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Conserved domains on  [gi|186478498|ref|NP_563960|]
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Plant invertase/pectin methylesterase inhibitor superfamily protein [Arabidopsis thaliana]

Protein Classification

plant invertase/pectin methylesterase inhibitor family protein( domain architecture ID 10204989)

plant invertase/pectin methylesterase inhibitor family protein similar to proteinaceous PME inhibitor (PMEI) which inhibits pectin methylesterase (PME) and invertase through formation of a non-covalent 1:1 complex

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 61-216 2.01e-43

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: 142.96  E-value: 2.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  61 TSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAAS-----AAVHDCVSNVGDAVDQM 135
Cdd:cd15798    1 AICSSTPYPDLCKSSLSSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKSSGSnprekAALEDCLELLDDAVDDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 136 RGSLRQLREMnhrrpGDPAFRFQMSNVQTWMSAALTDEETCTDGVTEemEDGETKTAICDRVADVKRFTSNALALVNTYA 215
Cdd:cd15798   81 NRSLSELNSL-----SKDKFSERVDDVQTWLSAALTNQDTCLDGFEE--TGSTVKKELRASLKNVSKLTSNALALVNALA 153


                 .
gi 186478498 216 N 216
Cdd:cd15798  154 K 154
 
Name Accession Description Interval E-value
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 61-216 2.01e-43

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: 142.96  E-value: 2.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  61 TSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAAS-----AAVHDCVSNVGDAVDQM 135
Cdd:cd15798    1 AICSSTPYPDLCKSSLSSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKSSGSnprekAALEDCLELLDDAVDDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 136 RGSLRQLREMnhrrpGDPAFRFQMSNVQTWMSAALTDEETCTDGVTEemEDGETKTAICDRVADVKRFTSNALALVNTYA 215
Cdd:cd15798   81 NRSLSELNSL-----SKDKFSERVDDVQTWLSAALTNQDTCLDGFEE--TGSTVKKELRASLKNVSKLTSNALALVNALA 153


                 .
gi 186478498 216 N 216
Cdd:cd15798  154 K 154
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 57-210 4.15e-38

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: 129.41  E-value: 4.15e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498    57 DFIRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRA----ASAAVHDCVSNVGDAV 132
Cdd:smart00856   5 KLIDSICKSTDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTkdprLKAALKDCLELYDDAV 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186478498   133 DQMRGSLRQLremnhrrpgdpaFRFQMSNVQTWMSAALTDEETCTDGVTEemEDGETKTAICDRVADVKRFTSNALAL 210
Cdd:smart00856  85 DSLEKALEEL------------KSGDYDDVATWLSAALTDQDTCLDGFEE--NDDKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 57-210 2.14e-34

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: 119.96  E-value: 2.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498   57 DFIRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAAS-----AAVHDCVSNVGDA 131
Cdd:pfam04043   1 SLIKTACKKTPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKsakdkAALEDCLELYDDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478498  132 VDQMRGSLRQLREMNHRRpgdpafrfqmSNVQTWMSAALTDEETCTDGVtEEMEDGETKTAICDRVADVKRFTSNALAL 210
Cdd:pfam04043  81 VDELNRALDALKAGDSSR----------DDAQTWLSAALTNQDTCEDGF-KEAVKGQLKSSMKSPLRNLTKLTSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 28-215 3.86e-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: 3.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498   28 VLYLVTLLFICRTISAVRFPPEQPTTDDldfIRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAA 107
Cdd:TIGR01614   4 SLSLLLFLLLLSLVATSSSNSLNATQSL---IKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSNASDTLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  108 YLSKLSRRAAS----AAVHDCVSNVGDAVDQMRGSLRQLREMNHrrpgdpafrfqmSNVQTWMSAALTDEETCTDGVTEe 183
Cdd:TIGR01614  81 HISKLLLTKGDprdkSALEDCVELYSDAVDALDKALASLKSKDY------------SDAETWLSSALTDPSTCEDGFEE- 147

