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Conserved domains on  [gi|31982710|ref|NP_062515|]
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fascin-3 isoform 1 [Mus musculus]

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 2.10e-76

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: 235.41  E-value: 2.10e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 263 PTWVSLKSKSRRFLSVIYDAEVCAASERLTQMSLFQYECDSETPTLQLRSANGYYLAQRRHRAIIADGHPMESDTFFRVH 342
Cdd:cd23354   1 PTWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 31982710 343 WNCGKITLQSPNGRFLGIASDGLLMANVTIPGPNEELGIRFAN 385
Cdd:cd23354  81 WRCGKIILQASNGRYLGVKPNGLLTASALLPGPNEEFGVRLAN 123
beta-trefoil_FSCN-like super family cl49611
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
 386-498 7.61e-73

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.


The actual alignment was detected with superfamily member cd23358:

Pssm-ID: 483951  Cd Length: 113  Bit Score: 226.22  E-value: 7.61e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 386 RPFLVLRGRYGYVGSSSDHDLLKCNMDQPDCIQLLPCRQGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSSLL 465
Cdd:cd23358   1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLLPCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 31982710 466 TVLAPNGFYLRADRSGTLLADSEEITKECIWEF 498
Cdd:cd23358  81 AILAPNGCYLRGDNSGTLLADSEIITSECLWEF 113
beta-trefoil_FSCN-like super family cl49611
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
 16-142 3.50e-72

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.


The actual alignment was detected with superfamily member cd23346:

Pssm-ID: 483951  Cd Length: 127  Bit Score: 224.74  E-value: 3.50e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710  16 LRVGLISWAGTYLTFEAYKSSVTASAKSLGRRQTWELLVSNEHESQAVIRLKSLQGLYLLCEADGTVCYGRPRTSHHGCF 95
Cdd:cd23346   1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVIVSDYSDRQAVVELKGPQGLYLLVDKDGLVRCGTPDTKHHGLF 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 31982710  96 LLRFHRNGKWTLQCIISGRYLESDGEDVFCNSRVLSAYHMWTPRPAL 142
Cdd:cd23346  81 LLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127
beta-trefoil_FSCN-like super family cl49611
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
 143-261 2.23e-61

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.


The actual alignment was detected with superfamily member cd23350:

Pssm-ID: 483951  Cd Length: 119  Bit Score: 196.55  E-value: 2.23e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 143 HVHVILYSPIYHSYARADHTVGRIWVDAAIPCLEECGFLLHFQDGCYHLETSTHHFLSRVDRLVPQRSSQTAFHMQVRPR 222
Cdd:cd23350   1 HVHVVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 31982710 223 GLVALCDGEGGTLYPQGSHLLLGMGSAPMKGEEWFVLQH 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 2.10e-76

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: 235.41  E-value: 2.10e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 263 PTWVSLKSKSRRFLSVIYDAEVCAASERLTQMSLFQYECDSETPTLQLRSANGYYLAQRRHRAIIADGHPMESDTFFRVH 342
Cdd:cd23354   1 PTWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 31982710 343 WNCGKITLQSPNGRFLGIASDGLLMANVTIPGPNEELGIRFAN 385
Cdd:cd23354  81 WRCGKIILQASNGRYLGVKPNGLLTASALLPGPNEEFGVRLAN 123
beta-trefoil_FSCN3_rpt4 cd23358
fourth fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 386-498 7.61e-73

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: 226.22  E-value: 7.61e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 386 RPFLVLRGRYGYVGSSSDHDLLKCNMDQPDCIQLLPCRQGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSSLL 465
Cdd:cd23358   1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLLPCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 31982710 466 TVLAPNGFYLRADRSGTLLADSEEITKECIWEF 498
Cdd:cd23358  81 AILAPNGCYLRGDNSGTLLADSEIITSECLWEF 113
beta-trefoil_FSCN3_rpt1 cd23346
first fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 16-142 3.50e-72

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: 224.74  E-value: 3.50e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710  16 LRVGLISWAGTYLTFEAYKSSVTASAKSLGRRQTWELLVSNEHESQAVIRLKSLQGLYLLCEADGTVCYGRPRTSHHGCF 95
Cdd:cd23346   1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVIVSDYSDRQAVVELKGPQGLYLLVDKDGLVRCGTPDTKHHGLF 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 31982710  96 LLRFHRNGKWTLQCIISGRYLESDGEDVFCNSRVLSAYHMWTPRPAL 142
Cdd:cd23346  81 LLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127
beta-trefoil_FSCN3_rpt2 cd23350
second fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 143-261 2.23e-61

