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Conserved domains on  [gi|15234263|ref|NP_192902|]
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osmotin 34 [Arabidopsis thaliana]

Protein Classification

thaumatin family protein( domain architecture ID 10641270)

thaumatin family protein may be involved in host defense and a wide range of developmental processes, such as Arabidopsis thaliana pathogenesis-related protein 5 (PR-5) that is partially responsible for acquired pathogen resistance

CATH:  2.60.110.10
PubMed:  20204373|32696292|15080826
SCOP:  4002584

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
THN smart00205
Thaumatin family; The thaumatin family gathers proteins related to plant pathogenesis. The ...
 25-223 4.13e-120

Thaumatin family; The thaumatin family gathers proteins related to plant pathogenesis. The thaumatin family includes very basic members with extracellular and vacuolar localization. Thaumatin itsel is a potent sweet-tasting protein. Several members of this family display significant in vitro activity of inhibiting hyphal growth or spore germination of various fungi probably by a membrane permeabilizing mechanism.


:

Pssm-ID: 128501 [Multi-domain]  Cd Length: 218  Bit Score: 340.97  E-value: 4.13e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263     25 FEILNQCSYTVWAAASP-------GGGRRLDAGQSWRLDVAAGTKMARIWGRTNCNFDSSGRGRCQTGDCSGGLQCTGWG 97
Cdd:smart00205   1 FEFVNNCPYTVWAAALPsgkpqlsGGGFELNSGASWQLDAPPGTKMGRIWARTGCNFDASGRGRCATGDCGGVLQCNGWG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263     98 -QPPNTLAEYALNQFNNLDFYDISLVDGFNIPMEFSPT--SSNCHRILCTADINGQCPNVLRAPGG-----CNNPCTVFQ 169
Cdd:smart00205  81 gRPPATLAEFALNQFGGLDFYDVSLVDGFNIPMSFTPTggSGDCKGAGCTADLNAQCPAELQVPGGgsvvaCNSACTVFG 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15234263    170 TNQYCCTNGQG---SCSDTEYSRFFKQRCPDAYSYPQDDPTSTFTCTN-TNYRVVFCP 223
Cdd:smart00205 161 TDQYCCTGGQNnpeTCPPTNYSRIFKNACPDAYSYAYDDPTSTFTCTGgTNYKVTFCP 218
 
Name Accession Description Interval E-value
THN smart00205
Thaumatin family; The thaumatin family gathers proteins related to plant pathogenesis. The ...
 25-223 4.13e-120

Thaumatin family; The thaumatin family gathers proteins related to plant pathogenesis. The thaumatin family includes very basic members with extracellular and vacuolar localization. Thaumatin itsel is a potent sweet-tasting protein. Several members of this family display significant in vitro activity of inhibiting hyphal growth or spore germination of various fungi probably by a membrane permeabilizing mechanism.


Pssm-ID: 128501 [Multi-domain]  Cd Length: 218  Bit Score: 340.97  E-value: 4.13e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263     25 FEILNQCSYTVWAAASP-------GGGRRLDAGQSWRLDVAAGTKMARIWGRTNCNFDSSGRGRCQTGDCSGGLQCTGWG 97
Cdd:smart00205   1 FEFVNNCPYTVWAAALPsgkpqlsGGGFELNSGASWQLDAPPGTKMGRIWARTGCNFDASGRGRCATGDCGGVLQCNGWG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263     98 -QPPNTLAEYALNQFNNLDFYDISLVDGFNIPMEFSPT--SSNCHRILCTADINGQCPNVLRAPGG-----CNNPCTVFQ 169
Cdd:smart00205  81 gRPPATLAEFALNQFGGLDFYDVSLVDGFNIPMSFTPTggSGDCKGAGCTADLNAQCPAELQVPGGgsvvaCNSACTVFG 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15234263    170 TNQYCCTNGQG---SCSDTEYSRFFKQRCPDAYSYPQDDPTSTFTCTN-TNYRVVFCP 223
Cdd:smart00205 161 TDQYCCTGGQNnpeTCPPTNYSRIFKNACPDAYSYAYDDPTSTFTCTGgTNYKVTFCP 218
Thaumatin pfam00314
Thaumatin family;
29-223 2.58e-93