                         170       180       190
                  ....*....|....*....|....*....|..
gi 186478498  184 mEDGETKTAICDRVADVKRFTSNALALVNTYA 215
Cdd:TIGR01614 148 -LGGIVKSPLTKRNNNVKKLSSITLAIIKMLT 178
PLN02314 PLN02314
pectinesterase
 51-211 7.04e-18

pectinesterase


Pssm-ID: 215179 [Multi-domain]  Cd Length: 586  Bit Score: 81.41  E-value: 7.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  51 PTTDDLDFIRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAASA----AVHDCVS 126
Cdd:PLN02314  65 PELTPATSLKAVCSVTRYPESCISSISSLPTSNTTDPETLFKLSLKVAIDELSKLSDLPQKLINETNDErlksALRVCET 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 127 NVGDAVDQMRGSLRQLREMNHRRPGDPAfrfQMSNVQTWMSAALTDEETCTDGVTEEMEDGETKTAICDRV----ADVKR 202
Cdd:PLN02314 145 LFDDAIDRLNDSISSMQVGEGEKILSSS---KIDDLKTWLSATITDQETCIDALQELSQNKYANSTLTNEVktamSNSTE 221


                 ....*....
gi 186478498 203 FTSNALALV 211
Cdd:PLN02314 222 FTSNSLAIV 230
 
Name Accession Description Interval E-value
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 61-216 2.01e-43

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: 142.96  E-value: 2.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  61 TSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAAS-----AAVHDCVSNVGDAVDQM 135
Cdd:cd15798    1 AICSSTPYPDLCKSSLSSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKSSGSnprekAALEDCLELLDDAVDDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 136 RGSLRQLREMnhrrpGDPAFRFQMSNVQTWMSAALTDEETCTDGVTEemEDGETKTAICDRVADVKRFTSNALALVNTYA 215
Cdd:cd15798   81 NRSLSELNSL-----SKDKFSERVDDVQTWLSAALTNQDTCLDGFEE--TGSTVKKELRASLKNVSKLTSNALALVNALA 153


                 .
gi 186478498 216 N 216
Cdd:cd15798  154 K 154
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 57-210 4.15e-38

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: 129.41  E-value: 4.15e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498    57 DFIRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRA----ASAAVHDCVSNVGDAV 132
Cdd:smart00856   5 KLIDSICKSTDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTkdprLKAALKDCLELYDDAV 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186478498   133 DQMRGSLRQLremnhrrpgdpaFRFQMSNVQTWMSAALTDEETCTDGVTEemEDGETKTAICDRVADVKRFTSNALAL 210
Cdd:smart00856  85 DSLEKALEEL------------KSGDYDDVATWLSAALTDQDTCLDGFEE--NDDKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 57-210 2.14e-34

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: 119.96  E-value: 2.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498   57 DFIRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAAS-----AAVHDCVSNVGDA 131
Cdd:pfam04043   1 SLIKTACKKTPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKsakdkAALEDCLELYDDA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478498  132 VDQMRGSLRQLREMNHRRpgdpafrfqmSNVQTWMSAALTDEETCTDGVtEEMEDGETKTAICDRVADVKRFTSNALAL 210
Cdd:pfam04043  81 VDELNRALDALKAGDSSR----------DDAQTWLSAALTNQDTCEDGF-KEAVKGQLKSSMKSPLRNLTKLTSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 28-215 3.86e-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: 3.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498   28 VLYLVTLLFICRTISAVRFPPEQPTTDDldfIRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAA 107
Cdd:TIGR01614   4 SLSLLLFLLLLSLVATSSSNSLNATQSL---IKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSNASDTLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  108 YLSKLSRRAAS----AAVHDCVSNVGDAVDQMRGSLRQLREMNHrrpgdpafrfqmSNVQTWMSAALTDEETCTDGVTEe 183
Cdd:TIGR01614  81 HISKLLLTKGDprdkSALEDCVELYSDAVDALDKALASLKSKDY------------SDAETWLSSALTDPSTCEDGFEE- 147

