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: 281.32 E-value: 3.20e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418   7 HQVLKIQFGLINSDNRYLTAESFGYKVNASAPSLKRKQIWTLEQD-GDSSVVFLKSHLGRYLSADKDGKVSGEAEKPGSD 85
Cdd:cd23345     1 HQALKIQFGLINCENRYLTAEAFGFKVNASAPSLKKKQIWTLEQDeGDSSVVFLKSHLGRYLSADKDGKVSCEAEKPGRD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2118037418  86 GRFIIVTQSDGRWALQSEPYKRFFGGSEDKLSCFAQTITEAELWAVHLAI 135
Cdd:cd23345    81 CRFLIVAQSDGRWALQSEPHKRFFGGSEDKLSCFAQTITEAELWAVHLAI 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: 270.16 E-value: 4.37e-90

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 136 HPQANLLSVSRRRYAHLSAQEDEIATDSNIPWGVDSLITLTFQNKKYCLRTCDNRYLRNDGTLIKEPDPRAGYTLEFKAG 215
Cdd:cd23349     1 HPQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKAG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2118037418 216 KLAFKDCDGKYLAPMGPTGTLKSGRSSKPGKDELFDLEE 254
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: 262.14 E-value: 8.62e-87

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 256 HPQVVFLASNGRYVSIRQGVNVSANQDEETHHETFQMQIDKETKKCIFHSNTGSYWTLVSHGGIQATATEISASTMFDVE 335
Cdd:cd23353     1 HPQVVFQAANGRYVSIRQGVNVSANQDEETDHETFQMQIDKETKKCSFHTNTGKYWTLVAHGGIQSTATEVAANTMFDIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2118037418 336 WRGRRVALKAGNGKYICTKKNGQLAAVSDAVGEDEEFVLKLIN 378
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: 228.20 E-value: 1.75e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  11 KIQFGLINSDNRYLTAESFGYKVNASAPSLKRKQIWTLEQDG---DSSVVFLKSHLGRYLSADKDGKVSGEAEKPGSDGR 87
Cdd:cd23344     1 QIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPGdeaDSSAVLLRSHLGRYLAADKDGNVTCESEVPGPDCR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2118037418  88 FIIVTQSDGRWALQSEPYKRFFGGSEDKLSCFAQTITEAELWAVHLAI 135
Cdd:cd23344    81 FLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAM 128

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: 226.60 E-value: 3.43e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 379 RPILVLRGTHGFVCYHRNSNLLDANRSVYDVFHIIFNDGAYQIKGLGGKFWYVASNGTVCSDGEMSEDFFLEFRECSRVA 458
Cdd:cd23357     1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLIFSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRVA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2118037418 459 IKGKNGKYLRGDQAGTLRADADLLHRATLWEY 490
Cdd:cd23357    81 IKGKNGKYLRGDQAGTLKADAETVDSATLWEY 112

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: 221.31 E-value: 6.44e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  12 IQFGLINSDNRYLTAESFGYKVNASAPSLKRKQIWTLEQD-GDSSVVFLKSHLGRYLSADKDGKVSGEAEKPGSDGRFII 90
Cdd:cd23334     1 WKLGLINSSGKYLTAETFGFKVNASGTSLKKKQTWTLEQDeGGSETVYLKSHLGRYLSADKDGKVTCDAEEPGADERFLI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2118037418  91 VTQSDGRWALQSEPYKRFFGGSEDKLSCFAQTITEAELWAVHLAI 135
Cdd:cd23334    81 EYQPDGRWALKSEKHGRYLGGTGDNLSCFAKEVSESELWTVHLAI 125

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: 205.06 E-value: 1.17e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 136 HPQANLLSVSRRRYAHLSA-QEDEIATDSNIPWGVDSLITLTFQNKKYCLRTCDNRYLRNDGTLIKEPDPRAGYTLEFKA 214
Cdd:cd23348     1 HPQVNIYSVTRKRYAHLSArPADEIAVDRDVPWGVDSLITLVFQDQRYSVQTSDHRFLRHDGRLVARPEPATGYTLEFRS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2118037418 215 GKLAFKDCDGKYLAPMGPTGTLKSGRSSKPGKDELFDLEE 254
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: 201.29 E-value: 2.97e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 256 HPQVVFLASNGRYVSIRQGVNVSANQDEETHHETFQMQIDKETKKCIFHSNTGSYWTLVSHGGIQATATEISASTMFDVE 335
Cdd:cd23336     1 HPQVSLRAHNGKYVSIRQGVDVSANQDEETDTETFQLEFDKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2118037418 336 WR-GRRVALKAGNGKYICTKKNGQLAAVSDAVGEDEEFVLKLIN 378
Cdd:cd23336    81 WNdGGTVALKASNGKYVTAKPNGQLAATSDEVGEKEKFTLKLIN 124

