NCBI Conserved Domain Search

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: 269.76 E-value: 9.90e-90

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186   8 RALKLQFGLINYENRYLTAEAFGFKVNASGISMKKKQIWTLEQDEQDGQVVFLRSHLGRYLASDKDGKITCGAEKPDPDC 87
Cdd:cd23345     2 QALKIQFGLINCENRYLTAEAFGFKVNASAPSLKKKQIWTLEQDEGDSSVVFLKSHLGRYLSADKDGKVSCEAEKPGRDC 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2116737186  88 RFLIVPQSDGRWALQSEPYLRYFGGSADYLSCFAQAIGEQELWAVHLAL 136
Cdd:cd23345    82 RFLIVAQSDGRWALQSEPHKRFFGGSEDKLSCFAQTITEAELWAVHLAI 130

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: 245.13 E-value: 3.00e-80

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 137 HPQASLLSVARKRYAHLSASDGEISVDSNIPWGVDSLVTLVYLDGKYSLKTCDSRFLRNDGKLVKENTNTTSFTLELKSG 216
Cdd:cd23349     1 HPQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKAG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2116737186 217 KLAFKDCDGKYLSPVGPTGTLRSGRCSKPGKDELFDLEE 255
Cdd:cd23349    81 KLAFKDCDGKYLTPMGPTGTLKSGRSSKPGKDELFDLEE 119

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: 232.48 E-value: 3.20e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 257 HPQVVFQAANKRFVSVKQGVSISANQDVETDMETFQMEIDKETKKSMFRTNGGSYWTLVTHGEIQSTATEVEVNTMFDIE 336
Cdd:cd23353     1 HPQVVFQAANGRYVSIRQGVNVSANQDEETDHETFQMQIDKETKKCSFHTNTGKYWTLVAHGGIQSTATEVAANTMFDIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2116737186 337 WLGQRVALKASNGKYVCTKKNGQLSAVSDTVGDDELFLMKLIN 379
Cdd:cd23353    81 WRGRRVALKASNGKYVCTKKNGQLAAVSDSVGEDEEFTLKLIN 123

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: 222.42 E-value: 2.39e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186  11 KLQFGLINYENRYLTAEAFGFKVNASGISMKKKQIWTLEQ--DEQDGQVVFLRSHLGRYLASDKDGKITCGAEKPDPDCR 88
Cdd:cd23344     1 QIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQpgDEADSSAVLLRSHLGRYLAADKDGNVTCESEVPGPDCR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2116737186  89 FLIVPQSDGRWALQSEPYLRYFGGSADYLSCFAQAIGEQELWAVHLAL 136
Cdd:cd23344    81 FLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAM 128

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: 215.15 E-value: 1.61e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186  12 LQFGLINYENRYLTAEAFGFKVNASGISMKKKQIWTLEQDEQDGQVVFLRSHLGRYLASDKDGKITCGAEKPDPDCRFLI 91
Cdd:cd23334     1 WKLGLINSSGKYLTAETFGFKVNASGTSLKKKQTWTLEQDEGGSETVYLKSHLGRYLSADKDGKVTCDAEEPGADERFLI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2116737186  92 VPQSDGRWALQSEPYLRYFGGSADYLSCFAQAIGEQELWAVHLAL 136
Cdd:cd23334    81 EYQPDGRWALKSEKHGRYLGGTGDNLSCFAKEVSESELWTVHLAI 125

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: 212.35 E-value: 1.04e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 380 RPMLILRGENGFVCHHKNSNTLDANRSVYDIFSLIFNDGAYNVKSVNEKFWYVSSSGLVCSDGEKPEDFFLEFLEHGRIA 459
Cdd:cd23357     1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRVA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2116737186 460 IKGSNGKYLRGDQGGTLMGDGPTVDASSLWEY 491
Cdd:cd23357    81 IKGKNGKYLRGDQAGTLKADAETVDSATLWEY 112

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: 193.51 E-value: 2.86e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 137 HPQASLLSVARKRYAHLSAS-DGEISVDSNIPWGVDSLVTLVYLDGKYSLKTCDSRFLRNDGKLVKENTNTTSFTLELKS 215
Cdd:cd23348     1 HPQVNIYSVTRKRYAHLSARpADEIAVDRDVPWGVDSLITLVFQDQRYSVQTSDHRFLRHDGRLVARPEPATGYTLEFRS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2116737186 216 GKLAFKDCDGKYLSPVGPTGTLRSGRCSKPGKDELFDLEE 255
Cdd:cd23348    81 GKVAFRDCEGRYLAPSGPSGTLKAGKSTKVGKDELFVLEQ 120

