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Conserved domains on  [gi|11127599|dbj|BAB17684|]
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DC 1.2 homolog, partial [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 ...
 2-151 2.33e-40

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: 132.95  E-value: 2.33e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   2 LCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKlc 81
Cdd:cd15798  11 LCKSSLSSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKSSGSNPREKAALEDCLELLDDAVDDLNRSLSELN-- 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599  82 gsAKDQDQFAYHMSNAQTWTSAALTDENTCSDGFSGrvMDGRIKNSVRARIMNVGHETSNALSLINAFAK 151
Cdd:cd15798  89 --SLSKDKFSERVDDVQTWLSAALTNQDTCLDGFEE--TGSTVKKELRASLKNVSKLTSNALALVNALAK 154
 
Name Accession Description Interval E-value
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 2-151 2.33e-40

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: 132.95  E-value: 2.33e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   2 LCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKlc 81
Cdd:cd15798  11 LCKSSLSSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKSSGSNPREKAALEDCLELLDDAVDDLNRSLSELN-- 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599  82 gsAKDQDQFAYHMSNAQTWTSAALTDENTCSDGFSGrvMDGRIKNSVRARIMNVGHETSNALSLINAFAK 151
Cdd:cd15798  89 --SLSKDKFSERVDDVQTWLSAALTNQDTCLDGFEE--TGSTVKKELRASLKNVSKLTSNALALVNALAK 154
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 1-145 3.01e-36

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: 122.09  E-value: 3.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599      1 ALCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRmKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKL 80
Cdd:smart00856  18 DFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLK-KTKDPRLKAALKDCLELYDDAVDSLEKALEELKS 96

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11127599     81 CgsakdqdqfayHMSNAQTWTSAALTDENTCSDGFSGrvMDGRIKNSVRARIMNVGHETSNALSL 145
Cdd:smart00856  97 G-----------DYDDVATWLSAALTDQDTCLDGFEE--NDDKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 1-145 8.56e-29

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: 103.01  E-value: 8.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599     1 ALCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKl 80
Cdd:pfam04043  14 DLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYDDAVDELNRALDALK- 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11127599    81 cgsakdqdQFAYHMSNAQTWTSAALTDENTCSDGFSGRVmDGRIKNSVRARIMNVGHETSNALSL 145
Cdd:pfam04043  93 --------AGDSSRDDAQTWLSAALTNQDTCEDGFKEAV-KGQLKSSMKSPLRNLTKLTSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 2-147 1.47e-26

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: 98.26  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599     2 LCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGlKKREVEAIKDCVEEMNDTVDRLTKSVQELKLC 81
Cdd:TIGR01614  44 FCISTLKSDPSSAKADLQGLANISVSAALSNASDTLDHISKLLLTKG-DPRDKSALEDCVELYSDAVDALDKALASLKSK 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11127599    82 gsakdqdqfayHMSNAQTWTSAALTDENTCSDGFSGRvmDGRIKNSVRARIMNVGHETSNALSLIN 147
Cdd:TIGR01614 123 -----------DYSDAETWLSSALTDPSTCEDGFEEL--GGIVKSPLTKRNNNVKKLSSITLAIIK 175
PLN02313 PLN02313
Pectinesterase/pectinesterase inhibitor
 2-152 4.48e-17

Pectinesterase/pectinesterase inhibitor


Pssm-ID: 177947 [Multi-domain]  Cd Length: 587  Bit Score: 77.05  E-value: 4.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599    2 LCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRL-TRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKL 80
Cdd:PLN02313  74 LCFSAVAATGGKELTSQKEVIEASLNLTTKAVKHNYFAVKKLiAKRKGLTPREVTALHDCLETIDETLDELHVAVEDLHQ 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11127599   81 CGSAKDQDQfayHMSNAQTWTSAALTDENTCSDGFSGRVMDGRIKNSVRARIMNVGHETSNALSLINAFAKT 152
Cdd:PLN02313 154 YPKQKSLRK---HADDLKTLISSAITNQGTCLDGFSYDDADRKVRKALLKGQVHVEHMCSNALAMIKNMTET 222
 
