NCBI Conserved Domain Search

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: 260.07 E-value: 1.28e-85

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  22 KGWWTIGLINGQHKYMTAETFGFKLNANGASLKKKQLWTLEPSNTGESIIYLRSHLNKYLSVDQFGNVLCESDERDAGSR 101
Cdd:cd23347    1 SFTWTVGLINSQQKYLTAETFGFKVNANGSSLKKKQLWTLEPFGDGTNVVALRSHLGRYLSVDQFGNVTCEAEEKGEGSR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 281360572 102 FQISISEDGSGRWALKNESRGYFLGGTPDKLVCTAKTPGASEFWTVHLAA 151
Cdd:cd23347   81 FEIVISEDESGRWAFRNEERGYFLGGSGDKLVCTAKAPTDSELWTVHLAA 130

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: 245.96 E-value: 2.68e-80

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 274 LPQASFIAGLNLRYVSVKQGVDVTANQDEVGENETFQLEYDWSAHRWALRTTQDRYWCLSAGGGIQATGNRRCADALFEL 353
Cdd:cd23355    1 LPQAAFIAGLNSRYVSVKQGVDVTANQDEISDHETFQLEYDWSTKRWYIRTMQDRYWTLETAGGIQASADKKSANALFEL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 281360572 354 IWHGDGSLSFRANNGKFLATKRSGHLFATSESIEEIAKFYFYLIN 398
Cdd:cd23355   81 EWQEDGSVSFRANNGKFVGTKRSGHLFANSESIDEIAKFYFYLIN 125

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: 228.42 E-value: 1.46e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 152 RPQVNLRSIGRKRFAHLSESQDEIHVDANIPWGEDTLFTLEFRaeEGGRYALHTCNNKYLNANGKLQVVCNEDCLFSAEY 231
Cdd:cd23351    1 RPQVNLRSAGRKRYARLSGDEDEIQVDANVPWGSDTLFTLEFR--DDGRYAIHTANGKYLNRDGKLVEECPEDCLFTLEY 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 281360572 232 HGGHLALRDRQGQYLSPIGSKAVLKSRSSSVTRDELFSLED 272
Cdd:cd23351   79 HAGQVAFRDRTGKYLAPIGSKAVLRTRSTSVTKDELFILED 119

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: 216.54 E-value: 4.73e-69

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 399 RPILVLKCEQGFVGYRTPGNLKLECNKATYETILVERAQKGLVHLKAHSGKYWRIEGESISVDADAPsDGFFLELREPTR 478
Cdd:cd23359    1 RPILVLKCEQGFVGYKSGSNPKLECNKASYETIQVERGDKGLVFFKGQSGKYWGVCGDGITADADAP-EGFYLELREPSR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 281360572 479 ICIRSQQGKYLGATKNGAFKLLDDGTDSATQWEF 512
Cdd:cd23359   80 LCIKTADGSYLMADKNGAFKVGDADPETATLWEF 113

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: 202.82 E-value: 1.45e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  25 WTIGLINGQHKYMTAETFGFKLNANGASLKKKQLWTLEPSNTGESIIYLRSHLNKYLSVDQFGNVLCESDERDAGSRFQI 104
Cdd:cd23334    1 WKLGLINSSGKYLTAETFGFKVNASGTSLKKKQTWTLEQDEGGSETVYLKSHLGRYLSADKDGKVTCDAEEPGADERFLI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 281360572 105 SISEDgsGRWALKNESRGYFLGGTPDKLVCTAKTPGASEFWTVHLA 150
Cdd:cd23334   81 EYQPD--GRWALKSEKHGRYLGGTGDNLSCFAKEVSESELWTVHLA 124

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: 190.12 E-value: 1.09e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 275 PQASFIAgLNLRYVSVKQGVDVTANQDEVGENETFQLEYDWSAHRWALRTTQDRYWCLSAGGGIQATGNRRCADALFELI 354
Cdd:cd23336    2 PQVSLRA-HNGKYVSIRQGVDVSANQDEETDTETFQLEFDKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 281360572 355 WHGDGSLSFRANNGKFLATKRSGHLFATSESIEEIAKFYFYLIN 398
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: 185.06 E-value: 6.78e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 153 PQVNLRSIGRKRFAHLSESQDEIHVDANIPWGEDTLFTLEFRaeeGGRYALHTCNNKYLNANGKLQVVCNEDCLFSAEYH 232
Cdd:cd23335    1 PQVNLYSVNRKRYARLDPEGDELRVDEDIPWGSDALITLEFD---DGRYALRTSDGRYLRSDGSLVDEPSDDTLFTLEFR 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 281360572 233 GGHLALRDRQGQYLSPIGSKAVLKSRSSSVTRDELFSLED 272
Cdd:cd23335   78 SGGLAFKDSEGKYLTAVGGSGVLKTRKKTVGKDELFSLED 117

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

Pssm-ID: 467445 Cd Length: 114 Bit Score: 153.87 E-value: 4.16e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 399 RPILVLKCEQGFVGYRTPGNLKLECNKATYETILVERAQKGLVHLKAHSGKYWRIEGE-SISVDADAPSDgFFLELREPT 477
Cdd:cd23337    1 RPILVLRGEYGFVGVKSGSSGKLECNKSTYDVFQLEYNNDGAYHLKGSNGKYWSVDSDgSVTADSAAPTP-FILEFRGQS 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 281360572 478 RICIRSQQGKYLGATKNGAFKLLDDGTDSATQWEF 512
Cdd:cd23337   80 KLAIKAPNGKYLKGEQNGLFKATGTEVDKATLWEY 114

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: 154.59 E-value: 5.00e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  28 GLINGQHKYMTAETFGFKLNANGASLKKKQLWTLEPSNTGESIIYLRSHLNKYLSVDQFGNVLCESDERDAGSRFQISIS 107
Cdd:cd23345    9 GLINCENRYLTAEAFGFKVNASAPSLKKKQIWTLEQDEGDSSVVFLKSHLGRYLSADKDGKVSCEAEKPGRDCRFLIVAQ 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 281360572 108 EDgsGRWALKNESRGYFLGGTPDKLVCTAKTPGASEFWTVHLA 150
Cdd:cd23345   89 SD--GRWALQSEPHKRFFGGSEDKLSCFAQTITEAELWAVHLA 129

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: 151.16 E-value: 8.97e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  27 IGLINGQHKYMTAETFGFKLNANGASLKKKQLWTLEPS--NTGESIIYLRSHLNKYLSVDQFGNVLCESDERDAGSRFQI 104
Cdd:cd23344    4 FGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPgdEADSSAVLLRSHLGRYLAADKDGNVTCESEVPGPDCRFLI 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 281360572 105 SISEDgsGRWALKNESRGYFLGGTPDKLVCTAKTPGASEFWTVHLAA 151
Cdd:cd23344   84 VAHDD--GRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAM 128

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: 127.64 E-value: 3.89e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 153 PQVNLRSIGRKRFAHLSESQDEIHVDANIPWGEDTLFTLEFRAeegGRYALHTCNNKYLNANGKLQVVCNEDCLFSAEYH 232
Cdd:cd23349    2 PQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQD---KKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 281360572 233 GGHLALRDRQGQYLSPIGSKAVLKS-RSSSVTRDELFSLED 272
Cdd:cd23349   79 AGKLAFKDCDGKYLTPMGPTGTLKSgRSSKPGKDELFDLEE 119

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: 125.52 E-value: 1.39e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572   33 QHKYMTAETFGFKLNANGASLKKKQLWTLEPSNtGESIIYLRSHLNKYLSVDQFGNVLCESDERDAGSRFQISIsedgSG 112
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDD-ERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEF----RG 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 281360572  113 RWALKNESRGYFLG-GTPDKLVCTAKTPGASEFWTV 147
Cdd:pfam06268  76 RWALLRESNGRYLGgGPSGLLKANASTVGKDELWTL 111