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: 191.66 E-value: 1.85e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 257 HPQVVFQAANKRFVSVKQGVSISANQDVETDMETFQMEIDKETKKSMFRTNGGSYWTLVTHGEIQSTATEVEVNTMFDIE 336
Cdd:cd23336     1 HPQVSLRAHNGKYVSIRQGVDVSANQDEETDTETFQLEFDKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2116737186 337 WL-GQRVALKASNGKYVCTKKNGQLSAVSDTVGDDELFLMKLIN 379
Cdd:cd23336    81 WNdGGTVALKASNGKYVTAKPNGQLAATSDEVGEKEKFTLKLIN 124

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: 179.67 E-value: 5.16e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 138 PQASLLSVARKRYAHLSASDGEISVDSNIPWGVDSLVTLVYLDGKYSLKTCDSRFLRNDGKLVKENTNTTSFTLELKSGK 217
Cdd:cd23335     1 PQVNLYSVNRKRYARLDPEGDELRVDEDIPWGSDALITLEFDDGRYALRTSDGRYLRSDGSLVDEPSDDTLFTLEFRSGG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2116737186 218 LAFKDCDGKYLSPVGPTGTLRSGRCsKPGKDELFDLEE 255
Cdd:cd23335    81 LAFKDSEGKYLTAVGGSGVLKTRKK-TVGKDELFSLED 117

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: 176.69 E-value: 9.17e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 258 PQVVFQAANKRFVSVKQGVSISANQDVETDMETFQMEIDKETKKSMFRTNGGSYWTLVTHGEIQSTATEVEVNTMFDIEW 337
Cdd:cd23352     2 PQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIEW 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2116737186 338 LGQRVALKASNGKYVCTKKNGQLSAVSDTVGDDELFLMKLIN 379
Cdd:cd23352    82 RDRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

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

Pssm-ID: 467455 Cd Length: 130 Bit Score: 166.86 E-value: 7.55e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186  15 GLINYENRYLTAEAFGFKVNASGISMKKKQIWTLEQDEQDGQVVFLRSHLGRYLASDKDGKITCGAEKPDPDCRFLIVPQ 94
Cdd:cd23347     7 GLINSQQKYLTAETFGFKVNANGSSLKKKQLWTLEPFGDGTNVVALRSHLGRYLSVDQFGNVTCEAEEKGEGSRFEIVIS 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2116737186  95 SD--GRWALQSEPYLRYFGGSADYLSCFAQAIGEQELWAVHLA 135
Cdd:cd23347    87 EDesGRWAFRNEERGYFLGGSGDKLVCTAKAPTDSELWTVHLA 129

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

Pssm-ID: 467459 Cd Length: 119 Bit Score: 143.30 E-value: 4.45e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 137 HPQASLLSVARKRYAHLSASDGEISVDSNIPWGVDSLVTLVY-LDGKYSLKTCDSRFLRNDGKLVKENTNTTSFTLELKS 215
Cdd:cd23351     1 RPQVNLRSAGRKRYARLSGDEDEIQVDANVPWGSDTLFTLEFrDDGRYAIHTANGKYLNRDGKLVEECPEDCLFTLEYHA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2116737186 216 GKLAFKDCDGKYLSPVGPTGTLRSgRCSKPGKDELFDLE 254
Cdd:cd23351    81 GQVAFRDRTGKYLAPIGSKAVLRT-RSTSVTKDELFILE 118

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

Pssm-ID: 467445 Cd Length: 114 Bit Score: 138.85 E-value: 1.52e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 380 RPMLILRGENGFVCHH-KNSNTLDANRSVYDIFSLIF-NDGAYNVKSVNEKFWYVSSSGLVCSDGEKPEDFFLEFLEHGR 457
Cdd:cd23337     1 RPILVLRGEYGFVGVKsGSSGKLECNKSTYDVFQLEYnNDGAYHLKGSNGKYWSVDSDGSVTADSAAPTPFILEFRGQSK 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2116737186 458 IAIKGSNGKYLRGDQGGTLMGDGPTVDASSLWEY 491
Cdd:cd23337    81 LAIKAPNGKYLKGEQNGLFKATGTEVDKATLWEY 114

