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: 263.63 E-value: 2.56e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  11 VIRFGLINADNKYLTAEMFGFKINASASSMKKKQVWTLEQSGDHGDSNAVFIKSHLGRYLASDKDGKVTADSEQPGPDCR 90
Cdd:cd23344    1 QIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPGDEADSSAVLLRSHLGRYLAADKDGNVTCESEVPGPDCR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 528467430  91 FLVIAHDDGRWSLQSEPHARYLGGTEDRIACFAQSISPAEKWNVHLAV 138
Cdd:cd23344   81 FLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAM 128

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: 230.86 E-value: 1.81e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430   8 ETLVIRFGLINADNKYLTAEMFGFKINASASSMKKKQVWTLEQsgDHGDSNAVFIKSHLGRYLASDKDGKVTADSEQPGP 87
Cdd:cd23345    2 QALKIQFGLINCENRYLTAEAFGFKVNASAPSLKKKQIWTLEQ--DEGDSSVVFLKSHLGRYLSADKDGKVSCEAEKPGR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528467430  88 DCRFLVIAHDDGRWSLQSEPHARYLGGTEDRIACFAQSISPAEKWNVHLAV 138
Cdd:cd23345   80 DCRFLIVAQSDGRWALQSEPHKRFFGGSEDKLSCFAQTITEAELWAVHLAI 130

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: 220.09 E-value: 1.71e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 139 HPQVNVYSIARKRYAHLCADR-NELAVDRDVPWGVDSLLTLVYLDHRYHLQTADNRFLSCGGTLTAKPDRDTGFTLEFRA 217
Cdd:cd23348    1 HPQVNIYSVTRKRYAHLSARPaDEIAVDRDVPWGVDSLITLVFQDQRYSVQTSDHRFLRHDGRLVARPEPATGYTLEFRS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 528467430 218 GKVAFRDATGKYIAPTGPTGTMKSGRSARVGKDELFVLEQ 257
Cdd:cd23348   81 GKVAFRDCEGRYLAPSGPSGTLKAGKSTKVGKDELFVLEQ 120

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: 213.22 E-value: 7.63e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  12 IRFGLINADNKYLTAEMFGFKINASASSMKKKQVWTLEQsgDHGDSNAVFIKSHLGRYLASDKDGKVTADSEQPGPDCRF 91
Cdd:cd23334    1 WKLGLINSSGKYLTAETFGFKVNASGTSLKKKQTWTLEQ--DEGGSETVYLKSHLGRYLSADKDGKVTCDAEEPGADERF 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 528467430  92 LVIAHDDGRWSLQSEPHARYLGGTEDRIACFAQSISPAEKWNVHLAV 138
Cdd:cd23334   79 LIEYQPDGRWALKSEKHGRYLGGTGDNLSCFAKEVSESELWTVHLAI 125

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: 205.97 E-value: 5.96e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 261 QVVLTASNDRNISMRQGVDLSANQDEESDQEVFQMEMDRESKRCAFRSFNGRYWSLTSSGAIQCSALTKSPSCFFDLEWK 340
Cdd:cd23352    3 QVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIEWR 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 528467430 341 GSKVALKASNGKYLAAKKNGQLAAAVDSAGEQEEFVLKLIN 381
Cdd:cd23352   83 DRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

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: 195.82 E-value: 4.16e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 139 HPQVNVYSIARKRYAHLCADRNELAVDRDVPWGVDSLLTLVYLDHRYHLQTADNRFLSCGGTLTAKPDRDTGFTLEFRAG 218
Cdd:cd23349    1 HPQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKAG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 528467430 219 KVAFRDATGKYIAPTGPTGTMKSGRSARVGKDELFVLEQ 257
Cdd:cd23349   81 KLAFKDCDGKYLTPMGPTGTLKSGRSSKPGKDELFDLEE 119

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: 190.86 E-value: 2.41e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 382 RPLIVLRGEHGFIGCRKQgTGTLDSNRSSYDVFQLEYNNNAYSLRDSVGKYWTVESDGSVISSGAAPVYFHFEFCDFNKV 461
Cdd:cd23356    1 RPIIVLRGEHGFIGCRKV-TGTLDSNRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKV 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 528467430 462 AIKTkEGKYLKGDHAGVLKASAQGIADATLWEY 494
Cdd:cd23356   80 AIKV-GGRYLKGDHAGVLKASAETVDPATLWEY 111

