|
Name |
Accession |
Description |
Interval |
E-value |
| PMEI-like_3 |
cd15798 |
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ... |
47-218 |
2.37e-44 |
|
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This subfamily contains inhibitors similar to those of pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) that catalyzes the demethylesterification of homogalacturonans in the cell wall. The proteinaceous PME inhibitor (PMEI) inhibits PME and invertase through formation of a non-covalent 1:1 complex. Depending on the mode of demethylesterification, PMEI activity results in either loosening or rigidification of the cell wall. PMEI has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. Thus, PMEI probably plays an important physiological role in PME regulation in plants, possessing several potential applications in a food-technological context.
Pssm-ID: 275442 [Multi-domain] Cd Length: 154 Bit Score: 145.66 E-value: 2.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 47 TSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSaakySGDGHQTASAViRDCVSNVED 126
Cdd:cd15798 1 AICSSTPYPDLCKSSLSSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKS----SGSNPREKAAL-EDCLELLDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 127 AVDEMRGSLRQLRDMngrgggtaarrSVETFRFQMSNVQTWMSAALTDEDTCTDGFEDMDegGLIKTTVCDRLEEVKRLT 206
Cdd:cd15798 76 AVDDLNRSLSELNSL-----------SKDKFSERVDDVQTWLSAALTNQDTCLDGFEETG--STVKKELRASLKNVSKLT 142
|
170
....*....|..
gi 1032296494 207 SNALALVNTYAN 218
Cdd:cd15798 143 SNALALVNALAK 154
|
|
| PMEI |
smart00856 |
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ... |
39-212 |
7.16e-41 |
|
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences, suggesting that both PMEs and their inhibitors are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.
Pssm-ID: 214860 [Multi-domain] Cd Length: 148 Bit Score: 136.35 E-value: 7.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 39 TNDLDFIRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSAakysgdGHQTASAVIR 118
Cdd:smart00856 1 APTSKLIDSICKSTDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKT------KDPRLKAALK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 119 DCVSNVEDAVDEMRGSLRQLrdmngrgggtaarrsvetFRFQMSNVQTWMSAALTDEDTCTDGFEDMDegGLIKTTVCDR 198
Cdd:smart00856 75 DCLELYDDAVDSLEKALEEL------------------KSGDYDDVATWLSAALTDQDTCLDGFEEND--DKVKSPLTKR 134
|
170
....*....|....
gi 1032296494 199 LEEVKRLTSNALAL 212
Cdd:smart00856 135 NDNLEKLTSNALAI 148
|
|
| PMEI |
pfam04043 |
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ... |
43-212 |
2.62e-37 |
|
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences (personal obs:C Yeats), suggesting that both PMEs and their inhibitor are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.
Pssm-ID: 461143 [Multi-domain] Cd Length: 148 Bit Score: 127.28 E-value: 2.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 43 DFIRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSAAKYSgdghqTASAVIRDCVS 122
Cdd:pfam04043 1 SLIKTACKKTPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSA-----KDKAALEDCLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 123 NVEDAVDEMRGSLRQLRDMNGRGggtaarrsvetfrfqmSNVQTWMSAALTDEDTCTDGFEDMDEGGLIKTTVcDRLEEV 202
Cdd:pfam04043 76 LYDDAVDELNRALDALKAGDSSR----------------DDAQTWLSAALTNQDTCEDGFKEAVKGQLKSSMK-SPLRNL 138
|
170
....*....|
gi 1032296494 203 KRLTSNALAL 212
Cdd:pfam04043 139 TKLTSNALAI 148
|
|
| PME_inhib |
TIGR01614 |
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ... |
43-217 |
3.72e-25 |
|
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, characterized by four conserved Cys residues, shown in a pectinesterase inhibitor from Kiwi to form two disulfide bonds: first to second and third to fourth. Roughly half the members of this family have the region described by this model followed immediately by a pectinesterase domain, pfam01095. This suggests that the pairing of the enzymatic domain and its inhibitor reflects a conserved regulatory mechanism for this enzyme family.
Pssm-ID: 273717 [Multi-domain] Cd Length: 178 Bit Score: 96.72 E-value: 3.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 43 DFIRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSAakysgdGHQTASAVIRDCVS 122
Cdd:TIGR01614 30 SLIKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSNASDTLDHISKLLLTK------GDPRDKSALEDCVE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 123 NVEDAVDEMRGSLRQLRDMNgrgggtaarrsvetfrfqMSNVQTWMSAALTDEDTCTDGFEDMdeGGLIKTTVCDRLEEV 202
Cdd:TIGR01614 104 LYSDAVDALDKALASLKSKD------------------YSDAETWLSSALTDPSTCEDGFEEL--GGIVKSPLTKRNNNV 163
|
170
....*....|....*
gi 1032296494 203 KRLTSNALALVNTYA 217
Cdd:TIGR01614 164 KKLSSITLAIIKMLT 178
|
|
| PLN02314 |
PLN02314 |
pectinesterase |
34-213 |
5.03e-18 |
|
pectinesterase
Pssm-ID: 215179 [Multi-domain] Cd Length: 586 Bit Score: 82.18 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 34 PNTTTTNDldFIRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSAAKysgdghQTA 113
Cdd:PLN02314 64 PPELTPAT--SLKAVCSVTRYPESCISSISSLPTSNTTDPETLFKLSLKVAIDELSKLSDLPQKLINETND------ERL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 114 SAVIRDCVSNVEDAVDEMRGSLRQlrdMNGRGGGTAARRSvetfrfQMSNVQTWMSAALTDEDTCTDGFEDMDEGGLIKT 193
Cdd:PLN02314 136 KSALRVCETLFDDAIDRLNDSISS---MQVGEGEKILSSS------KIDDLKTWLSATITDQETCIDALQELSQNKYANS 206
|
170 180
....*....|....*....|....
