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 497775    11 QIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRTHLGRYLAADKDGNVTCEREVPDGDCR 90
Cdd:cd23344   1 QIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPGDEADSSAVLLRSHLGRYLAADKDGNVTCESEVPGPDCR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 497775    91 FLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAM 138
Cdd:cd23344  81 FLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAM 128

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 497775   260 CAEVVLQAANEGNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIE 339
Cdd:cd23352   1 CPQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 497775   340 WCDRRITLRASNGKFVTAKKNGHVAASVETAGDSELFLMKLIN 382
Cdd:cd23352  81 WRDRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

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 497775    11 QIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRTHLGRYLAADKDGNVTCEREVPDGDCR 90
Cdd:cd23344   1 QIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPGDEADSSAVLLRSHLGRYLAADKDGNVTCESEVPGPDCR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 497775    91 FLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAM 138
Cdd:cd23344  81 FLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAM 128

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 497775   260 CAEVVLQAANEGNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIE 339
Cdd:cd23352   1 CPQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 497775   340 WCDRRITLRASNGKFVTAKKNGHVAASVETAGDSELFLMKLIN 382
Cdd:cd23352  81 WRDRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

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 497775      21 NKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDeagSAAVCLRTHLGRYLAADKDGNVTCEREVPDGDCRFLVVAHddGR 100
Cdd:pfam06268   2 NGYLVSERRGAHLNANRESLKRVQTFTLEFDDE---RYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFR--GR 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 497775     101 WSLQSEAHRRYFG-GTEDRLSCFAQSVSPAEKWSV 134
Cdd:pfam06268  77 WALLRESNGRYLGgGPSGLLKANASTVGKDELWTL 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 497775     142 VNIYSVTRKRYAHLSARPADEIAVDrdvpwgvdsLITLAFQDQRYSV--QTSDHRFLR--HDGRLVARPE---PATGFTL 214
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQ---------TFTLEFDDERYTVylRSHNGKYLScdADGRVVCEAErrsADTFFEL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 497775     215 EFRSGKVAFRDCEGRYLApSGPSGTLKAgKATKVGKDELFAL 256
Cdd:pfam06268  72 EFRGRWALLRESNGRYLG-GGPSGLLKA-NASTVGKDELWTL 111

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 497775    11 QIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRTHLGRYLAADKDGNVTCEREVPDGDCR 90
Cdd:cd23344   1 QIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPGDEADSSAVLLRSHLGRYLAADKDGNVTCESEVPGPDCR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 497775    91 FLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAM 138
Cdd:cd23344  81 FLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAM 128

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 497775   260 CAEVVLQAANEGNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIE 339
Cdd:cd23352   1 CPQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 497775   340 WCDRRITLRASNGKFVTAKKNGHVAASVETAGDSELFLMKLIN 382
Cdd:cd23352  81 WRDRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

first fascin-like domain, beta-trefoil fold, found in the fascin subfamily; The fascin family 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 first fascin-like beta-trefoil domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497775    12 IQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQppDEAGSAAVCLRTHLGRYLAADKDGNVTCEREVPDGDCRF 91
Cdd:cd23334   1 WKLGLINSSGKYLTAETFGFKVNASGTSLKKKQTWTLEQ--DEGGSETVYLKSHLGRYLSADKDGKVTCDAEEPGADERF 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 497775    92 LVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAM 138
Cdd:cd23334  79 LIEYQPDGRWALKSEKHGRYLGGTGDNLSCFAKEVSESELWTVHLAI 125

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 497775   139 HPQVNIYSVTRKRYAHLSArPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFRS 218
Cdd:cd23349   1 HPQANLLSVSRRRYAHLSV-QEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKA 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 497775   219 GKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQ 258
Cdd:cd23349  80 GKLAFKDCDGKYLTPMGPTGTLKSGRSSKPGKDELFDLEE 119

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 497775   260 CAEVVLQAANEGNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIE 339
Cdd:cd23336   1 HPQVSLRAHNGKYVSIRQGVDVSANQDEETDTETFQLEFDKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 497775   340 W-CDRRITLRASNGKFVTAKKNGHVAASVETAGDSELFLMKLIN 382
Cdd:cd23336  81 WnDGGTVALKASNGKYVTAKPNGQLAATSDEVGEKEKFTLKLIN 124

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 497775    15 GLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDeaGSAAVCLRTHLGRYLAADKDGNVTCEREVPDGDCRF-LV 93
Cdd:cd23347   7 GLINSQQKYLTAETFGFKVNANGSSLKKKQLWTLEPFGD--GTNVVALRSHLGRYLSVDQFGNVTCEAEEKGEGSRFeIV 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 497775    94 VAHD-DGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIA 137
Cdd:cd23347  85 ISEDeSGRWAFRNEERGYFLGGSGDKLVCTAKAPTDSELWTVHLA 129