                         170       180       190
                  ....*....|....*....|....*....|..
gi 186478498  184 mEDGETKTAICDRVADVKRFTSNALALVNTYA 215
Cdd:TIGR01614 148 -LGGIVKSPLTKRNNNVKKLSSITLAIIKMLT 178
PMEI-like_1 cd15801
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 58-212 1.30e-21

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: 86.62  E-value: 1.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  58 FIRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAASAAVH----DCVSNVGDAVD 133
Cdd:cd15801    1 LIEEACKKTLDPDLCVSALSSDPESKKADLRGLAELALKAAAENATATASYVSELLNTAKDPYVQqcleDCSENYEDAVE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478498 134 QMRGSLRQLREMNHRrpgdpafrfqmsNVQTWMSAALTDEETCTDGVTEEmedGETKTAICDRVADVKRFTSNALALVN 212
Cdd:cd15801   81 QLNDSLAALDSKAYG------------DVKTWVTAALADAETCEDAFKEK---PGDKSPLTARNGDFSKLCSIALAIIK 144
PLN02314 PLN02314
pectinesterase
 51-211 7.04e-18

pectinesterase


Pssm-ID: 215179 [Multi-domain]  Cd Length: 586  Bit Score: 81.41  E-value: 7.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  51 PTTDDLDFIRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAASA----AVHDCVS 126
Cdd:PLN02314  65 PELTPATSLKAVCSVTRYPESCISSISSLPTSNTTDPETLFKLSLKVAIDELSKLSDLPQKLINETNDErlksALRVCET 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 127 NVGDAVDQMRGSLRQLREMNHRRPGDPAfrfQMSNVQTWMSAALTDEETCTDGVTEEMEDGETKTAICDRV----ADVKR 202
Cdd:PLN02314 145 LFDDAIDRLNDSISSMQVGEGEKILSSS---KIDDLKTWLSATITDQETCIDALQELSQNKYANSTLTNEVktamSNSTE 221


                 ....*....
gi 186478498 203 FTSNALALV 211
Cdd:PLN02314 222 FTSNSLAIV 230
PLN02468 PLN02468
putative pectinesterase/pectinesterase inhibitor
 27-211 7.50e-18

putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178087 [Multi-domain]  Cd Length: 565  Bit Score: 81.46  E-value: 7.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  27 TVLYLVTLLFICRTISAV-----RFPPEQPTTDDLDFIRTS----CNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGV 97
Cdd:PLN02468  26 TIISLSSIILVAIVVAAVvgttaSSGNSEKTGNNGKSISTSvkavCDVTLYKDSCYETLAPAPKASQLQPEELFKYAVKV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  98 SLSRAKYTAAYLSK------LSRRAASAAVHDCVSNVGDAVDQMRGSLRQLREMNHRRPGDpafrfqmsNVQTWMSAALT 171
Cdd:PLN02468 106 AINELSKASQAFSNsegflgVKDNMTNAALNACQELLDLAIDNLNNSLTSSGGVSVLDNVD--------DLRTWLSSAGT 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 186478498 172 DEETCTDGVTEemedGETKTAICDRVADVKRFTSNALALV 211
Cdd:PLN02468 178 YQETCIDGLAE----PNLKSFGENHLKNSTELTSNSLAII 213
PMEI_like cd14859
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ...
 63-212 7.66e-16

