NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1063718288|ref|NP_001326183|]
View 

Plant invertase/pectin methylesterase inhibitor superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02197 super family cl31838
pectinesterase
 63-244 7.82e-27

pectinesterase


The actual alignment was detected with superfamily member PLN02197:

Pssm-ID: 177848 [Multi-domain]  Cd Length: 588  Bit Score: 108.17  E-value: 7.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288  63 TPHAKAVAGICTVIpTDTSLCCKTLKHVPTNDPIELIRALVAAAETSVKQSVTFLSGIKPKHMSDATAT--AVVNSCEKN 140
Cdd:PLN02197   35 SPQMKAVQGICQST-SDKASCVKTLEPVKSDDPNKLIKAFMLATKDAITKSSNFTGQTEGNMGSSISPNnkAVLDYCKRV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288 141 LNYALEDFADFWKATGKDVTTLAHNYFTCKKELMSIMGYHSTCLDDIEDKILLKEVGIGIGVGKNLTSDSFDVFNNLNTI 220
Cdd:PLN02197  114 FMYALEDLSTIVEEMGEDLNQIGSKIDQLKQWLTGVYNYQTDCLDDIEEDDLRKTIGEGIANSKILTSNAIDIFHSVVSA 193

                         170       180
                  ....*....|....*....|....*...
gi 1063718288 221 FKTFGIKVKLNEEDT----SPRPPPLSD 244
Cdd:PLN02197  194 MAKLNNKVDDFKNMTggipTPGAPPVVD 221
 
Name Accession Description Interval E-value
PLN02197 PLN02197
pectinesterase
 63-244 7.82e-27

pectinesterase


Pssm-ID: 177848 [Multi-domain]  Cd Length: 588  Bit Score: 108.17  E-value: 7.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288  63 TPHAKAVAGICTVIpTDTSLCCKTLKHVPTNDPIELIRALVAAAETSVKQSVTFLSGIKPKHMSDATAT--AVVNSCEKN 140
Cdd:PLN02197   35 SPQMKAVQGICQST-SDKASCVKTLEPVKSDDPNKLIKAFMLATKDAITKSSNFTGQTEGNMGSSISPNnkAVLDYCKRV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288 141 LNYALEDFADFWKATGKDVTTLAHNYFTCKKELMSIMGYHSTCLDDIEDKILLKEVGIGIGVGKNLTSDSFDVFNNLNTI 220
Cdd:PLN02197  114 FMYALEDLSTIVEEMGEDLNQIGSKIDQLKQWLTGVYNYQTDCLDDIEEDDLRKTIGEGIANSKILTSNAIDIFHSVVSA 193

                         170       180
                  ....*....|....*....|....*...
gi 1063718288 221 FKTFGIKVKLNEEDT----SPRPPPLSD 244
Cdd:PLN02197  194 MAKLNNKVDDFKNMTggipTPGAPPVVD 221
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 72-219 1.87e-21

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: 87.11  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288  72 ICTVIPtDTSLCCKTLKHVP---TNDPIELIRALVAAAETSVKQSVTFLSGIKPKHMSDATATAVVNSCEKNLNYALEDF 148
Cdd:cd15798     2 ICSSTP-YPDLCKSSLSSYAsssSTDPKELAKAALNAALDEAKKALALLSSLLKSSGSNPREKAALEDCLELLDDAVDDL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718288 149 ADFWKATGK-DVTTLAHNYFTCKKELMSIMGYHSTCLDDIEDKI--LLKEVGIGIGVGKNLTSDSFDVFNNLNT 219
Cdd:cd15798    81 NRSLSELNSlSKDKFSERVDDVQTWLSAALTNQDTCLDGFEETGstVKKELRASLKNVSKLTSNALALVNALAK 154
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 63-213 5.17e-19

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: 80.49  E-value: 5.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288   63 TPHAKAVAGICTVIPtDTSLCCKTLK---HVPTNDPIELIRALVAAAETSVKQSVTFLSGIKPKHMsDATATAVVNSCEK 139
Cdd:smart00856   1 APTSKLIDSICKSTD-YPDFCVSSLSsdpSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTK-DPRLKAALKDCLE 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718288  140 NLNYALEDFADFWKATGKdvttlaHNYFTCKKELMSIMGYHSTCLDDIEDK--ILLKEVGIGIGVGKNLTSDSFDV 213
Cdd:smart00856  79 LYDDAVDSLEKALEELKS------GDYDDVATWLSAALTDQDTCLDGFEENddKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 67-210 2.05e-08

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: 51.78  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288  67 KAVAGICTVIPtDTSLCCKTLKHVP---TNDPIELIRALVAAAETSVKQSVTFLSGIKPKHMSDATATAVVNSCEKNLNY 143
Cdd:pfam04043   1 SLIKTACKKTP-YPDLCVSSLSSDPasaASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYDD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288 144 ALEDFADFWKATGKDVTTLAhnyfTCKKELMSIMGYHSTCLDDIED---KILLKEVGIGIGVGKNLTSDS 210
Cdd:pfam04043  80 AVDELNRALDALKAGDSSRD----DAQTWLSAALTNQDTCEDGFKEavkGQLKSSMKSPLRNLTKLTSNA 145
 
