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Conserved domains on  [gi|9966791|ref|NP_065102|]
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fascin-3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_FSCN3_rpt3 cd23354
third fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 263-385 4.85e-78

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: 239.64  E-value: 4.85e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  263 PTWVSLRSKTGRFISVIYDGEVRAASERLNRMSLFQFECDSESPTVQLRSANGYYLSQRRHRAVMADGHPLESDTFFRMH 342
Cdd:cd23354   1 PTWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 9966791  343 WNCGRIILQSCRGRFLGIAPNSLLMANVILPGPNEEFGILFAN 385
Cdd:cd23354  81 WRCGKIILQASNGRYLGVKPNGLLTASALLPGPNEEFGVRLAN 123
beta-trefoil_FSCN3_rpt1 cd23346
first fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 16-142 1.09e-76

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: 236.29  E-value: 1.09e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791   16 LRVGLISWAGTYLTFEACKNTVTATAKSLGRRQTWEILVSNEHETQAVVRLKSVQGLYLLCECDGTVCYGRPRTSHHGCF 95
Cdd:cd23346   1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVIVSDYSDRQAVVELKGPQGLYLLVDKDGLVRCGTPDTKHHGLF 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 9966791   96 LLRFHRNSKWTLQCLISGRYLESNGKDVFCTSHVLSAYHMWTPRPAL 142
Cdd:cd23346  81 LLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127
beta-trefoil_FSCN3_rpt4 cd23358
fourth fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 386-498 5.18e-76

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: 234.31  E-value: 5.18e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  386 RSFLVLRGRYGYVGSSSGHDLIQCNQDQPDRIHLLPCRPGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSNLL 465
Cdd:cd23358   1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLLPCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 9966791  466 TVLAPNGFYMRADQSGTLLADSEDITRECIWEF 498
Cdd:cd23358  81 AILAPNGCYLRGDNSGTLLADSEIITSECLWEF 113
beta-trefoil_FSCN3_rpt2 cd23350
second fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 143-261 4.13e-73

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: 226.98  E-value: 4.13e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  143 HVHVILYSPIHRCYARADPTMGRIWVDAAVPCLEECGFLLHFRDGCYHLETSTHHFLSHVDRLFSQPSSQTAFHMQVRPG 222
Cdd:cd23350   1 HVHVVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 9966791  223 GLVALCDGEGGMLYPQGTHLLLGMGCNPMRGEEWFILQH 261
Cdd:cd23350  81 YLASFFDDCGSMLYPQGRSRLLLSGNIPINEEEWFIIKR 119
 
Name Accession Description Interval E-value
beta-trefoil_FSCN3_rpt3 cd23354
third fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 263-385 4.85e-78

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: 239.64  E-value: 4.85e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  263 PTWVSLRSKTGRFISVIYDGEVRAASERLNRMSLFQFECDSESPTVQLRSANGYYLSQRRHRAVMADGHPLESDTFFRMH 342
Cdd:cd23354   1 PTWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 9966791  343 WNCGRIILQSCRGRFLGIAPNSLLMANVILPGPNEEFGILFAN 385
Cdd:cd23354  81 WRCGKIILQASNGRYLGVKPNGLLTASALLPGPNEEFGVRLAN 123
beta-trefoil_FSCN3_rpt1 cd23346
first fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 16-142 1.09e-76

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: 236.29  E-value: 1.09e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791   16 LRVGLISWAGTYLTFEACKNTVTATAKSLGRRQTWEILVSNEHETQAVVRLKSVQGLYLLCECDGTVCYGRPRTSHHGCF 95
Cdd:cd23346   1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVIVSDYSDRQAVVELKGPQGLYLLVDKDGLVRCGTPDTKHHGLF 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 9966791   96 LLRFHRNSKWTLQCLISGRYLESNGKDVFCTSHVLSAYHMWTPRPAL 142
Cdd:cd23346  81 LLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127
beta-trefoil_FSCN3_rpt4 cd23358
fourth fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 386-498 5.18e-76