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: 184.39 E-value: 9.21e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 257 PQVVFLASNGRYVSIRQGVNVSANQDEETHHETFQMQIDKETKKCIFHSNTGSYWTLVSHGGIQATATEISASTMFDVEW 336
Cdd:cd23352     2 PQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIEW 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2118037418 337 RGRRVALKAGNGKYICTKKNGQLAAVSDAVGEDEEFVLKLIN 378
Cdd:cd23352    82 RDRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123

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

Pssm-ID: 467443 Cd Length: 117 Bit Score: 182.37 E-value: 4.43e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 137 PQANLLSVSRRRYAHLSAQEDEIATDSNIPWGVDSLITLTFQNKKYCLRTCDNRYLRNDGTLIKEPDPRAGYTLEFKAGK 216
Cdd:cd23335     1 PQVNLYSVNRKRYARLDPEGDELRVDEDIPWGSDALITLEFDDGRYALRTSDGRYLRSDGSLVDEPSDDTLFTLEFRSGG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2118037418 217 LAFKDCDGKYLAPMGPTGTLKSgRSSKPGKDELFDLEE 254
Cdd:cd23335    81 LAFKDSEGKYLTAVGGSGVLKT-RKKTVGKDELFSLED 117

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: 166.47 E-value: 9.54e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  15 GLINSDNRYLTAESFGYKVNASAPSLKRKQIWTLEQDGD-SSVVFLKSHLGRYLSADKDGKVSGEAEKPGSDGRFIIVTQ 93
Cdd:cd23347     7 GLINSQQKYLTAETFGFKVNANGSSLKKKQLWTLEPFGDgTNVVALRSHLGRYLSVDQFGNVTCEAEEKGEGSRFEIVIS 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2118037418  94 SD--GRWALQSEPYKRFFGGSEDKLSCFAQTITEAELWAVHLA 134
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: 148.69 E-value: 3.57e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 136 HPQANLLSVSRRRYAHLSAQEDEIATDSNIPWGVDSLITLTF-QNKKYCLRTCDNRYLRNDGTLIKEPDPRAGYTLEFKA 214
Cdd:cd23351     1 RPQVNLRSAGRKRYARLSGDEDEIQVDANVPWGSDTLFTLEFrDDGRYAIHTANGKYLNRDGKLVEECPEDCLFTLEYHA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2118037418 215 GKLAFKDCDGKYLAPMGPTGTLKSgRSSKPGKDELFDLE 253
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: 146.17 E-value: 2.37e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 379 RPILVLRGTHGFVCYHR-NSNLLDANRSVYDVFHIIF-NDGAYQIKGLGGKFWYVASNGTVCSDGEMSEDFFLEFRECSR 456
Cdd:cd23337     1 RPILVLRGEYGFVGVKSgSSGKLECNKSTYDVFQLEYnNDGAYHLKGSNGKYWSVDSDGSVTADSAAPTPFILEFRGQSK 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2118037418 457 VAIKGKNGKYLRGDQAGTLRADADLLHRATLWEY 490
Cdd:cd23337    81 LAIKAPNGKYLKGEQNGLFKATGTEVDKATLWEY 114