Name Accession Description Interval E-value
PLN02197 PLN02197
pectinesterase
 63-244 7.82e-27

pectinesterase


Pssm-ID: 177848 [Multi-domain]  Cd Length: 588  Bit Score: 108.17  E-value: 7.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288  63 TPHAKAVAGICTVIpTDTSLCCKTLKHVPTNDPIELIRALVAAAETSVKQSVTFLSGIKPKHMSDATAT--AVVNSCEKN 140
Cdd:PLN02197   35 SPQMKAVQGICQST-SDKASCVKTLEPVKSDDPNKLIKAFMLATKDAITKSSNFTGQTEGNMGSSISPNnkAVLDYCKRV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288 141 LNYALEDFADFWKATGKDVTTLAHNYFTCKKELMSIMGYHSTCLDDIEDKILLKEVGIGIGVGKNLTSDSFDVFNNLNTI 220
Cdd:PLN02197  114 FMYALEDLSTIVEEMGEDLNQIGSKIDQLKQWLTGVYNYQTDCLDDIEEDDLRKTIGEGIANSKILTSNAIDIFHSVVSA 193

                         170       180
                  ....*....|....*....|....*...
gi 1063718288 221 FKTFGIKVKLNEEDT----SPRPPPLSD 244
Cdd:PLN02197  194 MAKLNNKVDDFKNMTggipTPGAPPVVD 221
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 72-219 1.87e-21

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: 87.11  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288  72 ICTVIPtDTSLCCKTLKHVP---TNDPIELIRALVAAAETSVKQSVTFLSGIKPKHMSDATATAVVNSCEKNLNYALEDF 148
Cdd:cd15798     2 ICSSTP-YPDLCKSSLSSYAsssSTDPKELAKAALNAALDEAKKALALLSSLLKSSGSNPREKAALEDCLELLDDAVDDL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063718288 149 ADFWKATGK-DVTTLAHNYFTCKKELMSIMGYHSTCLDDIEDKI--LLKEVGIGIGVGKNLTSDSFDVFNNLNT 219
Cdd:cd15798    81 NRSLSELNSlSKDKFSERVDDVQTWLSAALTNQDTCLDGFEETGstVKKELRASLKNVSKLTSNALALVNALAK 154
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 63-213 5.17e-19

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: 80.49  E-value: 5.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288   63 TPHAKAVAGICTVIPtDTSLCCKTLK---HVPTNDPIELIRALVAAAETSVKQSVTFLSGIKPKHMsDATATAVVNSCEK 139
Cdd:smart00856   1 APTSKLIDSICKSTD-YPDFCVSSLSsdpSSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTK-DPRLKAALKDCLE 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063718288  140 NLNYALEDFADFWKATGKdvttlaHNYFTCKKELMSIMGYHSTCLDDIEDK--ILLKEVGIGIGVGKNLTSDSFDV 213
Cdd:smart00856  79 LYDDAVDSLEKALEELKS------GDYDDVATWLSAALTDQDTCLDGFEENddKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 67-210 2.05e-08

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: 51.78  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288  67 KAVAGICTVIPtDTSLCCKTLKHVP---TNDPIELIRALVAAAETSVKQSVTFLSGIKPKHMSDATATAVVNSCEKNLNY 143
Cdd:pfam04043   1 SLIKTACKKTP-YPDLCVSSLSSDPasaASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYDD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288 144 ALEDFADFWKATGKDVTTLAhnyfTCKKELMSIMGYHSTCLDDIED---KILLKEVGIGIGVGKNLTSDS 210
Cdd:pfam04043  80 AVDELNRALDALKAGDSSRD----DAQTWLSAALTNQDTCEDGFKEavkGQLKSSMKSPLRNLTKLTSNA 145
PLN02745 PLN02745
Putative pectinesterase/pectinesterase inhibitor
 47-237 3.78e-05

Putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178346 [Multi-domain]  Cd Length: 596  Bit Score: 44.46  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288  47 AATATAKPVKRTnylftphAKAVAGICTVIpTDTSLCCKTL-----KHVPTNDPIELIRALVAAAETSVKQSVTFLSGIK 121
Cdd:PLN02745   67 SPVKSESPVSQV-------DKIIQTVCNAT-LYKQTCENTLkkgteKDPSLAQPKDLLKSAIKAVNDDLDKVLKKVLSFK 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288 122 PKHMSDATAtavVNSCEKNLNYALEDFADFWKATGKDVTTLAHNYFTCKKELMSIMGYHSTCLDDIEDKILLKEVGIGIG 201
Cdd:PLN02745  139 FENPDEKDA---IEDCKLLVEDAKEELKASISRINDEVNKLAKNVPDLNNWLSAVMSYQETCIDGFPEGKLKSEMEKTFK 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1063718288 202 VGKNLTSDSFDVFNNLNTIFKTFGI-KVK----LNEEDTSP 237
Cdd:PLN02745  216 SSQELTSNSLAMVSSLTSFLSSFSVpKVLnrhlLAKESNSP 256
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 68-185 3.43e-03

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: 36.95  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063718288  68 AVAGICTVipTD-TSLCCKTLK---HVPTNDPIELIRALVAAAETSVKQSVTFLSGIKPKHMSDATATAVVNSCEKNLNY 143
Cdd:cd15800     3 SVKDICKK--TDyPALCLSTVKpflTKGKIDPVSALEAAIKALIAKTKQAKALAKKLAKSPSTSPEVKSALDVCKESYDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063718288 144 ALEDFadfwKATGKDVTtlAHNYFTCKKELMSIMGYHSTCLD 185
Cdd:cd15800    81 ALDNL----KKALKAIK--SRDIGTLNSMLSAAITDYSTCDD 116
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH