NCBI Conserved Domain Search

first fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; Fascin, also called fascin-1, 55 kDa actin-bundling protein, singed-like protein, or p55, is an actin-binding protein that contains 2 major actin binding sites. It is involved in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. It plays an important role for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. It mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to nerve growth factor (NGF). Fascin is composed of four fascin beta-trefoil domains, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the first fascin-like beta-trefoil domain.

Pssm-ID: 467452 Cd Length: 128 Bit Score: 272.49 E-value: 9.77e-91

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133  11 QIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCR 90
Cdd:cd23344    1 QIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPGDEADSSAVLLRSHLGRYLAADKDGNVTCESEVPGPDCR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 148687133  91 FLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAM 138
Cdd:cd23344   81 FLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAM 128

third fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; Fascin, also called fascin-1, 55 kDa actin-bundling protein, singed-like protein, or p55, is an actin-binding protein that contains 2 major actin binding sites. It is involved in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. It plays an important role for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. It mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to nerve growth factor (NGF). Fascin is composed of four fascin beta-trefoil domains, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the third fascin-like beta-trefoil domain.

Pssm-ID: 467460 Cd Length: 123 Bit Score: 263.36 E-value: 2.53e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 260 CAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIE 339
Cdd:cd23352    1 CPQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 148687133 340 WCDRRITLRASNGKFVTAKKNGQLAASVETAGDSELFLMKLIN 382
Cdd:cd23352   81 WRDRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

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.

Pssm-ID: 467456 Cd Length: 120 Bit Score: 259.76 E-value: 5.83e-86

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 139 HPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFRS 218
Cdd:cd23348    1 HPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLVFQDQRYSVQTSDHRFLRHDGRLVARPEPATGYTLEFRS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 148687133 219 GKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQ 258
Cdd:cd23348   81 GKVAFRDCEGRYLAPSGPSGTLKAGKSTKVGKDELFVLEQ 120

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.

Pssm-ID: 467453 [Multi-domain] Cd Length: 130 Bit Score: 241.26 E-value: 1.55e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133   8 EAVQIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQppDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPDG 87
Cdd:cd23345    2 QALKIQFGLINCENRYLTAEAFGFKVNASAPSLKKKQIWTLEQ--DEGDSSVVFLKSHLGRYLSADKDGKVSCEAEKPGR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148687133  88 DCRFLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAM 138
Cdd:cd23345   80 DCRFLIVAQSDGRWALQSEPHKRFFGGSEDKLSCFAQTITEAELWAVHLAI 130

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.

Pssm-ID: 467442 [Multi-domain] Cd Length: 125 Bit Score: 219.77 E-value: 2.39e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133  12 IQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQppDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCRF 91
Cdd:cd23334    1 WKLGLINSSGKYLTAETFGFKVNASGTSLKKKQTWTLEQ--DEGGSETVYLKSHLGRYLSADKDGKVTCDAEEPGADERF 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148687133  92 LVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAM 138
Cdd:cd23334   79 LIEYQPDGRWALKSEKHGRYLGGTGDNLSCFAKEVSESELWTVHLAI 125

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.

Pssm-ID: 467464 Cd Length: 111 Bit Score: 213.59 E-value: 4.89e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 383 RPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKVA 462
Cdd:cd23356    1 RPIIVLRGEHGFIGCRKVTGTLDSNRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 148687133 463 LKVGGRYLKGDHAGVLKACAETIDPASLWEY 493
Cdd:cd23356   81 IKVGGRYLKGDHAGVLKASAETVDPATLWEY 111

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

Pssm-ID: 467457 Cd Length: 119 Bit Score: 206.22 E-value: 3.31e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 139 HPQVNIYSVTRKRYAHLSArPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFRS 218
Cdd:cd23349    1 HPQANLLSVSRRRYAHLSV-QEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 148687133 219 GKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQ 258
Cdd:cd23349   80 GKLAFKDCDGKYLTPMGPTGTLKSGRSSKPGKDELFDLEE 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.

