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 2061546720 112 PYSLETLKGGTILGTRSLKGTSYCLFGRLSGCDVCLEHPSVSRYHAVLQHRASGPDGEcdsngPGFYLYDLGSTHGTFLN 191
Cdd:cd22677     1 PYSLEVLKNGVIVETLDLNGKSFYVFGRLPGCDVVLEHPSISRYHAVLQYRGDADDHD-----GGFYLYDLGSTHGTFLN 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2061546720 192 KTRIPPRTYCRVHVGHVVRFGGSTRLFILQG 222
Cdd:cd22677    76 KQRIPPKQYYRLRVGHVLKFGGSTRLYILQG 106

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2061546720    9 ETLASQDlSGDfkkPALPVSPAARSKAPASSSSNPEEVQKEGPTALQdSNSGEPDIPP-------PQPDCGDFRSLQEEQ 81
Cdd:PHA03247  2541 EELASDD-AGD---PPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVT-SRARRPDAPPqsarpraPVDDRGDPRGPAPPS 2615

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2061546720   82 SRPP-TAVSSPGGPARAPPYQEPPWGGPATAP 112
Cdd:PHA03247  2616 PLPPdTHAPDPPPPSPSPAANEPDPHPPPTVP 2647

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 2061546720 112 PYSLETLKGGTILGTRSLKGTSYCLFGRLSGCDVCLEHPSVSRYHAVLQHRASGPDGEcdsngPGFYLYDLGSTHGTFLN 191
Cdd:cd22677     1 PYSLEVLKNGVIVETLDLNGKSFYVFGRLPGCDVVLEHPSISRYHAVLQYRGDADDHD-----GGFYLYDLGSTHGTFLN 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2061546720 192 KTRIPPRTYCRVHVGHVVRFGGSTRLFILQG 222
Cdd:cd22677    76 KQRIPPKQYYRLRVGHVLKFGGSTRLYILQG 106

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2061546720 112 PYSLETLKGGTILGTRSLKGTSYcLFGRLSGCDVCLEHPSVSRYHAVLQHRasgpdgecdsnGPGFYLYDLGSTHGTFLN 191
Cdd:COG1716     1 MARLVVLEGPLAGRRFPLDGGPL-TIGRAPDNDIVLDDPTVSRRHARIRRD-----------GGGWVLEDLGSTNGTFVN 68

                          90       100       110
                  ....*....|....*....|....*....|
gi 2061546720 192 KTRIppRTYCRVHVGHVVRFGGSTRLFILQ 221
Cdd:COG1716    69 GQRV--TEPAPLRDGDVIRLGKTELRFRLS 96

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2061546720  137 FGRLS-GCDVCLEHPSVSRYHAVLQHRasgpdgecdsNGPGFYLYDLGSTHGTFLNKTRI 195
Cdd:smart00240   3 IGRSSeDCDIQLDGPSISRRHAVIVYD----------GGGRFYLIDLGSTNGTFVNGKRI 52

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2061546720 316 PKKALQGFFDREGEELEYEF-DEQGHS---TWLCRVRLpvddstGKQLVAEAIhSGKKKEAMIQCSLEACRIL 384
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEYvSEEGPPhspKFTVTVKV------DGKLYGSGT-GSSKKEAEQLAAEKALEKL 66

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 2061546720 112 PYSLETLKGGTILGTRSLKGTSYCLFGRLSGCDVCLEHPSVSRYHAVLQHRASGPDGEcdsngPGFYLYDLGSTHGTFLN 191
Cdd:cd22677     1 PYSLEVLKNGVIVETLDLNGKSFYVFGRLPGCDVVLEHPSISRYHAVLQYRGDADDHD-----GGFYLYDLGSTHGTFLN 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2061546720 192 KTRIPPRTYCRVHVGHVVRFGGSTRLFILQG 222
Cdd:cd22677    76 KQRIPPKQYYRLRVGHVLKFGGSTRLYILQG 106

