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: 275.58 E-value: 6.21e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998  11 KIQFGLINCGNKYLTAETFGFKINASATSMKKKQIWTLEQDGD--DSNMFFLKSHLGRYIAADKDGNVTGDSETPGEDCR 88
Cdd:cd23344    1 QIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPGDeaDSSAVLLRSHLGRYLAADKDGNVTCESEVPGPDCR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 115494998  89 FIITAHDDGRWSLQSEPHKRYLGGTEDRITCFAQTISIAEKWSVHIAM 136
Cdd:cd23344   81 FLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAM 128

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

Pssm-ID: 467460 Cd Length: 123 Bit Score: 257.97 E-value: 3.98e-85

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 257 LPQVVLTAGNDRNVSTRQGMDLSANQDEEGDQETFQMEISKDTKKCAFRTCTGKYWTLTANGGLQCTASTKSANCYFDIE 336
Cdd:cd23352    1 CPQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 115494998 337 WRGKKITLRATNGKYVAAKKNGQLAATIDSAGETEEFLMKLIN 379
Cdd:cd23352   81 WRDRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

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

Pssm-ID: 467456 Cd Length: 120 Bit Score: 253.98 E-value: 1.15e-83

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 137 HPQVNIFSVTRKRYAHLSSEQ-NEIAIDRDVPWGVDSLITLVFQDQRYHLQTSDNRFLKNDGSLSQTADKTTGYTLEFRS 215
Cdd:cd23348    1 HPQVNIYSVTRKRYAHLSARPaDEIAVDRDVPWGVDSLITLVFQDQRYSVQTSDHRFLRHDGRLVARPEPATGYTLEFRS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 115494998 216 GKVAFRDCTGKYLAPSGPSGTMKSGKSMKVGKDELFVLEQ 255
Cdd:cd23348   81 GKVAFRDCEGRYLAPSGPSGTLKAGKSTKVGKDELFVLEQ 120

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

Pssm-ID: 467453 [Multi-domain] Cd Length: 130 Bit Score: 238.95 E-value: 1.01e-77

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998  10 LKIQFGLINCGNKYLTAETFGFKINASATSMKKKQIWTLEQDGDDSNMFFLKSHLGRYIAADKDGNVTGDSETPGEDCRF 89
Cdd:cd23345    4 LKIQFGLINCENRYLTAEAFGFKVNASAPSLKKKQIWTLEQDEGDSSVVFLKSHLGRYLSADKDGKVSCEAEKPGRDCRF 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 115494998  90 IITAHDDGRWSLQSEPHKRYLGGTEDRITCFAQTISIAEKWSVHIAM 136
Cdd:cd23345   84 LIVAQSDGRWALQSEPHKRFFGGSEDKLSCFAQTITEAELWAVHLAI 130

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

Pssm-ID: 467464 Cd Length: 111 Bit Score: 226.68 E-value: 2.89e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 380 RPLIVLRGEHGFIGCRRVTGTLDSNRSSYDVFGLDFNDGAYSLRDCTGKYWMVGSESNVLSSSDTPVDFFLEFCNYNKVA 459
Cdd:cd23356    1 RPIIVLRGEHGFIGCRKVTGTLDSNRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 115494998 460 IKTTeGKYLKGDHAGVLKANADDLDSSTMWEY 491
Cdd:cd23356   81 IKVG-GRYLKGDHAGVLKASAETVDPATLWEY 111

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: 220.92 E-value: 8.46e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998  12 IQFGLINCGNKYLTAETFGFKINASATSMKKKQIWTLEQDGDDSNMFFLKSHLGRYIAADKDGNVTGDSETPGEDCRFII 91
Cdd:cd23334    1 WKLGLINSSGKYLTAETFGFKVNASGTSLKKKQTWTLEQDEGGSETVYLKSHLGRYLSADKDGKVTCDAEEPGADERFLI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 115494998  92 TAHDDGRWSLQSEPHKRYLGGTEDRITCFAQTISIAEKWSVHIAM 136
Cdd:cd23334   81 EYQPDGRWALKSEKHGRYLGGTGDNLSCFAKEVSESELWTVHLAI 125