Pssm-ID: 467443 Cd Length: 117 Bit Score: 199.31 E-value: 1.52e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 140 PQVNIYSVTRKRYAHLSARPaDEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFRSG 219
Cdd:cd23335    1 PQVNLYSVNRKRYARLDPEG-DELRVDEDIPWGSDALITLEFDDGRYALRTSDGRYLRSDGSLVDEPSDDTLFTLEFRSG 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 148687133 220 KVAFRDCEGRYLAPSGPSGTLKAGKaTKVGKDELFALE 257
Cdd:cd23335   80 GLAFKDSEGKYLTAVGGSGVLKTRK-KTVGKDELFSLE 116

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.

Pssm-ID: 467444 Cd Length: 124 Bit Score: 195.90 E-value: 3.90e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 260 CAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIE 339
Cdd:cd23336    1 HPQVSLRAHNGKYVSIRQGVDVSANQDEETDTETFQLEFDKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 148687133 340 W-CDRRITLRASNGKFVTAKKNGQLAASVETAGDSELFLMKLIN 382
Cdd:cd23336   81 WnDGGTVALKASNGKYVTAKPNGQLAATSDEVGEKEKFTLKLIN 124

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.

Pssm-ID: 467461 Cd Length: 123 Bit Score: 184.33 E-value: 1.15e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 262 QVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWC 341
Cdd:cd23353    3 QVVFQAANGRYVSIRQGVNVSANQDEETDHETFQMQIDKETKKCSFHTNTGKYWTLVAHGGIQSTATEVAANTMFDIEWR 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 148687133 342 DRRITLRASNGKFVTAKKNGQLAASVETAGDSELFLMKLIN 382
Cdd:cd23353   83 GRRVALKASNGKYVCTKKNGQLAAVSDSVGEDEEFTLKLIN 123

first fascin-like domain, beta-trefoil fold, found in Drosophila melanogaster protein singed and similar proteins; Protein singed acts as an actin-bundling protein that may have a role in the asymmetric organization and/or movement of cytoplasmic components. It has a role in somatic cells during the formation of adult bristles and hairs, and in the female germline during oogenesis. It interacts with Rab35, with stronger binding to the Rab35-GTP form compared to the Rab35-GDP form. Protein singed is composed of four fascin beta-trefoil domains, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the first fascin-like beta-trefoil domain.

Pssm-ID: 467455 Cd Length: 130 Bit Score: 154.92 E-value: 2.01e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133  15 GLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDeaGSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCRF-LV 93
Cdd:cd23347    7 GLINSQQKYLTAETFGFKVNANGSSLKKKQLWTLEPFGD--GTNVVALRSHLGRYLSVDQFGNVTCEAEEKGEGSRFeIV 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 148687133  94 VAHD-DGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIA 137
Cdd:cd23347   85 ISEDeSGRWAFRNEERGYFLGGSGDKLVCTAKAPTDSELWTVHLA 129

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.

Pssm-ID: 467459 Cd Length: 119 Bit Score: 145.61 E-value: 5.72e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 139 HPQVNIYSVTRKRYAHLSArPADEIAVDRDVPWGVDSLITLAF-QDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFR 217
Cdd:cd23351    1 RPQVNLRSAGRKRYARLSG-DEDEIQVDANVPWGSDTLFTLEFrDDGRYAIHTANGKYLNRDGKLVEECPEDCLFTLEYH 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 148687133 218 SGKVAFRDCEGRYLAPSGPSGTLKAgKATKVGKDELFALE 257
Cdd:cd23351   80 AGQVAFRDRTGKYLAPIGSKAVLRT-RSTSVTKDELFILE 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.

Pssm-ID: 467445 Cd Length: 114 Bit Score: 140.77 E-value: 2.59e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 383 RPIIVFRGEHGFIGCRKVT-GTLDANRSSYDVFQLEF-NDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNK 460
Cdd:cd23337    1 RPILVLRGEYGFVGVKSGSsGKLECNKSTYDVFQLEYnNDGAYHLKGSNGKYWSVDSDGSVTADSAAPTPFILEFRGQSK 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 148687133 461 VALKV-GGRYLKGDHAGVLKACAETIDPASLWEY 493
Cdd:cd23337   81 LAIKApNGKYLKGEQNGLFKATGTEVDKATLWEY 114

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.

