NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18391202|ref|NP_563878|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 31-166 6.96e-38

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: 126.71  E-value: 6.96e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202  31 ESRMINICSHTAYPSLCRPLVKR-----VTSPRKATHRTIQALEAKTKLALAETARFKNGN-------QAVSTCYETLGD 98
Cdd:cd15800   1 DPSVKDICKKTDYPALCLSTVKPfltkgKIDPVSALEAAIKALIAKTKQAKALAKKLAKSPstspevkSALDVCKESYDD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18391202  99 AVYNLASARKSIRKRDVPAMNTYLTAAVSDYGACVDGFIETQQVNAIQNAVVDLRKISSNCLALSTLI 166
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 ...
 31-166 6.96e-38

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: 126.71  E-value: 6.96e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202  31 ESRMINICSHTAYPSLCRPLVKR-----VTSPRKATHRTIQALEAKTKLALAETARFKNGN-------QAVSTCYETLGD 98
Cdd:cd15800   1 DPSVKDICKKTDYPALCLSTVKPfltkgKIDPVSALEAAIKALIAKTKQAKALAKKLAKSPstspevkSALDVCKESYDD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18391202  99 AVYNLASARKSIRKRDVPAMNTYLTAAVSDYGACVDGFIETQQVNAIQNAVVDLRKISSNCLALSTLI 166
Cdd:cd15800  81 ALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFAESGLVSPLAKINDLLKKLASNCLAIATLL 148
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 28-162 8.32e-25

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: 93.20  E-value: 8.32e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202     28 QVAESRMINICSHTAYPSLCRPLV-----KRVTSPRKATHRTIQALEAKTKLALAETARFKNGN------QAVSTCYETL 96
Cdd:smart00856   1 APTSKLIDSICKSTDYPDFCVSSLssdpsSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTkdprlkAALKDCLELY 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18391202     97 GDAVYNLASARKSIRKRDVPAMNTYLTAAVSDYGACVDGFIET--QQVNAIQNAVVDLRKISSNCLAL 162
Cdd:smart00856  81 DDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEENddKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 36-162 1.92e-12

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: 61.41  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202    36 NICSHTAYPSLC----RPLVKRVTSPR--------KATHRTIQALEAKTKLALAETARFKNGNQAVSTCYETLGDAVYNL 103
Cdd:pfam04043   5 TACKKTPYPDLCvsslSSDPASAASPPkglakaavNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYDDAVDEL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18391202   104 ASARKSIRKRDVPA--MNTYLTAAVSDYGACVDGFIET---QQVNAIQNAVVDLRKISSNCLAL 162
Cdd:pfam04043  85 NRALDALKAGDSSRddAQTWLSAALTNQDTCEDGFKEAvkgQLKSSMKSPLRNLTKLTSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 30-166 4.98e-09

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: 52.81  E-value: 4.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202    30 AESRMIN-ICSHTAYPSLCRPLVKrvTSPRKAT-------HRTIQALEAKTKLALA--ETARFKNGN----QAVSTCYET 95
Cdd:TIGR01614  27 ATQSLIKrICKKTEYPNFCISTLK--SDPSSAKadlqglaNISVSAALSNASDTLDhiSKLLLTKGDprdkSALEDCVEL 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18391202    96 LGDAVYNLASARKSIRKRDVPAMNTYLTAAVSDYGACVDGF--IETQQVNAIQNAVVDLRKISSNCLALSTLI 166
Cdd:TIGR01614 105 YSDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFeeLGGIVKSPLTKRNNNVKKLSSITLAIIKML 177
PLN02745 PLN02745
Putative pectinesterase/pectinesterase inhibitor
 36-162 5.59e-07

Putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178346 [Multi-domain]  Cd Length: 596  Bit Score: 48.31  E-value: 5.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202   36 NICSHTAYPSLCRPLVKRVT-------SPRKATHRTIQALEAKTKLALAETARFKNGNQ----AVSTCYETLGDAVYNLA 104
Cdd:PLN02745  84 TVCNATLYKQTCENTLKKGTekdpslaQPKDLLKSAIKAVNDDLDKVLKKVLSFKFENPdekdAIEDCKLLVEDAKEELK 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18391202  105 SARKSIR------KRDVPAMNTYLTAAVSDYGACVDGFIETQQVNAIQNAVVDLRKISSNCLAL 162
Cdd:PLN02745 164 ASISRINdevnklAKNVPDLNNWLSAVMSYQETCIDGFPEGKLKSEMEKTFKSSQELTSNSLAM 227
 
Name Accession Description Interval E-value
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 31-166 6.96e-38

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: 126.71  E-value: 6.96e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202  31 ESRMINICSHTAYPSLCRPLVKR-----VTSPRKATHRTIQALEAKTKLALAETARFKNGN-------QAVSTCYETLGD 98
Cdd:cd15800   1 DPSVKDICKKTDYPALCLSTVKPfltkgKIDPVSALEAAIKALIAKTKQAKALAKKLAKSPstspevkSALDVCKESYDD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18391202  99 AVYNLASARKSIRKRDVPAMNTYLTAAVSDYGACVDGFIETQQVNAIQNAVVDLRKISSNCLALSTLI 166
Cdd:cd15800  81 ALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFAESGLVSPLAKINDLLKKLASNCLAIATLL 148
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 28-162 8.32e-25