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: 188.58 E-value: 2.39e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 259 HGQVVLTASNDRNISMRQGVDLSANQDEESDQEVFQMEMDRESKRCAFRSFNGRYWSLTSSGAIQCSALTKSPSCFFDLE 338
Cdd:cd23336    1 HPQVSLRAHNGKYVSIRQGVDVSANQDEETDTETFQLEFDKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 528467430 339 W-KGSKVALKASNGKYLAAKKNGQLAAAVDSAGEQEEFVLKLIN 381
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: 179.70 E-value: 6.63e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 259 HGQVVLTASNDRNISMRQGVDLSANQDEESDQEVFQMEMDRESKRCAFRSFNGRYWSLTSSGAIQCSALTKSPSCFFDLE 338
Cdd:cd23353    1 HPQVVFQAANGRYVSIRQGVNVSANQDEETDHETFQMQIDKETKKCSFHTNTGKYWTLVAHGGIQSTATEVAANTMFDIE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 528467430 339 WKGSKVALKASNGKYLAAKKNGQLAAAVDSAGEQEEFVLKLIN 381
Cdd:cd23353   81 WRGRRVALKASNGKYVCTKKNGQLAAVSDSVGEDEEFTLKLIN 123

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: 176.20 E-value: 1.40e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 140 PQVNVYSIARKRYAHLCADRNELAVDRDVPWGVDSLLTLVYLDHRYHLQTADNRFLSCGGTLTAKPDRDTGFTLEFRAGK 219
Cdd:cd23335    1 PQVNLYSVNRKRYARLDPEGDELRVDEDIPWGSDALITLEFDDGRYALRTSDGRYLRSDGSLVDEPSDDTLFTLEFRSGG 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 528467430 220 VAFRDATGKYIAPTGPTGTMKSGRSaRVGKDELFVLE 256
Cdd:cd23335   81 LAFKDSEGKYLTAVGGSGVLKTRKK-TVGKDELFSLE 116

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: 164.66 E-value: 2.64e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 382 RPLIVLRGEHGFIGCRKQGTGTLDSNRSSYDVFQLEYNNN-AYSLRDSVGKYWTVESDGSVISSGAAPVYFHFEFCDFNK 460
Cdd:cd23337    1 RPILVLRGEYGFVGVKSGSSGKLECNKSTYDVFQLEYNNDgAYHLKGSNGKYWSVDSDGSVTADSAAPTPFILEFRGQSK 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 528467430 461 VAIKTKEGKYLKGDHAGVLKASAQGIADATLWEY 494
Cdd:cd23337   81 LAIKAPNGKYLKGEQNGLFKATGTEVDKATLWEY 114

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: 152.22 E-value: 2.58e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  15 GLINADNKYLTAEMFGFKINASASSMKKKQVWTLEQSGDhgDSNAVFIKSHLGRYLASDKDGKVTADSEQPGPDCRF-LV 93
Cdd:cd23347    7 GLINSQQKYLTAETFGFKVNANGSSLKKKQLWTLEPFGD--GTNVVALRSHLGRYLSVDQFGNVTCEAEEKGEGSRFeIV 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 528467430  94 IAHD-DGRWSLQSEPHARYLGGTEDRIACFAQSISPAEKWNVHLAV 138
Cdd:cd23347   85 ISEDeSGRWAFRNEERGYFLGGSGDKLVCTAKAPTDSELWTVHLAA 130

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: 144.07 E-value: 2.09e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 139 HPQVNVYSIARKRYAHLCADRNELAVDRDVPWGVDSLLTLVY-LDHRYHLQTADNRFLSCGGTLTAKPDRDTGFTLEFRA 217
Cdd:cd23351    1 RPQVNLRSAGRKRYARLSGDEDEIQVDANVPWGSDTLFTLEFrDDGRYAIHTANGKYLNRDGKLVEECPEDCLFTLEYHA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 528467430 218 GKVAFRDATGKYIAPTGPTGTMKSgRSARVGKDELFVLE 256
Cdd:cd23351   81 GQVAFRDRTGKYLAPIGSKAVLRT-RSTSVTKDELFILE 118