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 135.92 E-value: 2.04e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133   21 NKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDeagSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCRFLVVAHddGR 100
Cdd:pfam06268   2 NGYLVSERRGAHLNANRESLKRVQTFTLEFDDE---RYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFR--GR 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 148687133  101 WSLQSEAHRRYFG-GTEDRLSCFAQSVSPAEKWSV 134
Cdd:pfam06268  77 WALLRESNGRYLGgGPSGLLKANASTVGKDELWTL 111

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.

Pssm-ID: 467465 Cd Length: 112 Bit Score: 134.16 E-value: 8.97e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 383 RPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKVA 462
Cdd:cd23357    1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRVA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 148687133 463 LKV-GGRYLKGDHAGVLKACAETIDPASLWEY 493
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.

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 130.53 E-value: 1.92e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133  268 ANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCDRRITL 347
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 148687133  348 RASNGKFVTAKKNGQLAASVETAGDSELFLM 378
Cdd:pfam06268  81 RESNGRYLGGGPSGLLKANASTVGKDELWTL 111

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.

Pssm-ID: 467463 Cd Length: 125 Bit Score: 114.60 E-value: 2.41e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 263 VVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWC- 341
Cdd:cd23355    5 AFIAGLNSRYVSVKQGVDVTANQDEISDHETFQLEYDWSTKRWYIRTMQDRYWTLETAGGIQASADKKSANALFELEWQe 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 148687133 342 DRRITLRASNGKFVTAKKNGQLAASVETAGDSELFLMKLIN 382
Cdd:cd23355   85 DGSVSFRANNGKFVGTKRSGHLFANSESIDEIAKFYFYLIN 125

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

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 104.72 E-value: 6.14e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133  142 VNIYSVTRKRYAHLSARPADEIAVDrdvpwgvdsLITLAFQDQRYSV--QTSDHRFLR--HDGRLVARPE---PATGFTL 214
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQ---------TFTLEFDDERYTVylRSHNGKYLScdADGRVVCEAErrsADTFFEL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 148687133  215 EFRSGKVAFRDCEGRYLApSGPSGTLKAgKATKVGKDELFAL 256
Cdd:pfam06268  72 EFRGRWALLRESNGRYLG-GGPSGLLKA-NASTVGKDELWTL 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.

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 88.54 E-value: 3.16e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133  391 EHGFIGCRKVTGTLDANR---SSYDVFQLEFNDGAYN--IKDSTGKYWTVGSDSS-VTSSSDTPVDFFLEFCDYNKVALK 464
Cdd:pfam06268   1 ANGYLVSERRGAHLNANReslKRVQTFTLEFDDERYTvyLRSHNGKYLSCDADGRvVCEAERRSADTFFELEFRGRWALL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 148687133  465 --VGGRYLKGDHAGVLKACAETIDPASLWEY 493
Cdd:pfam06268  81 reSNGRYLGGGPSGLLKANASTVGKDELWTL 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.

Pssm-ID: 467454 Cd Length: 127 Bit Score: 84.91 E-value: 1.13e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133  12 IQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCRF 91
Cdd:cd23346    1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVIVSDYSDRQAVVELKGPQGLYLLVDKDGLVRCGTPDTKHHGLF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148687133  92 LVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAM 138
Cdd:cd23346   81 LLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127

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.

Pssm-ID: 467462 Cd Length: 123 Bit Score: 79.02 E-value: 1.25e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 261 AQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEW 340
Cdd:cd23354    2 TWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVEW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 148687133 341 CDRRITLRASNGKFVTAKKNGQLAASVETAGDSELFLMKLIN 382
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.

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 78.08 E-value: 2.26e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 262 QVVLQAANERNVSTRQGMD--LSANQDEETDQETFQLeIDRDTRKCAFRTHTGKYWTLTATGG--VQSTASTKNASCYFD 337
Cdd:cd00257    2 TVALKSSNGKYLSAENGGGgpLVANRDAAGPWETFTL-VDLGDGKVALKSSNGKYLSAENGGGgtLVANRTAIGPWETFT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 148687133 338 IEWC-DRRITLRASNGKFVTAKKN--GQLAASVETAGDSELF 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.