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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497775   383 RPIIAFRGEHGFIACRKVT-GTLDANRSSYDVFQLEF-NDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNK 460
Cdd:cd23337   1 RPILVLRGEYGFVGVKSGSsGKLECNKSTYDVFQLEYnNDGAYHLKGSNGKYWSVDSDGSVTADSAAPTPFILEFRGQSK 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 497775   461 VALKV-GGRYLKGDHAGVLKACAETIDPASLWEY 493
Cdd:cd23337  81 LAIKApNGKYLKGEQNGLFKATGTEVDKATLWEY 114

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 497775   383 RPIIAFRGEHGFIACRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKVA 462
Cdd:cd23357   1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRVA 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 497775   463 LKV-GGRYLKGDHAGVLKACAETIDPASLWEY 493
Cdd:cd23357  81 IKGkNGKYLRGDQAGTLKADAETVDSATLWEY 112

third 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 third fascin-like beta-trefoil domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497775   263 VVLQAANEGNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWC- 341
Cdd:cd23355   5 AFIAGLNSRYVSVKQGVDVTANQDEISDHETFQLEYDWSTKRWYIRTMQDRYWTLETAGGIQASADKKSANALFELEWQe 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 497775   342 DRRITLRASNGKFVTAKKNGHVAASVETAGDSELFLMKLIN 382
Cdd:cd23355  85 DGSVSFRANNGKFVGTKRSGHLFANSESIDEIAKFYFYLIN 125

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 497775     391 EHGFIACRKVTGTLDANR---SSYDVFQLEFNDGAYN--IKDSTGKYWTVGSDSS-VTSSSDTPVDFFLEFCDYNKVALK 464
Cdd:pfam06268   1 ANGYLVSERRGAHLNANReslKRVQTFTLEFDDERYTvyLRSHNGKYLSCDADGRvVCEAERRSADTFFELEFRGRWALL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 497775     465 --VGGRYLKGDHAGVLKACAETIDPASLWEY 493
Cdd:pfam06268  81 reSNGRYLGGGPSGLLKANASTVGKDELWTL 111

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 497775   263 VVLQAANEGNVSTRQGMD--LSANQDEETDQETFQLeIDRDTRKCAFRTHTGKYWTLTATGG--VQSTASTKNASCYFDI 338
Cdd:cd00257   3 VALKSSNGKYLSAENGGGgpLVANRDAAGPWETFTL-VDLGDGKVALKSSNGKYLSAENGGGgtLVANRTAIGPWETFTL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 497775   339 EWC-DRRITLRASNGKFVTAKKNGH--VAASVETAGDSELF 376
Cdd:cd00257  82 VPLgNGKVALKSANGKYLSADNGGGgtLIANATSIGAWEKF 122

second 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 second fascin-like beta-trefoil domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497775   139 HPQVNIYSVTRKRYAHlsARPA-DEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFR 217
Cdd:cd23350   1 HVHVVLYNIRSRCYAQ--ADPEeDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLR 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 497775   218 SG-KVAFRDCEGRYLAPSGPSGTLKAGKaTKVGKDELFALEQ 258
Cdd:cd23350  79 PGyLASFFDDCGSMLYPQGRSRLLLSGN-IPINEEEWFIIKR 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 497775   303 RKCAFRTHTGKYWTLTATGG--VQSTASTKNASCYFDIE-WCDRRITLRASNGKFVTA--KKNGHVAASVETAGDSELFL 377
Cdd:cd00257   1 GTVALKSSNGKYLSAENGGGgpLVANRDAAGPWETFTLVdLGDGKVALKSSNGKYLSAenGGGGTLVANRTAIGPWETFT 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 497775   378 MKLINRPIIAFRGEHG-FI-ACRKVTGTLDANRSS 410
Cdd:cd00257  81 LVPLGNGKVALKSANGkYLsADNGGGGTLIANATS 115

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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497775   289 TDQETFQLEIDRDtRKCAFRTHTGKYWTLTATGGVQSTASTKNAscyFDIEWCDR-RITLRASNGKFVTAKKNGHVAASV 367
Cdd:cd23337  28 STYDVFQLEYNND-GAYHLKGSNGKYWSVDSDGSVTADSAAPTP---FILEFRGQsKLAIKAPNGKYLKGEQNGLFKATG 103

                ....*....
gi 497775   368 ETAGDSELF 376
Cdd:cd23337 104 TEVDKATLW 112

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 497775   383 RPIIAFRGEHGFIACRKVTGTLDANRSSYDVFQL-EFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKV 461
Cdd:cd23358   1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLlPCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 497775   462 A-LKVGGRYLKGDHAGVLKACAETIDPASLWEY 493
Cdd:cd23358  81 AiLAPNGCYLRGDNSGTLLADSEIITSECLWEF 113