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

Pssm-ID: 467457 Cd Length: 119 Bit Score: 202.75 E-value: 6.95e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 137 HPQVNIFSVTRKRYAHLSSEQNEIAIDRDVPWGVDSLITLVFQDQRYHLQTSDNRFLKNDGSLSQTADKTTGYTLEFRSG 216
Cdd:cd23349    1 HPQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKAG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 115494998 217 KVAFRDCTGKYLAPSGPSGTMKSGKSMKVGKDELFVLEQ 255
Cdd:cd23349   81 KLAFKDCDGKYLTPMGPTGTLKSGRSSKPGKDELFDLEE 119

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

Pssm-ID: 467444 Cd Length: 124 Bit Score: 195.51 E-value: 5.47e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 258 PQVVLTAGNDRNVSTRQGMDLSANQDEEGDQETFQMEISKDTKKCAFRTCTGKYWTLTANGGLQCTASTKSANCYFDIEW 337
Cdd:cd23336    2 PQVSLRAHNGKYVSIRQGVDVSANQDEETDTETFQLEFDKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELEW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 115494998 338 R-GKKITLRATNGKYVAAKKNGQLAATIDSAGETEEFLMKLIN 379
Cdd:cd23336   82 NdGGTVALKASNGKYVTAKPNGQLAATSDEVGEKEKFTLKLIN 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: 190.88 E-value: 3.57e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 258 PQVVLTAGNDRNVSTRQGMDLSANQDEEGDQETFQMEISKDTKKCAFRTCTGKYWTLTANGGLQCTASTKSANCYFDIEW 337
Cdd:cd23353    2 PQVVFQAANGRYVSIRQGVNVSANQDEETDHETFQMQIDKETKKCSFHTNTGKYWTLVAHGGIQSTATEVAANTMFDIEW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 115494998 338 RGKKITLRATNGKYVAAKKNGQLAATIDSAGETEEFLMKLIN 379
Cdd:cd23353   82 RGRRVALKASNGKYVCTKKNGQLAAVSDSVGEDEEFTLKLIN 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: 188.53 E-value: 1.93e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 138 PQVNIFSVTRKRYAHLSSEQNEIAIDRDVPWGVDSLITLVFQDQRYHLQTSDNRFLKNDGSLSQTADKTTGYTLEFRSGK 217
Cdd:cd23335    1 PQVNLYSVNRKRYARLDPEGDELRVDEDIPWGSDALITLEFDDGRYALRTSDGRYLRSDGSLVDEPSDDTLFTLEFRSGG 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 115494998 218 VAFRDCTGKYLAPSGPSGTMKSGKSmKVGKDELFVLE 254
Cdd:cd23335   81 LAFKDSEGKYLTAVGGSGVLKTRKK-TVGKDELFSLE 116

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: 156.46 E-value: 6.79e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998  15 GLINCGNKYLTAETFGFKINASATSMKKKQIWTLEQDGDDSNMFFLKSHLGRYIAADKDGNVTGDSETPGEDCRFIITAH 94
Cdd:cd23347    7 GLINSQQKYLTAETFGFKVNANGSSLKKKQLWTLEPFGDGTNVVALRSHLGRYLSVDQFGNVTCEAEEKGEGSRFEIVIS 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 115494998  95 DD--GRWSLQSEPHKRYLGGTEDRITCFAQTISIAEKWSVHIA 135
Cdd:cd23347   87 EDesGRWAFRNEERGYFLGGSGDKLVCTAKAPTDSELWTVHLA 129

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

Pssm-ID: 467445 Cd Length: 114 Bit Score: 149.25 E-value: 1.71e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 380 RPLIVLRGEHGFIGCRRVT-GTLDSNRSSYDVFGLDF-NDGAYSLRDCTGKYWMVGSESNVLSSSDTPVDFFLEFCNYNK 457
Cdd:cd23337    1 RPILVLRGEYGFVGVKSGSsGKLECNKSTYDVFQLEYnNDGAYHLKGSNGKYWSVDSDGSVTADSAAPTPFILEFRGQSK 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 115494998 458 VAIKTTEGKYLKGDHAGVLKANADDLDSSTMWEY 491
Cdd:cd23337   81 LAIKAPNGKYLKGEQNGLFKATGTEVDKATLWEY 114