Name Accession Description Interval E-value
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 2-151 2.33e-40

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: 132.95  E-value: 2.33e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   2 LCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKlc 81
Cdd:cd15798  11 LCKSSLSSYASSSSTDPKELAKAALNAALDEAKKALALLSSLLKSSGSNPREKAALEDCLELLDDAVDDLNRSLSELN-- 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599  82 gsAKDQDQFAYHMSNAQTWTSAALTDENTCSDGFSGrvMDGRIKNSVRARIMNVGHETSNALSLINAFAK 151
Cdd:cd15798  89 --SLSKDKFSERVDDVQTWLSAALTNQDTCLDGFEE--TGSTVKKELRASLKNVSKLTSNALALVNALAK 154
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 1-145 3.01e-36

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: 122.09  E-value: 3.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599      1 ALCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRmKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKL 80
Cdd:smart00856  18 DFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFISKLLK-KTKDPRLKAALKDCLELYDDAVDSLEKALEELKS 96

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11127599     81 CgsakdqdqfayHMSNAQTWTSAALTDENTCSDGFSGrvMDGRIKNSVRARIMNVGHETSNALSL 145
Cdd:smart00856  97 G-----------DYDDVATWLSAALTDQDTCLDGFEE--NDDKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 1-145 8.56e-29

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: 103.01  E-value: 8.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599     1 ALCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKl 80
Cdd:pfam04043  14 DLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYDDAVDELNRALDALK- 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11127599    81 cgsakdqdQFAYHMSNAQTWTSAALTDENTCSDGFSGRVmDGRIKNSVRARIMNVGHETSNALSL 145
Cdd:pfam04043  93 --------AGDSSRDDAQTWLSAALTNQDTCEDGFKEAV-KGQLKSSMKSPLRNLTKLTSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 2-147 1.47e-26

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: 98.26  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599     2 LCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGlKKREVEAIKDCVEEMNDTVDRLTKSVQELKLC 81
Cdd:TIGR01614  44 FCISTLKSDPSSAKADLQGLANISVSAALSNASDTLDHISKLLLTKG-DPRDKSALEDCVELYSDAVDALDKALASLKSK 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11127599    82 gsakdqdqfayHMSNAQTWTSAALTDENTCSDGFSGRvmDGRIKNSVRARIMNVGHETSNALSLIN 147
Cdd:TIGR01614 123 -----------DYSDAETWLSSALTDPSTCEDGFEEL--GGIVKSPLTKRNNNVKKLSSITLAIIK 175
PLN02313 PLN02313
Pectinesterase/pectinesterase inhibitor
 2-152 4.48e-17

Pectinesterase/pectinesterase inhibitor


Pssm-ID: 177947 [Multi-domain]  Cd Length: 587  Bit Score: 77.05  E-value: 4.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599    2 LCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRL-TRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKL 80
Cdd:PLN02313  74 LCFSAVAATGGKELTSQKEVIEASLNLTTKAVKHNYFAVKKLiAKRKGLTPREVTALHDCLETIDETLDELHVAVEDLHQ 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11127599   81 CGSAKDQDQfayHMSNAQTWTSAALTDENTCSDGFSGRVMDGRIKNSVRARIMNVGHETSNALSLINAFAKT 152
Cdd:PLN02313 154 YPKQKSLRK---HADDLKTLISSAITNQGTCLDGFSYDDADRKVRKALLKGQVHVEHMCSNALAMIKNMTET 222
PMEI_like cd14859
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ...
 1-147 1.41e-15