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 71.53 E-value: 5.35e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133  13 QFGLISCGNKYLTAEAFGF-KVNASASSLKKKQIWTLEQPPDeaGSaaVCLRSHLGRYLAADKDGN--VTCEREVPDGDC 89
Cdd:cd00257    2 TVALKSSNGKYLSAENGGGgPLVANRDAAGPWETFTLVDLGD--GK--VALKSSNGKYLSAENGGGgtLVANRTAIGPWE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 148687133  90 RFLVVAHDDGRWSLQSeAHRRYF---GGTEDRLSCFAQSVSPAEKWSV 134
Cdd:cd00257   78 TFTLVPLGNGKVALKS-ANGKYLsadNGGGGTLIANATSIGAWEKFTI 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.

Pssm-ID: 467458 Cd Length: 119 Bit Score: 71.36 E-value: 5.61e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 139 HPQVNIYSVTRKRYAHlsARPA-DEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFR 217
Cdd:cd23350    1 HVHVVLYNIRSRCYAQ--ADPEeDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 148687133 218 SG-KVAFRDCEGRYLAPSGPSGTLKAGKaTKVGKDELFALEQ 258
Cdd:cd23350   79 PGyLASFFDDCGSMLYPQGRSRLLLSGN-IPINEEEWFIIKR 119

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

Pssm-ID: 467444 Cd Length: 124 Bit Score: 67.24 E-value: 1.58e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 212 FTLEF--RSGKVAFRDCEGRYLApSGPSGTLKAgKATKVGKDELFALE-QSCAQVVLQAANERNVSTRQGMDLSANQDEE 288
Cdd:cd23336   35 FQLEFdkETKKWAFRTNKGKYWS-LGPDGGIQA-TASSRSPNCLFELEwNDGGTVALKASNGKYVTAKPNGQLAATSDEV 112

                         90
                 ....*....|
gi 148687133 289 TDQETFQLEI 298
Cdd:cd23336  113 GEKEKFTLKL 122

fourth fascin-like domain, beta-trefoil fold, found in Drosophila melanogaster protein singed and similar proteins; Protein singed acts as an actin-bundling protein that may have a role in the asymmetric organization and/or movement of cytoplasmic components. It has a role in somatic cells during the formation of adult bristles and hairs, and in the female germline during oogenesis. It interacts with Rab35, with stronger binding to the Rab35-GTP form compared to the Rab35-GDP form. Protein singed is composed of four fascin beta-trefoil domains, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the fourth fascin-like beta-trefoil domain.

Pssm-ID: 467467 Cd Length: 113 Bit Score: 66.70 E-value: 2.02e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 383 RPIIVFRGEHGFIGCRKVTGT-LDANRSSYDVFQLEFND-GAYNIKDSTGKYWTVGSDSSVTSSSDtPVDFFLEFCDYNK 460
Cdd:cd23359    1 RPILVLKCEQGFVGYKSGSNPkLECNKASYETIQVERGDkGLVFFKGQSGKYWGVCGDGITADADA-PEGFYLELREPSR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 148687133 461 VALKVG-GRYLKGDHAGVLKACAETIDPASLWEY 493
Cdd:cd23359   80 LCIKTAdGSYLMADKNGAFKVGDADPETATLWEF 113

fourth fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, also called testis fascin, is a novel paralog of the actin-bundling protein fascin expressed specifically in the elongate spermatid head. Fascin-3 is composed of four fascin beta-trefoil domains, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the fourth fascin-like beta-trefoil domain.

Pssm-ID: 467466 Cd Length: 113 Bit Score: 63.28 E-value: 2.59e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 383 RPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQL-EFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKV 461
Cdd:cd23358    1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLlPCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 148687133 462 A-LKVGGRYLKGDHAGVLKACAETIDPASLWEY 493
Cdd:cd23358   81 AiLAPNGCYLRGDNSGTLLADSEIITSECLWEF 113

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.

Pssm-ID: 467445 Cd Length: 114 Bit Score: 61.04 E-value: 1.83e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 289 TDQETFQLEIDRDtRKCAFRTHTGKYWTLTATGGVQSTASTKNAscyFDIEWCDR-RITLRASNGKFVTAKKNGQLAASV 367
Cdd:cd23337   28 STYDVFQLEYNND-GAYHLKGSNGKYWSVDSDGSVTADSAAPTP---FILEFRGQsKLAIKAPNGKYLKGEQNGLFKATG 103


                 ....*....
gi 148687133 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.