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

Pssm-ID: 467459 Cd Length: 119 Bit Score: 148.69 E-value: 3.78e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 137 HPQVNIFSVTRKRYAHLSSEQNEIAIDRDVPWGVDSLITLVF-QDQRYHLQTSDNRFLKNDGSLSQTADKTTGYTLEFRS 215
Cdd:cd23351    1 RPQVNLRSAGRKRYARLSGDEDEIQVDANVPWGSDTLFTLEFrDDGRYAIHTANGKYLNRDGKLVEECPEDCLFTLEYHA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 115494998 216 GKVAFRDCTGKYLAPSGPSGTMKSgKSMKVGKDELFVLE 254
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: 147.25 E-value: 8.57e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 380 RPLIVLRGEHGFIGCRRVTGTLDSNRSSYDVFGLDFNDGAYSLRDCTGKYWMVGSESNVLSSSDTPVDFFLEFCNYNKVA 459
Cdd:cd23357    1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRVA 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 115494998 460 IKTTEGKYLKGDHAGVLKANADDLDSSTMWEY 491
Cdd:cd23357   81 IKGKNGKYLRGDQAGTLKADAETVDSATLWEY 112

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

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 128.60 E-value: 1.00e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998  266 NDRNVSTRQGMDLSANQDEEGDQETFQMEISKDTKKCAFRTCTGKYWTLTANGGLQCTASTKSANCYFDIEWRGKKITLR 345
Cdd:pfam06268   2 NGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALLR 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 115494998  346 ATNGKYVAAKKNGQLAATIDSAGETEEFLM 375
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: 123.46 E-value: 1.19e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 257 LPQVVLTAG-NDRNVSTRQGMDLSANQDEEGDQETFQMEISKDTKKCAFRTCTGKYWTLTANGGLQCTASTKSANCYFDI 335
Cdd:cd23355    1 LPQAAFIAGlNSRYVSVKQGVDVTANQDEISDHETFQLEYDWSTKRWYIRTMQDRYWTLETAGGIQASADKKSANALFEL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 115494998 336 EWRGK-KITLRATNGKYVAAKKNGQLAATIDSAGETEEFLMKLIN 379
Cdd:cd23355   81 EWQEDgSVSFRANNGKFVGTKRSGHLFANSESIDEIAKFYFYLIN 125

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

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 117.43 E-value: 1.23e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998   21 NKYLTAETFGFKINASATSMKKKQIWTLEQDgDDSNMFFLKSHLGRYIAADKDGNVTGDSETPGEDCRFiiTAHDDGRWS 100
Cdd:pfam06268   2 NGYLVSERRGAHLNANRESLKRVQTFTLEFD-DERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFF--ELEFRGRWA 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 115494998  101 LQSEPHKRYLG-GTEDRITCFAQTISIAEKWSV 132
Cdd:pfam06268  79 LLRESNGRYLGgGPSGLLKANASTVGKDELWTL 111

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

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 88.16 E-value: 3.93e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998  388 EHGFIGCRRVTGTLDSNR---SSYDVFGLDFNDGAYS--LRDCTGKYWMVGSESNVLSSSDTP-VDFFLEFCNYNKVAIK 461
Cdd:pfam06268   1 ANGYLVSERRGAHLNANReslKRVQTFTLEFDDERYTvyLRSHNGKYLSCDADGRVVCEAERRsADTFFELEFRGRWALL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 115494998  462 -TTEGKYLKGDHAGVLKANADDLDSSTMWEY 491
Cdd:pfam06268  81 rESNGRYLGGGPSGLLKANASTVGKDELWTL 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: 84.42 E-value: 1.07e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 380 RPLIVLRGEHGFIGCRRVTGT-LDSNRSSYDVFGLDFND-GAYSLRDCTGKYWMVGSESnVLSSSDTPVDFFLEFCNYNK 457
Cdd:cd23359    1 RPILVLKCEQGFVGYKSGSNPkLECNKASYETIQVERGDkGLVFFKGQSGKYWGVCGDG-ITADADAPEGFYLELREPSR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 115494998 458 VAIKTTEGKYLKGDHAGVLKANADDLDSSTMWEY 491
Cdd:cd23359   80 LCIKTADGSYLMADKNGAFKVGDADPETATLWEF 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: 81.16 E-value: 1.81e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 259 QVVLTAGNDRNVSTRQGMD--LSANQDEEGDQETFQMEISKDtKKCAFRTCTGKYWTLTANGG--LQCTASTKSANCYFD 334
Cdd:cd00257    2 TVALKSSNGKYLSAENGGGgpLVANRDAAGPWETFTLVDLGD-GKVALKSSNGKYLSAENGGGgtLVANRTAIGPWETFT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 115494998 335 IEWRGK-KITLRATNGKYVAAKKN--GQLAATIDSAGETEEF 373
Cdd:cd00257   81 LVPLGNgKVALKSANGKYLSADNGggGTLIANATSIGAWEKF 122