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: 234.31  E-value: 5.18e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  386 RSFLVLRGRYGYVGSSSGHDLIQCNQDQPDRIHLLPCRPGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSNLL 465
Cdd:cd23358   1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLLPCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 9966791  466 TVLAPNGFYMRADQSGTLLADSEDITRECIWEF 498
Cdd:cd23358  81 AILAPNGCYLRGDNSGTLLADSEIITSECLWEF 113
beta-trefoil_FSCN3_rpt2 cd23350
second fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 143-261 4.13e-73

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: 226.98  E-value: 4.13e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  143 HVHVILYSPIHRCYARADPTMGRIWVDAAVPCLEECGFLLHFRDGCYHLETSTHHFLSHVDRLFSQPSSQTAFHMQVRPG 222
Cdd:cd23350   1 HVHVVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 9966791  223 GLVALCDGEGGMLYPQGTHLLLGMGCNPMRGEEWFILQH 261
Cdd:cd23350  81 YLASFFDDCGSMLYPQGRSRLLLSGNIPINEEEWFIIKR 119
Fascin pfam06268
Fascin domain; This family consists of several eukaryotic fascin or singed proteins. The ...
 271-381 2.69e-38

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: 135.54  E-value: 2.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791    271 KTGRFISVIYDGEVRAASERLNRMSLFQFECDSESPTVQLRSANGYYLSQRRHRAVMADGHPLESDTFFRMHWNCGRIIL 350
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 9966791    351 QSCRGRFLGIAPNSLLMANVILPGPNEEFGI 381
Cdd:pfam06268  81 RESNGRYLGGGPSGLLKANASTVGKDELWTL 111
Fascin pfam06268
Fascin domain; This family consists of several eukaryotic fascin or singed proteins. The ...
 24-138 1.02e-25

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: 101.25  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791     24 AGTYLTFEACKNTVTATAKSLGRRQTWEILVSNEhetQAVVRLKSVQGLYLLCECDGTVCYGRPRTSHHGCFLLRFHrnS 103
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDE---RYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFR--G 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 9966791    104 KWTLQCLISGRYLESNGKDVF-CTSHVLSAYHMWTP 138
Cdd:pfam06268  76 RWALLRESNGRYLGGGPSGLLkANASTVGKDELWTL 111
 
Name Accession Description Interval E-value
beta-trefoil_FSCN3_rpt3 cd23354
third fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 263-385 4.85e-78

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: 239.64  E-value: 4.85e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  263 PTWVSLRSKTGRFISVIYDGEVRAASERLNRMSLFQFECDSESPTVQLRSANGYYLSQRRHRAVMADGHPLESDTFFRMH 342
Cdd:cd23354   1 PTWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 9966791  343 WNCGRIILQSCRGRFLGIAPNSLLMANVILPGPNEEFGILFAN 385
Cdd:cd23354  81 WRCGKIILQASNGRYLGVKPNGLLTASALLPGPNEEFGVRLAN 123
beta-trefoil_FSCN3_rpt1 cd23346
first fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 16-142 1.09e-76

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: 236.29  E-value: 1.09e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791   16 LRVGLISWAGTYLTFEACKNTVTATAKSLGRRQTWEILVSNEHETQAVVRLKSVQGLYLLCECDGTVCYGRPRTSHHGCF 95
Cdd:cd23346   1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVIVSDYSDRQAVVELKGPQGLYLLVDKDGLVRCGTPDTKHHGLF 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 9966791   96 LLRFHRNSKWTLQCLISGRYLESNGKDVFCTSHVLSAYHMWTPRPAL 142
Cdd:cd23346  81 LLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127
beta-trefoil_FSCN3_rpt4 cd23358
fourth fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 386-498 5.18e-76

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: 234.31  E-value: 5.18e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  386 RSFLVLRGRYGYVGSSSGHDLIQCNQDQPDRIHLLPCRPGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSNLL 465
Cdd:cd23358   1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLLPCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 9966791  466 TVLAPNGFYMRADQSGTLLADSEDITRECIWEF 498
Cdd:cd23358  81 AILAPNGCYLRGDNSGTLLADSEIITSECLWEF 113
beta-trefoil_FSCN3_rpt2 cd23350
second fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 143-261 4.13e-73