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: 196.55  E-value: 2.23e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 143 HVHVILYSPIYHSYARADHTVGRIWVDAAIPCLEECGFLLHFQDGCYHLETSTHHFLSRVDRLVPQRSSQTAFHMQVRPR 222
Cdd:cd23350   1 HVHVVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 31982710 223 GLVALCDGEGGTLYPQGSHLLLGMGSAPMKGEEWFVLQH 261
Cdd:cd23350  81 YLASFFDDCGSMLYPQGRSRLLLSGNIPINEEEWFIIKR 119
Fascin pfam06268
Fascin domain; This family consists of several eukaryotic fascin or singed proteins. The ...
 24-138 1.20e-30

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: 114.74  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710    24 AGTYLTFEAYKSSVTASAKSLGRRQTWELLVSNEhesQAVIRLKSLQGLYLLCEADGTVCYGRPRTSHHGCFLLRFHrnG 103
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDE---RYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFR--G 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 31982710   104 KWTLQCIISGRYLESDGEDVF-CNSRVLSAYHMWTP 138
Cdd:pfam06268  76 RWALLRESNGRYLGGGPSGLLkANASTVGKDELWTL 111
Fascin pfam06268
Fascin domain; This family consists of several eukaryotic fascin or singed proteins. The ...
 273-378 3.93e-30

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: 113.58  E-value: 3.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710   273 RRFLSVIYDAEVCAASERLTQMSLFQYECDSETPTLQLRSANGYYLAQRRHRAIIADGHPMESDTFFRVHWNCGKITLQS 352
Cdd:pfam06268   3 GYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALLRE 82

                          90       100
                  ....*....|....*....|....*.
gi 31982710   353 PNGRFLGIASDGLLMANVTIPGPNEE 378
Cdd:pfam06268  83 SNGRYLGGGPSGLLKANASTVGKDEL 108
 
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 2.10e-76

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: 235.41  E-value: 2.10e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 263 PTWVSLKSKSRRFLSVIYDAEVCAASERLTQMSLFQYECDSETPTLQLRSANGYYLAQRRHRAIIADGHPMESDTFFRVH 342
Cdd:cd23354   1 PTWVSLKAKNGRYISIIYGVEVYANSERLTPLSLFQFEVDPNTPAVQLRTVNGRYLAQRGHRSVIADGKGTESETFFRVE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 31982710 343 WNCGKITLQSPNGRFLGIASDGLLMANVTIPGPNEELGIRFAN 385
Cdd:cd23354  81 WRCGKIILQASNGRYLGVKPNGLLTASALLPGPNEEFGVRLAN 123
beta-trefoil_FSCN3_rpt4 cd23358
fourth fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 386-498 7.61e-73

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: 226.22  E-value: 7.61e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 386 RPFLVLRGRYGYVGSSSDHDLLKCNMDQPDCIQLLPCRQGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSSLL 465
Cdd:cd23358   1 RSFLILRGKYGYVGSSSHHDVLQCNLPEPDQISLLPCKPGFYHFQGQNGSFWSITSDGTFRAWGKFALNFCIEIQGSNLL 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 31982710 466 TVLAPNGFYLRADRSGTLLADSEEITKECIWEF 498
Cdd:cd23358  81 AILAPNGCYLRGDNSGTLLADSEIITSECLWEF 113
beta-trefoil_FSCN3_rpt1 cd23346
first fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 16-142 3.50e-72

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: 224.74  E-value: 3.50e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710  16 LRVGLISWAGTYLTFEAYKSSVTASAKSLGRRQTWELLVSNEHESQAVIRLKSLQGLYLLCEADGTVCYGRPRTSHHGCF 95
Cdd:cd23346   1 VRVGLINWAGKYLTAEYYGNSVTAAGKRLGRKQTWEVIVSDYSDRQAVVELKGPQGLYLLVDKDGLVRCGTPDTKHHGLF 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 31982710  96 LLRFHRNGKWTLQCIISGRYLESDGEDVFCNSRVLSAYHMWTPRPAL 142
Cdd:cd23346  81 LLKFHVSGKWTLQSLSTGGYLESDGEDVLCLSSTLCQEHLWIPHPAI 127
beta-trefoil_FSCN3_rpt2 cd23350
second fascin-like domain, beta-trefoil fold, found in fascin-3 and similar proteins; Fascin-3, ...
 143-261 2.23e-61

