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 183986779 136 HPQANLLSVARKRYAHLASPEGEIAVDCNIPWGVDALLTLVYMDGKYCLKTSDSRFLSNDGKLSSENGRGTGYTLELKSG 215
Cdd:cd23349    1 HPQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKAG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 183986779 216 KLAFKDCEGKYLTPMGPTGTLRSGRCSKPGKDELFDLEE 254
Cdd:cd23349   81 KLAFKDCDGKYLTPMGPTGTLKSGRSSKPGKDELFDLEE 119

fourth fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, also called retinal fascin, is a photoreceptor-specific paralog of the actin-bundling protein fascin. It may play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Fascin-2 is composed of four fascin beta-trefoil domains, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the fourth fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183986779 379 RPILILRGENGYVCHHKNSNTLDASRSVYDIFTLQFSDGAYHIKGAGGKFWYVSSSG*VCSDGDTPEDFSFEFLEHGRIA 458
Cdd:cd23357    1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRVA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 183986779 459 IRGKNGKYLRGDQGGNLKGDGETADSSSLWEY 490
Cdd:cd23357   81 IKGKNGKYLRGDQAGTLKADAETVDSATLWEY 112

second fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, also called retinal fascin, is a photoreceptor-specific paralog of the actin-bundling protein fascin. It may play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Fascin-2 is composed of four fascin beta-trefoil domains, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the second fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183986779 136 HPQANLLSVARKRYAHLASPEGEIAVDCNIPWGVDALLTLVYMDGKYCLKTSDSRFLSNDGKLSSENGRGTGYTLELKSG 215
Cdd:cd23349    1 HPQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKAG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 183986779 216 KLAFKDCEGKYLTPMGPTGTLRSGRCSKPGKDELFDLEE 254
Cdd:cd23349   81 KLAFKDCDGKYLTPMGPTGTLKSGRSSKPGKDELFDLEE 119

fourth fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, also called retinal fascin, is a photoreceptor-specific paralog of the actin-bundling protein fascin. It may play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Fascin-2 is composed of four fascin beta-trefoil domains, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the fourth fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183986779 379 RPILILRGENGYVCHHKNSNTLDASRSVYDIFTLQFSDGAYHIKGAGGKFWYVSSSG*VCSDGDTPEDFSFEFLEHGRIA 458
Cdd:cd23357    1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRVA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 183986779 459 IRGKNGKYLRGDQGGNLKGDGETADSSSLWEY 490
Cdd:cd23357   81 IKGKNGKYLRGDQAGTLKADAETVDSATLWEY 112

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183986779  264 ANNRFVSIRQGVSVSANQDDETDMETFQMEIDKDTRKCKFRTNEGNYWTLVAHGGIQSTATEAGANTMFDIVWLGRRVAL 343
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALL 80

                          90       100
                  ....*....|....*....|....*..
gi 183986779  344 RASNGKYVCTKKNGQLSAVSDSVGEDE 370
Cdd:pfam06268  81 RESNGRYLGGGPSGLLKANASTVGKDE 107

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 183986779 136 HPQANLLSVARKRYAHLASPEGEIAVDCNIPWGVDALLTLVYMDGKYCLKTSDSRFLSNDGKLSSENGRGTGYTLELKSG 215
Cdd:cd23349    1 HPQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKAG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 183986779 216 KLAFKDCEGKYLTPMGPTGTLRSGRCSKPGKDELFDLEE 254
Cdd:cd23349   81 KLAFKDCDGKYLTPMGPTGTLKSGRSSKPGKDELFDLEE 119

fourth fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, also called retinal fascin, is a photoreceptor-specific paralog of the actin-bundling protein fascin. It may play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Fascin-2 is composed of four fascin beta-trefoil domains, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the fourth fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183986779 379 RPILILRGENGYVCHHKNSNTLDASRSVYDIFTLQFSDGAYHIKGAGGKFWYVSSSG*VCSDGDTPEDFSFEFLEHGRIA 458
Cdd:cd23357    1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRVA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 183986779 459 IRGKNGKYLRGDQGGNLKGDGETADSSSLWEY 490
Cdd:cd23357   81 IKGKNGKYLRGDQAGTLKADAETVDSATLWEY 112