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 60.36 E-value: 3.29e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 303 RKCAFRTHTGKYWTLTATGG--VQSTASTKNASCYFDIE-WCDRRITLRASNGKFVTA--KKNGQLAASVETAGDSELFL 377
Cdd:cd00257    1 GTVALKSSNGKYLSAENGGGgpLVANRDAAGPWETFTLVdLGDGKVALKSSNGKYLSAenGGGGTLVANRTAIGPWETFT 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 148687133 378 MKLINRPIIVFRGEHG-FIGCRK-VTGTLDANRSS 410
Cdd:cd00257   81 LVPLGNGKVALKSANGkYLSADNgGGGTLIANATS 115

fascin-like domain, beta-trefoil fold, found in fungal FRG1 and similar proteins; This group includes Schizosaccharomyces pombe protein FRG1 (SpFRG1), which may have a role in the processing of pre-rRNA or in the assembly of rRNA into ribosomal subunits. It is a component of the spliceosome and may be involved in pre-mRNA splicing. SpFRG1 contains a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

Pssm-ID: 467447 Cd Length: 160 Bit Score: 61.42 E-value: 3.97e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133  55 AGSAAVCLRSHLGRYLAADKDGNVTCERE--------VPdgdcrflVVAHDDGRWSLQSeAHRRYFGGTEDRLSCF---- 122
Cdd:cd23339   73 VGTGKVTLKSAHGKYLSCDKFGVVTATREargpqeewTP-------VPRPDGGGFALQS-VYGKYLSVDEVAGGKLvvra 144

                         90
                 ....*....|...
gi 148687133 123 -AQSVSPAEKWSV 134
Cdd:cd23339  145 dAETVGFCETWRV 157

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.

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 59.21 E-value: 1.09e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 184 QRYSVQTSDHRFLR----HDGRLVARPEPATG---FTLEF-RSGKVAFRDCEGRYL-APSGPSGTLKAGkATKVGKDELF 254
Cdd:cd00257    1 GTVALKSSNGKYLSaengGGGPLVANRDAAGPwetFTLVDlGDGKVALKSSNGKYLsAENGGGGTLVAN-RTAIGPWETF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 148687133 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.

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 54.58 E-value: 4.02e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 343 RRITLRASNGKFVTA--KKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHG-FIGCRK-VTGTLDANRSSYD---VFQ 415
Cdd:cd00257    1 GTVALKSSNGKYLSAenGGGGPLVANRDAAGPWETFTLVDLGDGKVALKSSNGkYLSAENgGGGTLVANRTAIGpweTFT 80

                         90       100
                 ....*....|....*....|.
gi 148687133 416 LEFN-DGAYNIKDSTGKYWTV 435
Cdd:cd00257   81 LVPLgNGKVALKSANGKYLSA 101

fascin-like domain, beta-trefoil fold, found in Zobellia galactanivorans beta-porphyranase A (PorA) and similar proteins; PorA (EC 3.2.1.178) cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. It is inactive on the non-sulfated agarose portion of the porphyran backbone and displays a strict requirement for C6-sulfate in the -2 and +1-binding subsites. Members of this subfamily contain a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

Pssm-ID: 467450 [Multi-domain] Cd Length: 122 Bit Score: 48.00 E-value: 7.50e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 262 QVVLQAANERNVSTRQGM-DLSANQDEETDQETFQLEiDRDTRKCAFRTHTGKYwtLTATGGVQS---TASTKNASCYFD 337
Cdd:cd23342    3 TISLKGNNGKYVSSENGNkPMTANRTSVGSWEKFTVV-DAGNGKVALKGNNGKY--VSSENGTKPmtcNRTTIGAWEKFT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 148687133 338 -IEWCDRRITLRASNGKFVTAKKNGQ-LAASVETAGDSELF 376
Cdd:cd23342   80 wISLGNGTVALKGNNGKYVSSENGTNpMTCNRTSIGGWEKF 120

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.