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

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 78.85 E-value: 1.34e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998  13 QFGLINCGNKYLTAETFGF-KINASATSMKKKQIWTLEQDGDDSnmFFLKSHLGRYIAADKDGN--VTGDSETPGEDCRF 89
Cdd:cd00257    2 TVALKSSNGKYLSAENGGGgPLVANRDAAGPWETFTLVDLGDGK--VALKSSNGKYLSAENGGGgtLVANRTAIGPWETF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 115494998  90 IITAHDDGRWSLQSePHKRYL---GGTEDRITCFAQTISIAEKWSV 132
Cdd:cd00257   80 TLVPLGNGKVALKS-ANGKYLsadNGGGGTLIANATSIGAWEKFTI 124

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: 77.37 E-value: 3.04e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998  140 VNIFSVTRKRYAHLS-SEQNEIAIDrdvpwgvdsLITLVFQDQRY--HLQTSDNRFL--KNDGSLSQTADKT---TGYTL 211
Cdd:pfam06268   1 ANGYLVSERRGAHLNaNRESLKRVQ---------TFTLEFDDERYtvYLRSHNGKYLscDADGRVVCEAERRsadTFFEL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 115494998  212 EFRSGKVAFRDCTGKYLApSGPSGTMKSgKSMKVGKDELFVL 253
Cdd:pfam06268  72 EFRGRWALLRESNGRYLG-GGPSGLLKA-NASTVGKDELWTL 111

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

Pssm-ID: 467454 Cd Length: 127 Bit Score: 77.98 E-value: 3.29e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998  12 IQFGLINCGNKYLTAETFGFKINASATSMKKKQIWTL--EQDGDDSNMFFLKSHLGRYIAADKDGNVT-GDSETPGEDCr 88
Cdd:cd23346    1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVivSDYSDRQAVVELKGPQGLYLLVDKDGLVRcGTPDTKHHGL- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 115494998  89 FIITAHDDGRWSLQSEPHKRYLGGTEDRITCFAQTISIAEKWSVHIAM 136
Cdd:cd23346   80 FLLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127

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: 75.22 E-value: 1.98e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 380 RPLIVLRGEHGFIGCRRVTGTLDSNRSSYDVFGL-DFNDGAYSLRDCTGKYWMVGSESNVLSSSDTPVDFFLEFCNYNKV 458
Cdd:cd23358    1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLlPCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 115494998 459 AIKTTEGKYLKGDHAGVLKANADDLDSSTMWEY 491
Cdd:cd23358   81 AILAPNGCYLRGDNSGTLLADSEIITSECLWEF 113

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: 74.01 E-value: 6.01e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 258 PQVVLTAGNDRNVSTRQGMDLSANQDEEGDQETFQMEISKDTKKCAFRTCTGKYWTLTANGGLQCTASTKSANCYFDIEW 337
Cdd:cd23354    2 TWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVEW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 115494998 338 RGKKITLRATNGKYVAAKKNGQLAATIDSAGETEEFLMKLIN 379
Cdd:cd23354   82 RCGKIILQASNGRYLGVKPNGLLTASALLPGPNEEFGVRLAN 123