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 183986779  11 LQFGLINHENRYLTAEAFGFKVNASAPSLKKKQIWTLEQDDQDGQVVYLRSHLGRYLASDKDGKVSCEAETKENDCRFLI 90
Cdd:cd23334    1 WKLGLINSSGKYLTAETFGFKVNASGTSLKKKQTWTLEQDEGGSETVYLKSHLGRYLSADKDGKVTCDAEEPGADERFLI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 183986779  91 VAQSDGRWALQSETYLRFFGGSEDYLSCFAQTIGEAELWAMHLAL 135
Cdd:cd23334   81 EYQPDGRWALKSEKHGRYLGGTGDNLSCFAKEVSESELWTVHLAI 125

second 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 second fascin-like beta-trefoil domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183986779 136 HPQANLLSVARKRYAHL-ASPEGEIAVDCNIPWGVDALLTLVYMDGKYCLKTSDSRFLSNDGKLSSENGRGTGYTLELKS 214
Cdd:cd23348    1 HPQVNIYSVTRKRYAHLsARPADEIAVDRDVPWGVDSLITLVFQDQRYSVQTSDHRFLRHDGRLVARPEPATGYTLEFRS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 183986779 215 GKLAFKDCEGKYLTPMGPTGTLRSGRCSKPGKDELFDLEE 254
Cdd:cd23348   81 GKVAFRDCEGRYLAPSGPSGTLKAGKSTKVGKDELFVLEQ 120

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 183986779 137 PQANLLSVARKRYAHLASPEGEIAVDCNIPWGVDALLTLVYMDGKYCLKTSDSRFLSNDGKLSSENGRGTGYTLELKSGK 216
Cdd:cd23335    1 PQVNLYSVNRKRYARLDPEGDELRVDEDIPWGSDALITLEFDDGRYALRTSDGRYLRSDGSLVDEPSDDTLFTLEFRSGG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 183986779 217 LAFKDCEGKYLTPMGPTGTLRSGRCsKPGKDELFDLEE 254
Cdd:cd23335   81 LAFKDSEGKYLTAVGGSGVLKTRKK-TVGKDELFSLED 117

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 183986779 379 RPILILRGENGYVCHH-KNSNTLDASRSVYDIFTLQFS-DGAYHIKGAGGKFWYVSSSG*VCSDGDTPEDFSFEFLEHGR 456
Cdd:cd23337    1 RPILVLRGEYGFVGVKsGSSGKLECNKSTYDVFQLEYNnDGAYHLKGSNGKYWSVDSDGSVTADSAAPTPFILEFRGQSK 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 183986779 457 IAIRGKNGKYLRGDQGGNLKGDGETADSSSLWEY 490
Cdd:cd23337   81 LAIKAPNGKYLKGEQNGLFKATGTEVDKATLWEY 114

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 183986779 136 HPQANLLSVARKRYAHLASPEGEIAVDCNIPWGVDALLTLVY-MDGKYCLKTSDSRFLSNDGKLSSENGRGTGYTLELKS 214
Cdd:cd23351    1 RPQVNLRSAGRKRYARLSGDEDEIQVDANVPWGSDTLFTLEFrDDGRYAIHTANGKYLNRDGKLVEECPEDCLFTLEYHA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 183986779 215 GKLAFKDCEGKYLTPMGPTGTLRSgRCSKPGKDELFDLE 253
Cdd:cd23351   81 GQVAFRDRTGKYLAPIGSKAVLRT-RSTSVTKDELFILE 118