gi 1032296494 194 TVCDRL----EEVKRLTSNALALV 213
Cdd:PLN02314 207 TLTNEVktamSNSTEFTSNSLAIV 230
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PMEI-like_3 |
cd15798 |
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ... |
47-218 |
2.37e-44 |
|
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This subfamily contains inhibitors similar to those of pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) that catalyzes the demethylesterification of homogalacturonans in the cell wall. The proteinaceous PME inhibitor (PMEI) inhibits PME and invertase through formation of a non-covalent 1:1 complex. Depending on the mode of demethylesterification, PMEI activity results in either loosening or rigidification of the cell wall. PMEI has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. Thus, PMEI probably plays an important physiological role in PME regulation in plants, possessing several potential applications in a food-technological context.
Pssm-ID: 275442 [Multi-domain] Cd Length: 154 Bit Score: 145.66 E-value: 2.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 47 TSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSaakySGDGHQTASAViRDCVSNVED 126
Cdd:cd15798 1 AICSSTPYPDLCKSSLSSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKS----SGSNPREKAAL-EDCLELLDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 127 AVDEMRGSLRQLRDMngrgggtaarrSVETFRFQMSNVQTWMSAALTDEDTCTDGFEDMDegGLIKTTVCDRLEEVKRLT 206
Cdd:cd15798 76 AVDDLNRSLSELNSL-----------SKDKFSERVDDVQTWLSAALTNQDTCLDGFEETG--STVKKELRASLKNVSKLT 142
|
170
....*....|..
gi 1032296494 207 SNALALVNTYAN 218
Cdd:cd15798 143 SNALALVNALAK 154
|
|
| PMEI |
smart00856 |
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ... |
39-212 |
7.16e-41 |
|
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences, suggesting that both PMEs and their inhibitors are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.
Pssm-ID: 214860 [Multi-domain] Cd Length: 148 Bit Score: 136.35 E-value: 7.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 39 TNDLDFIRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSAakysgdGHQTASAVIR 118
Cdd:smart00856 1 APTSKLIDSICKSTDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKT------KDPRLKAALK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 119 DCVSNVEDAVDEMRGSLRQLrdmngrgggtaarrsvetFRFQMSNVQTWMSAALTDEDTCTDGFEDMDegGLIKTTVCDR 198
Cdd:smart00856 75 DCLELYDDAVDSLEKALEEL------------------KSGDYDDVATWLSAALTDQDTCLDGFEEND--DKVKSPLTKR 134
|
170
....*....|....
gi 1032296494 199 LEEVKRLTSNALAL 212
Cdd:smart00856 135 NDNLEKLTSNALAI 148
|
|
| PMEI |
pfam04043 |
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ... |
43-212 |
2.62e-37 |
|
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences (personal obs:C Yeats), suggesting that both PMEs and their inhibitor are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.
Pssm-ID: 461143 [Multi-domain] Cd Length: 148 Bit Score: 127.28 E-value: 2.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 43 DFIRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSAAKYSgdghqTASAVIRDCVS 122
Cdd:pfam04043 1 SLIKTACKKTPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSA-----KDKAALEDCLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 123 NVEDAVDEMRGSLRQLRDMNGRGggtaarrsvetfrfqmSNVQTWMSAALTDEDTCTDGFEDMDEGGLIKTTVcDRLEEV 202
Cdd:pfam04043 76 LYDDAVDELNRALDALKAGDSSR----------------DDAQTWLSAALTNQDTCEDGFKEAVKGQLKSSMK-SPLRNL 138
|
170
....*....|
gi 1032296494 203 KRLTSNALAL 212
Cdd:pfam04043 139 TKLTSNALAI 148
|
|
| PME_inhib |
TIGR01614 |
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ... |
43-217 |
3.72e-25 |
|
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, characterized by four conserved Cys residues, shown in a pectinesterase inhibitor from Kiwi to form two disulfide bonds: first to second and third to fourth. Roughly half the members of this family have the region described by this model followed immediately by a pectinesterase domain, pfam01095. This suggests that the pairing of the enzymatic domain and its inhibitor reflects a conserved regulatory mechanism for this enzyme family.