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: 226.98  E-value: 4.13e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  143 HVHVILYSPIHRCYARADPTMGRIWVDAAVPCLEECGFLLHFRDGCYHLETSTHHFLSHVDRLFSQPSSQTAFHMQVRPG 222
Cdd:cd23350   1 HVHVVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 9966791  223 GLVALCDGEGGMLYPQGTHLLLGMGCNPMRGEEWFILQH 261
Cdd:cd23350  81 YLASFFDDCGSMLYPQGRSRLLLSGNIPINEEEWFIIKR 119
beta-trefoil_FSCN_rpt1 cd23334
first fascin-like domain, beta-trefoil fold, found in the fascin subfamily; The fascin family ...
 16-142 3.64e-44

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: 151.59  E-value: 3.64e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791   16 LRVGLISWAGTYLTFEACKNTVTATAKSLGRRQTWEILVsnEHETQAVVRLKSVQGLYLLCECDGTVCYGRPRTSHHGCF 95
Cdd:cd23334   1 WKLGLINSSGKYLTAETFGFKVNASGTSLKKKQTWTLEQ--DEGGSETVYLKSHLGRYLSADKDGKVTCDAEEPGADERF 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 9966791   96 LLRFHRNSKWTLQCLISGRYLESNGKDVFCTSHVLSAYHMWTPRPAL 142
Cdd:cd23334  79 LIEYQPDGRWALKSEKHGRYLGGTGDNLSCFAKEVSESELWTVHLAI 125
beta-trefoil_FSCN_rpt4 cd23337
fourth fascin-like domain, beta-trefoil fold, found in the fascin subfamily; The fascin ...
 386-498 5.53e-39

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: 137.31  E-value: 5.53e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  386 RSFLVLRGRYGYVGSSSGH-DLIQCNQDQPDRIHLLPCRPGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSNL 464
Cdd:cd23337   1 RPILVLRGEYGFVGVKSGSsGKLECNKSTYDVFQLEYNNDGAYHLKGSNGKYWSVDSDGSVTADSAAPTPFILEFRGQSK 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 9966791  465 LTVLAPNGFYMRADQSGTLLADSEDITRECIWEF 498
Cdd:cd23337  81 LAIKAPNGKYLKGEQNGLFKATGTEVDKATLWEY 114
Fascin pfam06268
Fascin domain; This family consists of several eukaryotic fascin or singed proteins. The ...
 271-381 2.69e-38

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: 135.54  E-value: 2.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791    271 KTGRFISVIYDGEVRAASERLNRMSLFQFECDSESPTVQLRSANGYYLSQRRHRAVMADGHPLESDTFFRMHWNCGRIIL 350
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALL 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 9966791    351 QSCRGRFLGIAPNSLLMANVILPGPNEEFGI 381
Cdd:pfam06268  81 RESNGRYLGGGPSGLLKANASTVGKDELWTL 111
beta-trefoil_FSCN_rpt3 cd23336
third fascin-like domain, beta-trefoil fold, found in the fascin subfamily; The fascin ...
 263-385 1.41e-36

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: 131.18  E-value: 1.41e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  263 PTWVSLRSKTGRFISVIYDGEVRAASERLNRMSLFQFECDSESPTVQLRSANGYYLSQRRHRAVMADGHPLESDTFFRMH 342
Cdd:cd23336   1 HPQVSLRAHNGKYVSIRQGVDVSANQDEETDTETFQLEFDKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 9966791  343 WN-CGRIILQSCRGRFLGIAPNSLLMANVILPGPNEEFGILFAN 385
Cdd:cd23336  81 WNdGGTVALKASNGKYVTAKPNGQLAATSDEVGEKEKFTLKLIN 124
beta-trefoil_FSCN_rpt2 cd23335
second fascin-like domain, beta-trefoil fold, found in the fascin subfamily; The fascin ...
 145-261 2.38e-36

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: 130.36  E-value: 2.38e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  145 HVILYSPIHRCYARADPTMGRIWVDAAVPCLEECGFLLHFRDGCYHLETSTHHFLSHVDRLFSQPSSQTAFHMQVRPGGL 224
Cdd:cd23335   2 QVNLYSVNRKRYARLDPEGDELRVDEDIPWGSDALITLEFDDGRYALRTSDGRYLRSDGSLVDEPSDDTLFTLEFRSGGL 81