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 183986779 257 PQVVFQAA-NNRFVSIRQGVSVSANQDDETDMETFQMEIDKDTRKCKFRTNEGNYWTLVAHGGIQSTATEAGANTMFDIV 335
Cdd:cd23355    2 PQAAFIAGlNSRYVSVKQGVDVTANQDEISDHETFQLEYDWSTKRWYIRTMQDRYWTLETAGGIQASADKKSANALFELE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 183986779 336 WLGR-RVALRASNGKYVCTKKNGQLSAVSDSVGEDEQLILKLIN 378
Cdd:cd23355   82 WQEDgSVSFRANNGKFVGTKRSGHLFANSESIDEIAKFYFYLIN 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 183986779  387 ENGYVCHHKNSNTLDASR---SVYDIFTLQFSDGAY--HIKGAGGKFWYVSSSG*VCSDGDTP-EDFSFEFLEHGRIAI- 459
Cdd:pfam06268   1 ANGYLVSERRGAHLNANReslKRVQTFTLEFDDERYtvYLRSHNGKYLSCDADGRVVCEAERRsADTFFELEFRGRWALl 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 183986779  460 RGKNGKYLRGDQGGNLKGDGETADSSSLWEY 490
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 183986779 258 QVVFQAANNRFVSIRQGV--SVSANQDDETDMETFQMeIDKDTRKCKFRTNEGNYWTLVAHGG--IQSTATEAGANTMFD 333
Cdd:cd00257    2 TVALKSSNGKYLSAENGGggPLVANRDAAGPWETFTL-VDLGDGKVALKSSNGKYLSAENGGGgtLVANRTAIGPWETFT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 183986779 334 IVWLG-RRVALRASNGKYVCTKKN--GQLSAVSDSVGEDEQLIL 374
Cdd:cd00257   81 LVPLGnGKVALKSANGKYLSADNGggGTLIANATSIGAWEKFTI 124

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 183986779 257 PQVVFQAANNRFVSIRQGVSVSANQDDETDMETFQMEIDKDTRKCKFRTNEGNYWTLVAHGGIQSTATEAGANTMFDIVW 336
Cdd:cd23354    2 TWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVEW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 183986779 337 LGRRVALRASNGKYVCTKKNGQLSAVSDSVGEDEQLILKLIN 378
Cdd:cd23354   82 RCGKIILQASNGRYLGVKPNGLLTASALLPGPNEEFGVRLAN 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 183986779  12 QFGLINHENRYLTAEAFGF-KVNASAPSLKKKQIWTLEqdDQDGQVVYLRSHLGRYLA--SDKDGKVSCEAETKENDCRF 88
Cdd:cd00257    2 TVALKSSNGKYLSAENGGGgPLVANRDAAGPWETFTLV--DLGDGKVALKSSNGKYLSaeNGGGGTLVANRTAIGPWETF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 183986779  89 LIVAQSDGRWALQSE--TYLRFFGGSEDYLSCFAQTIGEAELWAM 131
Cdd:cd00257   80 TLVPLGNGKVALKSAngKYLSADNGGGGTLIANATSIGAWEKFTI 124

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 183986779 136 HPQANLLSVARKRYAHLASPEGEIAVDCNIPWGVDALLTLVYMDGKYCLKTSDSRFLSNDGKLSSENGRGTGYTLELKSG 215
Cdd:cd23350    1 HVHVVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 183986779 216 KL-AFKDCEGKYLTPMGPTGTLRSGrCSKPGKDELFDLE 253
Cdd:cd23350   81 YLaSFFDDCGSMLYPQGRSRLLLSG-NIPINEEEWFIIK 118

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 183986779 338 GRRVALRASNGKYVCTKK-NGQLSAVSDSVGEDEQLIlklinrpilILRGENGYVchhknsntldasrsvydiftlqfsd 416
Cdd:cd23342    1 GSTISLKGNNGKYVSSENgNKPMTANRTSVGSWEKFT---------VVDAGNGKV------------------------- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183986779 417 gayHIKGAGGKfwYVSSSG*----VCsDGDTPED---FSFEFLEHGRIAIRGKNGKYLRGDQGGNlkgdGETADSSSL-- 487
Cdd:cd23342   47 ---ALKGNNGK--YVSSENGtkpmTC-NRTTIGAwekFTWISLGNGTVALKGNNGKYVSSENGTN----PMTCNRTSIgg 116

