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 1937876556 260 CAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIE 339
Cdd:cd23352     1 CPQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1937876556 340 WCERRITLRASNGKFVTAKKNGQLAATVETAGDSELFLMKLIN 382
Cdd:cd23352    81 WRDRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

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 1937876556 383 RPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKVA 462
Cdd:cd23356     1 RPIIVLRGEHGFIGCRKVTGTLDSNRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVA 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1937876556 463 LKVGGRYLKGDHAGVLKACAETIDPATLWEY 493
Cdd:cd23356    81 IKVGGRYLKGDHAGVLKASAETVDPATLWEY 111

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 1937876556 260 CAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIE 339
Cdd:cd23352     1 CPQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1937876556 340 WCERRITLRASNGKFVTAKKNGQLAATVETAGDSELFLMKLIN 382
Cdd:cd23352    81 WRDRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

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 1937876556 383 RPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKVA 462
Cdd:cd23356     1 RPIIVLRGEHGFIGCRKVTGTLDSNRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVA 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1937876556 463 LKVGGRYLKGDHAGVLKACAETIDPATLWEY 493
Cdd:cd23356    81 IKVGGRYLKGDHAGVLKASAETVDPATLWEY 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 1937876556 268 ANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCERRITL 347
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1937876556 348 RASNGKFVTAKKNGQLAATVETAGDSELFLM 378
Cdd:pfam06268  81 RESNGRYLGGGPSGLLKANASTVGKDELWTL 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 1937876556 391 EHGFIGCRKVTGTLDANR---SSYDVFQLEFNDGAYN--IKDSTGKYWTVGSDSS-VTSSSDTPVDFFLEFCDYNKVALK 464
Cdd:pfam06268   1 ANGYLVSERRGAHLNANReslKRVQTFTLEFDDERYTvyLRSHNGKYLSCDADGRvVCEAERRSADTFFELEFRGRWALL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1937876556 465 --VGGRYLKGDHAGVLKACAETIDPATLWEY 493
Cdd:pfam06268  81 reSNGRYLGGGPSGLLKANASTVGKDELWTL 111

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 1937876556 260 CAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIE 339
Cdd:cd23352     1 CPQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1937876556 340 WCERRITLRASNGKFVTAKKNGQLAATVETAGDSELFLMKLIN 382
Cdd:cd23352    81 WRDRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

first 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 first fascin-like beta-trefoil domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937876556   8 EAVQIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQppDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPDG 87
Cdd:cd23345     2 QALKIQFGLINCENRYLTAEAFGFKVNASAPSLKKKQIWTLEQ--DEGDSSVVFLKSHLGRYLSADKDGKVSCEAEKPGR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937876556  88 DCRFLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAM 138
Cdd:cd23345    80 DCRFLIVAQSDGRWALQSEPHKRFFGGSEDKLSCFAQTITEAELWAVHLAI 130

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 1937876556 383 RPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKVA 462
Cdd:cd23356     1 RPIIVLRGEHGFIGCRKVTGTLDSNRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVA 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1937876556 463 LKVGGRYLKGDHAGVLKACAETIDPATLWEY 493
Cdd:cd23356    81 IKVGGRYLKGDHAGVLKASAETVDPATLWEY 111

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937876556 140 PQVNIYSVTRKRYAHLSARPaDEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFRSG 219
Cdd:cd23335     1 PQVNLYSVNRKRYARLDPEG-DELRVDEDIPWGSDALITLEFDDGRYALRTSDGRYLRSDGSLVDEPSDDTLFTLEFRSG 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1937876556 220 KVAFRDCEGRYLAPSGPSGTLKAGKaTKVGKDELFALE 257
Cdd:cd23335    80 GLAFKDSEGKYLTAVGGSGVLKTRK-KTVGKDELFSLE 116

third 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 third fascin-like beta-trefoil domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937876556 262 QVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWC 341
Cdd:cd23353     3 QVVFQAANGRYVSIRQGVNVSANQDEETDHETFQMQIDKETKKCSFHTNTGKYWTLVAHGGIQSTATEVAANTMFDIEWR 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1937876556 342 ERRITLRASNGKFVTAKKNGQLAATVETAGDSELFLMKLIN 382
Cdd:cd23353    83 GRRVALKASNGKYVCTKKNGQLAAVSDSVGEDEEFTLKLIN 123

second 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 second fascin-like beta-trefoil domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937876556 139 HPQVNIYSVTRKRYAHLSArPADEIAVDRDVPWGVDSLITLAF-QDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFR 217
Cdd:cd23351     1 RPQVNLRSAGRKRYARLSG-DEDEIQVDANVPWGSDTLFTLEFrDDGRYAIHTANGKYLNRDGKLVEECPEDCLFTLEYH 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1937876556 218 SGKVAFRDCEGRYLAPSGPSGTLKAgKATKVGKDELFALE 257
Cdd:cd23351    80 AGQVAFRDRTGKYLAPIGSKAVLRT-RSTSVTKDELFILE 118

