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 568973828 138 HPQAHLLSVSRRRYVHLCLQEDEMAADGDMPWGVDALVTLIFQSRRYCLKSYDSRYLRSDGRLVWEPEAHACYTLEFKAG 217
Cdd:cd23349    1 HPQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKAG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568973828 218 KLAFKDCDGRYLAPVGPAGTLKAGRNTRPSKDELFDLEQ 256
Cdd:cd23349   81 KLAFKDCDGKYLTPMGPTGTLKSGRSSKPGKDELFDLEE 119

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 568973828 408 RPLLVLRGLDGFVCHRRGSNQLDTNRSTYDVFHLSFRDGAYQIRGRGGGFWYTGSHGSVCSDGDLAEDFLFEFRERGRLA 487
Cdd:cd23357    1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRVA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568973828 488 IRALSGKYLRGGASGLLRADADLPVGEALWEY 519
Cdd:cd23357   81 IKGKNGKYLRGDQAGTLKADAETVDSATLWEY 112

second fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; 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-2 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 second fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973828 138 HPQAHLLSVSRRRYVHLCLQEDEMAADGDMPWGVDALVTLIFQSRRYCLKSYDSRYLRSDGRLVWEPEAHACYTLEFKAG 217
Cdd:cd23349    1 HPQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKAG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568973828 218 KLAFKDCDGRYLAPVGPAGTLKAGRNTRPSKDELFDLEQ 256
Cdd:cd23349   81 KLAFKDCDGKYLTPMGPTGTLKSGRSSKPGKDELFDLEE 119

fourth fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; 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-2 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 fourth fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973828 408 RPLLVLRGLDGFVCHRRGSNQLDTNRSTYDVFHLSFRDGAYQIRGRGGGFWYTGSHGSVCSDGDLAEDFLFEFRERGRLA 487
Cdd:cd23357    1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRVA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568973828 488 IRALSGKYLRGGASGLLRADADLPVGEALWEY 519
Cdd:cd23357   81 IKGKNGKYLRGDQAGTLKADAETVDSATLWEY 112

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 568973828  266 ANRRYISVRQGINVSANQDEELGHETFLMQIDQETKKCTFYSSTGGYWTLVTHGGIQATATQVSANTMFEIEWHGRRVAL 345
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALL 80

                          90       100
                  ....*....|....*....|....*...
gi 568973828  346 KASNGRFVCMKKNGQLAAISDFVGEHSL 373
Cdd:pfam06268  81 RESNGRYLGGGPSGLLKANASTVGKDEL 108

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 568973828  141 AHLLSVSRRRYVHLCL-QEDEMAADgdmpwgvdaLVTLIFQSRRYC--LKSYDSRYLR--SDGRLVWEPE---AHACYTL 212
Cdd:pfam06268   1 ANGYLVSERRGAHLNAnRESLKRVQ---------TFTLEFDDERYTvyLRSHNGKYLScdADGRVVCEAErrsADTFFEL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568973828  213 EFKAGKLAFKDCDGRYLApVGPAGTLKAgRNTRPSKDELFDL 254
Cdd:pfam06268  72 EFRGRWALLRESNGRYLG-GGPSGLLKA-NASTVGKDELWTL 111

second fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; 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-2 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 second fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973828 138 HPQAHLLSVSRRRYVHLCLQEDEMAADGDMPWGVDALVTLIFQSRRYCLKSYDSRYLRSDGRLVWEPEAHACYTLEFKAG 217
Cdd:cd23349    1 HPQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKAG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568973828 218 KLAFKDCDGRYLAPVGPAGTLKAGRNTRPSKDELFDLEQ 256
Cdd:cd23349   81 KLAFKDCDGKYLTPMGPTGTLKSGRSSKPGKDELFDLEE 119

first fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; 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 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 first fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973828  11 KIQFGLVNDADRYLTAESFGFKVNASAASLKRKQIWVLEP--DPGQGTAVLFRSsHLGRYLSAEEDGRVACEMDQPGRDC 88
Cdd:cd23344    1 QIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQpgDEADSSAVLLRS-HLGRYLAADKDGNVTCESEVPGPDC 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568973828  89 RFLVLPQPDGRWVLQSEPHGRFFGGIEDRLSCFATAISPAELWTVHLAI 137
Cdd:cd23344   80 RFLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAM 128

fourth fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; 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-2 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 fourth fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973828 408 RPLLVLRGLDGFVCHRRGSNQLDTNRSTYDVFHLSFRDGAYQIRGRGGGFWYTGSHGSVCSDGDLAEDFLFEFRERGRLA 487
Cdd:cd23357    1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRVA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568973828 488 IRALSGKYLRGGASGLLRADADLPVGEALWEY 519
Cdd:cd23357   81 IKGKNGKYLRGDQAGTLKADAETVDSATLWEY 112

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973828 258 HPQVVLVAANRRYISVRQGINVSANQDEELGHETFLMQIDQETKKCTFYSSTGGYWTLVTHGGIQATATQVSANTMFEIE 337
Cdd:cd23336    1 HPQVSLRAHNGKYVSIRQGVDVSANQDEETDTETFQLEFDKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973828 338 WH-GRRVALKASNGRFVCMKKNGQLAAISDFVgehslpstawkeqmgvgsgqstspspaGEDELFTLKLIN 407
Cdd:cd23336   81 WNdGGTVALKASNGKYVTAKPNGQLAATSDEV---------------------------GEKEKFTLKLIN 124

third fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; 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 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973828 259 PQVVLVAANRRYISVRQGINVSANQDEELGHETFLMQIDQETKKCTFYSSTGGYWTLVTHGGIQATATQVSANTMFEIEW 338
Cdd:cd23352    2 PQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIEW 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568973828 339 HGRRVALKASNGRFVCMKKNGQLAAisdfvgehslpstawkeqmgvgsgqstSPSPAGEDELFTLKLIN 407
Cdd:cd23352   82 RDRRITLRASNGKYVTSKKNGQLAA---------------------------SVETAGESELFLMKLIN 123

first fascin-like domain, beta-trefoil fold, found in Drosophila melanogaster protein singed and similar proteins; 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. It interacts with Rab35, with stronger binding to the Rab35-GTP form compared to the Rab35-GDP form. Protein singed 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 first fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973828  15 GLVNDADRYLTAESFGFKVNASAASLKRKQIWVLEPDPGQGTAVLFRsSHLGRYLSAEEDGRVACEMDQPGRDCRFLVLP 94
Cdd:cd23347    7 GLINSQQKYLTAETFGFKVNANGSSLKKKQLWTLEPFGDGTNVVALR-SHLGRYLSVDQFGNVTCEAEEKGEGSRFEIVI 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568973828  95 QPD--GRWVLQSEPHGRFFGGIEDRLSCFATAISPAELWTVHLA 136
Cdd:cd23347   86 SEDesGRWAFRNEERGYFLGGSGDKLVCTAKAPTDSELWTVHLA 129

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 568973828   20 ADRYLTAESFGFKVNASAASLKRKQIWVLEPDPGqGTAVLFRsSHLGRYLSAEEDGRVACEMDQPGRDCRFLVLPQpdGR 99
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDE-RYTVYLR-SHNGKYLSCDADGRVVCEAERRSADTFFELEFR--GR 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568973828  100 WVLQSEPHGRFFG-GIEDRLSCFATAISPAELWTV 133
Cdd:pfam06268  77 WALLRESNGRYLGgGPSGLLKANASTVGKDELWTL 111

fourth fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; 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 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 fourth fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973828 408 RPLLVLRGLDGFVCHRRGSNQLDTNRSTYDVFHLSFRDGAYQIRGRGGGFWYTGSHGSVCSDGDLAEDFLFEFRERGRLA 487
Cdd:cd23356    1 RPIIVLRGEHGFIGCRKVTGTLDSNRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568973828 488 IRaLSGKYLRGGASGLLRADADLPVGEALWEY 519
Cdd:cd23356   81 IK-VGGRYLKGDHAGVLKASAETVDPATLWEY 111