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: 141.47 E-value: 1.39e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 382 RPLIVLRGEHGFIgCRKQGTGTLDSNRSSYDVFQLEYNNNAYSLRDSVGKYWTVESDGSVISSGAAPVYFHFEFCDFNKV 461
Cdd:cd23357    1 RPILVLRGEHGFV-CHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRV 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 528467430 462 AIKTKEGKYLKGDHAGVLKASAQGIADATLWEY 494
Cdd:cd23357   80 AIKGKNGKYLRGDQAGTLKADAETVDSATLWEY 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: 121.67 E-value: 4.07e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430   21 NKYLTAEMFGFKINASASSMKKKQVWTLEQSGDhgdSNAVFIKSHLGRYLASDKDGKVTADSEQPGPDCRFLVIAHddGR 100
Cdd:pfam06268   2 NGYLVSERRGAHLNANRESLKRVQTFTLEFDDE---RYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFR--GR 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 528467430  101 WSLQSEPHARYLG-GTEDRIACFAQSISPAEKWNV 134
Cdd:pfam06268  77 WALLRESNGRYLGgGPSGLLKANASTVGKDELWTL 111

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

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 120.13 E-value: 1.28e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  268 NDRNISMRQGVDLSANQDEESDQEVFQMEMDRESKRCAFRSFNGRYWSLTSSGAIQCSALTKSPSCFFDLEWKGSKVALK 347
Cdd:pfam06268   2 NGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALLR 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 528467430  348 ASNGKYLAAKKNGQLAAAVDSAGEQEEFVL 377
Cdd:pfam06268  82 ESNGRYLGGGPSGLLKANASTVGKDELWTL 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: 116.14 E-value: 6.52e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 262 VVLTASNDRNISMRQGVDLSANQDEESDQEVFQMEMDRESKRCAFRSFNGRYWSLTSSGAIQCSALTKSPSCFFDLEWKG 341
Cdd:cd23355    5 AFIAGLNSRYVSVKQGVDVTANQDEISDHETFQLEYDWSTKRWYIRTMQDRYWTLETAGGIQASADKKSANALFELEWQE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 528467430 342 S-KVALKASNGKYLAAKKNGQLAAAVDSAGEQEEFVLKLIN 381
Cdd:cd23355   85 DgSVSFRANNGKFVGTKRSGHLFANSESIDEIAKFYFYLIN 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: 89.42 E-value: 2.15e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 261 QVVLTASNDRNISMRQGVDLSANQDEESDQEVFQMEMDRESKRCAFRSFNGRYWSLTSSGAIQCSALTKSPSCFFDLEWK 340
Cdd:cd23354    3 WVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVEWR 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 528467430 341 GSKVALKASNGKYLAAKKNGQLAAAVDSAGEQEEFVLKLIN 381
Cdd:cd23354   83 CGKIILQASNGRYLGVKPNGLLTASALLPGPNEEFGVRLAN 123

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

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 88.16 E-value: 4.84e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  390 EHGFIGCRKQGtGTLDSNR---SSYDVFQLEYNNNAYS--LRDSVGKYWTVESDGSVISSGAAP-VYFHFEFCDFNKVAI 463
Cdd:pfam06268   1 ANGYLVSERRG-AHLNANReslKRVQTFTLEFDDERYTvyLRSHNGKYLSCDADGRVVCEAERRsADTFFELEFRGRWAL 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 528467430  464 KTK-EGKYLKGDHAGVLKASAQGIADATLWEY 494
Cdd:pfam06268  80 LREsNGRYLGGGPSGLLKANASTVGKDELWTL 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: 82.10 E-value: 7.19e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 382 RPLIVLRGEHGFIGCRKQGTGTLDSNRSSYDVFQLEYNNNAYS-LRDSVGKYWTVESDGsVISSGAAPVYFHFEFCDFNK 460
Cdd:cd23359    1 RPILVLKCEQGFVGYKSGSNPKLECNKASYETIQVERGDKGLVfFKGQSGKYWGVCGDG-ITADADAPEGFYLELREPSR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 528467430 461 VAIKTKEGKYLKGDHAGVLKASAQGIADATLWEY 494
Cdd:cd23359   80 LCIKTADGSYLMADKNGAFKVGDADPETATLWEF 113

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: 81.44 E-value: 1.71e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  12 IRFGLINADNKYLTAEMFGFKINASASSMKKKQVWTLEQSGDHGDSNAVFIKSHLGRYLASDKDGKVTADSEQPGPDCRF 91
Cdd:cd23346    1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVIVSDYSDRQAVVELKGPQGLYLLVDKDGLVRCGTPDTKHHGLF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 528467430  92 LVIAHDDGRWSLQSEPHARYLGGTEDRIACFAQSISPAEKWNVHLAV 138
Cdd:cd23346   81 LLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127

