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Conserved domains on  [gi|1002266795|ref|XP_015637729|]
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glucan 1,3-beta-glucosidase [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
243-512 2.45e-33

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 128.24  E-value: 2.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 243 YIVEDDFKFISASGLTAVRIPVGWWIASDPNPPAPYVGGSLQTLDNAFKWAEKYKLGVIIDLHAAPGSQNpwehsssrdg 322
Cdd:COG2730    26 NITEEDIDAIADWGFNTVRLPVSWERLQDPDNPYTLDEAYLERVDEVVDWAKARGLYVILDLHHAPGYQG---------- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 323 tqewGTSDANIAETVQVIDFLASRYAKSPSLLAVELMNEPFAprATLESLMKYYHDGYNAVRKYSSTAYVImsnrLGPHD 402
Cdd:COG2730    96 ----WYDAATQERFIAFWRQLAERYKDYPNVLGFELLNEPHG--ATWADWNALAQRAIDAIRATNPDRLII----VEGNN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 403 PTEFLQFANGFPRA----VIDVHYYTVFND-----LFNNLTVQQNIDfikSNFSSELKNVTTQNGPLtFVGEWVAEWRVP 473
Cdd:COG2730   166 WGGAHNLRALDPLDddnlVYSVHFYGPFVFthqgaWFAGPTYPANLE---ARLDNWGDWAADNGVPV-FVGEFGAYNDDP 241
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1002266795 474 NATKEEYQRYakvQMDVYGQATFGWSYWTLKNVNNHWNL 512
Cdd:COG2730   242 DASRLAWLRD---LLDYLEENGIGWTYWSFNPSGDTGGL 277
beta-trefoil_FSCN-like cd00257
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
87-193 2.39e-12

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: 63.83  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795  87 GAYLTAaDQGGAAAVVANRTqaAPSASETFKLWRINETTFNFRASSGRFVGAGSDGGAAVVAVAAAPGPSETFQVVRDDG 166
Cdd:cd00257    10 GKYLSA-ENGGGGPLVANRD--AAGPWETFTLVDLGDGKVALKSSNGKYLSAENGGGGTLVANRTAIGPWETFTLVPLGN 86
                          90       100
                  ....*....|....*....|....*...
gi 1002266795 167 DKsrVRIRAPNGHFLQI-ALGSNSVTAD 193
Cdd:cd00257    87 GK--VALKSANGKYLSAdNGGGGTLIAN 112
 
Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
243-512 2.45e-33

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 128.24  E-value: 2.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 243 YIVEDDFKFISASGLTAVRIPVGWWIASDPNPPAPYVGGSLQTLDNAFKWAEKYKLGVIIDLHAAPGSQNpwehsssrdg 322
Cdd:COG2730    26 NITEEDIDAIADWGFNTVRLPVSWERLQDPDNPYTLDEAYLERVDEVVDWAKARGLYVILDLHHAPGYQG---------- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 323 tqewGTSDANIAETVQVIDFLASRYAKSPSLLAVELMNEPFAprATLESLMKYYHDGYNAVRKYSSTAYVImsnrLGPHD 402
Cdd:COG2730    96 ----WYDAATQERFIAFWRQLAERYKDYPNVLGFELLNEPHG--ATWADWNALAQRAIDAIRATNPDRLII----VEGNN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 403 PTEFLQFANGFPRA----VIDVHYYTVFND-----LFNNLTVQQNIDfikSNFSSELKNVTTQNGPLtFVGEWVAEWRVP 473
Cdd:COG2730   166 WGGAHNLRALDPLDddnlVYSVHFYGPFVFthqgaWFAGPTYPANLE---ARLDNWGDWAADNGVPV-FVGEFGAYNDDP 241
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1002266795 474 NATKEEYQRYakvQMDVYGQATFGWSYWTLKNVNNHWNL 512
Cdd:COG2730   242 DASRLAWLRD---LLDYLEENGIGWTYWSFNPSGDTGGL 277
Cellulase pfam00150
Cellulase (glycosyl hydrolase family 5);
225-505 5.52e-17

Cellulase (glycosyl hydrolase family 5);


Pssm-ID: 395098 [Multi-domain]  Cd Length: 272  Bit Score: 81.27  E-value: 5.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 225 NGYGTAKATPILRNHWST--YIVEDDFKFISASGLTAVRIPVGWWIASDPNPPAPYVGGSLQTLDNAFKWAEKYKLGVII 302
Cdd:pfam00150   4 NGKPVQLRGVTHGGQWGNpyVTTKAMIDLVKDWGFNVVRLPVSWGGYVPNNPDYLIDENWLNRVDEVVDYAIDNGMYVII 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 303 DLHAAPGsqnpWEHsssrDGTQEWGTSDANIAEtvqVIDFLASRYaKSPSLLAVELMNEPFAPRATL--ESLMKYYHDGY 380
Cdd:pfam00150  84 DWHHDGG----WPG----DPNGNIDTAKAFFKK---IWTQIATRY-GNNPNVIFELMNEPHGNDQATwaDDVKDYAQEAI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 381 NAVRKYSSTAYVIMSNRLGPHDPTE-FLQFANGFPRAVIDVHYY--TVFNDLFNNLTVQQNIDfikSNFSSELKNVTTQN 457
Cdd:pfam00150 152 DAIRAAGPNNLIIVGGNSWSQNPDGaALNDPNDDDNLIYSVHFYapSDFSGTWFDCEDPTNLA---QRLRAAANWALDNG 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1002266795 458 GPLtFVGewvaEWRVPNATKeEYQRYAKVQMDVYGQATFGWSYWTLKN 505
Cdd:pfam00150 229 IPV-FIG----EFGGGNADG-PCRDEAEKWLDYLKENGISWTGWSNGN 270
beta-trefoil_FSCN-like cd00257
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
87-193 2.39e-12

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: 63.83  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795  87 GAYLTAaDQGGAAAVVANRTqaAPSASETFKLWRINETTFNFRASSGRFVGAGSDGGAAVVAVAAAPGPSETFQVVRDDG 166
Cdd:cd00257    10 GKYLSA-ENGGGGPLVANRD--AAGPWETFTLVDLGDGKVALKSSNGKYLSAENGGGGTLVANRTAIGPWETFTLVPLGN 86
                          90       100
                  ....*....|....*....|....*...
gi 1002266795 167 DKsrVRIRAPNGHFLQI-ALGSNSVTAD 193
Cdd:cd00257    87 GK--VALKSANGKYLSAdNGGGGTLIAN 112
 
Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
243-512 2.45e-33

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 128.24  E-value: 2.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 243 YIVEDDFKFISASGLTAVRIPVGWWIASDPNPPAPYVGGSLQTLDNAFKWAEKYKLGVIIDLHAAPGSQNpwehsssrdg 322
Cdd:COG2730    26 NITEEDIDAIADWGFNTVRLPVSWERLQDPDNPYTLDEAYLERVDEVVDWAKARGLYVILDLHHAPGYQG---------- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 323 tqewGTSDANIAETVQVIDFLASRYAKSPSLLAVELMNEPFAprATLESLMKYYHDGYNAVRKYSSTAYVImsnrLGPHD 402
Cdd:COG2730    96 ----WYDAATQERFIAFWRQLAERYKDYPNVLGFELLNEPHG--ATWADWNALAQRAIDAIRATNPDRLII----VEGNN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 403 PTEFLQFANGFPRA----VIDVHYYTVFND-----LFNNLTVQQNIDfikSNFSSELKNVTTQNGPLtFVGEWVAEWRVP 473
Cdd:COG2730   166 WGGAHNLRALDPLDddnlVYSVHFYGPFVFthqgaWFAGPTYPANLE---ARLDNWGDWAADNGVPV-FVGEFGAYNDDP 241
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1002266795 474 NATKEEYQRYakvQMDVYGQATFGWSYWTLKNVNNHWNL 512
Cdd:COG2730   242 DASRLAWLRD---LLDYLEENGIGWTYWSFNPSGDTGGL 277
Cellulase pfam00150
Cellulase (glycosyl hydrolase family 5);
225-505 5.52e-17

Cellulase (glycosyl hydrolase family 5);


Pssm-ID: 395098 [Multi-domain]  Cd Length: 272  Bit Score: 81.27  E-value: 5.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 225 NGYGTAKATPILRNHWST--YIVEDDFKFISASGLTAVRIPVGWWIASDPNPPAPYVGGSLQTLDNAFKWAEKYKLGVII 302
Cdd:pfam00150   4 NGKPVQLRGVTHGGQWGNpyVTTKAMIDLVKDWGFNVVRLPVSWGGYVPNNPDYLIDENWLNRVDEVVDYAIDNGMYVII 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 303 DLHAAPGsqnpWEHsssrDGTQEWGTSDANIAEtvqVIDFLASRYaKSPSLLAVELMNEPFAPRATL--ESLMKYYHDGY 380
Cdd:pfam00150  84 DWHHDGG----WPG----DPNGNIDTAKAFFKK---IWTQIATRY-GNNPNVIFELMNEPHGNDQATwaDDVKDYAQEAI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795 381 NAVRKYSSTAYVIMSNRLGPHDPTE-FLQFANGFPRAVIDVHYY--TVFNDLFNNLTVQQNIDfikSNFSSELKNVTTQN 457
Cdd:pfam00150 152 DAIRAAGPNNLIIVGGNSWSQNPDGaALNDPNDDDNLIYSVHFYapSDFSGTWFDCEDPTNLA---QRLRAAANWALDNG 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1002266795 458 GPLtFVGewvaEWRVPNATKeEYQRYAKVQMDVYGQATFGWSYWTLKN 505
Cdd:pfam00150 229 IPV-FIG----EFGGGNADG-PCRDEAEKWLDYLKENGISWTGWSNGN 270
beta-trefoil_FSCN-like cd00257
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
87-193 2.39e-12

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: 63.83  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795  87 GAYLTAaDQGGAAAVVANRTqaAPSASETFKLWRINETTFNFRASSGRFVGAGSDGGAAVVAVAAAPGPSETFQVVRDDG 166
Cdd:cd00257    10 GKYLSA-ENGGGGPLVANRD--AAGPWETFTLVDLGDGKVALKSSNGKYLSAENGGGGTLVANRTAIGPWETFTLVPLGN 86
                          90       100
                  ....*....|....*....|....*...
gi 1002266795 167 DKsrVRIRAPNGHFLQI-ALGSNSVTAD 193
Cdd:cd00257    87 GK--VALKSANGKYLSAdNGGGGTLIAN 112
beta-trefoil_FSCN-like cd00257
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
81-161 8.52e-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: 8.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002266795  81 LKAvAAGAYLTAaDQGGAAAVVANRTQaaPSASETFKLWRINETTFNFRASSGRFVGAGSDGGAAVVAVAAAPGPSETFQ 160
Cdd:cd00257    48 LKS-SNGKYLSA-ENGGGGTLVANRTA--IGPWETFTLVPLGNGKVALKSANGKYLSADNGGGGTLIANATSIGAWEKFT 123

                  .
gi 1002266795 161 V 161
Cdd:cd00257   124 I 124
beta-trefoil_FSCN-like cd00257
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ...
124-193 2.47e-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: 41.10  E-value: 2.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002266795 124 TTFNFRASSGRFVGAGSDGGAAVVAVAAAPGPSETFQVVRDDGDKsrVRIRAPNGHFLQIALGSNS-VTAD 193
Cdd:cd00257     1 GTVALKSSNGKYLSAENGGGGPLVANRDAAGPWETFTLVDLGDGK--VALKSSNGKYLSAENGGGGtLVAN 69
 
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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