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: 69.00  E-value: 1.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   1 ALCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGLkKREVEAIKDCVEEMNDTVDRLTKSVQELKl 80
Cdd:cd14859   8 KLCVSSLSSDPRSSTADLKGLANIALDAALANASDTQAFIAKLLKSTKD-PALKKALRDCADDYDDAVDDLEDAINALL- 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11127599  81 cgsakdqdqfAYHMSNAQTWTSAALTDENTCSDGFSGRvmdGRIKNSVRARIMNVGHETSNALSLIN 147
Cdd:cd14859  86 ----------SGDYDDAKTHVSAALDDADTCEEAFKES---SGLPSPLTTRNDDLKRLCSIALAIIL 139
PLN02484 PLN02484
probable pectinesterase/pectinesterase inhibitor
 1-148 2.26e-15

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178102 [Multi-domain]  Cd Length: 587  Bit Score: 71.86  E-value: 2.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599    1 ALCVHSLSVYANDIQTSPKRLAETAIAVTLSRAqSTKLFVSRLTRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKL 80
Cdd:PLN02484  87 NLCVDSLLDFPGSLTASESDLIHISFNMTLQHF-SKALYLSSTISYVQMPPRVRSAYDSCLELLDDSVDALSRALSSVVP 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11127599   81 C-GSAKDQDqfayhmsnAQTWTSAALTDENTCSDGFSGrVMDGRIKNSVRARIMNVGHETSNALSLINA 148
Cdd:PLN02484 166 SsGGGSPQD--------VVTWLSAALTNHDTCTEGFDG-VNGGEVKDQMTGALKDLSELVSNCLAIFSA 225
PMEI-like_4 cd15799
plant invertase/pectin methylesterase inhibitor domain-containing protein; This subfamily ...
 1-148 5.11e-13

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: 62.43  E-value: 5.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   1 ALCVHSLS-VYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLtRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELk 79
Cdd:cd15799  13 IPSVSSSAnALSAQCLKVPLDVFLAALKTTVDRIQSALSMVSKL-RNGSDDPRLSNALSDCLELLDFSADRLSWSLSAL- 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11127599  80 lcgsakdQDQFAYHMSNAQTWTSAALTDENTCSDGFSGRvmdGRIKNSVRARIMNVGHETSNALSLINA 148
Cdd:cd15799  91 -------QNPKGDSGSDARTWLSAALTNHDTCLDGLEET---GVVKSLVAAALSNLTSLLREALAMVAS 149
PMEI-like_1 cd15801
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 2-148 2.18e-12

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: 60.81  E-value: 2.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   2 LCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLtrMKGLKKREV-EAIKDCVEEMNDTVDRLTKSVQELkl 80
Cdd:cd15801  14 LCVSALSSDPESKKADLRGLAELALKAAAENATATASYVSEL--LNTAKDPYVqQCLEDCSENYEDAVEQLNDSLAAL-- 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11127599  81 cgSAKDQDQfayhmsnAQTWTSAALTDENTCSDGFSgrvMDGRIKNSVRARIMNVGHETSNALSLINA 148
Cdd:cd15801  90 --DSKAYGD-------VKTWVTAALADAETCEDAFK---EKPGDKSPLTARNGDFSKLCSIALAIIKL 145
PLN02506 PLN02506
putative pectinesterase/pectinesterase inhibitor
 17-145 6.56e-11

putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 215280 [Multi-domain]  Cd Length: 537  Bit Score: 59.18  E-value: 6.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   17 SPKRLAETAIAVTLSRAqstKLFVSRLTRMKGL--KKREVEAIKDCVEEMNDTVDRLTKSVQELKlcgSAKDQDQFAYHM 94
Cdd:PLN02506  65 TPHSVLSAALKATLDEA---RLAIDMITKFNALsiSYREQVAIEDCKELLDFSVSELAWSLLEMN---KIRAGHDNVAYE 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 11127599   95 SNAQTWTSAALTDENTCSDGFSGrvMDGRIKNSVRARIMNVGHETSNALSL 145
Cdd:PLN02506 139 GNLKAWLSAALSNQDTCLEGFEG--TDRHLENFIKGSLKQVTQLISNVLAM 187
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 1-148 1.81e-09