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: 79.68 E-value: 5.24e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  142 VNVYSIARKRYAHLCADRNELavdrdvpwGVDSLLTLVYLDHRY--HLQTADNRFLSCG--GTLTAKPDR---DTGFTLE 214
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESL--------KRVQTFTLEFDDERYtvYLRSHNGKYLSCDadGRVVCEAERrsaDTFFELE 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 528467430  215 FRAGKVAFRDATGKYIApTGPTGTMKSgRSARVGKDELFVL 255
Cdd:pfam06268  73 FRGRWALLRESNGRYLG-GGPSGLLKA-NASTVGKDELWTL 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.

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 79.62 E-value: 6.38e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 260 GQVVLTASNDRNISMRQGVD--LSANQDEESDQEVFQMEmDRESKRCAFRSFNGRYWSLTS--SGAIQCSALTKSPSCFF 335
Cdd:cd00257    1 GTVALKSSNGKYLSAENGGGgpLVANRDAAGPWETFTLV-DLGDGKVALKSSNGKYLSAENggGGTLVANRTAIGPWETF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 528467430 336 DLEWKGS-KVALKASNGKYLAAKKN--GQLAAAVDSAGEQEEFVL 377
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: 75.77 E-value: 1.36e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  13 RFGLINADNKYLTAEMFGF-KINASASSMKKKQVWTLEQSGDhgdsNAVFIKSHLGRYLA--SDKDGKVTADSEQPGPDC 89
Cdd:cd00257    2 TVALKSSNGKYLSAENGGGgPLVANRDAAGPWETFTLVDLGD----GKVALKSSNGKYLSaeNGGGGTLVANRTAIGPWE 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 528467430  90 RFLVIAHDDGRWSLQSePHARYL---GGTEDRIACFAQSISPAEKWNV 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: 70.20 E-value: 1.21e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 139 HPQVNVYSIARKRYAHLCADRNELAVDRDVPWGVDSLLTLVYLDHRYHLQTADNRFLSCGGTLTAKPDRDTGFTLEFRAG 218
Cdd:cd23350    1 HVHVVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 528467430 219 -KVAFRDATGKYIAPTGPTGTMKSGrSARVGKDELFVLEQ 257
Cdd:cd23350   81 yLASFFDDCGSMLYPQGRSRLLLSG-NIPINEEEWFIIKR 119

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: 69.83 E-value: 1.31e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 382 RPLIVLRGEHGFIGcRKQGTGTLDSNRSSYDVFQL-EYNNNAYSLRDSVGKYWTVESDGSVISSGAAPVYFHFEFCDFNK 460
Cdd:cd23358    1 RSFLILRGKYGYVG-SSSHHDVLQCNLPEPDQISLlPCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNL 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 528467430 461 VAIKTKEGKYLKGDHAGVLKASAQGIADATLWEY 494
Cdd:cd23358   80 LAILAPNGCYLRGDNSGTLLADSEIITSECLWEF 113

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

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 69.61 E-value: 2.19e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 302 KRCAFRSFNGRYWSLTSS--GAIQCSALTKSPSCFFDLE-WKGSKVALKASNGKYLAA--KKNGQLAAAVDSAGEQEEFV 376
Cdd:cd00257    1 GTVALKSSNGKYLSAENGggGPLVANRDAAGPWETFTLVdLGDGKVALKSSNGKYLSAenGGGGTLVANRTAIGPWETFT 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 528467430 377 LKLINRPLIVLRGEHG-FIGCRKQGTGTLDSNRSS 410
Cdd:cd00257   81 LVPLGNGKVALKSANGkYLSADNGGGGTLIANATS 115

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: 66.91 E-value: 1.87e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 342 SKVALKASNGKYLAA--KKNGQLAAAVDSAGEQEefvlklinrplivlrgehgfigcrkqgtgtldsnrssydVFQLEYN 419
Cdd:cd00257    1 GTVALKSSNGKYLSAenGGGGPLVANRDAAGPWE---------------------------------------TFTLVDL 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 420 -NNAYSLRDSVGKYWTVES--DGSVISSGAAPV---YFHFEFCDFNKVAIKTKEGKYL--KGDHAGVLKASAQGIADATL 491
Cdd:cd00257   42 gDGKVALKSSNGKYLSAENggGGTLVANRTAIGpweTFTLVPLGNGKVALKSANGKYLsaDNGGGGTLIANATSIGAWEK 121