Pssm-ID: 273717 [Multi-domain] Cd Length: 178 Bit Score: 96.72 E-value: 3.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 43 DFIRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSAakysgdGHQTASAVIRDCVS 122
Cdd:TIGR01614 30 SLIKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSNASDTLDHISKLLLTK------GDPRDKSALEDCVE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 123 NVEDAVDEMRGSLRQLRDMNgrgggtaarrsvetfrfqMSNVQTWMSAALTDEDTCTDGFEDMdeGGLIKTTVCDRLEEV 202
Cdd:TIGR01614 104 LYSDAVDALDKALASLKSKD------------------YSDAETWLSSALTDPSTCEDGFEEL--GGIVKSPLTKRNNNV 163
|
170
....*....|....*
gi 1032296494 203 KRLTSNALALVNTYA 217
Cdd:TIGR01614 164 KKLSSITLAIIKMLT 178
|
|
| PMEI-like_1 |
cd15801 |
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ... |
44-214 |
5.11e-22 |
|
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily contains inhibitors similar to those of pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) that catalyzes the demethylesterification of homogalacturonans in the cell wall, and cell-wall invertases (CWIs) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. The proteinaceous PME inhibitor (PMEI) inhibits PME and invertase through formation of a non-covalent 1:1 complex. Cell-wall inhibitor of beta-fructosidase from tobacco (CIF) interacts with CWI in a strictly pH-dependent manner, modulated between pH 4 and 6, with rapid dissociation at neutral pH mediated by structure rearrangement or surface charge pattern in the binding interface. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF.
Pssm-ID: 275445 [Multi-domain] Cd Length: 146 Bit Score: 87.77 E-value: 5.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 44 FIRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLsrsaakYSGDGHQTASAVIRDCVSN 123
Cdd:cd15801 1 LIEEACKKTLDPDLCVSALSSDPESKKADLRGLAELALKAAAENATATASYVSEL------LNTAKDPYVQQCLEDCSEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 124 VEDAVDEMRGSLRQLRDMNGRGggtaarrsvetfrfqmsnVQTWMSAALTDEDTCTDGFEdmDEGGlIKTTVCDRLEEVK 203
Cdd:cd15801 75 YEDAVEQLNDSLAALDSKAYGD------------------VKTWVTAALADAETCEDAFK--EKPG-DKSPLTARNGDFS 133
|
170
....*....|.
gi 1032296494 204 RLTSNALALVN 214
Cdd:cd15801 134 KLCSIALAIIK 144
|
|
| PLN02314 |
PLN02314 |
pectinesterase |
34-213 |
5.03e-18 |
|
pectinesterase
Pssm-ID: 215179 [Multi-domain] Cd Length: 586 Bit Score: 82.18 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 34 PNTTTTNDldFIRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSAAKysgdghQTA 113
Cdd:PLN02314 64 PPELTPAT--SLKAVCSVTRYPESCISSISSLPTSNTTDPETLFKLSLKVAIDELSKLSDLPQKLINETND------ERL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 114 SAVIRDCVSNVEDAVDEMRGSLRQlrdMNGRGGGTAARRSvetfrfQMSNVQTWMSAALTDEDTCTDGFEDMDEGGLIKT 193
Cdd:PLN02314 136 KSALRVCETLFDDAIDRLNDSISS---MQVGEGEKILSSS------KIDDLKTWLSATITDQETCIDALQELSQNKYANS 206
|
170 180
....*....|....*....|....
gi 1032296494 194 TVCDRL----EEVKRLTSNALALV 213
Cdd:PLN02314 207 TLTNEVktamSNSTEFTSNSLAIV 230
|
|
| PMEI_like |
cd14859 |
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ... |
49-214 |
2.59e-17 |
|
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) catalyzes the demethylesterification of homogalacturonans in the cell wall. Its activity is regulated by the proteinaceous PME inhibitor (PMEI) which inhibits PME and invertase through formation of a non-covalent 1:1 complex. Depending on the mode of demethylesterification, PMEI activity results in either loosening or rigidification of the cell wall. PMEI has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. Thus, PMEI probably plays an important physiological role in PME regulation in plants, possessing several potential applications in a food-technological context. CIF (cell-wall inhibitor of beta-fructosidase from tobacco) is structurally similar to PMEI and these members are also included in this model. Comparison of the CIF/INV1 structure with the complex between PMEI/PME suggests a common targeting mechanism in PMEI and CIF. However, CIF and PMEI use distinct surface areas to selectively inhibit very different enzymatic scaffolds.
Pssm-ID: 275438 [Multi-domain] Cd Length: 140 Bit Score: 75.16 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 49 CNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSAakysgdGHQTASAVIRDCVSNVEDAV 128
Cdd:cd14859 1 CKKTSYYKLCVSSLSSDPRSSTADLKGLANIALDAALANASDTQAFIAKLLKST------KDPALKKALRDCADDYDDAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 129 DEMRGSLRQLRDMNgrgggtaarrsvetfrfqMSNVQTWMSAALTDEDTCTDGFEdmdEGGLIKTTVCDRLEEVKRLTSN 208
Cdd:cd14859 75 DDLEDAINALLSGD------------------YDDAKTHVSAALDDADTCEEAFK---ESSGLPSPLTTRNDDLKRLCSI 133
|
....*.
gi 1032296494 209 ALALVN 214
Cdd:cd14859 134 ALAIIL 139
|
|
| PLN02468 |
PLN02468 |
putative pectinesterase/pectinesterase inhibitor |
45-213 |
8.63e-17 |
|
putative pectinesterase/pectinesterase inhibitor
Pssm-ID: 178087 [Multi-domain] Cd Length: 565 Bit Score: 78.38 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 45 IRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQakstaaflskLSRSAAKYSGDGH------QTASAVIR 118
Cdd:PLN02468 67 VKAVCDVTLYKDSCYETLAPAPKASQLQPEELFKYAVKVAINE----------LSKASQAFSNSEGflgvkdNMTNAALN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 119 DCVSNVEDAVDEMRGSLRQlrdmngrGGGTAARRSVETFRfqmsnvqTWMSAALTDEDTCTDGFEdmdEGGLiKTTVCDR 198
Cdd:PLN02468 137 ACQELLDLAIDNLNNSLTS-------SGGVSVLDNVDDLR-------TWLSSAGTYQETCIDGLA---EPNL-KSFGENH 198
|
170
....*....|....*
gi 1032296494 199 LEEVKRLTSNALALV 213
Cdd:PLN02468 199 LKNSTELTSNSLAII 213
|
|
| PLN02484 |
PLN02484 |
probable pectinesterase/pectinesterase inhibitor |
32-212 |
2.22e-16 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 178102 [Multi-domain] Cd Length: 587 Bit Score: 77.26 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 32 PRPNTTTTNDLDFIRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLsQAKSTAAFLSklsrSAAKYSGDGHQ 111
Cdd:PLN02484 63 TSPKSLHRKPTQAISKTCSKTRFPNLCVDSLLDFPGSLTASESDLIHISFNMTL-QHFSKALYLS----STISYVQMPPR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 112 TASAvIRDCVSNVEDAVDEMRGSLRQLrdMNGRGGGTAarrsvetfrfqmSNVQTWMSAALTDEDTCTDGFEDMDEGGlI 191
Cdd:PLN02484 138 VRSA-YDSCLELLDDSVDALSRALSSV--VPSSGGGSP------------QDVVTWLSAALTNHDTCTEGFDGVNGGE-V 201
|
170 180
....*....|....*....|.
gi 1032296494 192 KTTVCDRLEEVKRLTSNALAL 212
Cdd:PLN02484 202 KDQMTGALKDLSELVSNCLAI 222
|
|
| PMEI-like_4 |
cd15799 |
plant invertase/pectin methylesterase inhibitor domain-containing protein; This subfamily ... |
48-215 |
2.27e-16 |
|
plant invertase/pectin methylesterase inhibitor domain-containing protein; This subfamily contains inhibitors similar to those of pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) that catalyzes the demethylesterification of homogalacturonans in the cell wall, and cell-wall invertases (CWIs) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. The proteinaceous PME inhibitor (PMEI) inhibits PME and invertase through formation of a non-covalent 1:1 complex. Cell-wall inhibitor of beta-fructosidase from tobacco (CIF) interacts with CWI in a strictly pH-dependent manner, modulated between pH 4 and 6, with rapid dissociation at neutral pH mediated by structure rearrangement or surface charge pattern in the binding interface. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF.
Pssm-ID: 275443 [Multi-domain] Cd Length: 151 Bit Score: 73.21 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 48 SCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSrsaakysgdGHQTASAVIRDCVSNVEDA 127
Cdd:cd15799 9 LCLAIPSVSSSANALSAQCLKVPLDVFLAALKTTVDRIQSALSMVSKLRNGS---------DDPRLSNALSDCLELLDFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 128 VDEMRGSLRQLRDMNGRGGgtaarrsvetfrfqmSNVQTWMSAALTDEDTCTDGFedmDEGGLIKTTVCDRLEEVKRLTS 207
Cdd:cd15799 80 ADRLSWSLSALQNPKGDSG---------------SDARTWLSAALTNHDTCLDGL---EETGVVKSLVAAALSNLTSLLR 141
|
....*...
gi 1032296494 208 NALALVNT 215
Cdd:cd15799 142 EALAMVAS 149
|
|
| PMEI-like_2 |
cd15800 |
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ... |
49-214 |
2.52e-15 |
|
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily contains inhibitors similar to those of pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) that catalyzes the demethylesterification of homogalacturonans in the cell wall, and cell-wall invertases (CWIs) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. The proteinaceous PME inhibitor (PMEI) inhibits PME and invertase through formation of a non-covalent 1:1 complex. Cell-wall inhibitor of beta-fructosidase from tobacco (CIF) interacts with CWI in a strictly pH-dependent manner, modulated between pH 4 and 6, with rapid dissociation at neutral pH mediated by structure rearrangement or surface charge pattern in the binding interface. Comparison of the CIF/INV1 structure with the complex between the structurally CIF-related pectin methylesterase inhibitor (PMEI) and pectin methylesterase indicates a common targeting mechanism in PMEI and CIF.