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: 53.13  E-value: 1.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   1 ALCVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKl 80
Cdd:cd15800  15 ALCLSTVKPFLTKGKIDPVSALEAAIKALIAKTKQAKALAKKLAKSPSTSPEVKSALDVCKESYDDALDNLKKALKAIK- 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11127599  81 cgsAKDQDQFayhMSNaqtwTSAALTDENTCSDGFSgrvmDGRIKNSVRARIMNVGHETSNALSLINA 148
Cdd:cd15800  94 ---SRDIGTL---NSM----LSAAITDYSTCDDAFA----ESGLVSPLAKINDLLKKLASNCLAIATL 147
PLN02468 PLN02468
putative pectinesterase/pectinesterase inhibitor
 3-151 1.97e-09

putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178087 [Multi-domain]  Cd Length: 565  Bit Score: 54.88  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599    3 CVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGLK-KREVEAIKDCVEEMNDTVDRLTKSVQELKLC 81
Cdd:PLN02468  80 CYETLAPAPKASQLQPEELFKYAVKVAINELSKASQAFSNSEGFLGVKdNMTNAALNACQELLDLAIDNLNNSLTSSGGV 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   82 GSAKDQDQFayhmsnaQTWTSAALTDENTCSDGFSgrvmDGRIKNSVRARIMNVGHETSNALSLINAFAK 151
Cdd:PLN02468 160 SVLDNVDDL-------RTWLSSAGTYQETCIDGLA----EPNLKSFGENHLKNSTELTSNSLAIITWIGK 218
PLN02933 PLN02933
Probable pectinesterase/pectinesterase inhibitor
 16-146 3.78e-08

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178521 [Multi-domain]  Cd Length: 530  Bit Score: 51.16  E-value: 3.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   16 TSPKRLAETAIA---VTLSRAQ-STKLFVSRLTRM-KGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKlcgsakdqdQF 90
Cdd:PLN02933  46 TETKTIPELIIAdlnLTILKVNlASSNFSDLQTRLgPNLTHRERCAFEDCLGLLDDTISDLTTAISKLR---------SS 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11127599   91 AYHMSNAQTWTSAALTDENTCSDGFSGRVMDGR------IKNSVRARIMNVGHETSNALSLI 146
Cdd:PLN02933 117 SPEFNDVSMLLSNAMTNQDTCLDGFSTSDNENNndmtyeLPENLKESILDISNHLSNSLAML 178
PLN02745 PLN02745
Putative pectinesterase/pectinesterase inhibitor
 3-150 4.14e-08

Putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178346 [Multi-domain]  Cd Length: 596  Bit Score: 51.01  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599    3 CVHSLS--VYANDIQTSPKRLAETAIAVTlsrAQSTKLFVSRLTRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELkl 80
Cdd:PLN02745  95 CENTLKkgTEKDPSLAQPKDLLKSAIKAV---NDDLDKVLKKVLSFKFENPDEKDAIEDCKLLVEDAKEELKASISRI-- 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   81 cgsAKDQDQFAYHMSNAQTWTSAALTDENTCSDGFSgrvmDGRIKNSVRARIMNVGHETSNALSLINAFA 150
Cdd:PLN02745 170 ---NDEVNKLAKNVPDLNNWLSAVMSYQETCIDGFP----EGKLKSEMEKTFKSSQELTSNSLAMVSSLT 232
PLN02301 PLN02301
pectinesterase/pectinesterase inhibitor
 3-117 9.56e-08

pectinesterase/pectinesterase inhibitor


Pssm-ID: 215170 [Multi-domain]  Cd Length: 548  Bit Score: 49.88  E-value: 9.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599    3 CVHSLSVYANDIQTSPKR--LAETAIAVTLSRAQSTKLFVSRLTRMKGlKKREVEAIKDCVEEMNDTVDRLTKSVQELKL 80
Cdd:PLN02301  66 CQAMVSEIATNTVMKLNRvdLLQVLLKESTPHLQNTIEMASEIRIRIN-DPRDKAALADCVELMDLSKDRIKDSVEALGN 144

