FRG1-like domain; The human FRG1 gene maps to human chromosome 4q35 and has been identified as a candidate for facioscapulohumeral muscular dystrophy. Currently, the function of FRG1 is unknown.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955559    65 NSYIHALDTGLFTVGSPHKEDEGPDPPEQFTAIKLSDSRIALKSGYGKYLGINSEGVVVGRSDAIGSREQWEPVFQNGKM 144
Cdd:pfam06229   1 ASYLEAMDNGLFTTGEPHDVGEGPDPEEVFTAVKVSDEKIALKSGYGKYLGVNKDGILSARADAIGPREQFEPVFQEGKM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955559   145 ALLAANSCFISYSESGDIVAKNKTAGEEEMIKIRSCTEREVKRKDDIADEDRGDVKNCELNYVKKFQSFQDRKLRLNEED 224
Cdd:pfam06229  81 ALLAANGCFLSVDPSGDIVAKSKTAGEGEMVEIRSDAEREFKTTDRIPMEDRFDPRICESNYVKKFQKFQDKKLRLSDED 160

                         170       180
                  ....*....|....*....|....*....
gi 62955559   225 SGSLKKARTDGKFHEALLDRRSKMKADRY 253
Cdd:pfam06229 161 VKRLKKARKEGNFHETLLDRRVKMKHDRY 189

FRG1-like domain; The human FRG1 gene maps to human chromosome 4q35 and has been identified as a candidate for facioscapulohumeral muscular dystrophy. Currently, the function of FRG1 is unknown.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955559    65 NSYIHALDTGLFTVGSPHKEDEGPDPPEQFTAIKLSDSRIALKSGYGKYLGINSEGVVVGRSDAIGSREQWEPVFQNGKM 144
Cdd:pfam06229   1 ASYLEAMDNGLFTTGEPHDVGEGPDPEEVFTAVKVSDEKIALKSGYGKYLGVNKDGILSARADAIGPREQFEPVFQEGKM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955559   145 ALLAANSCFISYSESGDIVAKNKTAGEEEMIKIRSCTEREVKRKDDIADEDRGDVKNCELNYVKKFQSFQDRKLRLNEED 224
Cdd:pfam06229  81 ALLAANGCFLSVDPSGDIVAKSKTAGEGEMVEIRSDAEREFKTTDRIPMEDRFDPRICESNYVKKFQKFQDKKLRLSDED 160

                         170       180
                  ....*....|....*....|....*....
gi 62955559   225 SGSLKKARTDGKFHEALLDRRSKMKADRY 253
Cdd:pfam06229 161 VKRLKKARKEGNFHETLLDRRVKMKHDRY 189

FRG1-like domain; The human FRG1 gene maps to human chromosome 4q35 and has been identified as a candidate for facioscapulohumeral muscular dystrophy. Currently, the function of FRG1 is unknown.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955559    65 NSYIHALDTGLFTVGSPHKEDEGPDPPEQFTAIKLSDSRIALKSGYGKYLGINSEGVVVGRSDAIGSREQWEPVFQNGKM 144
Cdd:pfam06229   1 ASYLEAMDNGLFTTGEPHDVGEGPDPEEVFTAVKVSDEKIALKSGYGKYLGVNKDGILSARADAIGPREQFEPVFQEGKM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955559   145 ALLAANSCFISYSESGDIVAKNKTAGEEEMIKIRSCTEREVKRKDDIADEDRGDVKNCELNYVKKFQSFQDRKLRLNEED 224
Cdd:pfam06229  81 ALLAANGCFLSVDPSGDIVAKSKTAGEGEMVEIRSDAEREFKTTDRIPMEDRFDPRICESNYVKKFQKFQDKKLRLSDED 160

                         170       180
                  ....*....|....*....|....*....
gi 62955559   225 SGSLKKARTDGKFHEALLDRRSKMKADRY 253
Cdd:pfam06229 161 VKRLKKARKEGNFHETLLDRRVKMKHDRY 189

fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family includes actin-bundling/crosslinking proteins facsin1-4, singed, hisactophilin, and FSHD region gene 1 protein (FRG1). Fascin, also called fascin-1, is an actin-binding protein that contains 2 major actin binding sites. It is involved in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. It plays an important role for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. It mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to nerve growth factor (NGF). Fascin-2, also called retinal fascin, is a photoreceptor-specific paralog of the actin-bundling protein fascin. It may play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Fascin-3, also called testis fascin, is a novel paralog of the actin-bundling protein fascin expressed specifically in the elongate spermatid head. Protein singed acts as an actin-bundling protein that may have a role in the asymmetric organization and/or movement of cytoplasmic components. It has a role in somatic cells during the formation of adult bristles and hairs, and in the female germline during oogenesis. Hisactophilin is a histidine-rich actin-binding protein from Dictyostelium discoideum. It exists in two isoforms, hisactophilin-1 (HatA, also called HS I) and hisactophilin-2 (HatB, also called HS II), which are both myristoylated and distributed between plasma membrane and cytoplasm. Hisactophilin may act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments. Protein FRG1 binds to mRNA in a sequence-independent manner. It may play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. It may be involved in mRNA transport, as well as in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase KMT5B. This family also contains many homologs from bacteria, such as Zobellia galactanivorans beta-porphyranase A (PorA). PorA (EC 3.2.1.178) cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. It is inactive on the non-sulfated agarose portion of the porphyran backbone and displays a strict requirement for C6-sulfate in the -2 and +1-binding subsites. Members of this family contain a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The fascin subfamily contains four copies of the fascin-like domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955559  56 GTVAIEMHKNSYIHALDTGLFTVGSphkEDEGPDPPEQFTAIKLSDSRIALKSGYGKYLGINSE--GVVVGRSDAIGSRE 133
Cdd:cd00257   1 GTVALKSSNGKYLSAENGGGGPLVA---NRDAAGPWETFTLVDLGDGKVALKSSNGKYLSAENGggGTLVANRTAIGPWE 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 62955559 134 QWEPVFQ-NGKMALLAANSCFISYSESGD--IVAKNKTAGEEEMIKI 177
Cdd:cd00257  78 TFTLVPLgNGKVALKSANGKYLSADNGGGgtLIANATSIGAWEKFTI 124

fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family includes actin-bundling/crosslinking proteins facsin1-4, singed, hisactophilin, and FSHD region gene 1 protein (FRG1). Fascin, also called fascin-1, is an actin-binding protein that contains 2 major actin binding sites. It is involved in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. It plays an important role for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. It mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to nerve growth factor (NGF). Fascin-2, also called retinal fascin, is a photoreceptor-specific paralog of the actin-bundling protein fascin. It may play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Fascin-3, also called testis fascin, is a novel paralog of the actin-bundling protein fascin expressed specifically in the elongate spermatid head. Protein singed acts as an actin-bundling protein that may have a role in the asymmetric organization and/or movement of cytoplasmic components. It has a role in somatic cells during the formation of adult bristles and hairs, and in the female germline during oogenesis. Hisactophilin is a histidine-rich actin-binding protein from Dictyostelium discoideum. It exists in two isoforms, hisactophilin-1 (HatA, also called HS I) and hisactophilin-2 (HatB, also called HS II), which are both myristoylated and distributed between plasma membrane and cytoplasm. Hisactophilin may act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments. Protein FRG1 binds to mRNA in a sequence-independent manner. It may play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. It may be involved in mRNA transport, as well as in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase KMT5B. This family also contains many homologs from bacteria, such as Zobellia galactanivorans beta-porphyranase A (PorA). PorA (EC 3.2.1.178) cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. It is inactive on the non-sulfated agarose portion of the porphyran backbone and displays a strict requirement for C6-sulfate in the -2 and +1-binding subsites. Members of this family contain a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The fascin subfamily contains four copies of the fascin-like domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955559  40 DIVGGW--WTVKCFGEvtGTVAIEMHKNSYIHALDTGLFTVgspHKEDEGPDPPEQFTAIKLSDSRIALKSGYGKYLGIN 117
Cdd:cd00257  28 DAAGPWetFTLVDLGD--GKVALKSSNGKYLSAENGGGGTL---VANRTAIGPWETFTLVPLGNGKVALKSANGKYLSAD 102

                        90       100
                ....*....|....*....|.
gi 62955559 118 S--EGVVVGRSDAIGSREQWE 136
Cdd:cd00257 103 NggGGTLIANATSIGAWEKFT 123

third fascin-like domain, beta-trefoil fold, found in the fascin subfamily; The fascin subfamily includes fascin1-3 and Drosophila melanogaster protein singed. Fascin, also called fascin-1, 55 kDa actin-bundling protein, singed-like protein, or p55, is an actin-binding protein that contains 2 major actin binding sites. It is involved in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. It plays an important role for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. It mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to nerve growth factor (NGF). Fascin-2, also called retinal fascin, is a photoreceptor-specific paralog of the actin-bundling protein fascin. It may play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Fascin-3, also called testis fascin, is a novel paralog of the actin-bundling protein fascin expressed specifically in the elongate spermatid head. Protein singed acts as an actin-bundling protein that may have a role in the asymmetric organization and/or movement of cytoplasmic components. It has a role in somatic cells during the formation of adult bristles and hairs, and in the female germline during oogenesis. Members of this subfamily are composed of four fascin beta-trefoil domains, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the third fascin-like beta-trefoil domain.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62955559 103 RIALKSGYGKYLGINSEGVVVGRSDAIGSREQWEPVFQ-NGKMALLAANSCFISYSESGDIVAKNKTAGEEEMIKIR 178
Cdd:cd23336  45 KWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELEWNdGGTVALKASNGKYVTAKPNGQLAATSDEVGEKEKFTLK 121

Fascin domain; This family consists of several eukaryotic fascin or singed proteins. The fascins are a structurally unique and evolutionarily conserved group of actin cross-linking proteins. Fascins function in the organization of two major forms of actin-based structures: dynamic, cortical cell protrusions and cytoplasmic microfilament bundles. The cortical structures, which include filopodia, spikes, lamellipodial ribs, oocyte microvilli and the dendrites of dendritic cells, have roles in cell-matrix adhesion, cell interactions and cell migration, whereas the cytoplasmic actin bundles appear to participate in cell architecture. Dictyostelium hisactophilin, another actin-binding protein, is a submembranous pH sensor that signals slight changes of the H+ concentration to actin by inducing actin polymerization and binding to microfilaments only at pH values below seven. Members of this family are histidine rich, typically contain the repeated motif of HHXH.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955559    46 WTVKCFGEvTGTVAIEMHKNSYIHALDTGLFTVGSphkedEGPDPPEQFTaIKLSDSRIALKSGYGKYLGINSEGVVVGR 125
Cdd:pfam06268  27 FTLEFDDE-RYTVYLRSHNGKYLSCDADGRVVCEA-----ERRSADTFFE-LEFRGRWALLRESNGRYLGGGPSGLLKAN 99

                          90
                  ....*....|..
gi 62955559   126 SDAIGSREQWEP 137
Cdd:pfam06268 100 ASTVGKDELWTL 111