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: 71.31  E-value: 7.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  63 CNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAASAAV----HDCVSNVGDAVDQMRGS 138
Cdd:cd14859    1 CKKTSYYKLCVSSLSSDPRSSTADLKGLANIALDAALANASDTQAFIAKLLKSTKDPALkkalRDCADDYDDAVDDLEDA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186478498 139 LRQLREMNHrrpgdpafrfqmSNVQTWMSAALTDEETCTDGVTEEmedGETKTAICDRVADVKRFTSNALALVN 212
Cdd:cd14859   81 INALLSGDY------------DDAKTHVSAALDDADTCEEAFKES---SGLPSPLTTRNDDLKRLCSIALAIIL 139
PLN02313 PLN02313
Pectinesterase/pectinesterase inhibitor
 59-211 6.03e-15

Pectinesterase/pectinesterase inhibitor


Pssm-ID: 177947 [Multi-domain]  Cd Length: 587  Bit Score: 72.81  E-value: 6.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  59 IRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAAS------AAVHDCVSNVGDAV 132
Cdd:PLN02313  62 LKSVCSSTLYPELCFSAVAATGGKELTSQKEVIEASLNLTTKAVKHNYFAVKKLIAKRKGltprevTALHDCLETIDETL 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478498 133 DQMRGSLRQLremnHRRPGDPAFRFQMSNVQTWMSAALTDEETCTDGVTEEMEDGETKTAICDRVADVKRFTSNALALV 211
Cdd:PLN02313 142 DELHVAVEDL----HQYPKQKSLRKHADDLKTLISSAITNQGTCLDGFSYDDADRKVRKALLKGQVHVEHMCSNALAMI 216
PLN02484 PLN02484
probable pectinesterase/pectinesterase inhibitor
 59-210 7.99e-15

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178102 [Multi-domain]  Cd Length: 587  Bit Score: 72.63  E-value: 7.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  59 IRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSL---SRAKYTAAYLSKLSRRA-ASAAVHDCVSNVGDAVDQ 134
Cdd:PLN02484  76 ISKTCSKTRFPNLCVDSLLDFPGSLTASESDLIHISFNMTLqhfSKALYLSSTISYVQMPPrVRSAYDSCLELLDDSVDA 155

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186478498 135 MRGSLRQLREMNHrrPGDPafrfqmSNVQTWMSAALTDEETCTDGVtEEMEDGETKTAICDRVADVKRFTSNALAL 210
Cdd:PLN02484 156 LSRALSSVVPSSG--GGSP------QDVVTWLSAALTNHDTCTEGF-DGVNGGEVKDQMTGALKDLSELVSNCLAI 222
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 63-212 2.22e-13

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: 65.07  E-value: 2.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  63 CNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAAS-----AAVHDCVSNVGDAVDQMRG 137
Cdd:cd15800    8 CKKTDYPALCLSTVKPFLTKGKIDPVSALEAAIKALIAKTKQAKALAKKLAKSPSTspevkSALDVCKESYDDALDNLKK 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186478498 138 SLRQLREmnhrrpGDPAfrfqmsNVQTWMSAALTDEETCTDGVTEemedGETKTAICDRVADVKRFTSNALALVN 212
Cdd:cd15800   88 ALKAIKS------RDIG------TLNSMLSAAITDYSTCDDAFAE----SGLVSPLAKINDLLKKLASNCLAIAT 146
PLN02745 PLN02745
Putative pectinesterase/pectinesterase inhibitor
 48-217 6.87e-13

Putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178346 [Multi-domain]  Cd Length: 596  Bit Score: 66.80  E-value: 6.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  48 PEQPTTDDLDFIRTSCNTTLYPDVCYTSL--AGYASAVQDNPARLAKLAIG-VSLSRAKYTAAYLS-KLSRRAASAAVHD 123
Cdd:PLN02745  71 SESPVSQVDKIIQTVCNATLYKQTCENTLkkGTEKDPSLAQPKDLLKSAIKaVNDDLDKVLKKVLSfKFENPDEKDAIED 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 124 CVSNVGDAVDQMRGSLRQLremnhrrpGDPAFRFQmSNVQ---TWMSAALTDEETCTDGvteeMEDGETKTAICDRVADV 200
Cdd:PLN02745 151 CKLLVEDAKEELKASISRI--------NDEVNKLA-KNVPdlnNWLSAVMSYQETCIDG----FPEGKLKSEMEKTFKSS 217