Pssm-ID: 275444 [Multi-domain] Cd Length: 148 Bit Score: 70.08 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 49 CNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSAAKYSgdghqTASAVIRDCVSNVEDAV 128
Cdd:cd15800 8 CKKTDYPALCLSTVKPFLTKGKIDPVSALEAAIKALIAKTKQAKALAKKLAKSPSTSP-----EVKSALDVCKESYDDAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 129 DEMRGSlrqLRDMNGRGGGTAarrsvetfrfqMSNvqtwMSAALTDEDTCTDGFEDMDEggliKTTVCDRLEEVKRLTSN 208
Cdd:cd15800 83 DNLKKA---LKAIKSRDIGTL-----------NSM----LSAAITDYSTCDDAFAESGL----VSPLAKINDLLKKLASN 140
|
....*.
gi 1032296494 209 ALALVN 214
Cdd:cd15800 141 CLAIAT 146
|
|
| PLN02745 |
PLN02745 |
Putative pectinesterase/pectinesterase inhibitor |
45-219 |
1.14e-14 |
|
Putative pectinesterase/pectinesterase inhibitor
Pssm-ID: 178346 [Multi-domain] Cd Length: 596 Bit Score: 72.19 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 45 IRTSCNATLYPDVCFTSLSGYA--SAVQDSPARLAKLAIgvslsqaKSTAAFLSKLSRSAAKYSGDgHQTASAVIRDCVS 122
Cdd:PLN02745 82 IQTVCNATLYKQTCENTLKKGTekDPSLAQPKDLLKSAI-------KAVNDDLDKVLKKVLSFKFE-NPDEKDAIEDCKL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 123 NVEDAVDEMRGSLRQLRDMNGRgggtaarrsvetFRFQMSNVQTWMSAALTDEDTCTDGFEDmdegGLIKTTVCDRLEEV 202
Cdd:PLN02745 154 LVEDAKEELKASISRINDEVNK------------LAKNVPDLNNWLSAVMSYQETCIDGFPE----GKLKSEMEKTFKSS 217
|
170
....*....|....*..
gi 1032296494 203 KRLTSNALALVNTYANN 219
Cdd:PLN02745 218 QELTSNSLAMVSSLTSF 234
|
|
| PLN02698 |
PLN02698 |
Probable pectinesterase/pectinesterase inhibitor |
45-222 |
1.46e-10 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 178301 [Multi-domain] Cd Length: 497 Bit Score: 59.96 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 45 IRTSCNATLYPDVCFTSLSGYASAVQDSPARLaklaIGVSLSQAKSTAAFLSKLSRSAAkySGDGHQTASavIRDCVSNV 124
Cdd:PLN02698 25 VQRECSFTKYPSLCVQTLRGLRHDGVDIVSVL----VNKTISETNLPLSSSMGSSYQLS--LEEATYTPS--VSDSCERL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 125 edavdeMRGSLRQLRDmngrgggtAARRSVETFRFQMSNVQTWMSAALTDEDTCTDGFEDMDE--GGLIKTTVCDRLEEV 202
Cdd:PLN02698 97 ------MKMSLKRLRQ--------SLLALKGSSRKNKHDIQTWLSAALTFQQACKDSIVDSTGysGTSAISQISQKMDHL 162
|
170 180
....*....|....*....|
gi 1032296494 203 KRLTSNALALVNTYANNGAP 222
Cdd:PLN02698 163 SRLVSNSLALVNRITPNPKP 182
|
|
| PLN02313 |
PLN02313 |
Pectinesterase/pectinesterase inhibitor |
45-213 |
1.89e-10 |
|
Pectinesterase/pectinesterase inhibitor
Pssm-ID: 177947 [Multi-domain] Cd Length: 587 Bit Score: 59.71 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 45 IRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLsrsAAKYSGDGHQTASAvIRDCVSNV 124
Cdd:PLN02313 62 LKSVCSSTLYPELCFSAVAATGGKELTSQKEVIEASLNLTTKAVKHNYFAVKKL---IAKRKGLTPREVTA-LHDCLETI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 125 EDAVDEMRGSLRQLRDMNGRgggtaarrsvETFRFQMSNVQTWMSAALTDEDTCTDGFEDMDEGGLIKTTVCDRLEEVKR 204
Cdd:PLN02313 138 DETLDELHVAVEDLHQYPKQ----------KSLRKHADDLKTLISSAITNQGTCLDGFSYDDADRKVRKALLKGQVHVEH 207
|
....*....