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

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 132.84 E-value: 2.14e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186  20 ENRYLTAEAFGFKVNASGISMKKKQIWTLEQDEqDGQVVFLRSHLGRYLASDKDGKITCGAEKPDPDCRFLIVPQsdGRW 99
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDD-ERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFR--GRW 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2116737186 100 ALQSEPYLRYFG-GSADYLSCFAQAIGEQELWAV 132
Cdd:pfam06268  78 ALLRESNGRYLGgGPSGLLKANASTVGKDELWTL 111

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: 130.00 E-value: 3.03e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 380 RPMLILRGENGFVCHHKNSNTLDANRSVYDIFSLIFNDGAYNVKSVNEKFWYVSSSGLVCSDGEKPEDFFLEFLEHGRIA 459
Cdd:cd23356     1 RPIIVLRGEHGFIGCRKVTGTLDSNRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2116737186 460 IKgSNGKYLRGDQGGTLMGDGPTVDASSLWEY 491
Cdd:cd23356    81 IK-VGGRYLKGDHAGVLKASAETVDPATLWEY 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: 119.74 E-value: 1.48e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 265 ANKRFVSVKQGVSISANQDVETDMETFQMEIDKETKKSMFRTNGGSYWTLVTHGEIQSTATEVEVNTMFDIEWLGQRVAL 344
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2116737186 345 KASNGKYVCTKKNGQLSAVSDTVGDDELFLM 375
Cdd:pfam06268  81 RESNGRYLGGGPSGLLKANASTVGKDELWTL 111

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

Pssm-ID: 467463 Cd Length: 125 Bit Score: 116.14 E-value: 6.33e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 258 PQVVFQAA-NKRFVSVKQGVSISANQDVETDMETFQMEIDKETKKSMFRTNGGSYWTLVTHGEIQSTATEVEVNTMFDIE 336
Cdd:cd23355     2 PQAAFIAGlNSRYVSVKQGVDVTANQDEISDHETFQLEYDWSTKRWYIRTMQDRYWTLETAGGIQASADKKSANALFELE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2116737186 337 WLGQ-RVALKASNGKYVCTKKNGQLSAVSDTVGDDELFLMKLIN 379
Cdd:cd23355    82 WQEDgSVSFRANNGKFVGTKRSGHLFANSESIDEIAKFYFYLIN 125

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

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 93.16 E-value: 8.04e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 388 ENGFVCHHKNSNTLDANR---SVYDIFSLIFNDGAYNV--KSVNEKFWYVSSSGLVCSDGE-KPEDFFLEFLEHGRIAIK 461
Cdd:pfam06268   1 ANGYLVSERRGAHLNANReslKRVQTFTLEFDDERYTVylRSHNGKYLSCDADGRVVCEAErRSADTFFELEFRGRWALL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2116737186 462 -GSNGKYLRGDQGGTLMGDGPTVDASSLWEY 491
Cdd:pfam06268  81 rESNGRYLGGGPSGLLKANASTVGKDELWTL 111

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: 81.71 E-value: 1.35e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 258 PQVVFQAANKRFVSVKQGVSISANQDVETDMETFQMEIDKETKKSMFRTNGGSYWTLVTHGEIQSTATEVEVNTMFDIEW 337
Cdd:cd23354     2 TWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVEW 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2116737186 338 LGQRVALKASNGKYVCTKKNGQLSAVSDTVGDDELFLMKLIN 379
Cdd:cd23354    82 RCGKIILQASNGRYLGVKPNGLLTASALLPGPNEEFGVRLAN 123

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: 79.84 E-value: 4.71e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 380 RPMLILRGENGFVCHHKNSNTLDANRSVYDIFSLI-FNDGAYNVKSVNEKFWYVSSSGLVCSDGEKPEDFFLEFLEHGRI 458
Cdd:cd23358     1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLLpCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2116737186 459 AIKGSNGKYLRGDQGGTLMGDGPTVDASSLWEY 491
Cdd:cd23358    81 AILAPNGCYLRGDNSGTLLADSEIITSECLWEF 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: 77.59 E-value: 3.73e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186  12 LQFGLINYENRYLTAEAFGFKVNASGISMKKKQIWTLE-QDEQDGQ-VVFLRSHLGRYLASDKDGKITCGAEKPDPDCRF 89
Cdd:cd23346     1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVIvSDYSDRQaVVELKGPQGLYLLVDKDGLVRCGTPDTKHHGLF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2116737186  90 LIVPQSDGRWALQSEPYLRYFGGSADYLSCFAQAIGEQELWAVHLAL 136
Cdd:cd23346    81 LLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127