                 ..
gi 528467430 492 WE 493
Cdd:cd00257  122 FT 123

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: 66.43 E-value: 7.64e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  56 DSNAVFIKSHLGRYLASDKDGKVTADSEQPGPDCRF-LVIAHDDGRWSLQSePHARYLGGTED-----RIACFAQSISPA 129
Cdd:cd23339   74 GTGKVTLKSAHGKYLSCDKFGVVTATREARGPQEEWtPVPRPDGGGFALQS-VYGKYLSVDEVaggklVVRADAETVGFC 152


                 ....*
gi 528467430 130 EKWNV 134
Cdd:cd23339  153 ETWRV 157

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: 59.88 E-value: 3.80e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 288 SDQEVFQMEMDRESKrCAFRSFNGRYWSLTSSGAIQCSAltKSPSCFFdLEWKG-SKVALKASNGKYLAAKKNGQLAAAV 366
Cdd:cd23337   28 STYDVFQLEYNNDGA-YHLKGSNGKYWSVDSDGSVTADS--AAPTPFI-LEFRGqSKLAIKAPNGKYLKGEQNGLFKATG 103


                 ....*....
gi 528467430 367 DSAGEQEEF 375
Cdd:cd23337  104 TEVDKATLW 112

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

Pssm-ID: 467444 Cd Length: 124 Bit Score: 59.15 E-value: 1.10e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 192 NRFLSC--GGTLTAKPDRDTG---FTLEF--RAGKVAFRDATGKYIAPtGPTGTMKSGrSARVGKDELFVLE-QSHGQVV 263
Cdd:cd23336   11 GKYVSIrqGVDVSANQDEETDtetFQLEFdkETKKWAFRTNKGKYWSL-GPDGGIQAT-ASSRSPNCLFELEwNDGGTVA 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 528467430 264 LTASNDRNISMRQGVDLSANQDEESDQEVFQMEM 297
Cdd:cd23336   89 LKASNGKYVTAKPNGQLAATSDEVGEKEKFTLKL 122

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: 54.16 E-value: 5.08e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 260 GQVV-LTASNDRNISMRQGV-DLSANQDEESDQEVFQMEmDRESKRCAFRSFNGRYWSLTSSGA-IQCSALTKSPSCFFD 336
Cdd:cd23342    1 GSTIsLKGNNGKYVSSENGNkPMTANRTSVGSWEKFTVV-DAGNGKVALKGNNGKYVSSENGTKpMTCNRTTIGAWEKFT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 528467430 337 LEWKGS-KVALKASNGKYLAAKKNGQ-LAAAVDSAGEQEEF 375
Cdd:cd23342   80 WISLGNgTVALKGNNGKYVSSENGTNpMTCNRTSIGGWEKF 120

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: 54.16 E-value: 5.38e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 341 GSKVALKASNGKYLAAKK-NGQLAAAVDSAGEQEEFVLKLINRPLIVLRGEHGFIGCRKQGTGTLDSNRSSYDV---FQL 416
Cdd:cd23342    1 GSTISLKGNNGKYVSSENgNKPMTANRTSVGSWEKFTVVDAGNGKVALKGNNGKYVSSENGTKPMTCNRTTIGAwekFTW 80

                         90       100
                 ....*....|....*....|.
gi 528467430 417 E-YNNNAYSLRDSVGKYWTVE 436
Cdd:cd23342   81 IsLGNGTVALKGNNGKYVSSE 101

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: 48.03 E-value: 7.35e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 155 LCADR---NELAVDRDVPWGvDSLLTLVYL-DHRYHLQTADNRFLSC----GGTLTAkpDRDTG-----FTLEFRA-GKV 220
Cdd:cd00257   13 LSAENgggGPLVANRDAAGP-WETFTLVDLgDGKVALKSSNGKYLSAenggGGTLVA--NRTAIgpwetFTLVPLGnGKV 89

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 528467430 221 AFRDATGKYI-APTGPTGTMKSGRSArVGKDELFVL 255
Cdd:cd00257   90 ALKSANGKYLsADNGGGGTLIANATS-IGAWEKFTI 124