Thaumatin family;


Pssm-ID: 459757  Cd Length: 211  Bit Score: 272.91  E-value: 2.58e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263    29 NQCSYTVWAA-------ASPGGGRRLDAGQSWRLDVAAGTkMARIWGRTNCNFDSSGRgrCQTGDCSGGLQCTGW-GQPP 100
Cdd:pfam00314   1 NNCPFTIWPGiltnaghGPGTGGFELDPGQSRTFTVPDGW-SGRIWGRTGCSFDGSGS--CATGDCGGGLECNGAgGVPP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263   101 NTLAEYALNQFNNLDFYDISLVDGFNIPMEFSPTS-SNCHRILCTADINGQCPNVLRA------PGGCNNPCTVFQTNQY 173
Cdd:pfam00314  78 ATLAEFTLNGGGGQDFYDVSLVDGYNLPMSITPSGgGGCPVAGCAADLNSACPAELQVkspggkVVGCKSACLAFNTDEY 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15234263   174 CCTNGQGS---CSDTEYSRFFKQRCPDAYSYPQDDPTSTFTCTN-TNYRVVFCP 223
Cdd:pfam00314 158 CCTGAYATpetCKPTAYSKFFKAACPDAYSYAYDDATSTFTCPGgADYTITFCP 211
TLP-PA cd09218
allergenic/antifungal thaumatin-like proteins: plant and animal homologs; This subfamily is ...
 24-222 5.17e-79

allergenic/antifungal thaumatin-like proteins: plant and animal homologs; This subfamily is represented by the thaumatin-like proteins (TLPs), Cherry Allergen Pru Av 2 TLP, Peach PpAZ44 TLP (a propylene-induced TLP in abscission), the Caenorhabditis elegans thaumatin family member (thn-6), and other plant and animal homologs. TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Due to their inducible expression by environmental stresses such as pathogen/pest attack, drought and cold, plant TLPs are classified as the pathogenesis-related (PR) protein family 5 (PR5). Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. TLPs within this subfamily contain 16 conserved Cys residues.


Pssm-ID: 185757  Cd Length: 219  Bit Score: 236.75  E-value: 5.17e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263  24 TFEILNQCSYTVWAAASP--------GGGRRLDAGQSWRLDVAAGTKmARIWGRTNCNFDSSGRGRCQTGDCSGGLQCTG 95
Cdd:cd09218   1 TFTIYNKCPFTVWPGILGnaghpqlgGGGFELAPGQSRTIDAPSGWS-GRFWGRTGCSFDSSGKGSCATGDCGGGLECNG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263  96 -WGQPPNTLAEYALNQFNNLDFYDISLVDGFNIPMEFSPT--SSNCHRILCTADINGQCPNVL--RAPGG----CNNPCT 166
Cdd:cd09218  80 aGGAPPATLAEFTLGGSGGQDFYDVSLVDGYNLPVSITPQggSGGCRTAGCVADLNAVCPAELqvKNSGGrvvaCKSACL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263 167 VFQTNQYCCT---NGQGSCSDTEYSRFFKQRCPDAYSYPQDDPTSTFTCTN-TNYRVVFC 222
Cdd:cd09218 160 AFNTDEYCCRgayGTPETCKPTTYSRLFKNACPQAYSYAYDDPTSTFTCSSgANYVITFC 219
 
Name Accession Description Interval E-value
THN smart00205
Thaumatin family; The thaumatin family gathers proteins related to plant pathogenesis. The ...
 25-223 4.13e-120

Thaumatin family; The thaumatin family gathers proteins related to plant pathogenesis. The thaumatin family includes very basic members with extracellular and vacuolar localization. Thaumatin itsel is a potent sweet-tasting protein. Several members of this family display significant in vitro activity of inhibiting hyphal growth or spore germination of various fungi probably by a membrane permeabilizing mechanism.