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 2061546720 107 GPATAPYSLETLKGGTILGTRSLKGTSYCLFGRLS-GCDVCLEHPSVSRYHAVLQHRAsgpdgecdsNGPGFYLYDLGST 185
Cdd:cd22674     1 GKPPPGLHLDVVKDGKLIEKLMIDEKKYYLFGRNSdVCDFVLDHPSCSRVHAALVYHK---------HLNRVFLIDLGST 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2061546720 186 HGTFLNKTRIPPRTYCRVHVGHVVRFGGSTRLFILQG 222
Cdd:cd22674    72 HGTFVGGIRLEPHKPQQLPIDSTLRFGASTRRYILRE 108

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 2061546720 115 LETLKGGTILGTRSLKGTSYcLFGRLSGCDVCLEHPSVSRYHAVLQHrasgpdgecdsNGPGFYLYDLGSTHGTFLNKTR 194
Cdd:cd00060     2 LIVLDGDGGGREFPLTKGVV-TIGRSPDCDIVLDDPSVSRRHARIEV-----------DGGGVYLEDLGSTNGTFVNGKR 69

                          90       100
                  ....*....|....*....|.
gi 2061546720 195 IPPRTycRVHVGHVVRFGGST 215
Cdd:cd00060    70 ITPPV--PLQDGDVIRLGDTT 88

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2061546720 112 PYSLETLKGGTILGTRSLKGTSYcLFGRLSGCDVCLEHPSVSRYHAVLQHRasgpdgecdsnGPGFYLYDLGSTHGTFLN 191
Cdd:COG1716     1 MARLVVLEGPLAGRRFPLDGGPL-TIGRAPDNDIVLDDPTVSRRHARIRRD-----------GGGWVLEDLGSTNGTFVN 68

                          90       100       110
                  ....*....|....*....|....*....|
gi 2061546720 192 KTRIppRTYCRVHVGHVVRFGGSTRLFILQ 221
Cdd:COG1716    69 GQRV--TEPAPLRDGDVIRLGKTELRFRLS 96

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 2061546720 100 YQEPPWGGPATAPYSLETLKGGTILGTRSLKGTSYCLFGRLSG-CDVCLEHPSVSRYHAVLQHRA---SGPDGecdSNG- 174
Cdd:cd22718    23 YSEPPEARKPKKRWRLYPFKGDEALPVLYIHRQSAYLLGRDRKiADIPIDHPSCSKQHAVLQYRLveyTRPDG---TKGr 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2061546720 175 ---PgfYLYDLGSTHGTFLNKTRIPPRTYCRVHVGHVVRFGGSTRLFIL 220
Cdd:cd22718   100 rvrP--YIIDLESANGTFLNNKKIEPQRYYELKEKDVLKFGFSSREYVL 146

forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar proteins; TbPar42 is a nuclear protein that plays a key role in parasite cell proliferation. It exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, both connected by a linker. Its PPIase domain adopts a parvulin fold and reflects structural elements of Pin1-type proteins but is catalytically inactive. Its FHA domain may be involved in the binding of phosphorylated target proteins. The FHA domain is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2061546720 105 WGG-PATAPYsLETLKGGTILGTRSLKGTSYCLFGRLSGCDVCLEHPSVSRYHAVLQHRAsgpDGECdsngpgFYLYDLG 183
Cdd:cd22675     1 WAAlPAVACH-LQCLRDGVPLPPLGLDRFPFYLFGRSPVCDYVLEHPSISSVHAVLVFHG---EQKC------FVLMDLG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2061546720 184 STHGTFLNKTRIPPRTYCRVHVGHVVRFGGSTRLFILQ-GP 223
Cdd:cd22675    71 STNGVKLNGKRIEKGRPLPLPVGSVIQFGFSARKYKVRkGP 111

forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2061546720 133 SYCLFGRLSGCDVCLEHPSVSRYHAVLqhrasgpdgecDSNGPGFYLYDLGSTHGTFLNKTRIPPRTYCRVHVGHVVRFG 212
Cdd:cd22682    20 STIVIGRSVESQVQIDDDSVSRYHAKL-----------AVNPSAVSIIDLGSTNGTIVNGKKIPKLASCDLQNGDQIKIG 88