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 568973828  417 DGFVCHRRGSNQLDTNRST---YDVFHLSFRDGAY--QIRGRGGGFWYTGSHGSVCSDGD-LAEDFLFEFRERGRLAIRA 490
Cdd:pfam06268   2 NGYLVSERRGAHLNANRESlkrVQTFTLEFDDERYtvYLRSHNGKYLSCDADGRVVCEAErRSADTFFELEFRGRWALLR 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 568973828  491 LS-GKYLRGGASGLLRADADLPVGEALWEY 519
Cdd:pfam06268  82 ESnGRYLGGGPSGLLKANASTVGKDELWTL 111

fourth 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 fourth fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973828 408 RPLLVLRGLDGFVCHRRGSNQLDTNRSTYDVFHLS-FRDGAYQIRGRGGGFWYTGSHGSVCSDGDLAEDFLFEFRERGRL 486
Cdd:cd23358    1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLLpCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568973828 487 AIRALSGKYLRGGASGLLRADADLPVGEALWEY 519
Cdd:cd23358   81 AILAPNGCYLRGDNSGTLLADSEIITSECLWEF 113

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973828 259 PQVVLVAANRRYISVRQGINVSANQDEELGHETFLMQIDQETKKCTFYSSTGGYWTLVTHGGIQATATQVSANTMFEIEW 338
Cdd:cd23354    2 TWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVEW 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568973828 339 HGRRVALKASNGRFVCMKKNGQLAAISDFVG 369
Cdd:cd23354   82 RCGKIILQASNGRYLGVKPNGLLTASALLPG 112

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 568973828 260 QVVLVAANRRYISVRQGIN--VSANQDEELGHETFLMqIDQETKKCTFYSSTGGYWTLVTHGG--IQATATQVSANTMFE 335
Cdd:cd00257    2 TVALKSSNGKYLSAENGGGgpLVANRDAAGPWETFTL-VDLGDGKVALKSSNGKYLSAENGGGgtLVANRTAIGPWETFT 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568973828 336 IEWHG-RRVALKASNGRFVCMK--KNGQLAAISDFVGEH 371
Cdd:cd00257   81 LVPLGnGKVALKSANGKYLSADngGGGTLIANATSIGAW 119

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 568973828 182 RRYCLKSYDSRYLRSD----GRLVWEPEAHACY---TLEF-KAGKLAFKDCDGRYL-APVGPAGTLKAGRNTrPSKDELF 252
Cdd:cd00257    1 GTVALKSSNGKYLSAEngggGPLVANRDAAGPWetfTLVDlGDGKVALKSSNGKYLsAENGGGGTLVANRTA-IGPWETF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568973828 253 DLEQSHP-QVVLVAANRRYISVRQGIN--VSANQDEELGHETF 292
Cdd:cd00257   80 TLVPLGNgKVALKSANGKYLSADNGGGgtLIANATSIGAWEKF 122

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568973828 301 KKCTFYSSTGGYWTLVTHGG--IQATATQVSANTMFEIE-WHGRRVALKASNGRFVCM--KKNGQLAAISDFVGE 370
Cdd:cd00257    1 GTVALKSSNGKYLSAENGGGgpLVANRDAAGPWETFTLVdLGDGKVALKSSNGKYLSAenGGGGTLVANRTAIGP 75

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 568973828  44 QIWVLEPDPGQGTaVLFRSSHlGRYLSAEEDGRVACEMDQPGRDCRFLVLPQPD-GRWVLQSePHGRFFG-----GIEDR 117
Cdd:cd23339   65 QVWVATRVVGTGK-VTLKSAH-GKYLSCDKFGVVTATREARGPQEEWTPVPRPDgGGFALQS-VYGKYLSvdevaGGKLV 141