Pssm-ID: 467451 Cd Length: 133 Bit Score: 47.58 E-value: 1.24e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 220 KVAFRDCE-GRYLAPSGPSGTLKAGKATkVGKDELFALEQ-SCAQVVLQA-ANERNVSTRQGMDLSANQDEETD---QET 293
Cdd:cd23343    4 RIALRSAAtGKYVTVGEEGGALAADAED-AEEAETFELTDwGWGSHTLRSvANGKYVTTDDDGTLTASAEEAFGwfvKEV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148687133 294 FQLEIDRDTRkCAFRTHTGKYWTLTATGGVQSTASTKNASC-YFDIE 339
Cdd:cd23343   83 FRLEPQEDGT-VSLRTWNGRPVAVDEDGRLTVGEDDAAAEAeRFEKE 128

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.

Pssm-ID: 467450 [Multi-domain] Cd Length: 122 Bit Score: 46.46 E-value: 2.37e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 344 RITLRASNGKFVTAKK-NGQLAASVETAGDSELFLMKLINRPIIVFRGEHG-FIGCRKVTGTLDANRSSYDV---FQLEF 418
Cdd:cd23342    3 TISLKGNNGKYVSSENgNKPMTANRTSVGSWEKFTVVDAGNGKVALKGNNGkYVSSENGTKPMTCNRTTIGAwekFTWIS 82

                         90
                 ....*....|....*
gi 148687133 419 -NDGAYNIKDSTGKY 432
Cdd:cd23342   83 lGNGTVALKGNNGKY 97

fascin-like domain, beta-trefoil fold, found in FSHD region gene 1 protein (FRG1) and similar proteins; Protein FRG1 binds to mRNA in a sequence-independent manner. It may play a role in the regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. It may be involved in mRNA transport, as well as in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase KMT5B. FRG1 contains a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

Pssm-ID: 467446 Cd Length: 141 Bit Score: 46.37 E-value: 3.50e-06

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148687133 304 KCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCDRRITLRASNGKFVTAKKNGQLAASVETAGDSELF 376
Cdd:cd23338   64 KIALKSGYGKYLSVDSDGKVVGRSDAIGPREQWEPVFQDGKMALLGANNCFLSVNEDGDIVATSKTAGENEMI 136

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.

Pssm-ID: 467462 Cd Length: 123 Bit Score: 45.89 E-value: 4.03e-06

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148687133 185 RYSVQTSdHRFLRHDGRlvaRPEPATGFTLEFRSGKVAFRDCEGRYLAPSgPSGTLKAgKATKVGKDELFAL 256
Cdd:cd23354   54 RYLAQRG-HRSVIADGK---GTESETFFRVEWRCGKIILQASNGRYLGVK-PNGLLTA-SALLPGPNEEFGV 119

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.

Pssm-ID: 467445 Cd Length: 114 Bit Score: 42.55 E-value: 4.67e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148687133 186 YSVQTSDHRFLR--HDGRLVARPEPATGFTLEFRSG-KVAFRDCEGRYLApSGPSGTLKAgKATKVGKDELF 254
Cdd:cd23337   43 YHLKGSNGKYWSvdSDGSVTADSAAPTPFILEFRGQsKLAIKAPNGKYLK-GEQNGLFKA-TGTEVDKATLW 112

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.

Pssm-ID: 467451 Cd Length: 133 Bit Score: 41.41 E-value: 2.13e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148687133 306 AFRT-HTGKYWTLTATGGVQS-TASTKNASCYFDIE-WCDRRITLRA-SNGKFVTAKKNGQLAASVETAGD 372
Cdd:cd23343    6 ALRSaATGKYVTVGEEGGALAaDAEDAEEAETFELTdWGWGSHTLRSvANGKYVTTDDDGTLTASAEEAFG 76

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.

Pssm-ID: 467451 Cd Length: 133 Bit Score: 40.64 E-value: 3.05e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 262 QVVLQ-AANERNVSTRQGMD-LSANQDEETDQETFQLEiDRDTRKCAFRTH-TGKYWTLTATGGVQSTAS------TKNA 332
Cdd:cd23343    4 RIALRsAATGKYVTVGEEGGaLAADAEDAEEAETFELT-DWGWGSHTLRSVaNGKYVTTDDDGTLTASAEeafgwfVKEV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 148687133 333 scyFDIE-WCDRRITLRASNGKFVTAKKNGQLAASVETA-GDSELF 376
Cdd:cd23343   83 ---FRLEpQEDGTVSLRTWNGRPVAVDEDGRLTVGEDDAaAEAERF 125

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.