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

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 64.60 E-value: 1.28e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 340 KKITLRATNGKYVAA--KKNGQLAATIDSAGETEEFLMklinrplivlrgehgfigcrrvtgtldsnrssydvfgLDFND 417
Cdd:cd00257    1 GTVALKSSNGKYLSAenGGGGPLVANRDAAGPWETFTL-------------------------------------VDLGD 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 418 GAYSLRDCTGKYWMV--GSESNVLSSSDTPVD---FFLEFCNYNKVAIKTTEGKYL--KGDHAGVLKANADDLDSSTMWE 490
Cdd:cd00257   44 GKVALKSSNGKYLSAenGGGGTLVANRTAIGPwetFTLVPLGNGKVALKSANGKYLsaDNGGGGTLIANATSIGAWEKFT 123

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: 59.03 E-value: 8.94e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 137 HPQVNIFSVTRKRYAHLSSEQNEIAIDRDVPWGVDSLITLVFQDQRYHLQTSDNRFLKNDGSLSQTADKTTGYTLEFRSG 216
Cdd:cd23350    1 HVHVVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 115494998 217 -KVAFRDCTGKYLAPSGPSGTMKSGkSMKVGKDELFVLEQ 255
Cdd:cd23350   81 yLASFFDDCGSMLYPQGRSRLLLSG-NIPINEEEWFIIKR 119

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

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 59.21 E-value: 9.87e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 300 KKCAFRTCTGKYWTLTANGG--LQCTASTKSANCYFDIE-WRGKKITLRATNGKYVAA--KKNGQLAATIDSAGETEEFL 374
Cdd:cd00257    1 GTVALKSSNGKYLSAENGGGgpLVANRDAAGPWETFTLVdLGDGKVALKSSNGKYLSAenGGGGTLVANRTAIGPWETFT 80

                         90
                 ....*....|....*.
gi 115494998 375 MKLINRPLIVLRGEHG 390
Cdd:cd00257   81 LVPLGNGKVALKSANG 96

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: 59.88 E-value: 1.10e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998  54 DSNMFFLKSHLGRYIAADKDGNVTGDSE--TPGEDCRFIItAHDDGRWSLQSePHKRYLGGTED-----RITCFAQTISI 126
Cdd:cd23339   74 GTGKVTLKSAHGKYLSCDKFGVVTATREarGPQEEWTPVP-RPDGGGFALQS-VYGKYLSVDEVaggklVVRADAETVGF 151


                 ....*.
gi 115494998 127 AEKWSV 132
Cdd:cd23339  152 CETWRV 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: 57.96 E-value: 1.89e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 287 DQETFQMEiSKDTKKCAFRTCTGKYWTLTANGGLQCTASTKSAncyFDIEWRGK-KITLRATNGKYVAAKKNGQLAATID 365
Cdd:cd23337   29 TYDVFQLE-YNNDGAYHLKGSNGKYWSVDSDGSVTADSAAPTP---FILEFRGQsKLAIKAPNGKYLKGEQNGLFKATGT 104


                 ....*...
gi 115494998 366 SAGETEEF 373
Cdd:cd23337  105 EVDKATLW 112

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

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 52.66 E-value: 2.11e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 181 QRYHLQTSDNRFL----KNDGSLSQTADKTTGY---TLEF-RSGKVAFRDCTGKYL-APSGPSGTmksgksmkvgkdelf 251
Cdd:cd00257    1 GTVALKSSNGKYLsaenGGGGPLVANRDAAGPWetfTLVDlGDGKVALKSSNGKYLsAENGGGGT--------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 252 vleqslpqvvltagndrnvstrqgmdLSANQDEEGDQETFQMEISKDTKKcAFRTCTGKYWTLTANGG--LQCTASTKSA 329
Cdd:cd00257   66 --------------------------LVANRTAIGPWETFTLVPLGNGKV-ALKSANGKYLSADNGGGgtLIANATSIGA 118


                 ....*.
gi 115494998 330 NCYFDI 335
Cdd:cd00257  119 WEKFTI 124

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: 52.24 E-value: 2.77e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 259 QVVLTAGNDRNVSTRQGM-DLSANQDEEGDQETFQMEIsKDTKKCAFRTCTGKYwtLTANGG---LQCTASTKSANCYFD 334
Cdd:cd23342    3 TISLKGNNGKYVSSENGNkPMTANRTSVGSWEKFTVVD-AGNGKVALKGNNGKY--VSSENGtkpMTCNRTTIGAWEKFT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 115494998 335 IEWRG-KKITLRATNGKYVAAKKNGQ-LAATIDSAGETEEF 373
Cdd:cd23342   80 WISLGnGTVALKGNNGKYVSSENGTNpMTCNRTSIGGWEKF 120

fascin-like domain, beta-trefoil fold, found in uncharacterized beta-glucosidase-like proteins; This subfamily includes a group of uncharacterized proteins which may be related to beta-glucosidase/glycosyl hydrolase 3 family. They contain a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