                         90
                 ....*....|....*.
gi 568973828 118 LSCFATAISPAELWTV 133
Cdd:cd23339  142 VRADAETVGFCETWRV 157

FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) superfamily; The FGF superfamily includes FGF1-23 and similar proteins. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. They play essential roles in patterning and differentiation during vertebrate embryogenesis and have neurotrophic activities. FGFs have a high affinity for heparan sulfate proteoglycans and require heparan sulfate to activate one of four cell surface FGF receptors. Upon binding to FGF, the receptors dimerize, and their intracellular tyrosine kinase domains become active. The structure of FGFs is typical of the 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 568973828 301 KKCTFYSSTGGYWTLVTHGGIQATATQVSANTMFEIEWHGR-RVALKA-SNGRFVCMKKNGQLaaisdFVGEHSLPSTAW 378
Cdd:cd00058    1 RLVRLYSRTGYFLQILPDGTVNGTKDENSPYAILELQSVGTgLVRIKGvKTGRYLAMDKNGKL-----YGTKKPTEDCVF 75

                 ....
gi 568973828 379 KEQM 382
Cdd:cd00058   76 KETL 79

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568973828 310 GGYWTLVTHGGIQATATQVSANTMFEIEWHGRRVALKASNGRFVCMKKNGQLAAISDFVGE 370
Cdd:cd23338   72 GKYLSVDSDGKVVGRSDAIGPREQWEPVFQDGKMALLGANNCFLSVNEDGDIVATSKTAGE 132

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 8 (FGF8)-like family; The FGF8-like family includes FGF8, FGF17 and FGF18. FGF8, also called androgen-induced growth factor (AIGF), or heparin-binding growth factor 8 (HBGF8), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It is required for normal brain, eye, ear,, and limb development during embryogenesis. It is also required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. It plays a role in neurite outgrowth in hippocampal cells. FGF8 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. FGF17 plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. It is required for normal brain development. FGF17 interacts with FGFR3 and FGFR4. FGF18, also called zFGF5, plays an important role in the regulation of cell proliferation, cell differentiation, and cell migration. It is required for normal ossification and bone development. It stimulates hepatic and intestinal proliferation. FGF18 interacts FGFR3 and FGFR4. Members in this family contain a FGF domain with 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568973828 301 KKCTFYS-STGGYwTLVTHGGIQATATQVSANTMFEIE--WHGRRVALK-ASNGRFVCMKKNGQLAA 363
Cdd:cd23307    1 RSVRLYSrCSKKF-VRITGGRVDARGEKGSPYAKLTIEsvGFSGKVRIRgAKSGRYLCFNKKGKLVA 66

Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in growth and differentiation in a wide range of contexts. They are found in a wide range of organizms, from nematodes to humans. Most share an internal core region of high similarity, conserved residues in which are involved in binding with their receptors. On binding, they cause dimerization of their tyrosine kinase receptors leading to intracellular signalling. There are currently four known tyrosine kinase receptors for fibroblast growth factors. These receptors can each bind several different members of this family. Members of this family have a beta trefoil structure. Most have N-terminal signal peptides and are secreted. A few lack signal sequences but are secreted anyway; still others also lack the signal peptide but are found on the cell surface and within the extracellular matrix. A third group remain intracellular. They have central roles in development, regulating cell proliferation, migration and differentiation. On the other hand, they are important in tissue repair following injury in adult organizms.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568973828  306 YSSTGGYWTLVTHGG-IQATATQVSANTMFEIEWHGR-RVALKASN-GRFVCMKKNGQLAAISDFVGE 370
Cdd:pfam00167   6 YCRTGGFHLQILPDGkVDGTGEDGSPYSILEIESVSVgVVRIKGVEsGLYLAMNKKGRLYGSKNFTDE 73

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568973828  300 TKKCTFYSSTGGYWTLVTHGGIQATATQVSANTMFEIEWHGRRVALKASNGRFVCMKKNGQLAAISDFVGEH 371
Cdd:pfam06229  37 DEKIALKSGYGKYLGVNKDGILSARADAIGPREQFEPVFQEGKMALLAANGCFLSVDPSGDIVAKSKTAGEG 108