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: 196.55  E-value: 2.23e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 143 HVHVILYSPIYHSYARADHTVGRIWVDAAIPCLEECGFLLHFQDGCYHLETSTHHFLSRVDRLVPQRSSQTAFHMQVRPR 222
Cdd:cd23350   1 HVHVVLYNIRSRCYAQADPEEDRVWVDAPVPYNEECGFILRFRKGKYHLETSDHHYVSSAEKLVSQPSEKTALTLHLRPG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 31982710 223 GLVALCDGEGGTLYPQGSHLLLGMGSAPMKGEEWFVLQH 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 2.34e-41

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: 144.27  E-value: 2.34e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710  16 LRVGLISWAGTYLTFEAYKSSVTASAKSLGRRQTWELLVSNEHESqaVIRLKSLQGLYLLCEADGTVCYGRPRTSHHGCF 95
Cdd:cd23334   1 WKLGLINSSGKYLTAETFGFKVNASGTSLKKKQTWTLEQDEGGSE--TVYLKSHLGRYLSADKDGKVTCDAEEPGADERF 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 31982710  96 LLRFHRNGKWTLQCIISGRYLESDGEDVFCNSRVLSAYHMWTPRPAL 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 2.32e-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: 138.46  E-value: 2.32e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 386 RPFLVLRGRYGYVGS-SSDHDLLKCNMDQPDCIQLLPCRQGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSSL 464
Cdd:cd23337   1 RPILVLRGEYGFVGVkSGSSGKLECNKSTYDVFQLEYNNDGAYHLKGSNGKYWSVDSDGSVTADSAAPTPFILEFRGQSK 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 31982710 465 LTVLAPNGFYLRADRSGTLLADSEEITKECIWEF 498
Cdd:cd23337  81 LAIKAPNGKYLKGEQNGLFKATGTEVDKATLWEY 114
Fascin pfam06268
Fascin domain; This family consists of several eukaryotic fascin or singed proteins. The ...
 24-138 1.20e-30

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: 114.74  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710    24 AGTYLTFEAYKSSVTASAKSLGRRQTWELLVSNEhesQAVIRLKSLQGLYLLCEADGTVCYGRPRTSHHGCFLLRFHrnG 103
Cdd:pfam06268   1 ANGYLVSERRGAHLNANRESLKRVQTFTLEFDDE---RYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFR--G 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 31982710   104 KWTLQCIISGRYLESDGEDVF-CNSRVLSAYHMWTP 138
Cdd:pfam06268  76 RWALLRESNGRYLGGGPSGLLkANASTVGKDELWTL 111
Fascin pfam06268
Fascin domain; This family consists of several eukaryotic fascin or singed proteins. The ...
 273-378 3.93e-30

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: 113.58  E-value: 3.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710   273 RRFLSVIYDAEVCAASERLTQMSLFQYECDSETPTLQLRSANGYYLAQRRHRAIIADGHPMESDTFFRVHWNCGKITLQS 352
Cdd:pfam06268   3 GYLVSERRGAHLNANRESLKRVQTFTLEFDDERYTVYLRSHNGKYLSCDADGRVVCEAERRSADTFFELEFRGRWALLRE 82

                          90       100
                  ....*....|....*....|....*.
gi 31982710   353 PNGRFLGIASDGLLMANVTIPGPNEE 378
Cdd:pfam06268  83 SNGRYLGGGPSGLLKANASTVGKDEL 108
beta-trefoil_FSCN_rpt2 cd23335
second fascin-like domain, beta-trefoil fold, found in the fascin subfamily; The fascin ...
 145-261 4.30e-29

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: 110.72  E-value: 4.30e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 145 HVILYSPIYHSYARADHTVGRIWVDAAIPCLEECGFLLHFQDGCYHLETSTHHFLSRVDRLVPQRSSQTAFHMQVRPrGL 224
Cdd:cd23335   2 QVNLYSVNRKRYARLDPEGDELRVDEDIPWGSDALITLEFDDGRYALRTSDGRYLRSDGSLVDEPSDDTLFTLEFRS-GG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 31982710 225 VALCDGEGGTLYPQGS--HLLLGMGSApmKGEEWFVLQH 261
Cdd:cd23335  81 LAFKDSEGKYLTAVGGsgVLKTRKKTV--GKDELFSLED 117
beta-trefoil_FSCN_rpt3 cd23336
third fascin-like domain, beta-trefoil fold, found in the fascin subfamily; The fascin ...
 263-385 6.69e-29