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: 133.47 E-value: 1.45e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 379 RPILVLRGTHGFVCYHRNSNLLDANRSVYDVFHIIFNDGAYQIKGLGGKFWYVASNGTVCSDGEMSEDFFLEFRECSRVA 458
Cdd:cd23356     1 RPIIVLRGEHGFIGCRKVTGTLDSNRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2118037418 459 IKgKNGKYLRGDQAGTLRADADLLHRATLWEY 490
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: 129.76 E-value: 3.03e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  21 NRYLTAESFGYKVNASAPSLKRKQIWTLEQDGDSSVVFLKSHLGRYLSADKDGKVSGEAEKPGSDGRFIIVTQsdGRWAL 100
Cdd:pfam06268   2 NGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFR--GRWAL 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2118037418 101 QSEPYKRFFG-GSEDKLSCFAQTITEAELWAV 131
Cdd:pfam06268  80 LRESNGRYLGgGPSGLLKANASTVGKDELWTL 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: 121.28 E-value: 3.93e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 265 NGRYVSIRQGVNVSANQDEETHHETFQMQIDKETKKCIFHSNTGSYWTLVSHGGIQATATEISASTMFDVEWRGRRVALK 344
Cdd:pfam06268   2 NGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALLR 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2118037418 345 AGNGKYICTKKNGQLAAVSDAVGEDEEFVL 374
Cdd:pfam06268  82 ESNGRYLGGGPSGLLKANASTVGKDELWTL 111

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

Pssm-ID: 467463 Cd Length: 125 Bit Score: 120.77 E-value: 1.22e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 257 PQVVFLAS-NGRYVSIRQGVNVSANQDEETHHETFQMQIDKETKKCIFHSNTGSYWTLVSHGGIQATATEISASTMFDVE 335
Cdd:cd23355     2 PQAAFIAGlNSRYVSVKQGVDVTANQDEISDHETFQLEYDWSTKRWYIRTMQDRYWTLETAGGIQASADKKSANALFELE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2118037418 336 WRGR-RVALKAGNGKYICTKKNGQLAAVSDAVGEDEEFVLKLIN 378
Cdd:cd23355    82 WQEDgSVSFRANNGKFVGTKRSGHLFANSESIDEIAKFYFYLIN 125

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: 94.82 E-value: 2.36e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 379 RPILVLRGTHGFVCYHRNSN-LLDANRSVYDVFHIIFND-GAYQIKGLGGKFWYVASnGTVCSDGEMSEDFFLEFRECSR 456
Cdd:cd23359     1 RPILVLKCEQGFVGYKSGSNpKLECNKASYETIQVERGDkGLVFFKGQSGKYWGVCG-DGITADADAPEGFYLELREPSR 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2118037418 457 VAIKGKNGKYLRGDQAGTLRADADLLHRATLWEY 490
Cdd:cd23359    80 LCIKTADGSYLMADKNGAFKVGDADPETATLWEF 113

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

Pssm-ID: 467466 Cd Length: 113 Bit Score: 91.40 E-value: 3.54e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 379 RPILVLRGTHGFVCYHRNSNLLDANRSVYDVFHII-FNDGAYQIKGLGGKFWYVASNGTVCSDGEMSEDFFLEFRECSRV 457
Cdd:cd23358     1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLLpCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2118037418 458 AIKGKNGKYLRGDQAGTLRADADLLHRATLWEY 490
Cdd:cd23358    81 AILAPNGCYLRGDNSGTLLADSEIITSECLWEF 113

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

Pssm-ID: 467462 Cd Length: 123 Bit Score: 90.57 E-value: 9.90e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 257 PQVVFLASNGRYVSIRQGVNVSANQDEETHHETFQMQIDKETKKCIFHSNTGSYWTLVSHGGIQATATEISASTMFDVEW 336
Cdd:cd23354     2 TWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVEW 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2118037418 337 RGRRVALKAGNGKYICTKKNGQLAAVSDAVGEDEEFVLKLIN 378
Cdd:cd23354    82 RCGKIILQASNGRYLGVKPNGLLTASALLPGPNEEFGVRLAN 123

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

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 88.54 E-value: 3.15e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 139 ANLLSVSRRRYAHLSA-QEDEIATDsnipwgvdsLITLTFQNKKYC--LRTCDNRYLR--NDGTLIKEPDPRA---GYTL 210
Cdd:pfam06268   1 ANGYLVSERRGAHLNAnRESLKRVQ---------TFTLEFDDERYTvyLRSHNGKYLScdADGRVVCEAERRSadtFFEL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2118037418 211 EFKAGKLAFKDCDGKYLApMGPTGTLKSgRSSKPGKDELFDL 252
Cdd:pfam06268  72 EFRGRWALLRESNGRYLG-GGPSGLLKA-NASTVGKDELWTL 111

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

Pssm-ID: 461865 [Multi-domain] Cd Length: 111 Bit Score: 85.46 E-value: 4.57e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 388 HGFVCYHRNSNLLDANR---SVYDVFHIIFNDGAY--QIKGLGGKFWYVASNGTVCSDGE-MSEDFFLEFRECSRVAIKG 461
Cdd:pfam06268   2 NGYLVSERRGAHLNANReslKRVQTFTLEFDDERYtvYLRSHNGKYLSCDADGRVVCEAErRSADTFFELEFRGRWALLR 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2118037418 462 K-NGKYLRGDQAGTLRADADLLHRATLWEY 490
Cdd:pfam06268  82 EsNGRYLGGGPSGLLKANASTVGKDELWTL 111

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

Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 80.39 E-value: 3.68e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 258 QVVFLASNGRYVSIRQGVN--VSANQDEETHHETFQMqIDKETKKCIFHSNTGSYWTLVSHGG--IQATATEISASTMFD 333
Cdd:cd00257     2 TVALKSSNGKYLSAENGGGgpLVANRDAAGPWETFTL-VDLGDGKVALKSSNGKYLSAENGGGgtLVANRTAIGPWETFT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2118037418 334 VEWRG-RRVALKAGNGKYICTKKN--GQLAAVSDAVGEDEEFVL 374
Cdd:cd00257    81 LVPLGnGKVALKSANGKYLSADNGggGTLIANATSIGAWEKFTI 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: 75.28 E-value: 2.74e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  12 IQFGLINSDNRYLTAESFGYKVNASAPSLKRKQIWTL---EQDGDSSVVFLKSHLGRYLSADKDGKVS-GEAEKPGSdGR 87
Cdd:cd23346     1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVivsDYSDRQAVVELKGPQGLYLLVDKDGLVRcGTPDTKHH-GL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2118037418  88 FIIVTQSDGRWALQSEPYKRFFGGSEDKLSCFAQTITEAELWAVHLAI 135
Cdd:cd23346    80 FLLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127

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: 6.02e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  13 QFGLINSDNRYLTAESFG-YKVNASAPSLKRKQIWTLEQDGDSSVvFLKSHLGRYLSAD--KDGKVSGEAEKPGSDGRFI 89
Cdd:cd00257     2 TVALKSSNGKYLSAENGGgGPLVANRDAAGPWETFTLVDLGDGKV-ALKSSNGKYLSAEngGGGTLVANRTAIGPWETFT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2118037418  90 IVTQSDGRWALQSePYKRFF---GGSEDKLSCFAQTITEAELWAV 131
Cdd:cd00257    81 LVPLGNGKVALKS-ANGKYLsadNGGGGTLIANATSIGAWEKFTI 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: 64.60 E-value: 1.12e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 180 KKYCLRTCDNRYLR----NDGTLI---KEPDPRAGYTLEF-KAGKLAFKDCDGKYL-APMGPTGTLKSGRSSkPGKDELF 250
Cdd:cd00257     1 GTVALKSSNGKYLSaengGGGPLVanrDAAGPWETFTLVDlGDGKVALKSSNGKYLsAENGGGGTLVANRTA-IGPWETF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2118037418 251 DLEESHP-QVVFLASNGRYVSIRQGVN--VSANQDEETHHETFQM 292
Cdd:cd00257    80 TLVPLGNgKVALKSANGKYLSADNGGGgtLIANATSIGAWEKFTI 124

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

Pssm-ID: 467447 Cd Length: 160 Bit Score: 62.96 E-value: 1.13e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  53 DSSVVFLKSHLGRYLSADKDGKVSGEAEKPGSDGRFIIV-TQSDGRWALQSePYKRFFGGSEDKLSCF-----AQTITEA 126
Cdd:cd23339    74 GTGKVTLKSAHGKYLSCDKFGVVTATREARGPQEEWTPVpRPDGGGFALQS-VYGKYLSVDEVAGGKLvvradAETVGFC 152


                  ....*
gi 2118037418 127 ELWAV 131
Cdd:cd23339   153 ETWRV 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: 55.35 E-value: 2.23e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 339 RRVALKAGNGKYIC--TKKNGQLAAVSDAVGEDEEFVLKLINRPILVLRGTHG-FVC-YHRNSNLLDANRSVYD---VFH 411
Cdd:cd00257     1 GTVALKSSNGKYLSaeNGGGGPLVANRDAAGPWETFTLVDLGDGKVALKSSNGkYLSaENGGGGTLVANRTAIGpweTFT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 412 IIFNDGayqikglggkfwyvasngtvcsdgemsedfflefrecSRVAIKGKNGKYLR--GDQAGTLRADADllhRATLWE 489
Cdd:cd00257    81 LVPLGN-------------------------------------GKVALKSANGKYLSadNGGGGTLIANAT---SIGAWE 120

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: 53.64 E-value: 7.22e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 136 HPQANLLSVSRRRYAHLSAQEDEIATDSNIPWGVDSLITLTFQNKKYCLRTCDNRYLRNDGTLIKEPDPRAGYTLEFKAG 215
Cdd:cd23350     1 HVHVVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                          90       100
                  ....*....|....*....|....*
gi 2118037418 216 KL-AFKDCDGKYLAPMGPTGTLKSG 239
Cdd:cd23350    81 YLaSFFDDCGSMLYPQGRSRLLLSG 105

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: 50.25 E-value: 1.03e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 285 THHETFQMQIdKETKKCIFHSNTGSYWTLVSHGGIQATATEisaSTMFDVEWRGR-RVALKAGNGKYICTKKNGQLAAVS 363
Cdd:cd23337    28 STYDVFQLEY-NNDGAYHLKGSNGKYWSVDSDGSVTADSAA---PTPFILEFRGQsKLAIKAPNGKYLKGEQNGLFKATG 103


                  ....*....
gi 2118037418 364 DAVGEDEEF 372
Cdd:cd23337   104 TEVDKATLW 112

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: 51.65 E-value: 1.22e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  44 QIWTLEQDGDSSVVFlKSHLGRYLSADKDGKVSGEAEKPGSDGRFIIVTQsDGRWALQSepYKRFFGGSEDKLSCFAQTI 123
Cdd:pfam06229  28 EVFTAVKVSDEKIAL-KSGYGKYLGVNKDGILSARADAIGPREQFEPVFQ-EGKMALLA--ANGCFLSVDPSGDIVAKSK 103


                  ....
gi 2118037418 124 TEAE 127
Cdd:pfam06229 104 TAGE 107

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: 48.77 E-value: 4.33e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 338 GRRVALKAGNGKYICTKK-NGQLAAVSDAVGEDEEFVLklinrpilvlrgthgfvcyhrnsnlldanrsvydvfhIIFND 416
Cdd:cd23342     1 GSTISLKGNNGKYVSSENgNKPMTANRTSVGSWEKFTV-------------------------------------VDAGN 43

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2118037418 417 GAYQIKGLGGKfwYVAS-NGT---VCSDGEMS--EDFFLEFRECSRVAIKGKNGKYLRGDQ 471
Cdd:cd23342    44 GKVALKGNNGK--YVSSeNGTkpmTCNRTTIGawEKFTWISLGNGTVALKGNNGKYVSSEN 102

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: 48.73 E-value: 4.65e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 263 ASNGRYVSIRQGVNV-SANQDEETHHETFQMQiD----KETkkciFHS-NTGSYWTLVSHGGIQATATEISastmfdvEW 336
Cdd:cd23343    10 AATGKYVTVGEEGGAlAADAEDAEEAETFELT-DwgwgSHT----LRSvANGKYVTTDDDGTLTASAEEAF-------GW 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2118037418 337 -----------RGRRVALKAGNGKYICTKKNGQLAAV-SDAVGEDEEFVL 374
Cdd:cd23343    78 fvkevfrlepqEDGTVSLRTWNGRPVAVDEDGRLTVGeDDAAAEAERFEK 127

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: 47.14 E-value: 2.19e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  59 LKSHLGRYLSADKDGKVSGEAEKPGSDGRFIIVTQsDGRWALQSePYKRFFGGSED-KLSCFAQTITEAE 127
Cdd:cd23338    67 LKSGYGKYLSVDSDGKVVGRSDAIGPREQWEPVFQ-DGKMALLG-ANNCFLSVNEDgDIVATSKTAGENE 134

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: 46.11 E-value: 3.84e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2118037418  55 SVVFLKSHLGRYLSAD--KDGKVSGEAEKPGSDGRFIIVTQSDGRWALQS 102
Cdd:cd00257     1 GTVALKSSNGKYLSAEngGGGPLVANRDAAGPWETFTLVDLGDGKVALKS 50

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: 45.27 E-value: 9.68e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  19 SDNRYLTAESFGYkVNASApslKR------KQIWTLEQDGDSSVVfLKSHLGRYLSADKDGKVS-GEAEKPGSDGRFIIV 91
Cdd:cd23343    54 ANGKYVTTDDDGT-LTASA---EEafgwfvKEVFRLEPQEDGTVS-LRTWNGRPVAVDEDGRLTvGEDDAAAEAERFEKE 128


                  ....*
gi 2118037418  92 TQSDG 96
Cdd:cd23343   129 VVEDG 133

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: 43.76 E-value: 2.44e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 216 KLAFKDCDGKYLAPMGPTGTLKSGRSSkPGKDELFDLEEsHP--QVVFLASNGRYVSIRQGVN-VSANQDEETHHETFqm 292
Cdd:cd23342     3 TISLKGNNGKYVSSENGNKPMTANRTS-VGSWEKFTVVD-AGngKVALKGNNGKYVSSENGTKpMTCNRTTIGAWEKF-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 293 qidketkkcifhsntgsywTLVSHGgiqatateisastmfdvewrGRRVALKAGNGKYICTKKNGQ-LAAVSDAVGEDEE 371
Cdd:cd23342    79 -------------------TWISLG--------------------NGTVALKGNNGKYVSSENGTNpMTCNRTSIGGWEK 119


                  .
gi 2118037418 372 F 372
Cdd:cd23342   120 F 120

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: 44.06 E-value: 2.92e-05

                          10        20        30
                  ....*....|....*....|....*....|...
gi 2118037418 340 RVALKAGNGKYICTKKNGQLAAVSDAVGEDEEF 372
Cdd:cd23338    64 KIALKSGYGKYLSVDSDGKVVGRSDAIGPREQW 96

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: 43.56 E-value: 7.71e-05

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2118037418 339 RRVALKAGNGKYICTKKNGQLAAVSDAVGEDEEFVL 374
Cdd:pfam06229  38 EKIALKSGYGKYLGVNKDGILSARADAIGPREQFEP 73

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: 41.45 E-value: 1.52e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2118037418 215 GKLAFKDCDGKYLAPMGPTGTLKSGRSSkPGKDELFDLEESHPQVVFL-ASNGRYVSIRQGVN-VSANQDEETHHETFQ 291
Cdd:cd23342    44 GKVALKGNNGKYVSSENGTKPMTCNRTT-IGAWEKFTWISLGNGTVALkGNNGKYVSSENGTNpMTCNRTSIGGWEKFT 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: 41.78 E-value: 2.31e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418   2 PTNgIHQVL---KI----QFGLINSDNRYLTAESFGyKVNASAPSLKRKQIWTLEQDGDSSVVFLKSHLGRYLSADKDG- 73
Cdd:cd23339    60 PTD-VRQVWvatRVvgtgKVTLKSAHGKYLSCDKFG-VVTATREARGPQEEWTPVPRPDGGGFALQSVYGKYLSVDEVAg 137

                          90       100
                  ....*....|....*....|
gi 2118037418  74 ---KVSGEAEKPGSDGRFII 90
Cdd:cd23339   138 gklVVRADAETVGFCETWRV 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: 41.05 E-value: 2.41e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  13 QFGLINSDNRYLTAESfGYKVNASAPSLKRKQIWTLEQDGDSSVVFLKSHLGRYLSADKDGKVSGEAEKPGSDGRFIIVT 92
Cdd:cd23336     3 QVSLRAHNGKYVSIRQ-GVDVSANQDEETDTETFQLEFDKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELEW 81

                          90
                  ....*....|
gi 2118037418  93 QSDGRWALQS 102
Cdd:cd23336    82 NDGGTVALKA 91

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: 40.33 E-value: 3.64e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2118037418 216 KLAFKDCDGKYLApMGPTGTLKSGRSSKpGKDELFDLEESHPQVVFLASNGRYVSIRQGVNVSANQDEETHHETFQMQI 294
Cdd:cd23352    45 KCAFRTHTGKYWT-LTANGGVQSTASTK-NASCYFDIEWRDRRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKL 121

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

Pssm-ID: 467451 Cd Length: 133 Bit Score: 40.26 E-value: 3.96e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418  19 SDNRYLTAESFGYKVNASAPSLKRKQIWTLEQDGDSSVVFLKSHLGRYLSADKDGKVSGEAEKPGsdGRFI-----IVTQ 93
Cdd:cd23343    11 ATGKYVTVGEEGGALAADAEDAEEAETFELTDWGWGSHTLRSVANGKYVTTDDDGTLTASAEEAF--GWFVkevfrLEPQ 88


                  ....*....
gi 2118037418  94 SDGRWALQS 102
Cdd:cd23343    89 EDGTVSLRT 97

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

Pssm-ID: 467446 Cd Length: 141 Bit Score: 40.21 E-value: 6.01e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118037418 308 GSYWTLVSHGGIQATATEISASTMFDVEWRGRRVALKAGNGKYICTKKNGQLAAVSDAVGEDEEFVL 374
Cdd:cd23338    72 GKYLSVDSDGKVVGRSDAIGPREQWEPVFQDGKMALLGANNCFLSVNEDGDIVATSKTAGENEMIKI 138

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: 39.35 E-value: 7.33e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2118037418 301 CIFHSNTGSYWTlVSHGGIQATAteiSASTMFDVEWR-GRRVALKAGNGKYICTKKNGQLAAVSD 364
Cdd:cd23359    43 VFFKGQSGKYWG-VCGDGITADA---DAPEGFYLELRePSRLCIKTADGSYLMADKNGAFKVGDA 103

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: 40.10 E-value: 1.28e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2118037418 298 TKKCIFHSNTGSYWTLVSHGGIQATATEISASTMFDVEWRGRRVALKAGNGKYICTKKNGQLAAVSDAVGEDE 370
Cdd:pfam06229  37 DEKIALKSGYGKYLGVNKDGILSARADAIGPREQFEPVFQEGKMALLAANGCFLSVDPSGDIVAKSKTAGEGE 109

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: 37.92 E-value: 2.31e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118037418 409 VFHIIFNDGAYQIKglggkfwyvASNGT-VCSDGEMSED------FFLEFReCSRVAIKGKNGKYLRGDQA-GTLRA 477
Cdd:cd23335    36 LITLEFDDGRYALR---------TSDGRyLRSDGSLVDEpsddtlFTLEFR-SGGLAFKDSEGKYLTAVGGsGVLKT 102

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

Pssm-ID: 467450 [Multi-domain] Cd Length: 122 Bit Score: 37.21 E-value: 5.02e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2118037418 332 FDVEWRGR-RVALKAGNGKYICTKK-NGQLAAVSDAVGEDEEFVLKLINRPILVLRGTHG-FVCYHRNSNLLDANRS 405
Cdd:cd23342    36 FTVVDAGNgKVALKGNNGKYVSSENgTKPMTCNRTTIGAWEKFTWISLGNGTVALKGNNGkYVSSENGTNPMTCNRT 112

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: 36.72 E-value: 5.99e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118037418 260 VFLASNGRYVSIRQGV--NVSANQDEETHHETFQMQIDKETKKCifhsNTGSYWTLVSHGGIQATATEISASTMFDVEWR 337
Cdd:cd23341     4 AFKSHNGHFLSAEDGVvkTEHGHHDHHTHFHIENHGDDKVAIKT----HHGKYVAIDDNKQVYLSHHHHGDHTKFHLEHH 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2118037418 338 GRRVALKAGNGKYICTKKNGQLAAvSDAVGEDEEF 372
Cdd:cd23341    80 GGKVAIKGHHHHYIGVDHHGSVHT-SHHHGEDELF 113

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

Pssm-ID: 467447 Cd Length: 160 Bit Score: 37.15 E-value: 8.24e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2118037418 340 RVALKAGNGKYICTKKNGQLAAVSDAVGEDEEFVLKLI-NRPILVLRGTHG 389
Cdd:cd23339    77 KVTLKSAHGKYLSCDKFGVVTATREARGPQEEWTPVPRpDGGGFALQSVYG 127