gi 1032296494 205 LTSNALALV 213
Cdd:PLN02313 208 MCSNALAMI 216
|
|
| PLN02201 |
PLN02201 |
probable pectinesterase/pectinesterase inhibitor |
103-222 |
1.05e-09 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 177852 [Multi-domain] Cd Length: 520 Bit Score: 57.58 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 103 AKYSGDghQTASAVIRDCVSNVEDAVDEMRGSLRQLRDMNGRGGGTAARRSvetfrfqmsNVQTWMSAALTDEDTCTDGF 182
Cdd:PLN02201 63 DKVFGD--SRLSNAISDCLDLLDFAAEELSWSISASQNPNGKDNSTGDVGS---------DLRTWLSAALSNQDTCIEGF 131
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1032296494 183 EDMDegGLIKTTVCDRLEEVKRLTSNALALVNTYANNGAP 222
Cdd:PLN02201 132 DGTN--GIVKKLVAGSLSQVGSTVRELLTMVHPPPSKGKS 169
|
|
| PLN02995 |
PLN02995 |
Probable pectinesterase/pectinesterase inhibitor |
30-220 |
4.84e-09 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 178574 [Multi-domain] Cd Length: 539 Bit Score: 55.45 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 30 LLPRPNTTTT--NDLDfIRTSCNATLYPDVC---FTSLSGYASAVQDSPARLakLAIGVSLSQAKSTAAflsKLSRSAAK 104
Cdd:PLN02995 21 LCVHPLTTVAdgNSTD-IDGWCDKTPYPDPCkcyFKNHNGFRQPTQISEFRV--MLVEAAMDRAISARD---ELTNSGKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 105 YSGDGHQtasAVIRDCVSNVEDAVDEMRgslrqlRDMNGRGGGTAARRSVETFrfqmsNVQTWMSAALTDEDTCTDGFED 184
Cdd:PLN02995 95 CTDFKKQ---AVLADCIDLYGDTIMQLN------RTLQGVSPKAGAAKRCTDF-----DAQTWLSTALTNTETCRRGSSD 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1032296494 185 MDEGGLIKTTVCDrlEEVKRLTSNALAL---VNTYANNG 220
Cdd:PLN02995 161 LNVSDFITPIVSN--TKISHLISNCLAVngaLLTAGNNG 197
|
|
| PLN02506 |
PLN02506 |
putative pectinesterase/pectinesterase inhibitor |
72-212 |
1.61e-08 |
|
putative pectinesterase/pectinesterase inhibitor
Pssm-ID: 215280 [Multi-domain] Cd Length: 537 Bit Score: 54.17 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 72 SPARLAKLAIGVSLSQAKSTAAFLSKLSRSAAKYSgdgHQTAsavIRDCVSNVEDAVDEMRGSLRQLRDMngRGGGTAAR 151
Cdd:PLN02506 65 TPHSVLSAALKATLDEARLAIDMITKFNALSISYR---EQVA---IEDCKELLDFSVSELAWSLLEMNKI--RAGHDNVA 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032296494 152 RSvetfrfqmSNVQTWMSAALTDEDTCTDGFEDMDegGLIKTTVCDRLEEVKRLTSNALAL 212
Cdd:PLN02506 137 YE--------GNLKAWLSAALSNQDTCLEGFEGTD--RHLENFIKGSLKQVTQLISNVLAM 187
|
|
| PLN02416 |
PLN02416 |
probable pectinesterase/pectinesterase inhibitor |
35-213 |
4.84e-08 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 178037 [Multi-domain] Cd Length: 541 Bit Score: 52.62 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 35 NTTTTNDLDF----IRTSCNATLYPDVCFTSLSGYASaVQDSPARLAKLAigVSLSQAKSTAAFLSKLsRSAAKYSGDGH 110
Cdd:PLN02416 27 NASYTTSLDPhlssLTSFCKSTPYPDACFDSLKLSIS-INISPNILNFLL--QTLQTAISEAGKLTNL-LSGAGQSSNII 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 111 QTASAVIRDCVSNVEDAVDEMRGSLRQLRDMNGRgggtaarrsvetfrfQMSNVQTWMSAALTDEDTCTDGFEdmDEGGL 190
Cdd:PLN02416 103 EKQRGTIQDCKELHQITVSSLKRSVSRIQAGDSR---------------KLADARAYLSAALTNKNTCLEGLD--SASGP 165
|
170 180
....*....|....*....|...
gi 1032296494 191 IKTTVCDRLEEVKRLTSNALALV 213
Cdd:PLN02416 166 LKPKLVNSFTSTYKHVSNSLSML 188
|
|
| PLN02217 |
PLN02217 |
probable pectinesterase/pectinesterase inhibitor |
39-218 |
1.69e-07 |
|
probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215130 [Multi-domain] Cd Length: 670 Bit Score: 51.24 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 39 TNDLDFIRTSCNATLYPDVCFTSLSGYASAVQDsPARLAKLAIGVSLSQAKSTAaflsKLSRSAAKYSGDGHqtASAVIR 118
Cdd:PLN02217 50 TTSVKAIKDVCAPTDYKETCEDTLRKDAKNTSD-PLELVKTAFNATMKQISDVA----KKSQTMIELQKDPR--TKMALD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 119 DCVSNVEDAVDEMRGSLRQLrdmnGRgggtaarrsvetFRFQ-----MSNVQTWMSAALTDEDTCTDGFEDMDegGLIKT 193
Cdd:PLN02217 123 QCKELMDYAIGELSKSFEEL----GK------------FEFHkvdeaLIKLRIWLSATISHEQTCLDGFQGTQ--GNAGE 184
|
170 180
....*....|....*....|....*
gi 1032296494 194 TVCDRLEEVKRLTSNALALVNTYAN 218
Cdd:PLN02217 185 TIKKALKTAVQLTHNGLAMVSEMSN 209
|
|
| PLN02713 |
PLN02713 |
Probable pectinesterase/pectinesterase inhibitor |
47-212 |
1.87e-07 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215383 [Multi-domain] Cd Length: 566 Bit Score: 50.95 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 47 TSCNATLYPDVCFTSL-SGYASAVQDSparlAKLAIGVSLSQAKStaaFLSKLSRSAAKYSGDGHQTASAVIRDCVSNVE 125
Cdd:PLN02713 37 TICNTTPDPSFCKSVLpHNQPGNVYDY----GRFSVRKSLSQSRK---FLSLVDRYLKRNSTLLSKSAIRALEDCQFLAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 126 DAVDEMRGSlrqlrdmngrggGTAARRSVETFRF-QMSNVQTWMSAALTDEDTCTDGFEDMDEGGLIKTTVCDRLEEVKR 204
Cdd:PLN02713 110 LNIDFLLSS------------FETVNSSSKTLSDpQADDVQTLLSAILTNQQTCLDGLQAASSAWSVRNGLAVPLSNDTK 177
|
....*...