Pssm-ID: 128501 [Multi-domain]  Cd Length: 218  Bit Score: 340.97  E-value: 4.13e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263     25 FEILNQCSYTVWAAASP-------GGGRRLDAGQSWRLDVAAGTKMARIWGRTNCNFDSSGRGRCQTGDCSGGLQCTGWG 97
Cdd:smart00205   1 FEFVNNCPYTVWAAALPsgkpqlsGGGFELNSGASWQLDAPPGTKMGRIWARTGCNFDASGRGRCATGDCGGVLQCNGWG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263     98 -QPPNTLAEYALNQFNNLDFYDISLVDGFNIPMEFSPT--SSNCHRILCTADINGQCPNVLRAPGG-----CNNPCTVFQ 169
Cdd:smart00205  81 gRPPATLAEFALNQFGGLDFYDVSLVDGFNIPMSFTPTggSGDCKGAGCTADLNAQCPAELQVPGGgsvvaCNSACTVFG 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15234263    170 TNQYCCTNGQG---SCSDTEYSRFFKQRCPDAYSYPQDDPTSTFTCTN-TNYRVVFCP 223
Cdd:smart00205 161 TDQYCCTGGQNnpeTCPPTNYSRIFKNACPDAYSYAYDDPTSTFTCTGgTNYKVTFCP 218
Thaumatin pfam00314
Thaumatin family;
29-223 2.58e-93

Thaumatin family;


Pssm-ID: 459757  Cd Length: 211  Bit Score: 272.91  E-value: 2.58e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263    29 NQCSYTVWAA-------ASPGGGRRLDAGQSWRLDVAAGTkMARIWGRTNCNFDSSGRgrCQTGDCSGGLQCTGW-GQPP 100
Cdd:pfam00314   1 NNCPFTIWPGiltnaghGPGTGGFELDPGQSRTFTVPDGW-SGRIWGRTGCSFDGSGS--CATGDCGGGLECNGAgGVPP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263   101 NTLAEYALNQFNNLDFYDISLVDGFNIPMEFSPTS-SNCHRILCTADINGQCPNVLRA------PGGCNNPCTVFQTNQY 173
Cdd:pfam00314  78 ATLAEFTLNGGGGQDFYDVSLVDGYNLPMSITPSGgGGCPVAGCAADLNSACPAELQVkspggkVVGCKSACLAFNTDEY 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15234263   174 CCTNGQGS---CSDTEYSRFFKQRCPDAYSYPQDDPTSTFTCTN-TNYRVVFCP 223
Cdd:pfam00314 158 CCTGAYATpetCKPTAYSKFFKAACPDAYSYAYDDATSTFTCPGgADYTITFCP 211
TLP-PA cd09218
allergenic/antifungal thaumatin-like proteins: plant and animal homologs; This subfamily is ...
 24-222 5.17e-79

allergenic/antifungal thaumatin-like proteins: plant and animal homologs; This subfamily is represented by the thaumatin-like proteins (TLPs), Cherry Allergen Pru Av 2 TLP, Peach PpAZ44 TLP (a propylene-induced TLP in abscission), the Caenorhabditis elegans thaumatin family member (thn-6), and other plant and animal homologs. TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Due to their inducible expression by environmental stresses such as pathogen/pest attack, drought and cold, plant TLPs are classified as the pathogenesis-related (PR) protein family 5 (PR5). Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. TLPs within this subfamily contain 16 conserved Cys residues.