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 497775   343 RRITLRASNGKFVTA--KKNGHVAASVETAGDSELFLMKLINRPIIAFRGEHG-FI-ACRKVTGTLDANRSSYD---VFQ 415
Cdd:cd00257   1 GTVALKSSNGKYLSAenGGGGPLVANRDAAGPWETFTLVDLGDGKVALKSSNGkYLsAENGGGGTLVANRTAIGpweTFT 80

                        90       100
                ....*....|....*....|.
gi 497775   416 LEFN-DGAYNIKDSTGKYWTV 435
Cdd:cd00257  81 LVPLgNGKVALKSANGKYLSA 101

fascin-like domain, beta-trefoil fold, found in Zobellia galactanivorans beta-porphyranase A (PorA) and similar proteins; 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 subfamily 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497775   344 RITLRASNGKFVTAKK-NGHVAASVETAGDSELFLMKLINRPIIAFRGEHG-FIACRKVTGTLDANRSSYDV---FQLEF 418
Cdd:cd23342   3 TISLKGNNGKYVSSENgNKPMTANRTSVGSWEKFTVVDAGNGKVALKGNNGkYVSSENGTKPMTCNRTTIGAwekFTWIS 82

                        90
                ....*....|....*
gi 497775   419 -NDGAYNIKDSTGKY 432
Cdd:cd23342  83 lGNGTVALKGNNGKY 97

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497775   304 KCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCDRRITLRASNGKFVTAKKNGHVAASVETAGDSELF 376
Cdd:cd23338  64 KIALKSGYGKYLSVDSDGKVVGRSDAIGPREQWEPVFQDGKMALLGANNCFLSVNEDGDIVATSKTAGENEMI 136

fascin-like domain, beta-trefoil fold, found in uncharacterized beta-glucosidase-like proteins; This subfamily includes a group of uncharacterized proteins which may be related to beta-glucosidase/glycosyl hydrolase 3 family. They 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497775   220 KVAFRDCE-GRYLAPSGPSGTLKAGKATkVGKDELFALEQ-SCAEVVLQAANEGN-VSTRQGMDLSANQDEETD---QET 293
Cdd:cd23343   4 RIALRSAAtGKYVTVGEEGGALAADAED-AEEAETFELTDwGWGSHTLRSVANGKyVTTDDDGTLTASAEEAFGwfvKEV 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 497775   294 FQLEIDRDTRkCAFRTHTGKYWTLTATGGVQSTASTKNASC-YFDIE 339
Cdd:cd23343  83 FRLEPQEDGT-VSLRTWNGRPVAVDEDGRLTVGEDDAAAEAeRFEKE 128

fascin-like domain, beta-trefoil fold, found in uncharacterized beta-glucosidase-like proteins; This subfamily includes a group of uncharacterized proteins which may be related to beta-glucosidase/glycosyl hydrolase 3 family. They 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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497775   306 AFRT-HTGKYWTLTATGGVQS-TASTKNASCYFDIE-WCDRRITLRA-SNGKFVTAKKNGHVAASVETAGD 372
Cdd:cd23343   6 ALRSaATGKYVTVGEEGGALAaDAEDAEEAETFELTdWGWGSHTLRSvANGKYVTTDDDGTLTASAEEAFG 76

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 497775    11 QIQFGLISCGNKYLTAeAFGFKVNASASSLKKKQIWTLEQppdEAGSAAVCLRTHLGRYLAADKDGNVTCEREVPDGDCR 90
Cdd:cd23336   1 HPQVSLRAHNGKYVSI-RQGVDVSANQDEETDTETFQLEF---DKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCL 76

                        90
                ....*....|....*
gi 497775    91 FLVVAHDDGRWSLQS 105
Cdd:cd23336  77 FELEWNDGGTVALKA 91

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 497775   205 RPEPATGFTLEF--RSGKVAFRDCEGRYLAPSGPSGTLKAGKATKvgKDELFALEQSCAEVVLQAAN 269
Cdd:cd23354  28 RLTPLSLFQFEVdpNTPAVQLRTVNGRYLAQRGHRSVIADGKGTE--SETFFRVEWRCGKIILQASN 92

fourth 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 fourth fascin-like beta-trefoil domain.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497775   292 ETFQLEIDrDTRKCAFRTHTGKYWTLtATGGVQSTASTKNAscyFDIEWCD-RRITLRASNGKFVTAKKNG 361
Cdd:cd23359  31 ETIQVERG-DKGLVFFKGQSGKYWGV-CGDGITADADAPEG---FYLELREpSRLCIKTADGSYLMADKNG 96