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: 110.38  E-value: 6.69e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 263 PTWVSLKSKSRRFLSVIYDAEVCAASERLTQMSLFQYECDSETPTLQLRSANGYYLAQRRHRAIIADGHPMESDTFFRVH 342
Cdd:cd23336   1 HPQVSLRAHNGKYVSIRQGVDVSANQDEETDTETFQLEFDKETKKWAFRTNKGKYWSLGPDGGIQATASSRSPNCLFELE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 31982710 343 WN-CGKITLQSPNGRFLGIASDGLLMANVTIPGPNEELGIRFAN 385
Cdd:cd23336  81 WNdGGTVALKASNGKYVTAKPNGQLAATSDEVGEKEKFTLKLIN 124
beta-trefoil_FSCN1_rpt1 cd23344
first fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; Fascin, ...
 16-146 3.72e-18

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: 80.66  E-value: 3.72e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710  16 LRVGLISWAGTYLTFEAYKSSVTASAKSLGRRQTWELLVSNEHESQAVIRLKSLQGLYLLCEADGTVCyGRPRTSHHGC- 94
Cdd:cd23344   2 IQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPGDEADSSAVLLRSHLGRYLAADKDGNVT-CESEVPGPDCr 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 31982710  95 FLLRFHRNGKWTLQCIISGRYLESDGEDVFCNSRVLSAYHMWtprpalHVHV 146
Cdd:cd23344  81 FLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKW------SVHI 126
beta-trefoil_FSCN2_rpt4 cd23357
fourth fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, ...
 386-498 4.13e-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: 77.15  E-value: 4.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 386 RPFLVLRGRYGYVGSSSDHDLLKCNMDQPDCIQLLpCRQGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSSLL 465
Cdd:cd23357   1 RPILVLRGEHGFVCHHKGSNTLDANRSVYDVFQLI-FSDGAYQIKGQGGKFWYISSSGTVCSDGDMPEDFFFEFREHGRV 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 31982710 466 TVLAPNGFYLRADRSGTLLADSEEITKECIWEF 498
Cdd:cd23357  80 AIKGKNGKYLRGDQAGTLKADAETVDSATLWEY 112
beta-trefoil_FSCN2_rpt1 cd23345
first fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, ...
 16-137 2.77e-13

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: 66.76  E-value: 2.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710  16 LRVGLISWAGTYLTFEAYKSSVTASAKSLGRRQTWeLLVSNEHESQAVIrLKSLQGLYLLCEADGTVCYGRPRTSHHGCF 95
Cdd:cd23345   6 IQFGLINCENRYLTAEAFGFKVNASAPSLKKKQIW-TLEQDEGDSSVVF-LKSHLGRYLSADKDGKVSCEAEKPGRDCRF 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 31982710  96 LLRFHRNGKWTLQCIISGRYLESDGEDVFCNSRVLSAYHMWT 137
Cdd:cd23345  84 LIVAQSDGRWALQSEPHKRFFGGSEDKLSCFAQTITEAELWA 125
beta-trefoil_singed_rpt4 cd23359
fourth fascin-like domain, beta-trefoil fold, found in Drosophila melanogaster protein singed ...
 386-498 8.29e-11

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: 58.99  E-value: 8.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 386 RPFLVLRGRYGYVG-SSSDHDLLKCNMDQPDCIQLLPCRQGIYHFQAQGGSFWSITSfGTFRPWGKFALNFCIELQGSSL 464
Cdd:cd23359   1 RPILVLKCEQGFVGyKSGSNPKLECNKASYETIQVERGDKGLVFFKGQSGKYWGVCG-DGITADADAPEGFYLELREPSR 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 31982710 465 LTVLAPNGFYLRADRSGTLLADSEEITKECIWEF 498
Cdd:cd23359  80 LCIKTADGSYLMADKNGAFKVGDADPETATLWEF 113
beta-trefoil_FSCN2_rpt3 cd23353
third fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, ...
 266-385 1.85e-10