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: 44.88 E-value: 1.06e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 343 KVALK-ASNGKYLAA-KKNGQLAAAVDSAGEQEEFVLKlinrplivlrgehgfigcrkqgtgtldsnrssydvfqlEYNN 420
Cdd:cd23343    4 RIALRsAATGKYVTVgEEGGALAADAEDAEEAETFELT--------------------------------------DWGW 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 421 NAYSLRDSV-GKYWTVESDGSVISSgAAPVY-------FHFEFCDFNKVAIKTKEGKYLKGDHAGVLKASAQ-GIADATL 491
Cdd:cd23343   46 GSHTLRSVAnGKYVTTDDDGTLTAS-AEEAFgwfvkevFRLEPQEDGTVSLRTWNGRPVAVDEDGRLTVGEDdAAAEAER 124


                 ..
gi 528467430 492 WE 493
Cdd:cd23343  125 FE 126

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: 44.46 E-value: 1.10e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 312 RYWSLTSSG-AIQCSALT-KSPSCFFDLEWKGSKVALKASNGKYLaaKKNGQLaaaVDSAGEQEEFVLKLinRP-LIVLR 388
Cdd:cd23335   12 RYARLDPEGdELRVDEDIpWGSDALITLEFDDGRYALRTSDGRYL--RSDGSL---VDEPSDDTLFTLEF--RSgGLAFK 84

                         90       100       110
                 ....*....|....*....|....*....|...
gi 528467430 389 GEHG-FIGCRkQGTGTLDSNRSSY---DVFQLE 417
Cdd:cd23335   85 DSEGkYLTAV-GGSGVLKTRKKTVgkdELFSLE 116

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: 44.46 E-value: 1.34e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528467430 413 VFQLEYNNNAYSLRDSVGKYwtVESDGSVISSGAAPVYFHFEFCDfNKVAIKTKEGKYLKGDHA-GVLKASAQGI 486
Cdd:cd23335   36 LITLEFDDGRYALRTSDGRY--LRSDGSLVDEPSDDTLFTLEFRS-GGLAFKDSEGKYLTAVGGsGVLKTRKKTV 107

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: 44.51 E-value: 1.39e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  30 GFKINASASSMKKKQVWTLEQsgdHGDSNAVFIKSHLGRYLASDKDGKVTADSEQPGPDCRFLVIAHDDGRWSLQSePHA 109
Cdd:cd23336   19 GVDVSANQDEETDTETFQLEF---DKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELEWNDGGTVALKA-SNG 94

                         90       100
                 ....*....|....*....|....*.
gi 528467430 110 RYLG----GtedriACFAQSISPAEK 131
Cdd:cd23336   95 KYVTakpnG-----QLAATSDEVGEK 115

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: 44.11 E-value: 2.01e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 219 KVAFRDA-TGKYIAPTGPTGTMKSGrSARVGKDELFVLEQ-SHGQVVL-TASNDRNISMRQGVDLSANQDEESD---QEV 292
Cdd:cd23343    4 RIALRSAaTGKYVTVGEEGGALAAD-AEDAEEAETFELTDwGWGSHTLrSVANGKYVTTDDDGTLTASAEEAFGwfvKEV 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 528467430 293 FQMEMDRESkRCAFRSFNGRYWSLTSSGAIQCSA 326
Cdd:cd23343   83 FRLEPQEDG-TVSLRTWNGRPVAVDEDGRLTVGE 115

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: 44.33 E-value: 4.37e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467430   44 QVWTLEQSGDHGdsnaVFIKSHLGRYLASDKDGKVTADSEQPGPDCRFLVIaHDDGRWSLQSE 106
Cdd:pfam06229  28 EVFTAVKVSDEK----IALKSGYGKYLGVNKDGILSARADAIGPREQFEPV-FQEGKMALLAA 85

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: 42.61 E-value: 5.45e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 186 HLQTADNRFLSC---GGTLTAkpDRDT-----GFTLEfRA--GKVAFRDATGKYIAPTGPTGTMKSGRSArVGKDELFVL 255
Cdd:cd23342    5 SLKGNNGKYVSSengNKPMTA--NRTSvgsweKFTVV-DAgnGKVALKGNNGKYVSSENGTKPMTCNRTT-IGAWEKFTW 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 528467430 256 E-QSHGQVVLTASNDRNISMRQGVD-LSANQDEESDQEVFQ 294
Cdd:cd23342   81 IsLGNGTVALKGNNGKYVSSENGTNpMTCNRTSIGGWEKFT 121