                        170
                 ....*....|....*..
gi 186478498 201 KRFTSNALALVNTYANN 217
Cdd:PLN02745 218 QELTSNSLAMVSSLTSF 234
PMEI-like_4 cd15799
plant invertase/pectin methylesterase inhibitor domain-containing protein; This subfamily ...
 61-213 5.15e-12

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: 61.27  E-value: 5.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  61 TSCNTTLYPDVCYTSLAGYASAVQdnparlaklAIGVSLSRAKYTAAYLSKLS-RRAASAAVHDCVSNVGDAVDQMRGSL 139
Cdd:cd15799   17 SSSANALSAQCLKVPLDVFLAALK---------TTVDRIQSALSMVSKLRNGSdDPRLSNALSDCLELLDFSADRLSWSL 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186478498 140 RQLREMNhrrpgdpafRFQMSNVQTWMSAALTDEETCTDGVtEEMedGETKTAICDRVADVKRFTSNALALVNT 213
Cdd:cd15799   88 SALQNPK---------GDSGSDARTWLSAALTNHDTCLDGL-EET--GVVKSLVAAALSNLTSLLREALAMVAS 149
PLN02698 PLN02698
Probable pectinesterase/pectinesterase inhibitor
 59-217 3.43e-11

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178301 [Multi-domain]  Cd Length: 497  Bit Score: 61.88  E-value: 3.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  59 IRTSCNTTLYPDVCYTSLAGYASAVQDNPARLaklaIGVSLSRAKYTAAYLSKLSRRAASAAVHDCVSnVGDAVDQ-MRG 137
Cdd:PLN02698  25 VQRECSFTKYPSLCVQTLRGLRHDGVDIVSVL----VNKTISETNLPLSSSMGSSYQLSLEEATYTPS-VSDSCERlMKM 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 138 SLRQLREMNHRRPGDPafRFQMSNVQTWMSAALTDEETCTDGVTE--EMEDGETKTAICDRVADVKRFTSNALALVNTYA 215
Cdd:PLN02698 100 SLKRLRQSLLALKGSS--RKNKHDIQTWLSAALTFQQACKDSIVDstGYSGTSAISQISQKMDHLSRLVSNSLALVNRIT 177


                 ..
gi 186478498 216 NN 217
Cdd:PLN02698 178 PN 179
PLN02713 PLN02713
Probable pectinesterase/pectinesterase inhibitor
 19-181 2.92e-10

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215383 [Multi-domain]  Cd Length: 566  Bit Score: 59.04  E-value: 2.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  19 MGRQLYTTTVLYLVTLLFiCRTISAVRFPPEQPTTDDldfirTSCNTTLYPDVCYTSLAgyaSAVQDNPARLAKLAIGVS 98
Cdd:PLN02713   1 MSSKLILLTTLALLLLLF-FSSSSASDPPPSTPVSPS-----TICNTTPDPSFCKSVLP---HNQPGNVYDYGRFSVRKS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  99 LSRA-KYTA---AYL---SKLSRRAASAAVHDCVSNVGDAVDQMRGSLRQLREMNHRRPGdpafrFQMSNVQTWMSAALT 171
Cdd:PLN02713  72 LSQSrKFLSlvdRYLkrnSTLLSKSAIRALEDCQFLAGLNIDFLLSSFETVNSSSKTLSD-----PQADDVQTLLSAILT 146

                        170
                 ....*....|
gi 186478498 172 DEETCTDGVT 181
Cdd:PLN02713 147 NQQTCLDGLQ 156
PLN02506 PLN02506
putative pectinesterase/pectinesterase inhibitor
 86-210 4.38e-07

putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 215280 [Multi-domain]  Cd Length: 537  Bit Score: 49.55  E-value: 4.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  86 NPARLAKLAIGVSLSRAKYTAAYLSKLSRRAASA----AVHDCVSNVGDAVDQMRGSLRqlrEMNHRRPGDPAFRFQmSN 161
Cdd:PLN02506  65 TPHSVLSAALKATLDEARLAIDMITKFNALSISYreqvAIEDCKELLDFSVSELAWSLL---EMNKIRAGHDNVAYE-GN 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 186478498 162 VQTWMSAALTDEETCTDGVteEMEDGETKTAICDRVADVKRFTSNALAL 210
Cdd:PLN02506 141 LKAWLSAALSNQDTCLEGF--EGTDRHLENFIKGSLKQVTQLISNVLAM 187
PLN02416 PLN02416
probable pectinesterase/pectinesterase inhibitor
 59-211 5.16e-07

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178037 [Multi-domain]  Cd Length: 541  Bit Score: 49.54  E-value: 5.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  59 IRTSCNTTLYPDVCYTSLAGYASaVQDNPARLAKL--AIGVSLSRAkytaaylSKLSRRAASAAVHdcvSNVgdaVDQMR 136
Cdd:PLN02416  41 LTSFCKSTPYPDACFDSLKLSIS-INISPNILNFLlqTLQTAISEA-------GKLTNLLSGAGQS---SNI---IEKQR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 137 GSLRQLREMNH------------RRPGDPAfrfQMSNVQTWMSAALTDEETCTDGVteEMEDGETKTAICDRVADVKRFT 204
Cdd:PLN02416 107 GTIQDCKELHQitvsslkrsvsrIQAGDSR---KLADARAYLSAALTNKNTCLEGL--DSASGPLKPKLVNSFTSTYKHV 181


                 ....*..
gi 186478498 205 SNALALV 211
Cdd:PLN02416 182 SNSLSML 188
PLN02170 PLN02170
probable pectinesterase/pectinesterase inhibitor
 107-210 1.04e-06

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215114 [Multi-domain]  Cd Length: 529  Bit Score: 48.44  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 107 AYLSKLSRRAASAA----VHDCVSNVGDAVDqMRGSLRQLREMNHRRpgdpafrfqmSNVQTWMSAALTDEETCTDGVTE 182
Cdd:PLN02170  84 AFNLTLSHRTVQTHtfdpVNDCLELLDDTLD-MLSRIVVIKHADHDE----------EDVHTWLSAALTNQETCEQSLQE 152

                         90       100
                 ....*....|....*....|....*....
gi 186478498 183 EMEDGETKTAIcDRVA-DVKRFTSNALAL 210
Cdd:PLN02170 153 KSSSYKHGLAM-DFVArNLTGLLTNSLDL 180
PLN02217 PLN02217
probable pectinesterase/pectinesterase inhibitor
 49-216 5.54e-06

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215130 [Multi-domain]  Cd Length: 670  Bit Score: 46.62  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  49 EQPTTDDLDFIRTSCNTTLYPDVCYTSLAGYASAVQDnPARLAKLAIGVSL------SRAKYTAAYLSKLSRraASAAVH 122
Cdd:PLN02217  46 KGEITTSVKAIKDVCAPTDYKETCEDTLRKDAKNTSD-PLELVKTAFNATMkqisdvAKKSQTMIELQKDPR--TKMALD 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 123 DCVSNVGDAVDQMRGSLRQLREMNHRRPgDPAfrfqMSNVQTWMSAALTDEETCTDGVT-EEMEDGET-----KTAIcdr 196
Cdd:PLN02217 123 QCKELMDYAIGELSKSFEELGKFEFHKV-DEA----LIKLRIWLSATISHEQTCLDGFQgTQGNAGETikkalKTAV--- 194

                        170       180
                 ....*....|....*....|
gi 186478498 197 vadvkRFTSNALALVNTYAN 216
Cdd:PLN02217 195 -----QLTHNGLAMVSEMSN 209
PLN02995 PLN02995
Probable pectinesterase/pectinesterase inhibitor
 17-218 7.50e-06

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178574 [Multi-domain]  Cd Length: 539  Bit Score: 46.21  E-value: 7.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  17 LKMGRQLYTTTVLYLVTLLFIC-RTISAVrfpPEQPTTDdldfIRTSCNTTLYPDVC---YTSLAGYASAVQDNPARLak 92
Cdd:PLN02995   1 MNMMMQKISFLSLHLLLLLLLCvHPLTTV---ADGNSTD----IDGWCDKTPYPDPCkcyFKNHNGFRQPTQISEFRV-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  93 LAIGVSLSRAKYTAAYLSKLSRRAA----SAAVHDCVSNVGDAVDQMRGSLRQLREmnhrrPGDPAFRFQMSNVQTWMSA 168
Cdd:PLN02995  72 MLVEAAMDRAISARDELTNSGKNCTdfkkQAVLADCIDLYGDTIMQLNRTLQGVSP-----KAGAAKRCTDFDAQTWLST 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 186478498 169 ALTDEETCTDGvTEEMEDGETKTAICDRvADVKRFTSNALAlVN----TYANNG 218
Cdd:PLN02995 147 ALTNTETCRRG-SSDLNVSDFITPIVSN-TKISHLISNCLA-VNgallTAGNNG 197
PLN02708 PLN02708
Probable pectinesterase/pectinesterase inhibitor
 47-218 1.57e-05

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215379 [Multi-domain]  Cd Length: 553  Bit Score: 45.21  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  47 PPEQPTTDDLDfIRTSCNTTLYPDVCYTSLAGYASAVQD-NPARLAKLAIGVSLSRAKyTAAYLSKlSRRAASAAvhdcv 125
Cdd:PLN02708  36 PPPSSPSTPPQ-ILLACNATRFPDTCVSSLSNAGRVPPDpKPIQIIQSAISVSRENLK-TAQSMVK-SILDSSAG----- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 126 sNVgDAVDQMRGSLRQLREMNHR-RPGDPAF-RFQMSNVQTWMSAALTDEETCTDG---VTEEMEDGETKTAICDRVAdv 200
Cdd:PLN02708 108 -NV-NRTTAATNCLEVLSNSEHRiSSTDIALpRGKIKDARAWMSAALLYQYDCWSAlkyVNDTSQVNDTMSFLDSLIG-- 183

                        170
                 ....*....|....*...
gi 186478498 201 krFTSNALALVNTYANNG 218
Cdd:PLN02708 184 --LTSNALSMMASYDIFG 199
PLN02301 PLN02301
pectinesterase/pectinesterase inhibitor
 29-180 3.14e-05

pectinesterase/pectinesterase inhibitor


Pssm-ID: 215170 [Multi-domain]  Cd Length: 548  Bit Score: 44.10  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  29 LYLVtlLFICRTISAVRFPPEQ----PTTDDLDFIRTSCNTTLYPDVCYTSLAGYA--SAVQDNPARLAKLAIGVSLSRA 102
Cdd:PLN02301  21 LCLV--LSFVAILSSAALFTAPlistNSSSPPSLLQTLCDRAHDQDSCQAMVSEIAtnTVMKLNRVDLLQVLLKESTPHL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 103 KYTAAYLSKLSRRAA----SAAVHDCVSNVGDAVDQMRGSLRQLREMNHRrpgdpafrfQMSNVQTWMSAALTDEETCTD 178
Cdd:PLN02301  99 QNTIEMASEIRIRINdprdKAALADCVELMDLSKDRIKDSVEALGNVTSK---------SHADAHTWLSSVLTNHVTCLD 169


                 ..
gi 186478498 179 GV 180
Cdd:PLN02301 170 GI 171
PLN03043 PLN03043
Probable pectinesterase/pectinesterase inhibitor; Provisional
 62-211 7.01e-05

Probable pectinesterase/pectinesterase inhibitor; Provisional


Pssm-ID: 178606 [Multi-domain]  Cd Length: 538  Bit Score: 42.93  E-value: 7.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  62 SCNTTLYPDVCYTSLAGYASAVQDnPARLAKLAIGVSLSRA----KYTAAYLSKLSRRAAS-----AAVHDCVS----NV 128
Cdd:PLN03043   5 ACKSTLYPKLCRSILSTVKSSPSD-PYEYGKFSVKQCLKQArrlsKVINYYLTHENQPGKMtheeiGALADCGElselNV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 129 gDAVDQMRGSLRQLREMNHRRpgdpafrfqMSNVQTWMSAALTDEETCTDGVTEemEDGETKTAICDRVADVKRFTSNAL 208
Cdd:PLN03043  84 -DYLETISSELKSAELMTDAL---------VERVTSLLSGVVTNQQTCYDGLVD--SKSSFAAALGAPLGNLTRLYSVSL 151


                 ...
gi 186478498 209 ALV 211
Cdd:PLN03043 152 GLV 154
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 61-212 7.09e-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: 41.58  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  61 TSCNTTLYPDVCYTSLAGY--ASAVQDNPArLAKLAIGVSLSRAKYTAAYLSKLSRRA-----ASAAVHDCVSNVGDAVD 133
Cdd:cd15795    5 AAGDPNVDYDFCVSSLQSDprSRTAADLKG-LAVIATKLAIANATATKAKIEKLLKSKkypsdLKKALRDCLSLYSDAVD 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478498 134 QMRGSLRQLREmnhRRPGDpafrfqmsnVQTWMSAALTDEETCTDGVTeemEDGETKTAICDRVADVKRFTSNALALVN 212
Cdd:cd15795   84 SLKSALDALKS---GDYGD---------ANYDLSAATDAPVTCEDAFK---EAKIVVSPLTKENDELFQLALIALAITS 147
PLN02990 PLN02990
Probable pectinesterase/pectinesterase inhibitor
 59-216 1.94e-04

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215535 [Multi-domain]  Cd Length: 572  Bit Score: 41.93  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  59 IRTSCNTTLYPDVCYTSLAGyASAVQDNPARLAKLAIGVSL-----SRAKYTAAYLSKLSR-RAASAAVHDCVSNVGDAV 132
Cdd:PLN02990  56 VEAVCAPTDYKETCVNSLMK-ASPDSTQPLDLIKLGFNVTIrsindSIKKASGELKAKAANdPETKGALELCEKLMNDAT 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498 133 DQMRGSLRQLREMNhrrpgDPAFRFQMSNVQTWMSAALTDEETCTDGVteemedGETKTAICDRVADV----KRFTSNAL 208
Cdd:PLN02990 135 DDLKKCLDNFDGFS-----IDQIEDFVEDLRVWLSGSIAYQQTCMDTF------EEIKSNLSQDMLKIfktsRELTSNGL 203


                 ....*...
gi 186478498 209 ALVNTYAN 216
Cdd:PLN02990 204 AMITNISN 211
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 57-179 5.73e-03

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: 35.86  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478498  57 DFIRTSCNTTLYPDVCYTSLAGYASAVQDNPARLAKLAIGVSLSRAKYTAAYLSKLSRRAASAAV----HDCVSNVGDAV 132
Cdd:cd15797    3 ELIDTICKKTENPSFCLQILNSDPRSASADLVGLAQIAIDLAQSNATNTLKLIQSLIKSTTDPKLknryESCSKNYNDAI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 186478498 133 DQMRGSLRQLREMNHRrpgdpafrfQMSNVqtwMSAALTDEETCTDG 179
Cdd:cd15797   83 DALEEAKKSLSSGDYD---------GLNKA---ASAALDAVSTCEDE 117
 
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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