Pssm-ID: 185757  Cd Length: 219  Bit Score: 236.75  E-value: 5.17e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263  24 TFEILNQCSYTVWAAASP--------GGGRRLDAGQSWRLDVAAGTKmARIWGRTNCNFDSSGRGRCQTGDCSGGLQCTG 95
Cdd:cd09218   1 TFTIYNKCPFTVWPGILGnaghpqlgGGGFELAPGQSRTIDAPSGWS-GRFWGRTGCSFDSSGKGSCATGDCGGGLECNG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263  96 -WGQPPNTLAEYALNQFNNLDFYDISLVDGFNIPMEFSPT--SSNCHRILCTADINGQCPNVL--RAPGG----CNNPCT 166
Cdd:cd09218  80 aGGAPPATLAEFTLGGSGGQDFYDVSLVDGYNLPVSITPQggSGGCRTAGCVADLNAVCPAELqvKNSGGrvvaCKSACL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263 167 VFQTNQYCCT---NGQGSCSDTEYSRFFKQRCPDAYSYPQDDPTSTFTCTN-TNYRVVFC 222
Cdd:cd09218 160 AFNTDEYCCRgayGTPETCKPTTYSRLFKNACPQAYSYAYDDPTSTFTCSSgANYVITFC 219
TLP-P cd09217
thaumatin and allergenic/antifungal thaumatin-like proteins: plant homologs; This subfamily is ...
 25-223 2.49e-78

thaumatin and allergenic/antifungal thaumatin-like proteins: plant homologs; This subfamily is represented by the sweet-tasting protein thaumatin from the African berry Thaumatococcus daniellii, allergenic/antifungal Thaumatin-like proteins (TLPs), and related plant proteins. TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Plant TLPs are classified as pathogenesis-related (PR) protein family 5 (PR5), their expression is induced by environmental stresses such as pathogen/pest attack, drought and cold. TLPs in this subfamily include such proteins as zeamatin, found in high concentrations in cereal seeds, and osmotin, a salt-induced protein in osmotically stressed plants. Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). Thaumatin and TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. IgE-binding epitopes of mountain Cedar (Juniperus ashei) allergen Jun a 3, which interact with pooled IgE from patients suffering allergenic response to this allergen, were mainly located on the helical domain II; the best-conserved IgE-binding epitope predicted for TLPs corresponds to this region. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. Most TLPs contain 16 conserved Cys residues. A deletion within the third domain (domain II) of the Triticum aestivum thaumatin-like xylanase inhibitor is observed, thus, only 10 conserved Cys residues are present within this smaller TLP and similar homologs.


Pssm-ID: 185756  Cd Length: 151  Bit Score: 232.66  E-value: 2.49e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263  25 FEILNQCSYTVWAAASP-GGGRRLDAGQSWRLDVAAGTKMARIWGRTNCNFDSSGRGRCQTGDCSGGLQCTGWGQPPNTL 103
Cdd:cd09217   1 FTITNNCGYTVWPAATPvGGGRQLNPGQSWTIDVPAGTAGGRIWGRTGCSFDASGRGSCQTGDCGGVLSCTGSGKPPATL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263 104 AEYALNQfNNLDFYDISLVDGFNIPMEFSPTSSNCHRILCTADingqcpnvlrapggcnnpctvfqtnqycctngqgscs 183
Cdd:cd09217  81 AEYTLNQ-SGQDFYDISLVDGFNVPMDFSPTGGGCHAIPCAAN------------------------------------- 122

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15234263 184 dteysrffkqrCPDAYSYPQdDPTSTFTCT-NTNYRVVFCP 223
Cdd:cd09217 123 -----------CPDAYSYPK-DPTTTFTCPgGTNYRIVFCP 151
Thaumatin-like cd09215
the sweet-tasting protein, thaumatin, and thaumatin-like proteins involved in host defense; ...
 25-222 8.07e-56