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 11127599   81 CGSAKDqdqfayhmSNAQTWTSAALTDENTCSDGFSG 117
Cdd:PLN02301 145 VTSKSH--------ADAHTWLSSVLTNHVTCLDGING 173
PLN02217 PLN02217
probable pectinesterase/pectinesterase inhibitor
 16-147 1.59e-07

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215130 [Multi-domain]  Cd Length: 670  Bit Score: 49.32  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   16 TSPKRLAETAIAVTLSRAQSTklfVSRLTRMKGLKK--REVEAIKDCVEEMNDTVDRLTKSVQELklcgsakdqDQFAYH 93
Cdd:PLN02217  81 SDPLELVKTAFNATMKQISDV---AKKSQTMIELQKdpRTKMALDQCKELMDYAIGELSKSFEEL---------GKFEFH 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 11127599   94 -----MSNAQTWTSAALTDENTCSDGFSGrvMDGRIKNSVRARIMNVGHETSNALSLIN 147
Cdd:PLN02217 149 kvdeaLIKLRIWLSATISHEQTCLDGFQG--TQGNAGETIKKALKTAVQLTHNGLAMVS 205
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 3-118 2.21e-07

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: 47.36  E-value: 2.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   3 CVHSLSvyaNDIQTSPKR----LAETAIAVTLSRAQSTKLFVSRLTRMKGLKKREVEAIKDCVEEMNDTVDRLTKSVQEL 78
Cdd:cd15795  16 CVSSLQ---SDPRSRTAAdlkgLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKALRDCLSLYSDAVDSLKSALDAL 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 11127599  79 KlcgsakdqdqfAYHMSNAQTWTSAALTDENTCSDGFSGR 118
Cdd:cd15795  93 K-----------SGDYGDANYDLSAATDAPVTCEDAFKEA 121
PLN02314 PLN02314
pectinesterase
 3-146 6.01e-07

pectinesterase


Pssm-ID: 215179 [Multi-domain]  Cd Length: 586  Bit Score: 47.51  E-value: 6.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599    3 CVHSLSVYANDIQTSPKRLAETAIAVTLSRAQSTKLFVSRLTRmKGLKKREVEAIKDCVEEMNDTVDRLTKSVQELKLCG 82
Cdd:PLN02314  86 CISSISSLPTSNTTDPETLFKLSLKVAIDELSKLSDLPQKLIN-ETNDERLKSALRVCETLFDDAIDRLNDSISSMQVGE 164

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11127599   83 saKDQDQFAYHMSNAQTWTSAALTDENTCSDGF----SGRVMDGRIKNSVRARIMNVGHETSNALSLI 146
Cdd:PLN02314 165 --GEKILSSSKIDDLKTWLSATITDQETCIDALqelsQNKYANSTLTNEVKTAMSNSTEFTSNSLAIV 230
PLN02170 PLN02170
probable pectinesterase/pectinesterase inhibitor
 15-116 1.49e-05

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215114 [Multi-domain]  Cd Length: 529  Bit Score: 43.43  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   15 QTSPKRLAETAIAVTLSRAQSTKLFVSRLTRMKGLKKREVEA-----IKDCVEEMNDTVDRLTKSVQELKlcgsaKDQDQ 89
Cdd:PLN02170  55 RSSPSSSSKQGFLSSVQESMNHALFARSLAFNLTLSHRTVQThtfdpVNDCLELLDDTLDMLSRIVVIKH-----ADHDE 129

                         90       100
                 ....*....|....*....|....*..
gi 11127599   90 fayhmSNAQTWTSAALTDENTCSDGFS 116
Cdd:PLN02170 130 -----EDVHTWLSAALTNQETCEQSLQ 151
PLN02201 PLN02201
probable pectinesterase/pectinesterase inhibitor
 40-147 1.83e-05

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 177852 [Multi-domain]  Cd Length: 520  Bit Score: 43.33  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   40 VSRLTRMKGlKKREVEAIKDCVEEMNDTVDRLTKSVQELKlcgSAKDQDQFAYHM-SNAQTWTSAALTDENTCSDGFSGr 118
Cdd:PLN02201  59 VSQFDKVFG-DSRLSNAISDCLDLLDFAAEELSWSISASQ---NPNGKDNSTGDVgSDLRTWLSAALSNQDTCIEGFDG- 133