Pssm-ID: 467451 Cd Length: 133 Bit Score: 46.42 E-value: 3.67e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 341 KITLR-ATNGKYVAA-KKNGQLAATIDSAGETEEFlmklinrplivlrgehgfigcrrvtgtldsnrssyDVFglDFNDG 418
Cdd:cd23343    4 RIALRsAATGKYVTVgEEGGALAADAEDAEEAETF-----------------------------------ELT--DWGWG 46

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115494998 419 AYSLRDC-TGKYWMVGSESNVLSSSDTPVDFF----LEFCNY--NKVAIKTTEGKYLKGDHAGVLKANADD 482
Cdd:cd23343   47 SHTLRSVaNGKYVTTDDDGTLTASAEEAFGWFvkevFRLEPQedGTVSLRTWNGRPVAVDEDGRLTVGEDD 117

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

Pssm-ID: 467444 Cd Length: 124 Bit Score: 42.59 E-value: 5.86e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998  13 QFGLINCGNKYLTAEtFGFKINASATSMKKKQIWTLEQDgDDSNMFFLKSHLGRYIAADKDGNVTGDSETPGEDCRFIIT 92
Cdd:cd23336    3 QVSLRAHNGKYVSIR-QGVDVSANQDEETDTETFQLEFD-KETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELE 80

                         90
                 ....*....|.
gi 115494998  93 AHDDGRWSLQS 103
Cdd:cd23336   81 WNDGGTVALKA 91

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: 42.22 E-value: 6.82e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 339 GKKITLRATNGKYVAAKK-NGQLAATIDSAGETEEFLMKLINRPLIVLRGEHG-FIGCRRVTGTLDSNRSSYDV---FGL 413
Cdd:cd23342    1 GSTISLKGNNGKYVSSENgNKPMTANRTSVGSWEKFTVVDAGNGKVALKGNNGkYVSSENGTKPMTCNRTTIGAwekFTW 80

                         90
                 ....*....|....*..
gi 115494998 414 -DFNDGAYSLRDCTGKY 429
Cdd:cd23342   81 iSLGNGTVALKGNNGKY 97

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: 41.78 E-value: 9.43e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115494998 183 YHLQTSDNRFLK--NDGSLSQTADKTTGYTLEFRSG-KVAFRDCTGKYLApSGPSGTMKSgKSMKVGKDELF 251
Cdd:cd23337   43 YHLKGSNGKYWSvdSDGSVTADSAAPTPFILEFRGQsKLAIKAPNGKYLK-GEQNGLFKA-TGTEVDKATLW 112

fascin-like domain, beta-trefoil fold, found in uncharacterized beta-glucosidase-like proteins; This subfamily includes a group of uncharacterized proteins which may be related to beta-glucosidase/glycosyl hydrolase 3 family. They contain a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

Pssm-ID: 467451 Cd Length: 133 Bit Score: 41.80 E-value: 1.27e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 259 QVVLT-AGNDRNVSTRQGMD-LSANQDEEGDQETFQMEiskD------TkkcaFRTC-TGKYWTLTANGGLQCTAS---- 325
Cdd:cd23343    4 RIALRsAATGKYVTVGEEGGaLAADAEDAEEAETFELT---DwgwgshT----LRSVaNGKYVTTDDDGTLTASAEeafg 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 115494998 326 --TKSAncyFDIEWRGK-KITLRATNGKYVAAKKNGQLAATIDSAGETEE 372
Cdd:cd23343   77 wfVKEV---FRLEPQEDgTVSLRTWNGRPVAVDEDGRLTVGEDDAAAEAE 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: 41.00 E-value: 3.44e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115494998  22 KYLTAETFGfKINASATSMKKKQIWTLEQdGDDSNMFFLKSHLGRYIAADKDGN----VTGDSETPGEDCRFII 91
Cdd:cd23339   86 KYLSCDKFG-VVTATREARGPQEEWTPVP-RPDGGGFALQSVYGKYLSVDEVAGgklvVRADAETVGFCETWRV 157