the sweet-tasting protein, thaumatin, and thaumatin-like proteins involved in host defense; This family is represented by the sweet-tasting protein thaumatin from the African berry Thaumatococcus daniellii and thaumatin-like proteins (TLPs) involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Plant TLPs are classified as pathogenesis-related (PR) protein family 5 (PR5), their expression is induced by environmental stresses such as pathogen/pest attack, drought and cold. TLPs included in this family are such proteins as zeamatin, found in high concentrations in cereal seeds; osmotin, a salt-induced protein in osmotically stressed plants; and PpAZ44, a propylene-induced TLP in abscission of young fruit. Several members of the plant TLP family have been reported as food allergens from fruits (i.e., cherry, Pru av 2; bell pepper, Cap a1; tomatoes, Lyc e NP24) and pollen allergens from conifers (i.e., mountain cedar, Jun a 3; Arizona cypress, Cup a3; Japanese cedar, Cry j3). Thaumatin and TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. It has been proposed that the antifungal activity of plant PR5 proteins relies on the strong electronegative character of this cleft. Some TLPs hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. Most TLPs contain 16 conserved Cys residues. A deletion within the third domain (domain II) of the Triticum aestivum thaumatin-like xylanase inhibitor is observed, thus, only 10 conserved Cys residues are present within this smaller TLP and similar homologs.


Pssm-ID: 185754  Cd Length: 157  Bit Score: 175.72  E-value: 8.07e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263  25 FEILNQCSYTVWAAASPG-------GGRRLDAGQSWRLDVAAGTKmARIWGRTNCNFD-SSGRGRCQTGDCSGGLQCTGW 96
Cdd:cd09215   1 FTITNRCPYTIWPAIFTQvgkgpytGGFELNPGETKSFDVSAGWQ-GRIWARTNCSFNaNSGGNACLTGDCNGGLNCQGT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263  97 GQPPNTLAEYALNQFNNLDFYDISLVDGFNIPMEFSPTSSNCHRILCTAdingqcpnvlrapggcnnpctvfqtnqycct 176
Cdd:cd09215  80 GGPPATLAEFTLSGGGGLDYYDISLVDGYNLPMSITPQPGECPTPICAA------------------------------- 128

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15234263 177 ngqgscsdteysrffkqrCPDAYSYPQDDPTSTFTC-TNTNYRVVFC 222
Cdd:cd09215 129 ------------------CPDAYSYAYDDQTSTFTCpGGAGYEVVFC 157
GH64-TLP-SF cd08961
glycoside hydrolase family 64 (beta-1,3-glucanases which produce specific pentasaccharide ...
 25-221 2.69e-42

glycoside hydrolase family 64 (beta-1,3-glucanases which produce specific pentasaccharide oligomers) and thaumatin-like proteins; This superfamily includes glycoside hydrolases of family 64 (GH64), these are mostly bacterial beta-1,3-glucanases which cleave long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers and are implicated in fungal cell wall degradation. Also included in this superfamily are thaumatin, the sweet-tasting protein from the African berry Thaumatococcus daniellii, and thaumatin-like proteins (TLPs) which are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. Like GH64s, some TLPs also hydrolyze the beta-1,3-glucans of the type commonly found in fungal walls. Plant TLPs are classified as pathogenesis-related (PR) protein family 5 (PR5), their expression is induced by environmental stresses such as pathogen/pest attack, drought and cold. Several members of the plant TLP family have been reported as food allergens from fruits, and pollen allergens from conifers. Streptomyces matensis laminaripentaose-producing, beta-1,3-glucanase (GH64-LPHase), and TLPs have in common, a core N-terminal barrel domain (domain I) composed of 10 beta-strands, two coming from the C-terminal region of the protein. In TLPs, this core domain is flanked by two shorter domains (domains II and III). Small TLPs, such as Triticum aestivum thaumatin-like xylanase inhibitor, have a deletion in the third domain (domain II). GH64-LPHase has a second C-terminal domain which corresponds positional to, but is much larger than, domain III of TLP. GH64-LPHase and TLPs are described as crescent-fold structures. Critical functional residues, common to GH64-LPHase and TLPs are a Glu and an Asp residue. LPHase has an electronegative, substrate-binding cleft and the afore mentioned conserved Glu and Asp residues are the catalytic residues essential for beta-1,3-glucan cleavage. In TLPs, these residues are two of the four conserved residues which contribute to the strong electronegative character of the cleft which is associated with the antifungal activity of TLPs.