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: 75.94 E-value: 9.87e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 380 RPMLILRGENGFVCHHKNSNT-LDANRSVYDIFSLIFND-GAYNVKSVNEKFWYVSSSGlVCSDGEKPEDFFLEFLEHGR 457
Cdd:cd23359     1 RPILVLKCEQGFVGYKSGSNPkLECNKASYETIQVERGDkGLVFFKGQSGKYWGVCGDG-ITADADAPEGFYLELREPSR 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2116737186 458 IAIKGSNGKYLRGDQGGTLMGDGPTVDASSLWEY 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: 75.00 E-value: 2.77e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 259 QVVFQAANKRFVSVKQGV--SISANQDVETDMETFQMeIDKETKKSMFRTNGGSYWTLVTH--GEIQSTATEVEVNTMFD 334
Cdd:cd00257     2 TVALKSSNGKYLSAENGGggPLVANRDAAGPWETFTL-VDLGDGKVALKSSNGKYLSAENGggGTLVANRTAIGPWETFT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2116737186 335 IEWLG-QRVALKASNGKYVCTKKN--GQLSAVSDTVGDDELF 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: 66.52 E-value: 2.72e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186  13 QFGLINYENRYLTAEAFGF-KVNASGISMKKKQIWTLEqdEQDGQVVFLRSHLGRYLA--SDKDGKITCGAEKPDPDCRF 89
Cdd:cd00257     2 TVALKSSNGKYLSAENGGGgPLVANRDAAGPWETFTLV--DLGDGKVALKSSNGKYLSaeNGGGGTLVANRTAIGPWETF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2116737186  90 LIVPQSDGRWALQSEP--YLRYFGGSADYLSCFAQAIGEQELWAV 132
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: 64.98 E-value: 1.05e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 340 QRVALKASNGKYVC--TKKNGQLSAVSDTVGDDELFLMKLINRPMLILRGENG-FVC-HHKNSNTLDANRSVYDifslif 415
Cdd:cd00257     1 GTVALKSSNGKYLSaeNGGGGPLVANRDAAGPWETFTLVDLGDGKVALKSSNGkYLSaENGGGGTLVANRTAIG------ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2116737186 416 ndgaynvksVNEKFWYVSSSGlvcsdgekpedffleflehGRIAIKGSNGKYLR--GDQGGTLMGDGPTVDASSLWE 490
Cdd:cd00257    75 ---------PWETFTLVPLGN-------------------GKVALKSANGKYLSadNGGGGTLIANATSIGAWEKFT 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: 62.67 E-value: 6.60e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 181 GKYSLKTCDSRFLR----NDGKLVkenTNTTS------FTLE-LKSGKLAFKDCDGKYLSPV-GPTGTLRSGRcSKPGKD 248
Cdd:cd00257     1 GTVALKSSNGKYLSaengGGGPLV---ANRDAagpwetFTLVdLGDGKVALKSSNGKYLSAEnGGGGTLVANR-TAIGPW 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2116737186 249 ELFDLEESHP-QVVFQAANKRFVSVKQGVS--ISANQDVETDMETFQM 293
Cdd:cd00257    77 ETFTLVPLGNgKVALKSANGKYLSADNGGGgtLIANATSIGAWEKFTI 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: 61.87 E-value: 1.20e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 339 GQRVALKASNGKYVCTKK-NGQLSAVSDTVGDDELFLMKLINRPMLILRGENG-FVCHHKNSNTLDANRsvydifslifn 416
Cdd:cd23342     1 GSTISLKGNNGKYVSSENgNKPMTANRTSVGSWEKFTVVDAGNGKVALKGNNGkYVSSENGTKPMTCNR----------- 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2116737186 417 dgayNVKSVNEKFWYVSSSGlvcsdgekpedffleflehGRIAIKGSNGKYLRGDQGGT-LMGDGPTVDAsslWE 490
Cdd:cd23342    70 ----TTIGAWEKFTWISLGN-------------------GTVALKGNNGKYVSSENGTNpMTCNRTSIGG---WE 118