gi 1032296494 205 LTSNALAL 212
Cdd:PLN02713 178 LYSVSLAL 185
|
|
| PLN02990 |
PLN02990 |
Probable pectinesterase/pectinesterase inhibitor |
29-218 |
2.66e-07 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215535 [Multi-domain] Cd Length: 572 Bit Score: 50.41 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 29 RLLPRPNTTTTNDLDFIrtsCNATLYPDVCFTSLSGyASAVQDSPARLAKLAIGVSLsqaKSTAAFLSKLSrSAAKYSGD 108
Cdd:PLN02990 43 KIVPVQIKTTTKAVEAV---CAPTDYKETCVNSLMK-ASPDSTQPLDLIKLGFNVTI---RSINDSIKKAS-GELKAKAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 109 GHQTASAVIRDCVSNVEDAVDEMRGSLRQLRDMngrgggtaarrSVETFRFQMSNVQTWMSAALTDEDTCTDGFEDmdeg 188
Cdd:PLN02990 115 NDPETKGALELCEKLMNDATDDLKKCLDNFDGF-----------SIDQIEDFVEDLRVWLSGSIAYQQTCMDTFEE---- 179
|
170 180 190
....*....|....*....|....*....|....
gi 1032296494 189 glIKTTVCDRLEEV----KRLTSNALALVNTYAN 218
Cdd:PLN02990 180 --IKSNLSQDMLKIfktsRELTSNGLAMITNISN 211
|
|
| PLN03043 |
PLN03043 |
Probable pectinesterase/pectinesterase inhibitor; Provisional |
48-213 |
3.29e-07 |
|
Probable pectinesterase/pectinesterase inhibitor; Provisional
Pssm-ID: 178606 [Multi-domain] Cd Length: 538 Bit Score: 50.25 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 48 SCNATLYPDVCFTSLSGYASAVQDsPARLAKLAIGVSLSQAKSTAAFLSKLSRSAAKYSGDGHQTASAViRDCVSNVEDA 127
Cdd:PLN03043 5 ACKSTLYPKLCRSILSTVKSSPSD-PYEYGKFSVKQCLKQARRLSKVINYYLTHENQPGKMTHEEIGAL-ADCGELSELN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 128 VDEMR---GSLRQLRDMNGrgggtaarRSVEtfrfqmsNVQTWMSAALTDEDTCTDGFEDMDEGglIKTTVCDRLEEVKR 204
Cdd:PLN03043 83 VDYLEtisSELKSAELMTD--------ALVE-------RVTSLLSGVVTNQQTCYDGLVDSKSS--FAAALGAPLGNLTR 145
|
....*....
gi 1032296494 205 LTSNALALV 213
Cdd:PLN03043 146 LYSVSLGLV 154
|
|
| PLN02301 |
PLN02301 |
pectinesterase/pectinesterase inhibitor |
24-213 |
6.01e-06 |
|
pectinesterase/pectinesterase inhibitor
Pssm-ID: 215170 [Multi-domain] Cd Length: 548 Bit Score: 46.41 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 24 SISAVRLLPRPNTTTTNDLDFIRTSCNATLYPDVCFTSLSGYA--SAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRS 101
Cdd:PLN02301 32 SSAALFTAPLISTNSSSPPSLLQTLCDRAHDQDSCQAMVSEIAtnTVMKLNRVDLLQVLLKESTPHLQNTIEMASEIRIR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 102 AakysgDGHQTASAVIrDCVSNVEDAVDEMRGSLRQLrdmngrgggtaARRSVETFrfqmSNVQTWMSAALTDEDTCTDG 181
Cdd:PLN02301 112 I-----NDPRDKAALA-DCVELMDLSKDRIKDSVEAL-----------GNVTSKSH----ADAHTWLSSVLTNHVTCLDG 170
|
170 180 190
....*....|....*....|....*....|..
gi 1032296494 182 FEdmdegGLIKTTVCDRLEEVKRLTSNALALV 213
Cdd:PLN02301 171 IN-----GPSRQSMKPGLKDLISRARTSLAIL 197
|
|
| PMEI |
cd15797 |
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ... |
43-214 |
6.92e-06 |
|
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy class 8 of carbohydrate esterases) catalyzes the demethylesterification of homogalacturonans in the cell wall. Its activity is regulated by the proteinaceous PME inhibitor (PMEI) which inhibits PME and invertase through formation of a non-covalent 1:1 complex. Depending on the mode of demethylesterification, PMEI activity results in either loosening or rigidification of the cell wall. PMEI has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. Thus, PMEI probably plays an important physiological role in PME regulation in plants, possessing several potential applications in a food-technological context.
