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Conserved domains on  [gi|15223571|ref|NP_176055|]
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Plant invertase/pectin methylesterase inhibitor superfamily protein [Arabidopsis thaliana]

Protein Classification

PMEI domain-containing protein( domain architecture ID 10657211)

PMEI domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 32-170 1.19e-22

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: 88.20  E-value: 1.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571     32 APTMILIDSICVNTKNMYYCEQSIISKLGNPHAEIKTIADIAAFNAVYLITSAGNYIrDKFIPIAENPLVKNQLVLCLAT 111
Cdd:smart00856   1 APTSKLIDSICKSTDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFI-SKLLKKTKDPRLKAALKDCLEL 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15223571    112 YRAVQKLLEGAYLADRRGDYSDMRHYQSSVLGMLDNCKTDF--------DYMVRTNWGVRLMINISL 170
Cdd:smart00856  80 YDDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFeenddkvkSPLTKRNDNLEKLTSNAL 146
 
Name Accession Description Interval E-value
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 32-170 1.19e-22

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: 88.20  E-value: 1.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571     32 APTMILIDSICVNTKNMYYCEQSIISKLGNPHAEIKTIADIAAFNAVYLITSAGNYIrDKFIPIAENPLVKNQLVLCLAT 111
Cdd:smart00856   1 APTSKLIDSICKSTDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFI-SKLLKKTKDPRLKAALKDCLEL 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15223571    112 YRAVQKLLEGAYLADRRGDYSDMRHYQSSVLGMLDNCKTDF--------DYMVRTNWGVRLMINISL 170
Cdd:smart00856  80 YDDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFeenddkvkSPLTKRNDNLEKLTSNAL 146
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 37-176 3.53e-12

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: 60.90  E-value: 3.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571  37 LIDSICVNTKNMYYCEQSIISKLGNPHAEIKTIADIA-------AFNAVYLITSagnyirdkFIPIAENPLVKNQLVLCL 109
Cdd:cd15797   4 LIDTICKKTENPSFCLQILNSDPRSASADLVGLAQIAidlaqsnATNTLKLIQS--------LIKSTTDPKLKNRYESCS 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15223571 110 ATYRAVQKLLEGAYLADRRGDYSDMRHYQSSVLGMLDNCKTDF-------DYMVRTNWGVRLMINISLLATRQL 176
Cdd:cd15797  76 KNYNDAIDALEEAKKSLSSGDYDGLNKAASAALDAVSTCEDELskppkdpSPLAKYNRDVEDLCDIILVISDLL 149
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 1-176 8.39e-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: 52.42  E-value: 8.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571     1 MGFLQRISLMITSLIILHTIPSTtsisitPDAPTMILIDSICVNTKNMYYCEQSIISKLGNPHAEIKTIADIAAFNAVYL 80
Cdd:TIGR01614   1 MASSLSLLLFLLLLSLVATSSSN------SLNATQSLIKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571    81 ITSAGNYIrDKFIPIAENPLVKNQLVLCLATYRAVQKLLEGAYLADRRGDYSDMRHYQSSVLGMLDNCKTDF-------- 152
Cdd:TIGR01614  75 ASDTLDHI-SKLLLTKGDPRDKSALEDCVELYSDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFeelggivk 153

                         170       180
                  ....*....|....*....|....
gi 15223571   153 DYMVRTNWGVRLMINISLLATRQL 176
Cdd:TIGR01614 154 SPLTKRNNNVKKLSSITLAIIKML 177
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 37-170 1.12e-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: 43.30  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571    37 LIDSICVNTKNMYYCEQSIISKLGNPHAEIKTIADIAAFNAVYLITSAGNYIRDKFIPIAENPLVKNQLVLCLATYRAVQ 116
Cdd:pfam04043   2 LIKTACKKTPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYDDAV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15223571   117 KLLEGAYLADRRGDY--SDMRHYQSSVLGMLDNCKTDFDYMVRTNWGVRL---------MINISL 170
Cdd:pfam04043  82 DELNRALDALKAGDSsrDDAQTWLSAALTNQDTCEDGFKEAVKGQLKSSMksplrnltkLTSNAL 146
 