Pssm-ID: 467462 Cd Length: 123 Bit Score: 39.34 E-value: 8.30e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 205 RPEPATGFTLEF--RSGKVAFRDCEGRYLAPSGPSGTLKAGKATKvgKDELFALEQSCAQVVLQAANERNVSTRQGMDLS 282
Cdd:cd23354   28 RLTPLSLFQFEVdpNTPAVQLRTVNGRYLAQRGHRSVIADGKGTE--SETFFRVEWRCGKIILQASNGRYLGVKPNGLLT 105

                         90
                 ....*....|..
gi 148687133 283 ANQDEETDQETF 294
Cdd:cd23354  106 ASALLPGPNEEF 117

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.

Pssm-ID: 467444 Cd Length: 124 Bit Score: 39.12 E-value: 9.28e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133  11 QIQFGLISCGNKYLTAeAFGFKVNASASSLKKKQIWTLEQppdEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCR 90
Cdd:cd23336    1 HPQVSLRAHNGKYVSI-RQGVDVSANQDEETDTETFQLEF---DKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCL 76

                         90
                 ....*....|....*
gi 148687133  91 FLVVAHDDGRWSLQS 105
Cdd:cd23336   77 FELEWNDGGTVALKA 91

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.

Pssm-ID: 467449 Cd Length: 115 Bit Score: 39.03 E-value: 1.02e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 304 KCAFRTHTGKYwtLTATGGVQSTAS-TKNASCYFDIEWC-DRRITLRASNGKFVTAKKNGQLAASVETAGDSELFLMKLI 381
Cdd:cd23341    2 KRAFKSHNGHF--LSAEDGVVKTEHgHHDHHTHFHIENHgDDKVAIKTHHGKYVAIDDNKQVYLSHHHHGDHTKFHLEHH 79

                         90
                 ....*....|....*.
gi 148687133 382 NRPiIVFRGEHG-FIG 396
Cdd:cd23341   80 GGK-VAIKGHHHhYIG 94

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.

Pssm-ID: 467450 [Multi-domain] Cd Length: 122 Bit Score: 37.98 E-value: 2.58e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 218 SGKVAFRDCEGRYLAPSGPSGTLKAGKATkVGKDELFALE-QSCAQVVLQAANERNVSTRQGMD-LSANQDEETDQETFQ 295
Cdd:cd23342   43 NGKVALKGNNGKYVSSENGTKPMTCNRTT-IGAWEKFTWIsLGNGTVALKGNNGKYVSSENGTNpMTCNRTSIGGWEKFT 121

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.

Pssm-ID: 368803 Cd Length: 189 Bit Score: 38.94 E-value: 3.14e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148687133  301 DTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCDRRITLRASNGKFVTAKKNGQLAASVETAGDSELF 376
Cdd:pfam06229  36 SDEKIALKSGYGKYLGVNKDGILSARADAIGPREQFEPVFQEGKMALLAANGCFLSVDPSGDIVAKSKTAGEGEMV 111

fourth fascin-like domain, beta-trefoil fold, found in Drosophila melanogaster protein singed and similar proteins; Protein singed acts as an actin-bundling protein that may have a role in the asymmetric organization and/or movement of cytoplasmic components. It has a role in somatic cells during the formation of adult bristles and hairs, and in the female germline during oogenesis. It interacts with Rab35, with stronger binding to the Rab35-GTP form compared to the Rab35-GDP form. Protein singed is composed of four fascin beta-trefoil domains, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the fourth fascin-like beta-trefoil domain.

Pssm-ID: 467467 Cd Length: 113 Bit Score: 36.27 E-value: 9.05e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148687133 292 ETFQLEIDrDTRKCAFRTHTGKYWTLtATGGVQSTASTKNAscyFDIEWCD-RRITLRASNGKFVTAKKNGQL---AASV 367
Cdd:cd23359   31 ETIQVERG-DKGLVFFKGQSGKYWGV-CGDGITADADAPEG---FYLELREpSRLCIKTADGSYLMADKNGAFkvgDADP 105


                 ...
gi 148687133 368 ETA 370
Cdd:cd23359  106 ETA 108