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 9966791  225 vALCDGEGGMLYPQGT--HLLLGMGCNpmRGEEWFILQH 261
Cdd:cd23335  82 -AFKDSEGKYLTAVGGsgVLKTRKKTV--GKDELFSLED 117
Fascin pfam06268
Fascin domain; This family consists of several eukaryotic fascin or singed proteins. The ...
 24-138 1.02e-25

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: 101.25  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791     24 AGTYLTFEACKNTVTATAKSLGRRQTWEILVSNEhetQAVVRLKSVQGLYLLCECDGTVCYGRPRTSHHGCFLLRFHrnS 103
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDE---RYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFR--G 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 9966791    104 KWTLQCLISGRYLESNGKDVF-CTSHVLSAYHMWTP 138
Cdd:pfam06268  76 RWALLRESNGRYLGGGPSGLLkANASTVGKDELWTL 111
beta-trefoil_FSCN2_rpt4 cd23357
fourth fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, ...
 386-498 1.77e-17

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: 77.92  E-value: 1.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  386 RSFLVLRGRYGYVGSSSGHDLIQCNQDQPDRIHLLpCRPGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSNLL 465
Cdd:cd23357   1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLI-FSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRV 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 9966791  466 TVLAPNGFYMRADQSGTLLADSEDITRECIWEF 498
Cdd:cd23357  80 AIKGKNGKYLRGDQAGTLKADAETVDSATLWEY 112
beta-trefoil_FSCN1_rpt1 cd23344
first fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; Fascin, ...
 16-146 8.28e-14

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: 68.34  E-value: 8.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791   16 LRVGLISWAGTYLTFEACKNTVTATAKSLGRRQTWEILVSNEHETQAVVRLKSVQGLYLLCECDGTVCyGRPRTSHHGC- 94
Cdd:cd23344   2 IQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPGDEADSSAVLLRSHLGRYLAADKDGNVT-CESEVPGPDCr 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 9966791   95 FLLRFHRNSKWTLQCLISGRYLESNGKDVFCTSHVLSAYHMWtprpalHVHV 146
Cdd:cd23344  81 FLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKW------SVHI 126
beta-trefoil_FSCN-like cd00257
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
 266-379 3.15e-10

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: 57.66  E-value: 3.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  266 VSLRSKTGRFISVI--YDGEVRAASERLNRMSLFQFECDSESpTVQLRSANGYYLS--QRRHRAVMADGHPLESDTFFRM 341
Cdd:cd00257   3 VALKSSNGKYLSAEngGGGPLVANRDAAGPWETFTLVDLGDG-KVALKSSNGKYLSaeNGGGGTLVANRTAIGPWETFTL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 9966791  342 HWN-CGRIILQSCRGRFLGIAPNSL--LMANVILPGPNEEF 379
Cdd:cd00257  82 VPLgNGKVALKSANGKYLSADNGGGgtLIANATSIGAWEKF 122
beta-trefoil_singed_rpt4 cd23359
fourth fascin-like domain, beta-trefoil fold, found in Drosophila melanogaster protein singed ...
 386-498 1.06e-09

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: 55.91  E-value: 1.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  386 RSFLVLRGRYGYVG-SSSGHDLIQCNQDQPDRIHLLPCRPGIYHFQAQGGSFWSITSfGTFRPWGKFALNFCIELQGSNL 464
Cdd:cd23359   1 RPILVLKCEQGFVGyKSGSNPKLECNKASYETIQVERGDKGLVFFKGQSGKYWGVCG-DGITADADAPEGFYLELREPSR 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 9966791  465 LTVLAPNGFYMRADQSGTLLADSEDITRECIWEF 498
Cdd:cd23359  80 LCIKTADGSYLMADKNGAFKVGDADPETATLWEF 113
beta-trefoil_FSCN2_rpt1 cd23345
first fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, ...
 16-137 1.07e-09