Pssm-ID: 275441 [Multi-domain] Cd Length: 149 Bit Score: 44.34 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 43 DFIRTSCNATLYPDVCFTSLSGYASAVQDSPARLAKLAIGVSLSQAKSTAAFLSKLSRSAAKysgdghQTASAVIRDCVS 122
Cdd:cd15797 3 ELIDTICKKTENPSFCLQILNSDPRSASADLVGLAQIAIDLAQSNATNTLKLIQSLIKSTTD------PKLKNRYESCSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 123 NVEDAVDEMRGSLRQLRDMNGRGggtaARRSVetfrfqmsnvqtwmSAALTDEDTCTDGFEDMDEgglIKTTVCDRLEEV 202
Cdd:cd15797 77 NYNDAIDALEEAKKSLSSGDYDG----LNKAA--------------SAALDAVSTCEDELSKPPK---DPSPLAKYNRDV 135
|
170
....*....|..
gi 1032296494 203 KRLTSNALALVN 214
Cdd:cd15797 136 EDLCDIILVISD 147
|
|
| PLN02708 |
PLN02708 |
Probable pectinesterase/pectinesterase inhibitor |
32-220 |
1.16e-05 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 215379 [Multi-domain] Cd Length: 553 Bit Score: 45.59 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 32 PRPNTTTTNDLDfIRTSCNATLYPDVCFTSLSGYASAVQD-SPARLAKLAIGVSLSQAKSTAaflSKLSRSAAKYSGDGH 110
Cdd:PLN02708 35 PPPPSSPSTPPQ-ILLACNATRFPDTCVSSLSNAGRVPPDpKPIQIIQSAISVSRENLKTAQ---SMVKSILDSSAGNVN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 111 QTASAviRDCV---SNVEDAVDEMRGSLRqlrdmngRGGGTAARrsvetfrfqmsnvqTWMSAALTDEDTCTDGFEDMDE 187
Cdd:PLN02708 111 RTTAA--TNCLevlSNSEHRISSTDIALP-------RGKIKDAR--------------AWMSAALLYQYDCWSALKYVND 167
|
170 180 190
....*....|....*....|....*....|...
gi 1032296494 188 GGLIKTTVCdRLEEVKRLTSNALALVNTYANNG 220
Cdd:PLN02708 168 TSQVNDTMS-FLDSLIGLTSNALSMMASYDIFG 199
|
|
| PMEI-Pla_a_1_like |
cd15795 |
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ... |
47-214 |
3.28e-05 |
|
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen allergen Pla a 1 belongs to a class of allergens related to proteinaceous invertase and pectin methylesterase inhibitors. Platanus acerifolia is an important cause of pollinosis; Pla a 1 has a prevalence of about 80% among plane tree pollen-allergic patients. Recombinant Pla a 1 binds IgE in vitro, similar to its natural counterpart, rendering it suitable for specific diagnosis and structural studies. Invertase inhibitors are structurally similar to those of pectin methylesterase (PMEIs), an enzyme that is involved in the control of pectin metabolism and is structurally unrelated to invertases. All inhibitors share a size of about 18 kDa, two strictly conserved disulfide bridges and only moderate sequence homology (about 20% sequence identity).
Pssm-ID: 275439 [Multi-domain] Cd Length: 148 Bit Score: 42.35 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 47 TSCNATLYPDVCFTSLSGY--ASAVQDSPArLAKLAIGVSLSQAKSTAAFLSKLSRSaakySGDGHQTASAvIRDCVSNV 124
Cdd:cd15795 5 AAGDPNVDYDFCVSSLQSDprSRTAADLKG-LAVIATKLAIANATATKAKIEKLLKS----KKYPSDLKKA-LRDCLSLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032296494 125 EDAVDEMRGSLRqlrdmngrgggtaarrSVETFRFQMSNvqTWMSAALTDEDTCTDGFEdmdEGGLIKTTVCDRLEEVKR 204
Cdd:cd15795 79 SDAVDSLKSALD----------------ALKSGDYGDAN--YDLSAATDAPVTCEDAFK---EAKIVVSPLTKENDELFQ 137
|
170
....*....|
gi 1032296494 205 LTSNALALVN 214
Cdd:cd15795 138 LALIALAITS 147
|
|
| PLN02933 |
PLN02933 |
Probable pectinesterase/pectinesterase inhibitor |
119-186 |
1.33e-03 |
|
Probable pectinesterase/pectinesterase inhibitor
Pssm-ID: 178521 [Multi-domain] Cd Length: 530 Bit Score: 39.22 E-value: 1.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032296494 119 DCVSNVEDAVDEMRGSLRQLRDMNgrgggtaarrsvetfrFQMSNVQTWMSAALTDEDTCTDGFEDMD 186
Cdd:PLN02933 94 DCLGLLDDTISDLTTAISKLRSSS----------------PEFNDVSMLLSNAMTNQDTCLDGFSTSD 145
|
|
| |