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: 58.37  E-value: 1.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 266 VSLKSKSRRFLSVIYDAEVCAASERLTQMSLFQYECDSETPTLQLRSANGYYLAQRRHRAIIADGHPMESDTFFRVHWNC 345
Cdd:cd23353   4 VVFQAANGRYVSIRQGVNVSANQDEETDHETFQMQIDKETKKCSFHTNTGKYWTLVAHGGIQSTATEVAANTMFDIEWRG 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 31982710 346 GKITLQSPNGRFLGIASDGLLMANVTIPGPNEELGIRFAN 385
Cdd:cd23353  84 RRVALKASNGKYVCTKKNGQLAAVSDSVGEDEEFTLKLIN 123
beta-trefoil_FSCN1_rpt2 cd23348
second fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; Fascin, ...
 143-260 8.32e-10

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: 56.38  E-value: 8.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 143 HVHVILYSPIYHSYAR-ADHTVGRIWVDAAIPCLEECGFLLHFQDGCYHLETSTHHFLSRVDRLVPQRSSQTAFHMQVRP 221
Cdd:cd23348   1 HPQVNIYSVTRKRYAHlSARPADEIAVDRDVPWGVDSLITLVFQDQRYSVQTSDHRFLRHDGRLVARPEPATGYTLEFRS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 31982710 222 rGLVALCDGEGGTLYPQGSHLLLGMG-SAPMKGEEWFVLQ 260
Cdd:cd23348  81 -GKVAFRDCEGRYLAPSGPSGTLKAGkSTKVGKDELFVLE 119
beta-trefoil_singed_rpt1 cd23347
first fascin-like domain, beta-trefoil fold, found in Drosophila melanogaster protein singed ...
 18-147 1.40e-08

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: 53.22  E-value: 1.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710  18 VGLISWAGTYLTFEAYKSSVTASAKSLGRRQTWELLVSneHESQAVIRLKSLQGLYL--------LCEADgTVCYGRprt 89
Cdd:cd23347   6 VGLINSQQKYLTAETFGFKVNANGSSLKKKQLWTLEPF--GDGTNVVALRSHLGRYLsvdqfgnvTCEAE-EKGEGS--- 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31982710  90 shhgcfllRFH------RNGKWTLQCIISGRYLESDGEDVFCNSRVLSAYHMWtprpalHVHVI 147
Cdd:cd23347  80 --------RFEivisedESGRWAFRNEERGYFLGGSGDKLVCTAKAPTDSELW------TVHLA 129
beta-trefoil_FSCN1_rpt4 cd23356
fourth fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; Fascin, ...
 386-498 2.60e-08

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: 51.80  E-value: 2.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 386 RPFLVLRGRYGYVGSSSDHDLLKCNMDQPDCIQLlPCRQGIYHFQAQGGSFWSITSFGTFRPWGKFALNFCIELQGSSLL 465
Cdd:cd23356   1 RPIIVLRGEHGFIGCRKVTGTLDSNRSSYDVFQL-EFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKV 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 31982710 466 TVlAPNGFYLRADRSGTLLADSEEITKECIWEF 498
Cdd:cd23356  80 AI-KVGGRYLKGDHAGVLKASAETVDPATLWEY 111
beta-trefoil_FSCN1_rpt3 cd23352
third fascin-like domain, beta-trefoil fold, found in fascin and similar proteins; Fascin, ...
 266-385 3.40e-07

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: 49.19  E-value: 3.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 266 VSLKSKSRRFLSVIYDAEVCAASERLTQMSLFQYECDSETPTLQLRSANGYYLAQRRHRAIIADGHPMESDTFFRVHWNC 345
Cdd:cd23352   4 VVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTANGGVQSTASTKNASCYFDIEWRD 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 31982710 346 GKITLQSPNGRFLGIASDGLLMANVTIPGPNEELGIRFAN 385
Cdd:cd23352  84 RRITLRASNGKYVTSKKNGQLAASVETAGESELFLMKLIN 123
beta-trefoil_FSCN-like cd00257
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
 266-377 3.74e-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: 48.81  E-value: 3.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 266 VSLKSKSRRFLS--------VIYDAEVCAASERltqmslFQYEcDSETPTLQLRSANGYYL-AQRRHR-AIIADG-HPME 334
Cdd:cd00257   3 VALKSSNGKYLSaenggggpLVANRDAAGPWET------FTLV-DLGDGKVALKSSNGKYLsAENGGGgTLVANRtAIGP 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 31982710 335 SDTFFRVHWNCGKITLQSPNGRFLGIASDGL--LMANVTIPGPNE 377
Cdd:cd00257  76 WETFTLVPLGNGKVALKSANGKYLSADNGGGgtLIANATSIGAWE 120
beta-trefoil_singed_rpt2 cd23351
second fascin-like domain, beta-trefoil fold, found in Drosophila melanogaster protein singed ...
 156-261 2.98e-06