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: 93.20  E-value: 8.32e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202     28 QVAESRMINICSHTAYPSLCRPLV-----KRVTSPRKATHRTIQALEAKTKLALAETARFKNGN------QAVSTCYETL 96
Cdd:smart00856   1 APTSKLIDSICKSTDYPDFCVSSLssdpsSSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTkdprlkAALKDCLELY 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18391202     97 GDAVYNLASARKSIRKRDVPAMNTYLTAAVSDYGACVDGFIET--QQVNAIQNAVVDLRKISSNCLAL 162
Cdd:smart00856  81 DDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEENddKVKSPLTKRNDNLEKLTSNALAI 148
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 37-162 8.29e-15

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: 67.46  E-value: 8.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202  37 ICSHTAYPSLC-----RPLVKRVTSPRKATHRTIQALEAKTKLALAETARFKNGN-------QAVSTCYETLGDAVYNLA 104
Cdd:cd15798   2 ICSSTPYPDLCksslsSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKSSgsnprekAALEDCLELLDDAVDDLN 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18391202 105 SARKSIR-------KRDVPAMNTYLTAAVSDYGACVDGFIET--QQVNAIQNAVVDLRKISSNCLAL 162
Cdd:cd15798  82 RSLSELNslskdkfSERVDDVQTWLSAALTNQDTCLDGFEETgsTVKKELRASLKNVSKLTSNALAL 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 36-162 1.92e-12

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: 61.41  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202    36 NICSHTAYPSLC----RPLVKRVTSPR--------KATHRTIQALEAKTKLALAETARFKNGNQAVSTCYETLGDAVYNL 103
Cdd:pfam04043   5 TACKKTPYPDLCvsslSSDPASAASPPkglakaavNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYDDAVDEL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18391202   104 ASARKSIRKRDVPA--MNTYLTAAVSDYGACVDGFIET---QQVNAIQNAVVDLRKISSNCLAL 162
Cdd:pfam04043  85 NRALDALKAGDSSRddAQTWLSAALTNQDTCEDGFKEAvkgQLKSSMKSPLRNLTKLTSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 30-166 4.98e-09

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: 52.81  E-value: 4.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202    30 AESRMIN-ICSHTAYPSLCRPLVKrvTSPRKAT-------HRTIQALEAKTKLALA--ETARFKNGN----QAVSTCYET 95
Cdd:TIGR01614  27 ATQSLIKrICKKTEYPNFCISTLK--SDPSSAKadlqglaNISVSAALSNASDTLDhiSKLLLTKGDprdkSALEDCVEL 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18391202    96 LGDAVYNLASARKSIRKRDVPAMNTYLTAAVSDYGACVDGF--IETQQVNAIQNAVVDLRKISSNCLALSTLI 166
Cdd:TIGR01614 105 YSDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFeeLGGIVKSPLTKRNNNVKKLSSITLAIIKML 177
PLN02745 PLN02745
Putative pectinesterase/pectinesterase inhibitor
 36-162 5.59e-07

Putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178346 [Multi-domain]  Cd Length: 596  Bit Score: 48.31  E-value: 5.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202   36 NICSHTAYPSLCRPLVKRVT-------SPRKATHRTIQALEAKTKLALAETARFKNGNQ----AVSTCYETLGDAVYNLA 104
Cdd:PLN02745  84 TVCNATLYKQTCENTLKKGTekdpslaQPKDLLKSAIKAVNDDLDKVLKKVLSFKFENPdekdAIEDCKLLVEDAKEELK 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18391202  105 SARKSIR------KRDVPAMNTYLTAAVSDYGACVDGFIETQQVNAIQNAVVDLRKISSNCLAL 162
Cdd:PLN02745 164 ASISRINdevnklAKNVPDLNNWLSAVMSYQETCIDGFPEGKLKSEMEKTFKSSQELTSNSLAM 227
PMEI_like cd14859
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ...
 38-165 8.99e-06

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: 43.19  E-value: 8.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202  38 CSHTAYPSLCRPLVK-----RVTSPRKATHRTIQALEAKTKLALAETARFKNGN------QAVSTCYETLGDAVYNLASA 106
Cdd:cd14859   1 CKKTSYYKLCVSSLSsdprsSTADLKGLANIALDAALANASDTQAFIAKLLKSTkdpalkKALRDCADDYDDAVDDLEDA 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202 107 RKSIRKRDVPAMNTYLTAAVSDYGACVDGFIETQQVNA-IQNAVVDLRKISSNCLALSTL 165
Cdd:cd14859  81 INALLSGDYDDAKTHVSAALDDADTCEEAFKESSGLPSpLTTRNDDLKRLCSIALAIILL 140
PMEI-like_1 cd15801
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 38-166 3.31e-05