                  ....*.
gi 2061546720 213 GSTRLF 218
Cdd:cd22682    89 NTIFKF 94

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2061546720 138 GRLSGCDVCLEHPSVSRYHAVLqhrasgpdgECDSNgpGFYLYDLGSTHGTFLN-KTRIPPRTYCRVHVGHVVRFG 212
Cdd:cd22665    26 GRDPSCSVVLPDKSVSKQHACI---------EVDGG--THLIEDLGSTNGTRIGnKVRLKPNVRYELIDGDLLLFG 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2061546720 131 GTSYCLfGRLSGCDVCLEHPSVSRYHAVLQHRasgpdgecdsnGPGFYLYDLGSTHGTFLNKTRIP 196
Cdd:cd22694    15 GSSVRI-GRDPDADVRLDDPRVSRRHALLEFD-----------GDGWVYTDLGSRNGTYLNGRRVQ 68

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 2061546720 125 GTRSLKGTSYCLFGRlSGCDVCLEHPSVSRYHAVLQHRASGPDGEcdsngpgfyLYDLGSTHGTFLNKTRIPPRTYCRVH 204
Cdd:cd22724    13 GTRHRLPREMIFVGR-DDCELMLQSRSVDKQHAVINYDASTDEHK---------VKDLGSLNGTFVNDVRIPEQTYITLK 82

                          90
                  ....*....|....*....
gi 2061546720 205 VGHVVRFGGSTRLF-ILQG 222
Cdd:cd22724    83 LDDKLRFGYDTNLFtVVRG 101

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 2061546720 143 CDVCLEHPSVSRYHAVLQHrasgpDGECDSNgpgfYLYDLGSTHGTFLNKTRIPPRTYCRVHVGHVVRFGGSTRLFILQ 221
Cdd:cd22725    30 CELMLQSRSVDKQHAVINY-----DQDTDEH----WVKDLGSLNGTFVNDVRIPDQKYITLKLNDVIRFGYDSNMYVLE 99

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        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2061546720 135 CLFGRLSGCDVCLEHPSVSRYHAVLqhrasgpdgECDSNGPgFYLYDLGSTHGTFLNKTRIPPRT 199
Cdd:cd22673    23 CTFGRDLSCDIRIQLPGVSREHCRI---------EVDENGK-AYLENLSTTNPTLVNGKAIEKSA 77

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 2061546720 129 LKGTSYCLFGRLSG-------CDVCLEHPSVSRYHAVLQHRASgpDGECDSngpgfYLYDLGSTHGTFLNKTRIPPRTYC 201
Cdd:cd22681    36 LNSPSCYLIGREKGesteivvADIGIPEETCSKQHCVIQFRNV--KGILKP-----YIMDLDSSNGTCLNDNVIPSSRYV 108

                          90
                  ....*....|
gi 2061546720 202 RVHVGHVVRF 211
Cdd:cd22681   109 ELRSGDVITF 118

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2061546720 137 FGRLSGCDVCLEHPSVSRYHAVLqhrasgpdgECDSNGPgfYLYDLGSTHGTFLNKTRIpprTYCRVHVGHVVRFG 212
Cdd:cd22737    25 IGRASDNDIVIPEGSVSRHHATL---------VPTPGGT--QIRDLRSTNGTFVNGLRV---DAALLHDGDVVTIG 86

forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2061546720 117 TLKGGTIlgtrslkgtsyclfGRLSGC--DVCLEHPSVSRYHAVLqhrasgpdGECDSNGPgFYLYDLGSTHGTFLNKTR 194
Cdd:cd22686    24 TATGATI--------------GREKDHghTIRIPELGVSKFHAEI--------YYDDDEQS-YTIVDLGSQNGTYLNGVR 80

                          90       100
                  ....*....|....*....|....*...
gi 2061546720 195 IP-PRTYCRVHV---GHVVRFGGSTRLF 218
Cdd:cd22686    81 ISqPKEKSDPYPlthGDELKIGETTLLF 108

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2061546720    9 ETLASQDlSGDfkkPALPVSPAARSKAPASSSSNPEEVQKEGPTALQdSNSGEPDIPP-------PQPDCGDFRSLQEEQ 81
Cdd:PHA03247  2541 EELASDD-AGD---PPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVT-SRARRPDAPPqsarpraPVDDRGDPRGPAPPS 2615