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

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 39.95 E-value: 5.19e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 175 TLVFQ-DQRYHLQTSDNRFLKNDGSLSQT--ADKTTGYTLE-FR-----SGKVAFRDCTGKYL-APSGPSGTMKSGKSmK 244
Cdd:cd00257   37 TLVDLgDGKVALKSSNGKYLSAENGGGGTlvANRTAIGPWEtFTlvplgNGKVALKSANGKYLsADNGGGGTLIANAT-S 115


                 ....*....
gi 115494998 245 VGKDELFVL 253
Cdd:cd00257  116 IGAWEKFTI 124

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: 40.23 E-value: 7.33e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115494998 341 KITLRATNGKYVAAKKNGQLAATIDSAGETEEF-LMKLINRPLIVLRGEHG-FIGCRRVTG 399
Cdd:cd23339   77 KVTLKSAHGKYLSCDKFGVVTATREARGPQEEWtPVPRPDGGGFALQSVYGkYLSVDEVAG 137

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: 39.07 E-value: 1.02e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115494998 410 VFGLDFNDGAYSLRDCTGKYwmvgsesnvLSSSDTPVD-------FFLEFcNYNKVAIKTTEGKYLKGDHA-GVLKAN 479
Cdd:cd23335   36 LITLEFDDGRYALRTSDGRY---------LRSDGSLVDepsddtlFTLEF-RSGGLAFKDSEGKYLTAVGGsGVLKTR 103

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: 38.64 E-value: 1.23e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 301 KCAFRTCTGKYwtLTA-NGGLQCTASTKSANCYFDIEWRG-KKITLRATNGKYVAAKKNGQLAATIDSAGETEEFLMKLI 378
Cdd:cd23341    2 KRAFKSHNGHF--LSAeDGVVKTEHGHHDHHTHFHIENHGdDKVAIKTHHGKYVAIDDNKQVYLSHHHHGDHTKFHLEHH 79

                         90
                 ....*....|....*.
gi 115494998 379 NRPlIVLRGEHG-FIG 393
Cdd:cd23341   80 GGK-VAIKGHHHhYIG 94

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: 38.67 E-value: 1.74e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115494998 283 DEEG--DQETFQ-MEISkDTKkCAFRTCTGKYWTLTANGGLQCTASTKSANCYFDIEWRGKKITLRATNGKYVAAKKNGQ 359
Cdd:cd23338   45 EGEGpdPEEIFTaIKVS-DTK-IALKSGYGKYLSVDSDGKVVGRSDAIGPREQWEPVFQDGKMALLGANNCFLSVNEDGD 122

                         90
                 ....*....|..
gi 115494998 360 LAATIDSAGETE 371
Cdd:cd23338  123 IVATSKTAGENE 134

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: 38.33 E-value: 2.34e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 115494998  65 GRYIAADKDGNV-TGDSETPGEDCRFIITAHDDGRWSLQSEPHKRYLGGTEDRI 117
Cdd:cd23343   13 GKYVTVGEEGGAlAADAEDAEEAETFELTDWGWGSHTLRSVANGKYVTTDDDGT 66

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: 37.41 E-value: 3.40e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115494998 185 LQTSDNRFLKNDGSLSQTAD-----KTTGYTLEFRSGKVAFRDCTGKYLAPSgPSGTMkSGKSMKVGKDELFVL 253
Cdd:cd23354   48 LRTVNGRYLAQRGHRSVIADgkgteSETFFRVEWRCGKIILQASNGRYLGVK-PNGLL-TASALLPGPNEEFGV 119

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: 37.56 E-value: 4.44e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115494998  21 NKYLTAETFGFkINASATSMKK---KQIWTLEQDGDDSnmFFLKSHLGRYIAADKDGNVT-GDSETPGEDCRFIIT 92
Cdd:cd23343   56 GKYVTTDDDGT-LTASAEEAFGwfvKEVFRLEPQEDGT--VSLRTWNGRPVAVDEDGRLTvGEDDAAAEAERFEKE 128