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: 60.18 E-value: 4.03e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 137 HPQASLLSVARKRYAHLSASDGEISVDSNIPWGVDSLVTLVYLDGKYSLKTCDSRFLRNDGKLVKENTNTTSFTLELKSG 216
Cdd:cd23350     1 HVHVVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2116737186 217 KL-AFKDCDGKYLSPVGPTGTLRSGrCSKPGKDELFDLE 254
Cdd:cd23350    81 YLaSFFDDCGSMLYPQGRSRLLLSG-NIPINEEEWFIIK 118

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: 53.04 E-value: 1.55e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186  56 QVVFLRSHLGRYLASD--KDGKITCGAEKPDPDCRFLIVPQSDGRWALQSEP--YLRYFGGSADYLSCFAQAIGEQELWA 131
Cdd:cd00257     1 GTVALKSSNGKYLSAEngGGGPLVANRDAAGPWETFTLVDLGDGKVALKSSNgkYLSAENGGGGTLVANRTAIGPWETFT 80

                          90       100
                  ....*....|....*....|....*..
gi 2116737186 132 VHLALHPQASLLSVArKRYahLSASDG 158
Cdd:cd00257    81 LVPLGNGKVALKSAN-GKY--LSADNG 104

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: 50.64 E-value: 6.99e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 257 HPQVVFQAANKrFVSVKQGvsisANQDVE---TDMETFQMEIdKETKKSMFRTNGGSYWTLVTHGEIQSTATEvevNTMF 333
Cdd:cd23337     1 RPILVLRGEYG-FVGVKSG----SSGKLEcnkSTYDVFQLEY-NNDGAYHLKGSNGKYWSVDSDGSVTADSAA---PTPF 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2116737186 334 DIEWLGQ-RVALKASNGKYVCTKKNGQLSAVSDTVGDDELF 373
Cdd:cd23337    72 ILEFRGQsKLAIKAPNGKYLKGEQNGLFKATGTEVDKATLW 112

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: 49.48 E-value: 5.17e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186  57 VVFLRSHLGRYLASDKDGKITCGAEKPDPDCRFLIVPQSD-GRWALQSePYLRYFG-----GSADYLSCFAQAIGEQELW 130
Cdd:cd23339    77 KVTLKSAHGKYLSCDKFGVVTATREARGPQEEWTPVPRPDgGGFALQS-VYGKYLSvdevaGGKLVVRADAETVGFCETW 155


                  ..
gi 2116737186 131 AV 132
Cdd:cd23339   156 RV 157

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: 46.83 E-value: 1.99e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186  13 QFGLINYENRYLTAeAFGFKVNASGISMKKKQIWTLEQDEQDGQVVFlRSHLGRYLASDKDGKITCGAEKPDPDCRFLIV 92
Cdd:cd23336     3 QVSLRAHNGKYVSI-RQGVDVSANQDEETDTETFQLEFDKETKKWAF-RTNKGKYWSLGPDGGIQATASSRSPNCLFELE 80

                          90
                  ....*....|.
gi 2116737186  93 PQSDGRWALQS 103
Cdd:cd23336    81 WNDGGTVALKA 91

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: 46.49 E-value: 3.08e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 154 SASDGEISVDSNIPWGvDSLVTLVYL-DGKYSLKTCDSRFLR----NDGKLV---KENTNTTSFTLE-LKSGKLAFKDCD 224
Cdd:cd00257    17 NGGGGPLVANRDAAGP-WETFTLVDLgDGKVALKSSNGKYLSaengGGGTLVanrTAIGPWETFTLVpLGNGKVALKSAN 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 2116737186 225 GKYLS-PVGPTGTLRSGRcSKPGKDELFDL 253
Cdd:cd00257    96 GKYLSaDNGGGGTLIANA-TSIGAWEKFTI 124