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: 43.32 E-value: 5.57e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528467430 342 SKVALKASNGKYLAAKKNGQLAAAVDSAGEQEEFVLKLI-NRPLIVLRGEHG-FIGC 396
Cdd:cd23339   76 GKVTLKSAHGKYLSCDKFGVVTATREARGPQEEWTPVPRpDGGGFALQSVYGkYLSV 132

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: 41.66 E-value: 1.08e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528467430 291 EVFQMEMDrESKRCAFRSFNGRYWSLTSSGAiqcSALTKSPSCFFdLEWK-GSKVALKASNGKYLAAKKNG 360
Cdd:cd23359   31 ETIQVERG-DKGLVFFKGQSGKYWGVCGDGI---TADADAPEGFY-LELRePSRLCIKTADGSYLMADKNG 96

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: 41.32 E-value: 1.26e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 280 LSANQdeeSDQEVFQMEMDRESKRcaFRSFNGRYWSLTSSGAIqCSALTKSPSCFFDLEWKGsKVALKASNGKYLAAKKN 359
Cdd:cd23357   22 LDANR---SVYDVFQLIFSDGAYQ--IKGQGGKFWYISSSGTV-CSDGDMPEDFFFEFREHG-RVAIKGKNGKYLRGDQA 94

                         90
                 ....*....|
gi 528467430 360 GQLAAAVDSA 369
Cdd:cd23357   95 GTLKADAETV 104

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: 40.64 E-value: 2.86e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 409 SSYDVFQLEYNNNA--YSLRDSVGKYWTVESDGSVISSGA---APVYFHFEFCDFNKVAIKTKEGKYLKGDHAGVLKASA 483
Cdd:cd23355   31 SDHETFQLEYDWSTkrWYIRTMQDRYWTLETAGGIQASADkksANALFELEWQEDGSVSFRANNGKFVGTKRSGHLFANS 110


                 ....*
gi 528467430 484 QGIAD 488
Cdd:cd23355  111 ESIDE 115

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: 42.02 E-value: 2.95e-04

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 528467430  342 SKVALKASNGKYLAAKKNGQLAAAVDSAGEQEEFVL 377
Cdd:pfam06229  38 EKIALKSGYGKYLGVNKDGILSARADAIGPREQFEP 73

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: 40.65 E-value: 3.25e-04

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 528467430 341 GSKVALKASNGKYLAAKKNGQLAAAVDSAGEQEEFVL 377
Cdd:cd23334   44 SETVYLKSHLGRYLSADKDGKVTCDAEEPGADERFLI 80

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: 40.98 E-value: 3.29e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 305 AFRSFNGRYWSLTSSG-------AIqcsaltkSPSCFFDLEWKGSKVALKASNGKYLAAKKNGQLAAAVDSAGEQEEFVL 377
Cdd:cd23338   66 ALKSGYGKYLSVDSDGkvvgrsdAI-------GPREQWEPVFQDGKMALLGANNCFLSVNEDGDIVATSKTAGENEMIKI 138

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: 40.27 E-value: 4.55e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528467430 292 VFQMEMDRE-SKRCAFRSFNGRYWSLTSSGAIQCSALTKSPSCFFDLEWKGS-KVALK-ASNGKYLA 355
Cdd:cd23334   34 TWTLEQDEGgSETVYLKSHLGRYLSADKDGKVTCDAEEPGADERFLIEYQPDgRWALKsEKHGRYLG 100

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: 39.91 E-value: 4.78e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  16 LINADNKYLTAEMFGFKINASASSMKKKQVWTLEqsgDHGDsNAVFIKSHLGRYLASDKDGK-VTADSEQPGPDCRFLVI 94
Cdd:cd23342    6 LKGNNGKYVSSENGNKPMTANRTSVGSWEKFTVV---DAGN-GKVALKGNNGKYVSSENGTKpMTCNRTTIGAWEKFTWI 81

                         90
                 ....*....|.
gi 528467430  95 AHDDGRWSLQS 105
Cdd:cd23342   82 SLGNGTVALKG 92