                 ..
gi 183986779 488 WE 489
Cdd:cd23342  117 WE 118

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 183986779 256 HPQVVFQAANNrFVSIRQGVS--VSANQddeTDMETFQMEIDKDtRKCKFRTNEGNYWTLVAHGGIQSTATEAganTMFD 333
Cdd:cd23337    1 RPILVLRGEYG-FVGVKSGSSgkLECNK---STYDVFQLEYNND-GAYHLKGSNGKYWSVDSDGSVTADSAAP---TPFI 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 183986779 334 IVWLGR-RVALRASNGKYVCTKKNGQLSAVSDSVGEDEQ 371
Cdd:cd23337   73 LEFRGQsKLAIKAPNGKYLKGEQNGLFKATGTEVDKATL 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 183986779  55 QVVYLRSHLGRYLASD--KDGKVSCEAETKENDCRFLIVAQSDGRWALQSET--YLRFFGGSEDYLSCFAQTIGEAELWA 130
Cdd:cd00257    1 GTVALKSSNGKYLSAEngGGGPLVANRDAAGPWETFTLVDLGDGKVALKSSNgkYLSAENGGGGTLVANRTAIGPWETFT 80

                 ..
gi 183986779 131 MH 132
Cdd:cd00257   81 LV 82

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 183986779 409 IFTLQFSDGA---YHIKGAGGKFWYVSSSG*VCSDGDTP---EDFSFEFLEHGRIAIRG-KNGKYLRGdQGGNLKGDGET 481
Cdd:cd23334   34 TWTLEQDEGGsetVYLKSHLGRYLSADKDGKVTCDAEEPgadERFLIEYQPDGRWALKSeKHGRYLGG-TGDNLSCFAKE 112

                 ....*..
gi 183986779 482 ADSSSLW 488
Cdd:cd23334  113 VSESELW 119

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 183986779 410 FTLQFSDGAYHIKGAGGKFwyvsssg*VCSDG---DTPED---FSFEFLEhGRIAIRGKNGKYLRG 469
Cdd:cd23335   37 ITLEFDDGRYALRTSDGRY--------LRSDGslvDEPSDdtlFTLEFRS-GGLAFKDSEGKYLTA 93

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 183986779  20 NRYLTAEAFGFKVNASAPSLKKKQIWTLEqdDQDGQVVYLRSHL-GRYLASDKDGKVSCEAE------TKENdcrFLIVA 92
Cdd:cd23343   13 GKYVTVGEEGGALAADAEDAEEAETFELT--DWGWGSHTLRSVAnGKYVTTDDDGTLTASAEeafgwfVKEV---FRLEP 87

                         90
                 ....*....|
gi 183986779  93 QSDGRWALQS 102
Cdd:cd23343   88 QEDGTVSLRT 97

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 183986779  297 DTRKCKFRTNEGNYWTLVAHGGIQSTATEAGANTMFDIVWLGRRVALRASNGKYVCTKKNGQLSAVSDSVGEDE 370
Cdd:pfam06229  36 SDEKIALKSGYGKYLGVNKDGILSARADAIGPREQFEPVFQEGKMALLAANGCFLSVDPSGDIVAKSKTAGEGE 109

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 183986779 409 IFTLQF-SDGAYHIKGAGGKfwYVSSSG*VCSDGDTPEDFSFEFlEHGRIAIRGKNGKYL 467
Cdd:cd23351   37 LFTLEFrDDGRYAIHTANGK--YLNRDGKLVEECPEDCLFTLEY-HAGQVAFRDRTGKYL 93

fascin-like domain, beta-trefoil fold, found in the hisactophilin subfamily; 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. Hisactophilin contains a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183986779 260 VFQAANNRFVSIRQGVSV--SANQDDETdmeTFQMEiDKDTRKCKFRTNEGNYWTLVAHGGIQSTATEAGANTMFDIVWL 337
Cdd:cd23341    4 AFKSHNGHFLSAEDGVVKteHGHHDHHT---HFHIE-NHGDDKVAIKTHHGKYVAIDDNKQVYLSHHHHGDHTKFHLEHH 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 183986779 338 GRRVALRASNGKYVCTKKNGQLSAvSDSVGEDE 370
Cdd:cd23341   80 GGKVAIKGHHHHYIGVDHHGSVHT-SHHHGEDE 111

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 183986779  18 HENRYLTA---EAFGFKVnasapslkkKQIWTLEqdDQDGQVVYLRSHLGRYLASDKDGKVSC-EAETKENDCRFLIVAQ 93
Cdd:cd23343   62 DDDGTLTAsaeEAFGWFV---------KEVFRLE--PQEDGTVSLRTWNGRPVAVDEDGRLTVgEDDAAAEAERFEKEVV 130