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: 56.36  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791   16 LRVGLISWAGTYLTFEACKNTVTATAKSLGRRQTWeILVSNEHETQaVVRLKSVQGLYLLCECDGTVCYGRPRTSHHGCF 95
Cdd:cd23345   6 IQFGLINCENRYLTAEAFGFKVNASAPSLKKKQIW-TLEQDEGDSS-VVFLKSHLGRYLSADKDGKVSCEAEKPGRDCRF 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 9966791   96 LLRFHRNSKWTLQCLISGRYLESNGKDVFCTSHVLSAYHMWT 137
Cdd:cd23345  84 LIVAQSDGRWALQSEPHKRFFGGSEDKLSCFAQTITEAELWA 125
beta-trefoil_FSCN1_rpt2 cd23348
second fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; Fascin, ...
 143-260 1.55e-09

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: 55.61  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  143 HVHVILYSPIHRCYARADPTMG-RIWVDAAVPCLEECGFLLHFRDGCYHLETSTHHFLSHVDRLFSQPSSQTAFHMQVRp 221
Cdd:cd23348   1 HPQVNIYSVTRKRYAHLSARPAdEIAVDRDVPWGVDSLITLVFQDQRYSVQTSDHRFLRHDGRLVARPEPATGYTLEFR- 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 9966791  222 GGLVALCDGEGGMLYPQGTHLLLGMGCNPMRG-EEWFILQ 260
Cdd:cd23348  80 SGKVAFRDCEGRYLAPSGPSGTLKAGKSTKVGkDELFVLE 119
beta-trefoil_FSCN2_rpt3 cd23353
third fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, ...
 266-379 2.99e-08

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: 52.20  E-value: 2.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  266 VSLRSKTGRFISVIYDGEVRAASERLNRMSLFQFECDSESPTVQLRSANGYYLSQRRHRAVMADGHPLESDTFFRMHWNC 345
Cdd:cd23353   4 VVFQAANGRYVSIRQGVNVSANQDEETDHETFQMQIDKETKKCSFHTNTGKYWTLVAHGGIQSTATEVAANTMFDIEWRG 83

                        90       100       110
                ....*....|....*....|....*....|....
gi 9966791  346 GRIILQSCRGRFLGIAPNSLLMANVILPGPNEEF 379
Cdd:cd23353  84 RRVALKASNGKYVCTKKNGQLAAVSDSVGEDEEF 117
beta-trefoil_FSCN1_rpt4 cd23356
fourth fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; Fascin, ...
 386-498 1.94e-07

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: 49.49  E-value: 1.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  386 RSFLVLRGRYGYVGSSSGHDLIQCNQDQPDRIHLlPCRPGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSNLL 465
Cdd:cd23356   1 RPIIVLRGEHGFIGCRKVTGTLDSNRSSYDVFQL-EFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKV 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 9966791  466 TVlAPNGFYMRADQSGTLLADSEDITRECIWEF 498
Cdd:cd23356  80 AI-KVGGRYLKGDHAGVLKASAETVDPATLWEY 111
beta-trefoil_FSCN-like cd00257
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
 307-415 7.14e-07

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


Pssm-ID: 467441 [Multi-domain]  Cd Length: 124  Bit Score: 48.03  E-value: 7.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  307 TVQLRSANGYYLS--QRRHRAVMADGHPLESDTFFRMHWNC-GRIILQSCRGRFLGI--APNSLLMANVILPGPNEEFGI 381
Cdd:cd00257   2 TVALKSSNGKYLSaeNGGGGPLVANRDAAGPWETFTLVDLGdGKVALKSSNGKYLSAenGGGGTLVANRTAIGPWETFTL 81

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 9966791  382 LFANRSFLVLRGRYG-YVG-SSSGHDLIQCNQDQPD 415
Cdd:cd00257  82 VPLGNGKVALKSANGkYLSaDNGGGGTLIANATSIG 117
beta-trefoil_FSCN1_rpt3 cd23352
third fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; Fascin, ...
 262-379 6.82e-06

