd22724   22 MIFVGRDDCELMLQSR----------SVDKQHAVINYD-------ASTDEHKVK----DLGSLNGTFVNDVRIPEQTYIT 80

                         90
                 ....*....|....*....
gi 148222109 329 LKEKDVLKFGFSSREYVVL 347
Cdd:cd22724   81 LKLDDKLRFGYDTNLFTVV 99

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 148222109 261 GRQRRiADIPIDHPSCSKQHAVLQYrmveftraNGTSGRRvrpYIIDLGSGNGTYLNNQRIEPQ-RYYELKEKDVLKFGF 339
Cdd:cd22678   28 GRIQR-GDIALKDDEVSGKHARIEW--------NSTGSKW---ELVDLGSLNGTLVNGESISPNgRPVVLSSGDVITLGS 95

                 ....*.
gi 148222109 340 SSREYV 345
Cdd:cd22678   96 ETKILV 101

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 148222109 236 WRLYPFKNDEALPVmYVHRQSAYLMGRQRRIADIPIDhPSCSKQHAVLQyrmVEFTRAN-GTSGRRVRPYIIDLgSGNGT 314
Cdd:cd22667    1 WWLLSEQDGAGTSY-YLLPGGEYTVGRKDCDIIIVDD-SSISRKHATLT---VLHPEANlSDPDTRPELTLKDL-SKYGT 74

                         90       100
                 ....*....|....*....|....
gi 148222109 315 YLNNQRIEPQRYYELKEKDVLKFG 338
Cdd:cd22667   75 FVNGEKLKGGSEVTLKDGDVITFG 98

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 148222109 267 ADIPIDHPSCSKQHAVLQYRMVEftraNGtsgrrvrpYII-DLGSGNGTYLNNQRIEpQRYYELKEKDVLKFGFSSREY 344
Cdd:cd22700   25 CDLVLQSPGVEEQHAVIEYSEQE----NC--------FVLqDLNTAQGTYVNDCRIQ-NAAVRLAPGDVLRFGFGGLPY 90

transcription termination factor Rho; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148222109   6 DKRRKRRAHSPVAVTIKQGRISPARQHRTRRTPSPRSSDGGSPHRHQGRRRSRSPSERKNKSSFKRSKSPKNKRHRSDSR 85
Cdd:PRK12678  79 RAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARA 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148222109  86 SPPPlevKIKQEKVEHSQRPHQEKPRKERGQEDHRRNRDRDQAEQDRYKHPRSRDKDRDRNREEQNLRAQREERQ 160
Cdd:PRK12678 159 DAAE---RTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRR 230

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 148222109 269 IPIDHPSCSKQHAVLQYRmveftrANGtsgrrvRPYIIDLGSGNGTYLNNQRIEPQRYYELKEKDVLKFG 338
Cdd:cd22663   36 VSTCPLMISRNHCVLKKN------DEG------QWTIKDNKSLNGVWVNGERIEPLKPYPLNEGDLIQLG 93

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148222109   95 KQEKVEHSQRPHQEKPRKERGQEDHRRNRDRDQAEQDRYKHPRSRDKDRDRNREEQNLRAQREERQFYNDRRRERRQRDD 174
Cdd:TIGR01642   9 REKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRRSRDRPRRRSRSVRSI 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 148222109  175 QAVEVQNEDVDNSTNEGNEGNSSK----EKPNFELSGALL 210
Cdd:TIGR01642  89 EQHRRRLRDRSPSNQWRKDDKKRSlwdiKPPGYELVTADQ 128

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 148222109 255 QSAYLMGRQRRIADIPIdhpsCSKQHAVLQYRMVEFTRANGTSGRRVRPYIIDLgSGNGTYLNNQRIEPQRYYELKEKDV 334
Cdd:cd22685   27 LCEYRIGRNPEVCDVFL----CSSQHPNLISREHAEIHAERDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRRELSDGDT 101

                         90       100
                 ....*....|....*....|.
gi 148222109 335 LKFGFSSREYVVLHETSDTSE 355
Cdd:cd22685  102 ITFGHKNGRRVKQWPYQKSSE 122

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148222109  257 AYLMGRQRRiADIPIDHPSCSKQHAVLQYRmveftrangtsGRRVRpyIIDLGSGNGTYLNNQRIEPQRyYELKEKDVLK 336
Cdd:pfam16697  18 RYRIGSDPD-CDIVLSDKEVSRVHLKLEVD-----------DEGWR--LDDLGSGNGTLVNGQRVTELG-IALRPGDRIE 82

                  ...
gi 148222109  337 FGF 339
Cdd:pfam16697  83 LGQ 85

forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148222109 260 MGRQRRIaDIPIDHPSCSKQHAVLQyrmVEFTRANgtsgrrvrpyIIDLGSGNGTYLNNQRIEpQRYYELKEKDVLKFG 338
Cdd:cd22683   25 IGRSRSC-DLVLSDPSISRFHAELR---LEQNGIN----------VIDNNSANGTFINGKRIK-GKTYILKNGDIIVFG 88

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148222109 261 GRQRRiADIPIDHPSCSKQHAvlqyrmvEFTRANGtsGRRVRpyiiDLGSGNGTYLNNQRIE 322
Cdd:cd22684   26 GRHPE-SDIFLDDVTVSRRHA-------EFRRAEG--GFVVR----DVGSLNGTYVNRERID 73

potassium uptake protein, Trk family; The proteins of the Trk family are derived from Gram-negative and Gram-positive bacteria, yeast and wheat. The proteins of E. coli K12 TrkH and TrkG as well as several yeast proteins have been functionally characterized.The E. coli TrkH and TrkG proteins are complexed to two peripheral membrane proteins, TrkA, an NAD-binding protein, and TrkE, an ATP-binding protein. This complex forms the potassium uptake system. This family is specific for the eukaryotic Trk system. [Transport and binding proteins, Cations and iron carrying compounds]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148222109   24 GRISPARQHRTRRTPSPRSSDGGSPHRHQGRRRSRSPSERKNKSSFKRSKSPKNKRHRSDSRSPPPlevkikqEKVEHSQ 103
Cdd:TIGR00934 168 GRVTVPHGSAKRRDFQDKLFSGEFVKRDEPDQNSPDVKSDTRADESISDLEFEKFAKRRGSRDVDP-------EDLYRSI 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148222109  104 RPHQEKPRKERGQEDHRRNRDRDQAEQDRYKHPRsRDKDRDRNREEQNLRAQREERQFYNDRRRERRQRDDQAVEVQNED 183
Cdd:TIGR00934 241 MMLQGIHERIREKSSANSRSDERSSESIQEQVER-RPSTSDIERNSQSLTRRYDDKSFDKAVRLRRSKTIDRAEACDLEE 319

                         170       180       190
                  ....*....|....*....|....*....|...
gi 148222109  184 VDNS-----TNEGNEGNSSKEKPNFELSGALLE 211
Cdd:TIGR00934 320 LDRAkdfekMTYDNWKAHHRKKKNFRPRGWNLK 352