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Conserved domains on  [gi|15219807|ref|NP_176275|]
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Plant invertase/pectin methylesterase inhibitor superfamily protein [Arabidopsis thaliana]

Protein Classification

PMEI-like_2 domain-containing protein( domain architecture ID 10205026)

PMEI-like_2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 28-162 1.97e-35

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: 120.54  E-value: 1.97e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807  28 EARFTSLCAQTAYPTLCRPLVKGP------NPRRATHSTIRALEAKTKLAITDSARFKSGNPT-------VAICYATLVD 94
Cdd:cd15800   1 DPSVKDICKKTDYPALCLSTVKPFltkgkiDPVSALEAAIKALIAKTKQAKALAKKLAKSPSTspevksaLDVCKESYDD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219807  95 ASFNLRRARTSIRKRNVMMLKMFLTAAVSDYGVCVNGFIDSHQVNTLQNDVDELRKMGTNCLLLATLI 162
Cdd:cd15800  81 ALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFAESGLVSPLAKINDLLKKLASNCLAIATLL 148
 
Name Accession Description Interval E-value
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 28-162 1.97e-35

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: 120.54  E-value: 1.97e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807  28 EARFTSLCAQTAYPTLCRPLVKGP------NPRRATHSTIRALEAKTKLAITDSARFKSGNPT-------VAICYATLVD 94
Cdd:cd15800   1 DPSVKDICKKTDYPALCLSTVKPFltkgkiDPVSALEAAIKALIAKTKQAKALAKKLAKSPSTspevksaLDVCKESYDD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219807  95 ASFNLRRARTSIRKRNVMMLKMFLTAAVSDYGVCVNGFIDSHQVNTLQNDVDELRKMGTNCLLLATLI 162
Cdd:cd15800  81 ALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFAESGLVSPLAKINDLLKKLASNCLAIATLL 148
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 25-158 2.27e-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: 79.34  E-value: 2.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807     25 QATEARFTSLCAQTAYPTLCR------PLVKGPNPRRATHSTIRALEAKTKLAIT--DSARFKSGNPT----VAICYATL 92
Cdd:smart00856   1 APTSKLIDSICKSTDYPDFCVsslssdPSSSATDPKDLAKIAIKVALSQATKTLSfiSKLLKKTKDPRlkaaLKDCLELY 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219807     93 VDASFNLRRARTSIRKRNVMMLKMFLTAAVSDYGVCVNGF--IDSHQVNTLQNDVDELRKMGTNCLLL 158
Cdd:smart00856  81 DDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFeeNDDKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 33-156 7.60e-05

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: 40.61  E-value: 7.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807    33 SLCAQTAYPTLCR------PLVKGPNPR-------RATHSTIRALEAKTKLAITDSARFKSGNPTVAICYATLVDASFNL 99
Cdd:pfam04043   5 TACKKTPYPDLCVsslssdPASAASPPKglakaavNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYDDAVDEL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219807   100 RRARTSIRKRNVMM--LKMFLTAAVSDYGVCVNGF---IDSHQVNTLQNDVDELRKMGTNCL 156
Cdd:pfam04043  85 NRALDALKAGDSSRddAQTWLSAALTNQDTCEDGFkeaVKGQLKSSMKSPLRNLTKLTSNAL 146
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 1-158 2.32e-04

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: 39.71  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807     1 MASRNTIqMYLTTVVAIV--ILLAASQATEARFTSLCAQTAYPTLCRPLVKgPNPRRATHS-------TIRALEAKTKLA 71
Cdd:TIGR01614   1 MASSLSL-LLFLLLLSLVatSSSNSLNATQSLIKRICKKTEYPNFCISTLK-SDPSSAKADlqglaniSVSAALSNASDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807    72 IT--DSARFKSGNPTVAICYATLV----DASFNLRRARTSIRKRNVMMLKMFLTAAVSDYGVCVNGF--IDSHQVNTLQN 143
Cdd:TIGR01614  79 LDhiSKLLLTKGDPRDKSALEDCVelysDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFeeLGGIVKSPLTK 158

                         170
                  ....*....|....*
gi 15219807   144 DVDELRKMGTNCLLL 158
Cdd:TIGR01614 159 RNNNVKKLSSITLAI 173
 
Name Accession Description Interval E-value
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 28-162 1.97e-35

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: 120.54  E-value: 1.97e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807  28 EARFTSLCAQTAYPTLCRPLVKGP------NPRRATHSTIRALEAKTKLAITDSARFKSGNPT-------VAICYATLVD 94
Cdd:cd15800   1 DPSVKDICKKTDYPALCLSTVKPFltkgkiDPVSALEAAIKALIAKTKQAKALAKKLAKSPSTspevksaLDVCKESYDD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219807  95 ASFNLRRARTSIRKRNVMMLKMFLTAAVSDYGVCVNGFIDSHQVNTLQNDVDELRKMGTNCLLLATLI 162
Cdd:cd15800  81 ALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFAESGLVSPLAKINDLLKKLASNCLAIATLL 148
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 25-158 2.27e-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: 79.34  E-value: 2.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807     25 QATEARFTSLCAQTAYPTLCR------PLVKGPNPRRATHSTIRALEAKTKLAIT--DSARFKSGNPT----VAICYATL 92
Cdd:smart00856   1 APTSKLIDSICKSTDYPDFCVsslssdPSSSATDPKDLAKIAIKVALSQATKTLSfiSKLLKKTKDPRlkaaLKDCLELY 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219807     93 VDASFNLRRARTSIRKRNVMMLKMFLTAAVSDYGVCVNGF--IDSHQVNTLQNDVDELRKMGTNCLLL 158
Cdd:smart00856  81 DDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFeeNDDKVKSPLTKRNDNLEKLTSNALAI 148
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 33-156 6.56e-07

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: 46.28  E-value: 6.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807  33 SLCAQTAYPTLCR------PLVKGPNPRRATHSTIRALEAKTKLAITDSARFKSGNPT-------VAICYATLVDASFNL 99
Cdd:cd15798   1 AICSSTPYPDLCKsslssyASSSSTDPKELAKAALNAALDEAKKALALLSSLLKSSGSnprekaaLEDCLELLDDAVDDL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219807 100 RRARTSIRKRNVMM-------LKMFLTAAVSDYGVCVNGF--IDSHQVNTLQNDVDELRKMGTNCL 156
Cdd:cd15798  81 NRSLSELNSLSKDKfservddVQTWLSAALTNQDTCLDGFeeTGSTVKKELRASLKNVSKLTSNAL 146
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 33-156 7.60e-05

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: 40.61  E-value: 7.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807    33 SLCAQTAYPTLCR------PLVKGPNPR-------RATHSTIRALEAKTKLAITDSARFKSGNPTVAICYATLVDASFNL 99
Cdd:pfam04043   5 TACKKTPYPDLCVsslssdPASAASPPKglakaavNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYDDAVDEL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219807   100 RRARTSIRKRNVMM--LKMFLTAAVSDYGVCVNGF---IDSHQVNTLQNDVDELRKMGTNCL 156
Cdd:pfam04043  85 NRALDALKAGDSSRddAQTWLSAALTNQDTCEDGFkeaVKGQLKSSMKSPLRNLTKLTSNAL 146
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 1-158 2.32e-04

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: 39.71  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807     1 MASRNTIqMYLTTVVAIV--ILLAASQATEARFTSLCAQTAYPTLCRPLVKgPNPRRATHS-------TIRALEAKTKLA 71
Cdd:TIGR01614   1 MASSLSL-LLFLLLLSLVatSSSNSLNATQSLIKRICKKTEYPNFCISTLK-SDPSSAKADlqglaniSVSAALSNASDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219807    72 IT--DSARFKSGNPTVAICYATLV----DASFNLRRARTSIRKRNVMMLKMFLTAAVSDYGVCVNGF--IDSHQVNTLQN 143
Cdd:TIGR01614  79 LDhiSKLLLTKGDPRDKSALEDCVelysDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFeeLGGIVKSPLTK 158

                         170
                  ....*....|....*
gi 15219807   144 DVDELRKMGTNCLLL 158
Cdd:TIGR01614 159 RNNNVKKLSSITLAI 173
 
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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