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: 45.34  E-value: 6.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  262 CPTwVSLRSKTGRFISVIYDGEVRAASERLNRMSLFQFECDSESPTVQLRSANGYYLSQRRHRAVMADGHPLESDTFFRM 341
Cdd:cd23352   1 CPQ-VVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDI 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 9966791  342 HWNCGRIILQSCRGRFLGIAPNSLLMANVILPGPNEEF 379
Cdd:cd23352  80 EWRDRRITLRASNGKYVTSKKNGQLAASVETAGESELF 117
beta-trefoil_singed_rpt2 cd23351
second fascin-like domain, beta-trefoil fold, found in Drosophila melanogaster protein singed ...
 143-261 1.67e-05

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: 44.30  E-value: 1.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  143 HVHVILYSPIHRCYARADPTMGRIWVDAAVPCLEECGFLLHFR-DGCYHLETSTHHFLSHVDRLFSQPSSQTAFHMQVRp 221
Cdd:cd23351   1 RPQVNLRSAGRKRYARLSGDEDEIQVDANVPWGSDTLFTLEFRdDGRYAIHTANGKYLNRDGKLVEECPEDCLFTLEYH- 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 9966791  222 GGLVALCDGEGGMLYPQGTHLLLGMGCNPMRGEEWFILQH 261
Cdd:cd23351  80 AGQVAFRDRTGKYLAPIGSKAVLRTRSTSVTKDELFILED 119
beta-trefoil_FSCN2_rpt2 cd23349
second fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, ...
 143-260 7.79e-05

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: 42.13  E-value: 7.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  143 HVHVILYSPIHRCYARADPTMGRIWVDAAVPCLEECGFLLHFRDGCYHLETSTHHFLSHVDRLFSQPSSQTAFHMQVRPG 222
Cdd:cd23349   1 HPQANLLSVSRRRYAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKAG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 9966791  223 GLvALCDGEGGMLYPQGTHLLLGMGCNPMRG-EEWFILQ 260
Cdd:cd23349  81 KL-AFKDCDGKYLTPMGPTGTLKSGRSSKPGkDELFDLE 118
beta-trefoil_FSCN-like cd00257
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
 391-498 1.02e-04

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: 41.87  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791  391 LRGRYG-YVG-SSSGHDLIQCNQDQPD---RIHLLPCRPGIYHFQAQGGSFWSITSFG---------TFRPWGKFAlnfc 456
Cdd:cd00257   5 LKSSNGkYLSaENGGGGPLVANRDAAGpweTFTLVDLGDGKVALKSSNGKYLSAENGGggtlvanrtAIGPWETFT---- 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 9966791  457 IELQGSNLLTVLAPNGFYMRADQS--GTLLADSEDITRECIWEF 498
Cdd:cd00257  81 LVPLGNGKVALKSANGKYLSADNGggGTLIANATSIGAWEKFTI 124
beta-trefoil_singed_rpt1 cd23347
first fascin-like domain, beta-trefoil fold, found in Drosophila melanogaster protein singed ...
 18-147 1.65e-04

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: 41.67  E-value: 1.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966791   18 VGLISWAGTYLTFEACKNTVTATAKSLGRRQTWeILVSNeHETQAVVRLKSVQGLYLLCECDGTV-CYGRPRTSHHgcfl 96
Cdd:cd23347   6 VGLINSQQKYLTAETFGFKVNANGSSLKKKQLW-TLEPF-GDGTNVVALRSHLGRYLSVDQFGNVtCEAEEKGEGS---- 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9966791   97 lRFH------RNSKWTLQCLISGRYLESNGKDVFCTSHVLSAYHMWtprpalHVHVI 147
Cdd:cd23347  80 -RFEivisedESGRWAFRNEERGYFLGGSGDKLVCTAKAPTDSELW------TVHLA 129
beta-trefoil_FSCN_fungal_FRG1-like cd23339
fascin-like domain, beta-trefoil fold, found in fungal FRG1 and similar proteins; This group ...
 305-363 5.56e-03

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: 37.54  E-value: 5.56e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9966791  305 SPTVQLRSANGYYLSQRRHRAVMAD----GhPLESDTFFRMHwNCGRIILQSCRGRFLGIAPN 363
Cdd:cd23339  75 TGKVTLKSAHGKYLSCDKFGVVTATrearG-PQEEWTPVPRP-DGGGFALQSVYGKYLSVDEV 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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