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: 115.70 E-value: 7.76e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 153 PQVNLRSIGRKRFAHLSESQ-DEIHVDANIPWGEDTLFTLEFRAEeggRYALHTCNNKYLNANGKLQVVCNEDCLFSAEY 231
Cdd:cd23348    2 PQVNIYSVTRKRYAHLSARPaDEIAVDRDVPWGVDSLITLVFQDQ---RYSVQTSDHRFLRHDGRLVARPEPATGYTLEF 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 281360572 232 HGGHLALRDRQGQYLSPIGSKAVLKS-RSSSVTRDELFSLE 271
Cdd:cd23348   79 RSGKVAFRDCEGRYLAPSGPSGTLKAgKSTKVGKDELFVLE 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: 113.45 E-value: 7.02e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 275 PQASFIAGlNLRYVSVKQGVDVTANQDEVGENETFQLEYDWSAHRWALRTTQDRYWCLSAGGGIQATGNRRCADALFELI 354
Cdd:cd23353    2 PQVVFQAA-NGRYVSIRQGVNVSANQDEETDHETFQMQIDKETKKCSFHTNTGKYWTLVAHGGIQSTATEVAANTMFDIE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 281360572 355 WHGDgSLSFRANNGKFLATKRSGHLFATSESIEEIAKFYFYLIN 398
Cdd:cd23353   81 WRGR-RVALKASNGKYVCTKKNGQLAAVSDSVGEDEEFTLKLIN 123

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: 110.05 E-value: 1.06e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 274 LPQASFIAGlNLRYVSVKQGVDVTANQDEVGENETFQLEYDWSAHRWALRTTQDRYWCLSAGGGIQATGNRRCADALFEL 353
Cdd:cd23352    1 CPQVVLQAA-NERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 281360572 354 IWHgDGSLSFRANNGKFLATKRSGHLFATSESIEEIAKFYFYLIN 398
Cdd:cd23352   80 EWR-DRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

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

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 93.16 E-value: 8.35e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  155 VNLRSIGRKRFAHLSESQ-DEIHVDanipwgedtLFTLEFRaEEGGRYALHTCNNKYLN--ANGKLQVVCN---EDCLFS 228
Cdd:pfam06268   1 ANGYLVSERRGAHLNANReSLKRVQ---------TFTLEFD-DERYTVYLRSHNGKYLScdADGRVVCEAErrsADTFFE 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 281360572  229 AEYHGGHLALRDRQGQYLSpIGSKAVLKSRSSSVTRDELFSL 270
Cdd:pfam06268  71 LEFRGRWALLRESNGRYLG-GGPSGLLKANASTVGKDELWTL 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: 83.92 E-value: 1.52e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  284 NLRYVSVKQGVDVTANQDEVGENETFQLEYDWSAHRWALRTTQDRYWCLSAGGGIQATGNRRCADALFELIWHGdGSLSF 363
Cdd:pfam06268   2 NGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRG-RWALL 80

                          90       100
                  ....*....|....*....|...
gi 281360572  364 RANNGKFLATKRSGHLFATSESI 386
Cdd:pfam06268  81 RESNGRYLGGGPSGLLKANASTV 103

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: 76.38 E-value: 8.47e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 399 RPILVLKCEQGFVGYRTPGNLkLECNKATYETILVErAQKGLVHLKAHSGKYWRIEGE-SISVDADAPSDgFFLELREPT 477
Cdd:cd23357    1 RPILVLRGEHGFVCHHKGSNT-LDANRSVYDVFQLI-FSDGAYQIKGQGGKFWYISSSgTVCSDGDMPED-FFFEFREHG 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 281360572 478 RICIRSQQGKYLGATKNGAFKLLDDGTDSATQWEF 512
Cdd:cd23357   78 RVAIKGKNGKYLRGDQAGTLKADAETVDSATLWEY 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: 71.15 E-value: 6.36e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 286 RYVSVKQGVD--VTANQDEVGENETFQLEyDWSAHRWALRTTQDRYWCLSAGGG--IQATGNRRCADALFELIWHGDGSL 361
Cdd:cd00257   11 KYLSAENGGGgpLVANRDAAGPWETFTLV-DLGDGKVALKSSNGKYLSAENGGGgtLVANRTAIGPWETFTLVPLGNGKV 89