Name Accession Description Interval E-value
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 32-170 1.19e-22

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: 88.20  E-value: 1.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571     32 APTMILIDSICVNTKNMYYCEQSIISKLGNPHAEIKTIADIAAFNAVYLITSAGNYIrDKFIPIAENPLVKNQLVLCLAT 111
Cdd:smart00856   1 APTSKLIDSICKSTDYPDFCVSSLSSDPSSSATDPKDLAKIAIKVALSQATKTLSFI-SKLLKKTKDPRLKAALKDCLEL 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15223571    112 YRAVQKLLEGAYLADRRGDYSDMRHYQSSVLGMLDNCKTDF--------DYMVRTNWGVRLMINISL 170
Cdd:smart00856  80 YDDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFeenddkvkSPLTKRNDNLEKLTSNAL 146
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 37-176 3.53e-12

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: 60.90  E-value: 3.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571  37 LIDSICVNTKNMYYCEQSIISKLGNPHAEIKTIADIA-------AFNAVYLITSagnyirdkFIPIAENPLVKNQLVLCL 109
Cdd:cd15797   4 LIDTICKKTENPSFCLQILNSDPRSASADLVGLAQIAidlaqsnATNTLKLIQS--------LIKSTTDPKLKNRYESCS 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15223571 110 ATYRAVQKLLEGAYLADRRGDYSDMRHYQSSVLGMLDNCKTDF-------DYMVRTNWGVRLMINISLLATRQL 176
Cdd:cd15797  76 KNYNDAIDALEEAKKSLSSGDYDGLNKAASAALDAVSTCEDELskppkdpSPLAKYNRDVEDLCDIILVISDLL 149
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 1-176 8.39e-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: 52.42  E-value: 8.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571     1 MGFLQRISLMITSLIILHTIPSTtsisitPDAPTMILIDSICVNTKNMYYCEQSIISKLGNPHAEIKTIADIAAFNAVYL 80
Cdd:TIGR01614   1 MASSLSLLLFLLLLSLVATSSSN------SLNATQSLIKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571    81 ITSAGNYIrDKFIPIAENPLVKNQLVLCLATYRAVQKLLEGAYLADRRGDYSDMRHYQSSVLGMLDNCKTDF-------- 152
Cdd:TIGR01614  75 ASDTLDHI-SKLLLTKGDPRDKSALEDCVELYSDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFeelggivk 153

                         170       180
                  ....*....|....*....|....
gi 15223571   153 DYMVRTNWGVRLMINISLLATRQL 176
Cdd:TIGR01614 154 SPLTKRNNNVKKLSSITLAIIKML 177
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 37-170 1.12e-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: 43.30  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571    37 LIDSICVNTKNMYYCEQSIISKLGNPHAEIKTIADIAAFNAVYLITSAGNYIRDKFIPIAENPLVKNQLVLCLATYRAVQ 116
Cdd:pfam04043   2 LIKTACKKTPYPDLCVSSLSSDPASAASPPKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDCLELYDDAV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15223571   117 KLLEGAYLADRRGDY--SDMRHYQSSVLGMLDNCKTDFDYMVRTNWGVRL---------MINISL 170
Cdd:pfam04043  82 DELNRALDALKAGDSsrDDAQTWLSAALTNQDTCEDGFKEAVKGQLKSSMksplrnltkLTSNAL 146
PMEI_like cd14859
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ...
 42-152 6.75e-04

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: 38.18  E-value: 6.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15223571  42 CVNTKNMYYCEQSIISKLGNPHAEIKTIADIAAFNAVYLITSAGNYIrDKFIPIAENPLVKNQLVLCLATYRAVQKLLEG 121
Cdd:cd14859   1 CKKTSYYKLCVSSLSSDPRSSTADLKGLANIALDAALANASDTQAFI-AKLLKSTKDPALKKALRDCADDYDDAVDDLED 79

                        90       100       110
                ....*....|....*....|....*....|.
gi 15223571 122 AYLADRRGDYSDMRHYQSSVLGMLDNCKTDF 152
Cdd:cd14859  80 AINALLSGDYDDAKTHVSAALDDADTCEEAF 110
 
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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