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: 41.55  E-value: 3.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202  38 CSHTAYPSLCrplVKRVTSPRKATHRTIQALeakTKLALAETARfkNGN-------------------QAVSTCYETLGD 98
Cdd:cd15801   6 CKKTLDPDLC---VSALSSDPESKKADLRGL---AELALKAAAE--NATatasyvsellntakdpyvqQCLEDCSENYED 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18391202  99 AVYNLASARKSIRKRDVPAMNTYLTAAVSDYGACVDGFIETQQVNAI-QNAVVDLRKISSNCLALSTLI 166
Cdd:cd15801  78 AVEQLNDSLAALDSKAYGDVKTWVTAALADAETCEDAFKEKPGDKSPlTARNGDFSKLCSIALAIIKLL 146
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 31-166 8.24e-05

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: 40.48  E-value: 8.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202  31 ESRMINICSHTAYPSLCRPLVKRVTSPRKATHRTI----------QALEAKTKLA-LAETARFKNGNQAVSTCYETLGDA 99
Cdd:cd15797   2 EELIDTICKKTENPSFCLQILNSDPRSASADLVGLaqiaidlaqsNATNTLKLIQsLIKSTTDPKLKNRYESCSKNYNDA 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18391202 100 VYNLASARKSIRKRDVPAMNTYLTAAVSDYGACVDGF-IETQQVNAIQNAVVDLRKISSNCLALSTLI 166
Cdd:cd15797  82 IDALEEAKKSLSSGDYDGLNKAASAALDAVSTCEDELsKPPKDPSPLAKYNRDVEDLCDIILVISDLL 149
PLN02468 PLN02468
putative pectinesterase/pectinesterase inhibitor
 86-166 2.26e-04

putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178087 [Multi-domain]  Cd Length: 565  Bit Score: 40.63  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202   86 NQAVSTCYETLGDAVYNLASARKSIRKRDVPA----MNTYLTAAVSDYGACVDGFIETQQVNAIQNAVVDLRKISSNCLA 161
Cdd:PLN02468 132 NAALNACQELLDLAIDNLNNSLTSSGGVSVLDnvddLRTWLSSAGTYQETCIDGLAEPNLKSFGENHLKNSTELTSNSLA 211


                 ....*
gi 18391202  162 LSTLI 166
Cdd:PLN02468 212 IITWI 216
PLN02484 PLN02484
probable pectinesterase/pectinesterase inhibitor
 38-162 2.90e-04

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178102 [Multi-domain]  Cd Length: 587  Bit Score: 40.28  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202   38 CSHTAYPSLCRPLV-----KRVTSPRKATHRTIQALEAKTKLALAETARFKNGN------QAVSTCYETLGDAVYNLASA 106
Cdd:PLN02484  80 CSKTRFPNLCVDSLldfpgSLTASESDLIHISFNMTLQHFSKALYLSSTISYVQmpprvrSAYDSCLELLDDSVDALSRA 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18391202  107 RKSI-------RKRDVpamNTYLTAAVSDYGACVDGF--IETQQV-NAIQNAVVDLRKISSNCLAL 162
Cdd:PLN02484 160 LSSVvpssgggSPQDV---VTWLSAALTNHDTCTEGFdgVNGGEVkDQMTGALKDLSELVSNCLAI 222
PLN02313 PLN02313
Pectinesterase/pectinesterase inhibitor
 36-162 3.67e-04

Pectinesterase/pectinesterase inhibitor


Pssm-ID: 177947 [Multi-domain]  Cd Length: 587  Bit Score: 40.07  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202   36 NICSHTAYPSLCRPLV-----KRVTSPRK----ATHRTIQALE----AKTKLALAETARFKNGNQAVSTCYETLGDAVYN 102
Cdd:PLN02313  64 SVCSSTLYPELCFSAVaatggKELTSQKEvieaSLNLTTKAVKhnyfAVKKLIAKRKGLTPREVTALHDCLETIDETLDE 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18391202  103 LASA---------RKSIRKRdVPAMNTYLTAAVSDYGACVDGF----IETQQVNAIQNAVVDLRKISSNCLAL 162
Cdd:PLN02313 144 LHVAvedlhqypkQKSLRKH-ADDLKTLISSAITNQGTCLDGFsyddADRKVRKALLKGQVHVEHMCSNALAM 215
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 67-162 2.72e-03

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: 36.19  E-value: 2.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18391202  67 ALEAKTKLALAETARFKNGNQAVSTCYETLGDAVYNLASARKSIRKRDVPAMNTYLTAAVSDYGACVDGFIETQ-QVNAI 145
Cdd:cd15795  49 ATKAKIEKLLKSKKYPSDLKKALRDCLSLYSDAVDSLKSALDALKSGDYGDANYDLSAATDAPVTCEDAFKEAKiVVSPL 128

                        90
                ....*....|....*..
gi 18391202 146 QNAVVDLRKISSNCLAL 162
Cdd:cd15795 129 TKENDELFQLALIALAI 145
 
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