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 281360572 362 SFRANNGKFLATKRSGH--LFATSESIEEIAKFYF 394
Cdd:cd00257   90 ALKSANGKYLSADNGGGgtLIANATSIGAWEKFTI 124

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: 66.42 E-value: 3.66e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  27 IGLINGQHKYMTAETFGFKLNANGASLKKKQLWTLEPSNTGE--SIIYLRSHLNKYLSVDQFGNVLCESDERDAGSRFQI 104
Cdd:cd23346    3 VGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVIVSDYSDrqAVVELKGPQGLYLLVDKDGLVRCGTPDTKHHGLFLL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 281360572 105 SISedGSGRWALKNESRGYFLGGTPDKLVCTAKTPGASEFWTVHLA 150
Cdd:cd23346   83 KFH--VSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPA 126

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: 1.50e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  26 TIGLINGQHKYMTAETFGF-KLNANGASLKKKQLWTLEPSNTGesIIYLRSHLNKYLSVDQFGN--VLCESDERDAGSRF 102
Cdd:cd00257    2 TVALKSSNGKYLSAENGGGgPLVANRDAAGPWETFTLVDLGDG--KVALKSSNGKYLSAENGGGgtLVANRTAIGPWETF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 281360572 103 QisISEDGSGRWALKNeSRGYFL---GGTPDKLVCTAKTPGASEFWTV 147
Cdd:cd00257   80 T--LVPLGNGKVALKS-ANGKYLsadNGGGGTLIANATSIGAWEKFTI 124

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: 62.97 E-value: 3.69e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 399 RPILVLKCEQGFVGYRTPGNlKLECNKATYETILVErAQKGLVHLKAHSGKYWRIEGE-SISVDADAPSDgFFLELREPT 477
Cdd:cd23356    1 RPIIVLRGEHGFIGCRKVTG-TLDSNRSSYDVFQLE-FNDGAYNIKDSTGKYWTVGSDsAVTSSGDTPVD-FFFEFCDYN 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 281360572 478 RICIRSqQGKYLGATKNGAFKLLDDGTDSATQWEF 512
Cdd:cd23356   78 KVAIKV-GGRYLKGDHAGVLKASAETVDPATLWEY 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: 62.45 E-value: 8.56e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 283 LNLRYVSVKQGVDVTANQDEVGENETFQLEYDWSAHRWALRTTQDRYWCLSAGGGIQATGNRRCADALFELIWHGdGSLS 362
Cdd:cd23354    9 KNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVEWRC-GKII 87

                         90       100
                 ....*....|....*....|.
gi 281360572 363 FRANNGKFLATKRSGHLFATS 383
Cdd:cd23354   88 LQASNGRYLGVKPNGLLTASA 108

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: 57.28 E-value: 4.98e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 410 FVGYRTPGNLKLECNKAT---YETILVERAQKGLVHLKAHSGKYWRIEGESIS-VDADAPSDG----FFLELREPTRICI 481
Cdd:cd00257   12 YLSAENGGGGPLVANRDAagpWETFTLVDLGDGKVALKSSNGKYLSAENGGGGtLVANRTAIGpwetFTLVPLGNGKVAL 91

                         90       100       110
                 ....*....|....*....|....*....|
gi 281360572 482 RSQQGKYLGATKNGAFKLLDDGtDSATQWE 511
Cdd:cd00257   92 KSANGKYLSADNGGGGTLIANA-TSIGAWE 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: 57.23 E-value: 5.59e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 153 PQVNLRSIGRKRF-----AHLSESQDEIhvdanipwGEDTLFTLEFrAEEGGRYALHTCNNKY--LNANGKLQVV---CN 222
Cdd:cd23336    2 PQVSLRAHNGKYVsirqgVDVSANQDEE--------TDTETFQLEF-DKETKKWAFRTNKGKYwsLGPDGGIQATassRS 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 281360572 223 EDCLFSAEYH-GGHLALRDRQGQYLS--PIGSkavLKSRSSSVTRDELFSLE 271
Cdd:cd23336   73 PNCLFELEWNdGGTVALKASNGKYVTakPNGQ---LAATSDEVGEKEKFTLK 121

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

Pssm-ID: 467447 Cd Length: 160 Bit Score: 57.95 E-value: 5.88e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  60 TLEPSNT----------GESIIYLRSHLNKYLSVDQFGNVLCESDERDAGSRFQISISEDGsGRWALKNeSRGYFLGGTP 129
Cdd:cd23339   57 TAEPTDVrqvwvatrvvGTGKVTLKSAHGKYLSCDKFGVVTATREARGPQEEWTPVPRPDG-GGFALQS-VYGKYLSVDE 134

                         90       100
                 ....*....|....*....|...
gi 281360572 130 DKLV-----CTAKTPGASEFWTV 147
Cdd:cd23339  135 VAGGklvvrADAETVGFCETWRV 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: 53.43 E-value: 9.28e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  69 SIIYLRSHLNKYLSVDQFGN--VLCESDERDAGSRFQisISEDGSGRWALKNeSRGYFL---GGTPDKLVCTAKTPGASE 143
Cdd:cd00257    1 GTVALKSSNGKYLSAENGGGgpLVANRDAAGPWETFT--LVDLGDGKVALKS-SNGKYLsaeNGGGGTLVANRTAIGPWE 77

                         90
                 ....*....|....*.
gi 281360572 144 FWTVHLAARPQVNLRS 159
Cdd:cd00257   78 TFTLVPLGNGKVALKS 93

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: 48.26 E-value: 5.63e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 399 RPILVLKCEQGFVGyRTPGNLKLECNKATYETILVERAQKGLVHLKAHSGKYWRI-EGESISVDADAPSDgFFLELREPT 477
Cdd:cd23358    1 RSFLILRGKYGYVG-SSSHHDVLQCNLPEPDQISLLPCKPGFYHFQGQNGSFWSItSDGTFRAWGKFALN-FCIEIQGSN 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 281360572 478 RICIRSQQGKYLGATKNGAfkLLDDGT--DSATQWEF 512
Cdd:cd23358   79 LLAILAPNGCYLRGDNSGT--LLADSEiiTSECLWEF 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: 48.38 E-value: 6.39e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 280 IAGLNLRYVSVKQGV-DVTANQDEVGENETFQLEyDWSAHRWALRTTQDRYWCLSAGGG-IQATGNRRCADALFELIWHG 357
Cdd:cd23342    6 LKGNNGKYVSSENGNkPMTANRTSVGSWEKFTVV-DAGNGKVALKGNNGKYVSSENGTKpMTCNRTTIGAWEKFTWISLG 84

                         90
                 ....*....|....
gi 281360572 358 DGSLSFRANNGKFL 371
Cdd:cd23342   85 NGTVALKGNNGKYV 98

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: 46.04 E-value: 4.54e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 237 ALRD-RQGQYLSPIGSKAVLKSRSSSVTRDELFSLED----SLpqaSFIAGLNLRYVSVKQGVDVTANQDEVGE---NET 308
Cdd:cd23343    6 ALRSaATGKYVTVGEEGGALAADAEDAEEAETFELTDwgwgSH---TLRSVANGKYVTTDDDGTLTASAEEAFGwfvKEV 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 281360572 309 FQLEYDwSAHRWALRTTQDRYWCLSAGGGIQAT-GNRRCADALFEL 353
Cdd:cd23343   83 FRLEPQ-EDGTVSLRTWNGRPVAVDEDGRLTVGeDDAAAEAERFEK 127

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: 45.55 E-value: 6.39e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 155 VNLRSIGRKRFAHLSESQDEIHVDANIPWGEDTLFTLEFRaeeGGRYALHTCNNKYLNANGKLQVVCNEDCLFSAEYHGG 234
Cdd:cd23350    4 VVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFR---KGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 281360572 235 HL-ALRDRQGQYLSPIGSKAVLKSRSSSVTRDELFSLE 271
Cdd:cd23350   81 YLaSFFDDCGSMLYPQGRSRLLLSGNIPINEEEWFIIK 118

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

Pssm-ID: 467451 Cd Length: 133 Bit Score: 44.49 E-value: 1.73e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 286 RYVSVKQGVDV-TANQDEVGENETFQLEyDWSAHRWALRTTQ-DRYWCLSAGGGIQATgnrrcADA--------LFELIW 355
Cdd:cd23343   14 KYVTVGEEGGAlAADAEDAEEAETFELT-DWGWGSHTLRSVAnGKYVTTDDDGTLTAS-----AEEafgwfvkeVFRLEP 87

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 281360572 356 HGDGSLSFRANNGKFLATKRSGHLFAT-SESIEEIAKF 392
Cdd:cd23343   88 QEDGTVSLRTWNGRPVAVDEDGRLTVGeDDAAAEAERF 125

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: 43.72 E-value: 3.02e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 321 ALRTTQD-RYWCLSAGGG-IQATGNRRCADALFELI-WhGDGSLSFRA-NNGKFLATKRSGHLFATSESI 386
Cdd:cd23343    6 ALRSAATgKYVTVGEEGGaLAADAEDAEEAETFELTdW-GWGSHTLRSvANGKYVTTDDDGTLTASAEEA 74

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: 42.64 E-value: 5.48e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281360572 441 VHLKAHSGKYWRIE---GESISVDADAPSDG--FFLELREPTRICIRSQQGKYLGATKNGAFKLLDDGTDSATqWE 511
Cdd:cd00257    3 VALKSSNGKYLSAEnggGGPLVANRDAAGPWetFTLVDLGDGKVALKSSNGKYLSAENGGGGTLVANRTAIGP-WE 77

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

Pssm-ID: 467445 Cd Length: 114 Bit Score: 42.16 E-value: 6.39e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 307 ETFQLEYDWSAHrWALRTTQDRYWCLSAGGGIQATGNRrCADALFELiwHGDGSLSFRANNGKFLATKRSGHLFATSESI 386
Cdd:cd23337   31 DVFQLEYNNDGA-YHLKGSNGKYWSVDSDGSVTADSAA-PTPFILEF--RGQSKLAIKAPNGKYLKGEQNGLFKATGTEV 106


                 ....*...
gi 281360572 387 EEIAKFYF 394
Cdd:cd23337  107 DKATLWEY 114

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

Pssm-ID: 467450 [Multi-domain] Cd Length: 122 Bit Score: 41.83 E-value: 1.16e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 417 GNLKLECNKAT---YETILVERAQKGLVHLKAHSGKYWRIEGESISVDADAPSDG----FFLELREPTRICIRSQQGKYL 489
Cdd:cd23342   19 GNKPMTANRTSvgsWEKFTVVDAGNGKVALKGNNGKYVSSENGTKPMTCNRTTIGawekFTWISLGNGTVALKGNNGKYV 98

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: 42.13 E-value: 1.25e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  23 GWWTIGLIN----------GQHKYMTA-ETFGFKLnanGASLKKKQlwtlEPS--------NTGESIIYLRSHLNKYLSV 83
Cdd:cd23338    5 GWWKVKEFEeitgnvaiefGSGRYVKAlDNGLFTL---GAPHDEGE----GPDpeeiftaiKVSDTKIALKSGYGKYLSV 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281360572  84 DQFGNVLCESDERDAGSRFQIsISEDgsGRWALKNeSRGYFLGGTPD-KLVCTAKTPGASEF 144
Cdd:cd23338   78 DSDGKVVGRSDAIGPREQWEP-VFQD--GKMALLG-ANNCFLSVNEDgDIVATSKTAGENEM 135

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: 41.49 E-value: 1.69e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 153 PQV-----NLRSIGRKRFAHLSESQDEihvdanipWGEDTLFTLEFrAEEGGRYALHTCNNKY--LNANGKLQVVC---N 222
Cdd:cd23352    2 PQVvlqaaNERNVSTRQGMDLSANQDE--------ETDQETFQLEI-DRDTKKCAFRTHTGKYwtLTANGGVQSTAstkN 72

                         90       100
                 ....*....|....*....|....*.
gi 281360572 223 EDCLFSAEYHGGHLALRDRQGQYLSP 248
Cdd:cd23352   73 ASCYFDIEWRDRRITLRASNGKYVTS 98

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: 40.01 E-value: 3.86e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572  409 GFVGYRTPGNlKLECNKAT---YETILVE-RAQKGLVHLKAHSGKYWRIEGES-ISVDADAPSDGFFLELREPTRICIRS 483
Cdd:pfam06268   3 GYLVSERRGA-HLNANRESlkrVQTFTLEfDDERYTVYLRSHNGKYLSCDADGrVVCEAERRSADTFFELEFRGRWALLR 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 281360572  484 Q-QGKYLGATKNGAFKLLDDGTDSATQWEF 512
Cdd:pfam06268  82 EsNGRYLGGGPSGLLKANASTVGKDELWTL 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: 37.95 E-value: 2.68e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 236 LALRDRQGQYLS--PIGSKavLKSRSSSVTRDELFSLE--DSLPQASFIAGLNLRYVSVKQGVDVTANQDEVGENETFQL 311
Cdd:cd23334    3 LGLINSSGKYLTaeTFGFK--VNASGTSLKKKQTWTLEqdEGGSETVYLKSHLGRYLSADKDGKVTCDAEEPGADERFLI 80

                         90
                 ....*....|....*...
gi 281360572 312 EYDWSAhRWALRTTQDRY 329
Cdd:cd23334   81 EYQPDG-RWALKSEKHGR 97

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

Pssm-ID: 467447 Cd Length: 160 Bit Score: 38.69 E-value: 2.78e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 356 HGDGSLSFRANNGKFLATKRSGHLFATSESI--EEiakfyfylinrpilvlkceqgfvgyrtpgnlklecnkatyETILV 433
Cdd:cd23339   73 VGTGKVTLKSAHGKYLSCDKFGVVTATREARgpQE----------------------------------------EWTPV 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 281360572 434 ERAQKGLVHLKAHSGKYWRIE---GESISVDADAPSDGFflelrePTRICIRSQ 484
Cdd:cd23339  113 PRPDGGGFALQSVYGKYLSVDevaGGKLVVRADAETVGF------CETWRVRVQ 160

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: 3.67e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360572 110 GSGRWALKNESRGYFLGGTPDK--LVCTAKTPGASE-F------WTVHlaarpqvNLRSIGRKRFahLSESQDE-IHVDA 179
Cdd:cd23343    1 GVDRIALRSAATGKYVTVGEEGgaLAADAEDAEEAEtFeltdwgWGSH-------TLRSVANGKY--VTTDDDGtLTASA 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 281360572 180 NIPWG----EdtlfTLEFRAEEGGRYALHTCNNKYL--NANGKLQVVCNED 224
Cdd:cd23343   72 EEAFGwfvkE----VFRLEPQEDGTVSLRTWNGRPVavDEDGRLTVGEDDA 118

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: 37.51 E-value: 4.60e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281360572 321 ALRTTQDRYWCLSAGGGIQATgnrrcADA-----LFELIWHgDGSLSFRANNGKFLATKRSGHLFATSESIEE 388
Cdd:cd23338   66 ALKSGYGKYLSVDSDGKVVGR-----SDAigpreQWEPVFQ-DGKMALLGANNCFLSVNEDGDIVATSKTAGE 132