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: 39.47 E-value: 5.28e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528467430 185 YHLQTADNRFLSCG--GTLTAKPDRDTGFTLEFRAG-KVAFRDATGKYIapTG-PTGTMKSgRSARVGKDELF 253
Cdd:cd23337   43 YHLKGSNGKYWSVDsdGSVTADSAAPTPFILEFRGQsKLAIKAPNGKYL--KGeQNGLFKA-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: 39.87 E-value: 7.31e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  19 ADNKYLTAEMFGFKINASASSMKKKQVWTLEqsgDHGDSNAVFIKSHLGRYLASDKDGKVTADSEQPgpdcR-------F 91
Cdd:cd23343   11 ATGKYVTVGEEGGALAADAEDAEEAETFELT---DWGWGSHTLRSVANGKYVTTDDDGTLTASAEEA----FgwfvkevF 83

                         90
                 ....*....|....
gi 528467430  92 LVIAHDDGRWSLQS 105
Cdd:cd23343   84 RLEPQEDGTVSLRT 97

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: 39.85 E-value: 1.02e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  13 RFGLINADNKYLTAEMFGfKINASASSMKKKQVWTLEQSGDHGdsnAVFIKSHLGRYL--ASDKDGKVT--ADSEQPGPD 88
Cdd:cd23339   77 KVTLKSAHGKYLSCDKFG-VVTATREARGPQEEWTPVPRPDGG---GFALQSVYGKYLsvDEVAGGKLVvrADAETVGFC 152


                 ....*
gi 528467430  89 CRFLV 93
Cdd:cd23339  153 ETWRV 157

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: 38.26 E-value: 1.59e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 305 AFRSFNGRYWSlTSSGAIQCSALTKSPSCFFDLEWKG-SKVALKASNGKYLAAKKNGQLAAAVDSAGEQEEFVLKLINRP 383
Cdd:cd23341    4 AFKSHNGHFLS-AEDGVVKTEHGHHDHHTHFHIENHGdDKVAIKTHHGKYVAIDDNKQVYLSHHHHGDHTKFHLEHHGGK 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 528467430 384 LIVLRGEHGFIGCRKQGTGTLDSNRSSYDVFQ 415
Cdd:cd23341   83 VAIKGHHHHYIGVDHHGSVHTSHHHGEDELFE 114

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: 38.37 E-value: 1.60e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528467430 335 FDLEWKGS-KVALKASNGKYLAAKK-NGQLAAAVDSAGEQEEFVLKLINRPLIVLRGEHGFIGCRKQGTGTLDSNRSS 410
Cdd:cd23342   36 FTVVDAGNgKVALKGNNGKYVSSENgTKPMTCNRTTIGAWEKFTWISLGNGTVALKGNNGKYVSSENGTNPMTCNRTS 113

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: 38.72 E-value: 1.80e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430  67 GRYL-ASDKDGKVTADSEQPGPDCRFLVIAHDDGRWSLQSEPHARYLGGTEDriacfaqsispaekwnvhlavhpqvnvy 145
Cdd:cd23343   13 GKYVtVGEEGGALAADAEDAEEAETFELTDWGWGSHTLRSVANGKYVTTDDD---------------------------- 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528467430 146 siarkryahlcadrNELAVDRDVPWG--VDSLLTLV-YLDHRYHLQTADNRFLSCG--GTLTAKPDRDTG----FTLE 214
Cdd:cd23343   65 --------------GTLTASAEEAFGwfVKEVFRLEpQEDGTVSLRTWNGRPVAVDedGRLTVGEDDAAAeaerFEKE 128

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: 39.33 E-value: 2.20e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528467430  303 RCAFRSFNGRYWSLTSSGAIQCSALTKSPSCFFDLEWKGSKVALKASNGKYLAAKKNGQLAAAVDSAGEQE 373
Cdd:pfam06229  39 KIALKSGYGKYLGVNKDGILSARADAIGPREQFEPVFQEGKMALLAANGCFLSVDPSGDIVAKSKTAGEGE 109

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: 37.92 E-value: 4.60e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528467430 305 AFRSFNGRYWSLTSSGAIQCSALTKSPSCFFDLEWKGSK--VALKASNGKYL----AAKKNGQLAAAVDSAGEQEEFVLK 378
Cdd:cd23339   79 TLKSAHGKYLSCDKFGVVTATREARGPQEEWTPVPRPDGggFALQSVYGKYLsvdeVAGGKLVVRADAETVGFCETWRVR 158