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: 43.65 E-value: 2.51e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 261 VFQAANKRFVSVKQGVsISANQDVETDMETFQMEiDKETKKSMFRTNGGSYWTLVTHGEIQSTATEVEVNTMFDIEWLGQ 340
Cdd:cd23341     4 AFKSHNGHFLSAEDGV-VKTEHGHHDHHTHFHIE-NHGDDKVAIKTHHGKYVAIDDNKQVYLSHHHHGDHTKFHLEHHGG 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2116737186 341 RVALKASNGKYVCTKKNGQLSAvSDTVGDDELF 373
Cdd:cd23341    82 KVAIKGHHHHYIGVDHHGSVHT-SHHHGEDELF 113

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: 42.99 E-value: 4.01e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 184 SLKTCDSRFL--RNDGKLVKENTNT----TSFTLE-LKSGKLAFKDCDGKYLSPVGPTGTLRSGRcSKPGKDELFDLEES 256
Cdd:cd23342     5 SLKGNNGKYVssENGNKPMTANRTSvgswEKFTVVdAGNGKVALKGNNGKYVSSENGTKPMTCNR-TTIGAWEKFTWISL 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2116737186 257 HPQVV-FQAANKRFVSVKQGVS-ISANQDVETDMETFQ 292
Cdd:cd23342    84 GNGTVaLKGNNGKYVSSENGTNpMTCNRTSIGGWEKFT 121

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: 42.64 E-value: 6.68e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 202 ENTNTTSFTLELK--SGKLAFKDCDGKYLSpVGPTGTLRSGRCSKpGKDELFDLEESHPQVVFQAANKRFVSVKQGVSIS 279
Cdd:cd23352    28 EETDQETFQLEIDrdTKKCAFRTHTGKYWT-LTANGGVQSTASTK-NASCYFDIEWRDRRITLRASNGKYVTSKKNGQLA 105

                          90
                  ....*....|....*.
gi 2116737186 280 ANQDVETDMETFQMEI 295
Cdd:cd23352   106 ASVETAGESELFLMKL 121

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: 41.77 E-value: 8.82e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2116737186 329 VNTMFDIEWLGQRVALKASNGKYVCtkKNGQLsavSDTVGDDELFLMKLinRP-MLILRGENG 390
Cdd:cd23335    33 SDALITLEFDDGRYALRTSDGRYLR--SDGSL---VDEPSDDTLFTLEF--RSgGLAFKDSEG 88

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: 41.39 E-value: 1.39e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2116737186 180 DGKYSLKTCDSRFLR--NDGKLVKENTNTTSFTLELKSG-KLAFKDCDGKYLspVG-PTGTLRSgRCSKPGKDELF 251
Cdd:cd23337    40 DGAYHLKGSNGKYWSvdSDGSVTADSAAPTPFILEFRGQsKLAIKAPNGKYL--KGeQNGLFKA-TGTEVDKATLW 112

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: 41.36 E-value: 2.34e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186  46 WTLEQDEQDGQVVFLRSHLGRYLASDKDGKITCGA-----EKPDPDCRFLIVPQSDGRWALQSePYLRYFG-GSADYLSC 119
Cdd:cd23338     7 WKVKEFEEITGNVAIEFGSGRYVKALDNGLFTLGAphdegEGPDPEEIFTAIKVSDTKIALKS-GYGKYLSvDSDGKVVG 85

                          90
                  ....*....|.
gi 2116737186 120 FAQAIGEQELW 130
Cdd:cd23338    86 RSDAIGPREQW 96

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

Pssm-ID: 467444 Cd Length: 124 Bit Score: 39.51 E-value: 6.72e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 181 GKYSLKTCDSRF--LRNDGKLV---KENTNTTSFTLE-LKSGKLAFKDCDGKYLSpVGPTGTLRSGrCSKPGKDELFDLE 254
Cdd:cd23336    44 KKWAFRTNKGKYwsLGPDGGIQataSSRSPNCLFELEwNDGGTVALKASNGKYVT-AKPNGQLAAT-SDEVGEKEKFTLK 121

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

Pssm-ID: 368803 Cd Length: 189 Bit Score: 40.48 E-value: 9.03e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2116737186  67 YLASDKDGKITCGA-----EKPDPDCRFLIVPQSDGRWALQSEpYLRYFGGSADY-LSCFAQAIGEQELWAV 132
Cdd:pfam06229   3 YLEAMDNGLFTTGEphdvgEGPDPEEVFTAVKVSDEKIALKSG-YGKYLGVNKDGiLSARADAIGPREQFEP 73