                         90       100
                 ....*....|....*....|....*....
gi 11127599  119 vMDGRIKNSVRARIMNVGHETSNALSLIN 147
Cdd:PLN02201 134 -TNGIVKKLVAGSLSQVGSTVRELLTMVH 161
PLN02713 PLN02713
Probable pectinesterase/pectinesterase inhibitor
 25-145 2.29e-05

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215383 [Multi-domain]  Cd Length: 566  Bit Score: 43.24  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   25 AIAVTLSRAQSTKLFVSRLTRMKG--LKKREVEAIKDCVEEMNDTVDRLTKSVQELKlcgSAKDQDQFaYHMSNAQTWTS 102
Cdd:PLN02713  67 SVRKSLSQSRKFLSLVDRYLKRNStlLSKSAIRALEDCQFLAGLNIDFLLSSFETVN---SSSKTLSD-PQADDVQTLLS 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 11127599  103 AALTDENTCSDGFSGRVMDGRIKNSVRARIMNVGHETSNALSL 145
Cdd:PLN02713 143 AILTNQQTCLDGLQAASSAWSVRNGLAVPLSNDTKLYSVSLAL 185
PLN02416 PLN02416
probable pectinesterase/pectinesterase inhibitor
 3-146 1.73e-04

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178037 [Multi-domain]  Cd Length: 541  Bit Score: 40.68  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599    3 CVHSLSVYANdIQTSPKRLaeTAIAVTLSRAQSTKLFVSRLTRMKGLKKREVE----AIKDCVEEMNDTVDRLTKSVQEL 78
Cdd:PLN02416  54 CFDSLKLSIS-INISPNIL--NFLLQTLQTAISEAGKLTNLLSGAGQSSNIIEkqrgTIQDCKELHQITVSSLKRSVSRI 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11127599   79 KLCGSAKdqdqfayhMSNAQTWTSAALTDENTCSDGFSGrvMDGRIKNSVRARIMNVGHETSNALSLI 146
Cdd:PLN02416 131 QAGDSRK--------LADARAYLSAALTNKNTCLEGLDS--ASGPLKPKLVNSFTSTYKHVSNSLSML 188
PLN02995 PLN02995
Probable pectinesterase/pectinesterase inhibitor
 49-149 2.76e-04

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178574 [Multi-domain]  Cd Length: 539  Bit Score: 40.05  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   49 LKKREVeaIKDCVEEMNDTVDRLTKSVQELK-LCGSAKDQDQFayhmsNAQTWTSAALTDENTCSDGFSgrvmDGRIKNS 127
Cdd:PLN02995  98 FKKQAV--LADCIDLYGDTIMQLNRTLQGVSpKAGAAKRCTDF-----DAQTWLSTALTNTETCRRGSS----DLNVSDF 166

                         90       100
                 ....*....|....*....|....
gi 11127599  128 VRARIMN--VGHETSNALSLINAF 149
Cdd:PLN02995 167 ITPIVSNtkISHLISNCLAVNGAL 190
PLN02698 PLN02698
Probable pectinesterase/pectinesterase inhibitor
 60-147 1.77e-03

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178301 [Multi-domain]  Cd Length: 497  Bit Score: 37.61  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11127599   60 CVEEMNDTVDRLTKSVQELKlcGSAKDQDQfayhmsNAQTWTSAALTDENTCSDGF--SGRVMDGRIKNSVRARIMNVGH 137
Cdd:PLN02698  93 CERLMKMSLKRLRQSLLALK--GSSRKNKH------DIQTWLSAALTFQQACKDSIvdSTGYSGTSAISQISQKMDHLSR 164

                         90
                 ....*....|
gi 11127599  138 ETSNALSLIN 147
Cdd:PLN02698 165 LVSNSLALVN 174
 
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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