Pssm-ID: 185752  Cd Length: 153  Bit Score: 141.22  E-value: 2.69e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263  25 FEILNQCSYTVWAAASPG--------GGRRLDAGQSWRLDVAAGTKmARIWGRTNCNFDSSGRGRCQTGDCSGGLQCTGW 96
Cdd:cd08961   1 LTITNNCGYQVWIYNLGTelssapdaSGPGLAPGRSTTIQIPKGFS-GRIWFRTGCSMDFSGTTGCLTQDPGVVNPTDPN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263  97 GQPPNTLAEYALNQFNNLDFYDISLVDGFNIPMEFSPTSsnchrilctadingqcpnvlrapggcnnpctvfqtnqycct 176
Cdd:cd08961  80 RDPPFTLAEFTLNDFNSGDFIDSSLVDGFNAPMTVGPRR----------------------------------------- 118

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15234263 177 nGQGSCSDTEysrffkqrcpDAYSYPQDDPTSTFTCTN-TNYRVVF 221
Cdd:cd08961 119 -GDGTCLSTG----------DAYSYAFDDHESTFTCGGgRNYSLTF 153
TLP-F cd09219
thaumatin-like proteins: basidiomycete homologs; This subfamily is represented by Lentinula ...
 25-223 1.37e-38

thaumatin-like proteins: basidiomycete homologs; This subfamily is represented by Lentinula edodes TLG1, a thaumatin-like protein (TLP), as well as, other basidiomycete homologs. In general, TLPs are involved in host defense and a wide range of developmental processes in fungi, plants, and animals. TLG1 TLP is involved in lentinan degradation and fruiting body senescence. TLG1 expressed in Escherichia coli and Aspergillus oryzae exhibited beta-1,3-glucanase activity and demonstrated lentinan degrading activity. TLG1 is proposed to be involved in lentinan and cell wall degradation during senescence following harvest and spore diffusion. TLPs are three-domain, crescent-fold structures with either an electronegative, electropositive, or neutral cleft occurring between domains I and II. TLG1 from Lentinula edodes contains the required acidic amino acids conserved in the appropriate positions to possess an electronegative cleft. TLPs within this subfamily contain 13 conserved Cys residues; the number of total Cys residues in these TLPs varies from 16 in L. edodes TLG1 to 18 in other basidiomycete homologs.


Pssm-ID: 185758  Cd Length: 229  Bit Score: 133.98  E-value: 1.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263  25 FEILNQCSYTVWAAASPGG-----------GRRLDAGQSWRLDVAAGTKMARIWGRTNCNF-DSSGRGRCQTGDCSGGLQ 92
Cdd:cd09219   1 FTVKNSCSSTIWPAMFTGGnfidavpdqatGWEAAAGGQVEFTVPDNWTAGRIWARTGCDFsDNPGPFSCLTGGCGGGLT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15234263  93 CTGWGQPPNTLAEYALNQfNNLDFYDISLVDGFNIPMEFSPtSSNCHRILCTADINGQCPNVLRAPG-------GCNNPC 165
Cdd:cd09219  81 CENSDQPPASLAEFTLIG-GKEDNYDISLVDGFNIPLNITN-NITCPQPQCQVDLNVLCPALLRGPLdqkgvnlGCISPC 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15234263 166 TVFQT--NQYCCTNGQGSCSDT------EYSRFFKQRCPDAYSYPQDDPTST--FTC---TNTNYRVVFCP 223
Cdd:cd09219 159 NRDKNhdDSPSCCTGSHNKPETcpqsgvGNYAYFKDNCPTAYAYAYDEKSHTalWTCgdsKSADYTVTFCP 229
 
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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