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: 46.22  E-value: 2.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 156 YARADHTVGRIWVDAAIPCLEECGFLLHF-QDGCYHLETSTHHFLSRVDRLVPQRSSQTAFHMQVRpRGLVALCDGEGGT 234
Cdd:cd23351  14 YARLSGDEDEIQVDANVPWGSDTLFTLEFrDDGRYAIHTANGKYLNRDGKLVEECPEDCLFTLEYH-AGQVAFRDRTGKY 92

                        90       100
                ....*....|....*....|....*..
gi 31982710 235 LYPQGSHLLLGMGSAPMKGEEWFVLQH 261
Cdd:cd23351  93 LAPIGSKAVLRTRSTSVTKDELFILED 119
beta-trefoil_FSCN-like cd00257
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
 346-498 5.99e-06

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: 45.34  E-value: 5.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 346 GKITLQSPNGRFLGI--ASDGLLMANVTIPGPNEelgiRFanrpflvlrgrygyvgsssdhdllkcnmdqpdciQLLPCR 423
Cdd:cd00257   1 GTVALKSSNGKYLSAenGGGGPLVANRDAAGPWE----TF----------------------------------TLVDLG 42

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 424 QGIYHFQAQGGSFWSITSFG---------TFRPWGKFAlnfcIELQGSSLLTVLAPNGFYLRADRS--GTLLADSEEITK 492
Cdd:cd00257  43 DGKVALKSSNGKYLSAENGGggtlvanrtAIGPWETFT----LVPLGNGKVALKSANGKYLSADNGggGTLIANATSIGA 118


                ....*.
gi 31982710 493 ECIWEF 498
Cdd:cd00257 119 WEKFTI 124
beta-trefoil_FSCN_FRG1 cd23338
fascin-like domain, beta-trefoil fold, found in FSHD region gene 1 protein (FRG1) and similar ...
 263-382 1.50e-04

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


Pssm-ID: 467446  Cd Length: 141  Bit Score: 41.75  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 263 PTWVSLKSKSRRFLSVIYDAEVCAASErltqmslfqyecdsetptlqlrsangyylaqrrhrAIiadGhPMEsdtFFRVH 342
Cdd:cd23338  62 DTKIALKSGYGKYLSVDSDGKVVGRSD-----------------------------------AI---G-PRE---QWEPV 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 31982710 343 WNCGKITLQSPNGRFLGIASDGLLMANVTIPGPNEELGIR 382
Cdd:cd23338 100 FQDGKMALLGANNCFLSVNEDGDIVATSKTAGENEMIKIR 139
beta-trefoil_singed_rpt3 cd23355
third fascin-like domain, beta-trefoil fold, found in Drosophila melanogaster protein singed ...
 274-369 2.80e-04

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: 40.64  E-value: 2.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 274 RFLSVIYDAEVCAASERLTQMSLFQYECDSETPTLQLRSANGYYLAQRRHRAIIADGHPMESDTFFRVHWNC-GKITLQS 352
Cdd:cd23355  13 RYVSVKQGVDVTANQDEISDHETFQLEYDWSTKRWYIRTMQDRYWTLETAGGIQASADKKSANALFELEWQEdGSVSFRA 92

                        90
                ....*....|....*..
gi 31982710 353 PNGRFLGIASDGLLMAN 369
Cdd:cd23355  93 NNGKFVGTKRSGHLFAN 109
beta-trefoil_FSCN2_rpt2 cd23349
second fascin-like domain, beta-trefoil fold, found in fascin-2 and similar proteins; Fascin-2, ...
 156-260 2.38e-03

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: 37.89  E-value: 2.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982710 156 YARADHTVGRIWVDAAIPCLEECGFLLHFQDGCYHLETSTHHFLSRVDRLVPQRSSQTAFHMQVRPrGLVALCDGEGGTL 235
Cdd:cd23349  14 YAHLSVQEDEIATDSNIPWGVDALITLIFQDKKYCLKTCDSRFLRNDGKLVKEPGPGTGYTLEFKA-GKLAFKDCDGKYL 92

                        90       100
                ....*....|....*....|....*..
gi 31982710 236 YPQG--SHLLLGMGSAPMKgEEWFVLQ 260
Cdd:cd23349  93 TPMGptGTLKSGRSSKPGK-DELFDLE 118
 
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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