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 1937876556  21 NKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDeagSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCRFLVVAHddGR 100
Cdd:pfam06268   2 NGYLVSERRGAHLNANRESLKRVQTFTLEFDDE---RYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFR--GR 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1937876556 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 1937876556 268 ANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCERRITL 347
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1937876556 348 RASNGKFVTAKKNGQLAATVETAGDSELFLM 378
Cdd:pfam06268  81 RESNGRYLGGGPSGLLKANASTVGKDELWTL 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 1937876556 142 VNIYSVTRKRYAHLSARPADEIAVDrdvpwgvdsLITLAFQDQRYSV--QTSDHRFLR--HDGRLVARPE---PATGFTL 214
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQ---------TFTLEFDDERYTVylRSHNGKYLScdADGRVVCEAErrsADTFFEL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1937876556 215 EFRSGKVAFRDCEGRYLApSGPSGTLKAgKATKVGKDELFAL 256
Cdd:pfam06268  72 EFRGRWALLRESNGRYLG-GGPSGLLKA-NASTVGKDELWTL 111

first 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 first fascin-like beta-trefoil domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937876556  12 IQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCRF 91
Cdd:cd23346     1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVIVSDYSDRQAVVELKGPQGLYLLVDKDGLVRCGTPDTKHHGLF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1937876556  92 LVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAM 138
Cdd:cd23346    81 LLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127

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 1937876556 262 QVVLQAANERNVSTRQGMD--LSANQDEETDQETFQLeIDRDTRKCAFRTHTGKYWTLTATGG--VQSTASTKNASCYFD 337
Cdd:cd00257     2 TVALKSSNGKYLSAENGGGgpLVANRDAAGPWETFTL-VDLGDGKVALKSSNGKYLSAENGGGgtLVANRTAIGPWETFT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1937876556 338 IEWCE-RRITLRASNGKFVTAKKN--GQLAATVETAGDSELF 376
Cdd:cd00257    81 LVPLGnGKVALKSANGKYLSADNGggGTLIANATSIGAWEKF 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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937876556  13 QFGLISCGNKYLTAEAFGF-KVNASASSLKKKQIWTLEQPPDeaGSaaVCLRSHLGRYLAADKDGN--VTCEREVPDGDC 89
Cdd:cd00257     2 TVALKSSNGKYLSAENGGGgPLVANRDAAGPWETFTLVDLGD--GK--VALKSSNGKYLSAENGGGgtLVANRTAIGPWE 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1937876556  90 RFLVVAHDDGRWSLQSeAHRRYF---GGTEDRLSCFAQSVSPAEKWSV 134
Cdd:cd00257    78 TFTLVPLGNGKVALKS-ANGKYLsadNGGGGTLIANATSIGAWEKFTI 124

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 1937876556 212 FTLEF--RSGKVAFRDCEGRYLApSGPSGTLKAgKATKVGKDELFALE-QSCAQVVLQAANERNVSTRQGMDLSANQDEE 288
Cdd:cd23336    35 FQLEFdkETKKWAFRTNKGKYWS-LGPDGGIQA-TASSRSPNCLFELEwNDGGTVALKASNGKYVTAKPNGQLAATSDEV 112

                          90
                  ....*....|
gi 1937876556 289 TDQETFQLEI 298
Cdd:cd23336   113 GEKEKFTLKL 122

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 1937876556 289 TDQETFQLEIDRDtRKCAFRTHTGKYWTLTATGGVQSTASTKNAscyFDIEWCER-RITLRASNGKFVTAKKNGQLAATV 367
Cdd:cd23337    28 STYDVFQLEYNND-GAYHLKGSNGKYWSVDSDGSVTADSAAPTP---FILEFRGQsKLAIKAPNGKYLKGEQNGLFKATG 103

