fascin-like domain, beta-trefoil fold, found in FSHD region gene 1 protein (FRG1) and similar proteins; Protein FRG1 binds to mRNA in a sequence-independent manner. It may play a role in the 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. FRG1 contains 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183448195   9 DIVGIWWTVSNFGEISGTIAIEMDKGAYIHALDNGLFTLGAPHREvDEGPSPPEQFTAVKLSDSRIALKSGYGKYLGINS 88
Cdd:cd23338    1 LAHGGWWKVKEFEEITGNVAIEFGSGRYVKALDNGLFTLGAPHDE-GEGPDPEEIFTAIKVSDTKIALKSGYGKYLSVDS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183448195  89 DGLVVGRSDAIGPREQWEPVFQDGKMALLASNSCFIRCNEAGDIEAKNKTAGEEEMIKIRSC 150
Cdd:cd23338   80 DGKVVGRSDAIGPREQWEPVFQDGKMALLGANNCFLSVNEDGDIVATSKTAGENEMIKIRSN 141

fascin-like domain, beta-trefoil fold, found in FSHD region gene 1 protein (FRG1) and similar proteins; Protein FRG1 binds to mRNA in a sequence-independent manner. It may play a role in the 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. FRG1 contains 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183448195   9 DIVGIWWTVSNFGEISGTIAIEMDKGAYIHALDNGLFTLGAPHREvDEGPSPPEQFTAVKLSDSRIALKSGYGKYLGINS 88
Cdd:cd23338    1 LAHGGWWKVKEFEEITGNVAIEFGSGRYVKALDNGLFTLGAPHDE-GEGPDPEEIFTAIKVSDTKIALKSGYGKYLSVDS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183448195  89 DGLVVGRSDAIGPREQWEPVFQDGKMALLASNSCFIRCNEAGDIEAKNKTAGEEEMIKIRSC 150
Cdd:cd23338   80 DGKVVGRSDAIGPREQWEPVFQDGKMALLGANNCFLSVNEDGDIVATSKTAGENEMIKIRSN 141

fascin-like domain, beta-trefoil fold, found in FSHD region gene 1 protein (FRG1) and similar proteins; Protein FRG1 binds to mRNA in a sequence-independent manner. It may play a role in the 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. FRG1 contains 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183448195   9 DIVGIWWTVSNFGEISGTIAIEMDKGAYIHALDNGLFTLGAPHREvDEGPSPPEQFTAVKLSDSRIALKSGYGKYLGINS 88
Cdd:cd23338    1 LAHGGWWKVKEFEEITGNVAIEFGSGRYVKALDNGLFTLGAPHDE-GEGPDPEEIFTAIKVSDTKIALKSGYGKYLSVDS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183448195  89 DGLVVGRSDAIGPREQWEPVFQDGKMALLASNSCFIRCNEAGDIEAKNKTAGEEEMIKIRSC 150
Cdd:cd23338   80 DGKVVGRSDAIGPREQWEPVFQDGKMALLGANNCFLSVNEDGDIVATSKTAGENEMIKIRSN 141

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 183448195  25 GTIAIEMDKGAYIHALDNGLFTLGAphreVDEGPSPPEQFTAVKLSDSRIALKSGYGKYLGINS--DGLVVGRSDAIGPR 102
Cdd:cd00257    1 GTVALKSSNGKYLSAENGGGGPLVA----NRDAAGPWETFTLVDLGDGKVALKSSNGKYLSAENggGGTLVANRTAIGPW 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 183448195 103 EQWEPVFQ-DGKMALLASNSCFIRC--NEAGDIEAKNKTAGEEEMIKI 147
Cdd:cd00257   77 ETFTLVPLgNGKVALKSANGKYLSAdnGGGGTLIANATSIGAWEKFTI 124

fascin-like domain, beta-trefoil fold, found in fungal FRG1 and similar proteins; This group includes Schizosaccharomyces pombe protein FRG1 (SpFRG1), which may have a role in the processing of pre-rRNA or in the assembly of rRNA into ribosomal subunits. It is a component of the spliceosome and may be involved in pre-mRNA splicing. SpFRG1 contains 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183448195  64 FTAVKLSDS-RIALKSGYGKYLGINSDGLVVGRSDAIGPREQWEPVFQD--GKMALLASNSCFIRCNEAGD----IEAKN 136
Cdd:cd23339   67 WVATRVVGTgKVTLKSAHGKYLSCDKFGVVTATREARGPQEEWTPVPRPdgGGFALQSVYGKYLSVDEVAGgklvVRADA 146

                         90
                 ....*....|..
gi 183448195 137 KTAGEEEMIKIR 148
Cdd:cd23339  147 ETVGFCETWRVR 158

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183448195   73 RIALKSGYGKYLGINSDGLVVGRSDAIGPREQWEPVFQDGKMALLASNSCFIRCNEAGDIEAKNKTAGEEEM 144
Cdd:pfam06268  37 TVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALLRESNGRYLGGGPSGLLKANASTVGKDEL 108

fourth 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 in this family 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 fourth fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 183448195  75 ALKSGYGKYLGINSDGLVVGRSDAIGP-----REQwepvfqdGKMALLASNSCFIRCNEAGDIEAKNKTAGEEEMI 145
Cdd:cd23337   44 HLKGSNGKYWSVDSDGSVTADSAAPTPfilefRGQ-------SKLAIKAPNGKYLKGEQNGLFKATGTEVDKATLW 112

second 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 second fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183448195  71 DSRIALKSGYGKYLgiNSDG-LVvgrsDAIGPREQWEPVFQDGKMALLASNSCFIRCNEA-GDIEAKNKTAGEEE 143
Cdd:cd23335   43 DGRYALRTSDGRYL--RSDGsLV----DEPSDDTLFTLEFRSGGLAFKDSEGKYLTAVGGsGVLKTRKKTVGKDE 111

third fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, also called testis fascin, is a novel paralog of the actin-bundling protein fascin expressed specifically in the elongate spermatid head. Fascin-3 is 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183448195  42 NGLFTLGAPHREV--DEGPSPPEQFTAVKLSDSRIALKSGYGKYLGINSDGLVVGRSDAIGPREQ 104
Cdd:cd23354   52 NGRYLAQRGHRSViaDGKGTESETFFRVEWRCGKIILQASNGRYLGVKPNGLLTASALLPGPNEE 116