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2061546720   82 SRPP-TAVSSPGGPARAPPYQEPPWGGPATAP 112
Cdd:PHA03247  2616 PLPPdTHAPDPPPPSPSPAANEPDPHPPPTVP 2647

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2061546720 145 VCLEHPSVSRYHAVLQHRASGPdgecdsngpgFYLYDLGSTHGTFLNKTRIPPRTYCRVHVGHVVRFG 212
Cdd:cd22663    36 VSTCPLMISRNHCVLKKNDEGQ----------WTIKDNKSLNGVWVNGERIEPLKPYPLNEGDLIQLG 93

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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2061546720 137 FGRLSGCDVCLEHPSVSRYHAVLqhRASGPDgecDSNGPGFYLYDLgSTHGTFLNKTRI 195
Cdd:cd22670    26 IGRSPSCDIVINDPFVSRTHCRI--YSVQFD---ESSAPLVYVEDL-SSNGTYLNGKLI 78

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2061546720 127 RSLKGTSYcLFGRLSGCDVCLEHPSVSRYHAVLQHRASgpdgecdsngpGFYLYDLGSTHGTFLNKTRI 195
Cdd:pfam16697  12 FPLEGGRY-RIGSDPDCDIVLSDKEVSRVHLKLEVDDE-----------GWRLDDLGSGNGTLVNGQRV 68

second double-stranded RNA binding motif of DEAH box protein 9 (DHX9) and similar proteins; DHX9 (EC 3.6.4.13; also known as ATP-dependent RNA helicase A, DExH-box helicase 9 (DDX9), Leukophysin (LKP), nuclear DNA helicase II (NDH II), NDH2, or RNA helicase A) is a multifunctional ATP-dependent nucleic acid helicase that unwinds DNA and RNA in a 3' to 5' direction and plays important roles in many processes, such as DNA replication, transcriptional activation, post-transcriptional RNA regulation, mRNA translation and RNA-mediated gene silencing. It contains two double-stranded RNA binding motifs (DSRMs) at the N-terminal region. This model corresponds to the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2061546720 317 KKALQGFFDREGEELEYEFDEQG---HSTWLCRVRLPVDdSTGKQLVAEAiHSGKKKEAMIQCSLEACRIL 384
Cdd:cd19855     5 KSRLNEFLQKNKIPAEYKYTSVGpdhNRSFIAELSIFVK-QLGKTIYARE-TGSNKKLASQSCALSLVRQL 73

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2061546720 316 PKKALQGFFDREGEELEYEF-DEQGHS---TWLCRVRLpvddstGKQLVAEAIhSGKKKEAMIQCSLEACRIL 384
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEYvSEEGPPhspKFTVTVKV------DGKLYGSGT-GSSKKEAEQLAAEKALEKL 66

DNA polymerase III subunits gamma and tau; Validated

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2061546720  23 PALPVSPAARSKAPASSSSNPEEVQKEGPTALQDSNSGEPDIP-PPQPDCGDFRSLQEEQSRPPTAVSSPGGPARAPPYQ 101
Cdd:PRK07764  698 PAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPlPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPS 777

                  ...
gi 2061546720 102 EPP 104
Cdd:PRK07764  778 PPS 780

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2061546720 135 CLFGRLSGCDVCleHPS---VSRYHAVLQHrasgpdgecDSNGpGFYLYDLgSTHGTFLNKTRI 195
Cdd:cd22672    23 FTIGRAKDCDLS--FPGnklVSGDHCKIIR---------DEKG-QVWLEDT-STNGTLVNKVKV 73

transferase, transferring glycosyl groups

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2061546720 423 LIEKKRLNRMKKAGKI-DEKpetfESLVAKLNDAERELSEISERLKASSQVLSESP-SQDSLDAFMSEMKSGSTLDGVSR 500
Cdd:PLN02939  146 LLNQARLQALEDLEKIlTEK----EALQGKINILEMRLSETDARIKLAAQEKIHVEiLEEQLEKLRNELLIRGATEGLCV 221

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2061546720 501 KKLHLRTFELRKEQQRLKGLIKIVKpAEIPELKKTE 536
Cdd:PLN02939  222 HSLSKELDVLKEENMLLKDDIQFLK-AELIEVAETE 256