                  ....*....
gi 1937876556 368 ETAGDSELF 376
Cdd:cd23337   104 TEVDKATLW 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 1937876556 184 QRYSVQTSDHRFLR----HDGRLVARPEPATG---FTLEF-RSGKVAFRDCEGRYL-APSGPSGTLKAGkATKVGKDELF 254
Cdd:cd00257     1 GTVALKSSNGKYLSaengGGGPLVANRDAAGPwetFTLVDlGDGKVALKSSNGKYLsAENGGGGTLVAN-RTAIGPWETF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1937876556 255 ALE-QSCAQVVLQAANERNVSTRQGMD--LSANQDEETDQETFQL 296
Cdd:cd00257    80 TLVpLGNGKVALKSANGKYLSADNGGGgtLIANATSIGAWEKFTI 124

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937876556 343 RRITLRASNGKFVTA--KKNGQLAATVETAGDSElflmklinrpiivfrgehgfigcrkvtgtldanrssydVFQLEFN- 419
Cdd:cd00257     1 GTVALKSSNGKYLSAenGGGGPLVANRDAAGPWE--------------------------------------TFTLVDLg 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937876556 420 DGAYNIKDSTGKYWTVGSDSSVTSSSDTPVD-----FFLEFCDYNKVALK-VGGRYL--KGDHAGVLKACAETIDPATLW 491
Cdd:cd00257    43 DGKVALKSSNGKYLSAENGGGGTLVANRTAIgpwetFTLVPLGNGKVALKsANGKYLsaDNGGGGTLIANATSIGAWEKF 122

                  .
gi 1937876556 492 E 492
Cdd:cd00257   123 T 123

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 1937876556 262 QVVLQAANERNVSTRQGM-DLSANQDEETDQETFQLEiDRDTRKCAFRTHTGKYwtltatggVQSTASTKNASCYFD-IE 339
Cdd:cd23342     3 TISLKGNNGKYVSSENGNkPMTANRTSVGSWEKFTVV-DAGNGKVALKGNNGKY--------VSSENGTKPMTCNRTtIG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1937876556 340 WCER---------RITLRASNGKFVTAKKNGQ-LAATVETAGDSELF 376
Cdd:cd23342    74 AWEKftwislgngTVALKGNNGKYVSSENGTNpMTCNRTSIGGWEKF 120

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 1937876556 304 KCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCERRITLRASNGKFVTAKKNGQLAATVETAGDSELF 376
Cdd:cd23338    64 KIALKSGYGKYLSVDSDGKVVGRSDAIGPREQWEPVFQDGKMALLGANNCFLSVNEDGDIVATSKTAGENEMI 136

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937876556 186 YSVQTSDHRFLR--HDGRLVARPEPATGFTLEFRSG-KVAFRDCEGRYLApSGPSGTLKAgKATKVGKDELF 254
Cdd:cd23337    43 YHLKGSNGKYWSvdSDGSVTADSAAPTPFILEFRGQsKLAIKAPNGKYLK-GEQNGLFKA-TGTEVDKATLW 112

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 1937876556 205 RPEPATGFTLEF--RSGKVAFRDCEGRYLAPSGPSGTLKAGKATKvgKDELFALEQSCAQVVLQAANERNVSTRQGMDLS 282
Cdd:cd23354    28 RLTPLSLFQFEVdpNTPAVQLRTVNGRYLAQRGHRSVIADGKGTE--SETFFRVEWRCGKIILQASNGRYLGVKPNGLLT 105

                          90
                  ....*....|..
gi 1937876556 283 ANQDEETDQETF 294
Cdd:cd23354   106 ASALLPGPNEEF 117

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 1937876556 262 QVVLQ-AANERNVSTRQGMD-LSANQDEETDQETFQLEiDRDTRKCAFRTH-TGKYWTLTATGGVQSTAS------TKNA 332
Cdd:cd23343     4 RIALRsAATGKYVTVGEEGGaLAADAEDAEEAETFELT-DWGWGSHTLRSVaNGKYVTTDDDGTLTASAEeafgwfVKEV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1937876556 333 scyFDIE-WCERRITLRASNGKFVTAKKNGQLAATVETA-GDSELF 376
Cdd:cd23343    83 ---FRLEpQEDGTVSLRTWNGRPVAVDEDGRLTVGEDDAaAEAERF 125

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 1937876556 218 SGKVAFRDCEGRYLAPSGPSGTLKAGKATkVGKDELFALE-QSCAQVVLQAANERNVSTRQGMD-LSANQDEETDQETFQ 295
Cdd:cd23342    43 NGKVALKGNNGKYVSSENGTKPMTCNRTT-IGAWEKFTWIsLGNGTVALKGNNGKYVSSENGTNpMTCNRTSIGGWEKFT 121