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: 38.66 E-value: 1.43e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2116737186 392 VCHHKNSNTLDANR--SVYDIFSLIFNDGAYNVKSVNEKfwYVSSSGLVCSDGEKPEDFFLEFlEHGRIAIKGSNGKYL 468
Cdd:cd23349    17 LSVQEDEIATDSNIpwGVDALITLIFQDKKYCLKTCDSR--FLRNDGKLVKEPGPGTGYTLEF-KAGKLAFKDCDGKYL 92

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: 1.48e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 264 AANKRFVSVKQ-GVSISANQDVETDMETFQMEiD----KETKKSMfrTNGgSYWTLVTHGEIQSTATEV---EVNTMFDI 335
Cdd:cd23343    10 AATGKYVTVGEeGGALAADAEDAEEAETFELT-DwgwgSHTLRSV--ANG-KYVTTDDDGTLTASAEEAfgwFVKEVFRL 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2116737186 336 EWLGQ-RVALKASNGKYVCTKKNGQLSAVSDT-VGDDELF 373
Cdd:cd23343    86 EPQEDgTVSLRTWNGRPVAVDEDGRLTVGEDDaAAEAERF 125

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: 2.08e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 217 KLAFKDCDGKYLSpVGPTGTLRsGRCSKPGKDELFdleeshpQVVFQ-------AANKRFVSVKQGVSISANQDVETDME 289
Cdd:cd23338    64 KIALKSGYGKYLS-VDSDGKVV-GRSDAIGPREQW-------EPVFQdgkmallGANNCFLSVNEDGDIVATSKTAGENE 134


                  ....
gi 2116737186 290 TFQM 293
Cdd:cd23338   135 MIKI 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: 37.95 E-value: 2.37e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 410 IFSLIFNDGAYNV---KSVNEKFWYVSSSGLVCSDGEKP---EDFFLEFLEHGRIAIKGSN-GKYLRGdQGGTLMGDGPT 482
Cdd:cd23334    34 TWTLEQDEGGSETvylKSHLGRYLSADKDGKVTCDAEEPgadERFLIEYQPDGRWALKSEKhGRYLGG-TGDNLSCFAKE 112


                  ....*..
gi 2116737186 483 VDASSLW 489
Cdd:cd23334   113 VSESELW 119

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: 38.28 E-value: 2.45e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186 304 FRTNGGSYWTLVTHGEIQSTATEVEVNTMFDIEWLGQRVALKASNGKYVCTKKNGQLSAVSDTVGDDELF 373
Cdd:cd23338    67 LKSGYGKYLSVDSDGKVVGRSDAIGPREQWEPVFQDGKMALLGANNCFLSVNEDGDIVATSKTAGENEMI 136

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: 2.45e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2116737186  20 ENRYLTA---EAFGFKVnasgismkkKQIWTLEqdEQDGQVVFLRSHLGRYLASDKDGKITCGAEK-PDPDCRFLIVPQS 95
Cdd:cd23343    63 DDGTLTAsaeEAFGWFV---------KEVFRLE--PQEDGTVSLRTWNGRPVAVDEDGRLTVGEDDaAAEAERFEKEVVE 131


                  ..
gi 2116737186  96 DG 97
Cdd:cd23343   132 DG 133

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

Pssm-ID: 368803 Cd Length: 189 Bit Score: 38.56 E-value: 3.25e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2116737186 299 TKKSMFRTNGGSYWTLVTHGEIQSTATEVEVNTMFDIEWLGQRVALKASNGKYVCTKKNGQLSAVSDTVGDDELF 373
Cdd:pfam06229  37 DEKIALKSGYGKYLGVNKDGILSARADAIGPREQFEPVFQEGKMALLAANGCFLSVDPSGDIVAKSKTAGEGEMV 111

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

Pssm-ID: 467443 Cd Length: 117 Bit Score: 36.37 E-value: 7.59e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2116737186 411 FSLIFNDGAYNVKSVNEKFwyvsssglVCSDG---EKPED---FFLEFLEhGRIAIKGSNGKYLRGDQG-GTLM 477
Cdd:cd23335    37 ITLEFDDGRYALRTSDGRY--------LRSDGslvDEPSDdtlFTLEFRS-GGLAFKDSEGKYLTAVGGsGVLK 101