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Conserved domains on  [gi|15237979|ref|NP_199505|]
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Plant invertase/pectin methylesterase inhibitor superfamily protein [Arabidopsis thaliana]

Protein Classification

PMEI-Pla_a_1_like domain-containing protein( domain architecture ID 10204980)

PMEI-Pla_a_1_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 28-174 1.63e-59

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: 182.18  E-value: 1.63e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979  28 CKKATATSPKFKYNLCVTSLETNPQAKTAKDLAGLVMASTKNAVTKATTLKGTVDKIIKGKKVNKMTAMPLRDCLQLYTD 107
Cdd:cd15795   1 CKKAAAGDPNVDYDFCVSSLQSDPRSRTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKALRDCLSLYSD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15237979 108 AIGSLNEALAGVKSRNYPTVKTVLSAAMDTPSTCETGFKERKA-PSPVTKENDNLYQMILIPLAFTNM 174
Cdd:cd15795  81 AVDSLKSALDALKSGDYGDANYDLSAATDAPVTCEDAFKEAKIvVSPLTKENDELFQLALIALAITSM 148
 
Name Accession Description Interval E-value
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 28-174 1.63e-59

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: 182.18  E-value: 1.63e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979  28 CKKATATSPKFKYNLCVTSLETNPQAKTAKDLAGLVMASTKNAVTKATTLKGTVDKIIKGKKVNKMTAMPLRDCLQLYTD 107
Cdd:cd15795   1 CKKAAAGDPNVDYDFCVSSLQSDPRSRTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKALRDCLSLYSD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15237979 108 AIGSLNEALAGVKSRNYPTVKTVLSAAMDTPSTCETGFKERKA-PSPVTKENDNLYQMILIPLAFTNM 174
Cdd:cd15795  81 AVDSLKSALDALKSGDYGDANYDLSAATDAPVTCEDAFKEAKIvVSPLTKENDELFQLALIALAITSM 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 1-175 3.21e-34

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: 118.68  E-value: 3.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979     1 MKFLLYLVTFFVL--------SNGLANGQTLIRNSCKKATatspkfKYNLCVTSLETNPQAKTAkDLAGLVMASTKNAVT 72
Cdd:TIGR01614   1 MASSLSLLLFLLLlslvatssSNSLNATQSLIKRICKKTE------YPNFCISTLKSDPSSAKA-DLQGLANISVSAALS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979    73 KATTLKGTVdKIIKGKKVNKMTAMPLRDCLQLYTDAIGSLNEALAGVKSRNYPTVKTVLSAAMDTPSTCETGFKERKA-- 150
Cdd:TIGR01614  74 NASDTLDHI-SKLLLTKGDPRDKSALEDCVELYSDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFEELGGiv 152

                         170       180
                  ....*....|....*....|....*
gi 15237979   151 PSPVTKENDNLYQMILIPLAFTNML 175
Cdd:TIGR01614 153 KSPLTKRNNNVKKLSSITLAIIKML 177
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 18-171 1.17e-33

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: 116.32  E-value: 1.17e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979     18 ANGQTLIRNSCKKATatspkfKYNLCVTSLETNPQAKTAkDLAGLVMASTKNAVTKATTLKGTVDKIIKgKKVNKMTAMP 97
Cdd:smart00856   1 APTSKLIDSICKSTD------YPDFCVSSLSSDPSSSAT-DPKDLAKIAIKVALSQATKTLSFISKLLK-KTKDPRLKAA 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237979     98 LRDCLQLYTDAIGSLNEALAGVKSRNYPTVKTVLSAAMDTPSTCETGFKER--KAPSPVTKENDNLYQMILIPLAF 171
Cdd:smart00856  73 LKDCLELYDDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEENddKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 22-170 3.29e-26

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: 97.23  E-value: 3.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979    22 TLIRNSCKKATAtspkfkYNLCVTSLETNPQAKTAKdLAGLVMASTKNAVTKATTLKGTVDKIIKGKKVNKMTAMPLRDC 101
Cdd:pfam04043   1 SLIKTACKKTPY------PDLCVSSLSSDPASAASP-PKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDC 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237979   102 LQLYTDAIGSLNEALAGVKSRNYP--TVKTVLSAAMDTPSTCETGFKERKAP---SPVTKENDNLYQMILIPLA 170
Cdd:pfam04043  74 LELYDDAVDELNRALDALKAGDSSrdDAQTWLSAALTNQDTCEDGFKEAVKGqlkSSMKSPLRNLTKLTSNALA 147
PLN02484 PLN02484
probable pectinesterase/pectinesterase inhibitor
 41-147 1.10e-05

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178102 [Multi-domain]  Cd Length: 587  Bit Score: 44.52  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979   41 NLCVTSLETNPQAKTA--KDLAGLVMASTKNAVTKATTLKGTVdkiikgkkvnKMTAMPLR------DCLQLYTDAIGSL 112
Cdd:PLN02484  87 NLCVDSLLDFPGSLTAseSDLIHISFNMTLQHFSKALYLSSTI----------SYVQMPPRvrsaydSCLELLDDSVDAL 156

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15237979  113 NEALAGVKS----RNYPTVKTVLSAAMDTPSTCETGFKE 147
Cdd:PLN02484 157 SRALSSVVPssggGSPQDVVTWLSAALTNHDTCTEGFDG 195
 
Name Accession Description Interval E-value
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 28-174 1.63e-59

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: 182.18  E-value: 1.63e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979  28 CKKATATSPKFKYNLCVTSLETNPQAKTAKDLAGLVMASTKNAVTKATTLKGTVDKIIKGKKVNKMTAMPLRDCLQLYTD 107
Cdd:cd15795   1 CKKAAAGDPNVDYDFCVSSLQSDPRSRTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKALRDCLSLYSD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15237979 108 AIGSLNEALAGVKSRNYPTVKTVLSAAMDTPSTCETGFKERKA-PSPVTKENDNLYQMILIPLAFTNM 174
Cdd:cd15795  81 AVDSLKSALDALKSGDYGDANYDLSAATDAPVTCEDAFKEAKIvVSPLTKENDELFQLALIALAITSM 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 1-175 3.21e-34

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: 118.68  E-value: 3.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979     1 MKFLLYLVTFFVL--------SNGLANGQTLIRNSCKKATatspkfKYNLCVTSLETNPQAKTAkDLAGLVMASTKNAVT 72
Cdd:TIGR01614   1 MASSLSLLLFLLLlslvatssSNSLNATQSLIKRICKKTE------YPNFCISTLKSDPSSAKA-DLQGLANISVSAALS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979    73 KATTLKGTVdKIIKGKKVNKMTAMPLRDCLQLYTDAIGSLNEALAGVKSRNYPTVKTVLSAAMDTPSTCETGFKERKA-- 150
Cdd:TIGR01614  74 NASDTLDHI-SKLLLTKGDPRDKSALEDCVELYSDAVDALDKALASLKSKDYSDAETWLSSALTDPSTCEDGFEELGGiv 152

                         170       180
                  ....*....|....*....|....*
gi 15237979   151 PSPVTKENDNLYQMILIPLAFTNML 175
Cdd:TIGR01614 153 KSPLTKRNNNVKKLSSITLAIIKML 177
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 18-171 1.17e-33

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: 116.32  E-value: 1.17e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979     18 ANGQTLIRNSCKKATatspkfKYNLCVTSLETNPQAKTAkDLAGLVMASTKNAVTKATTLKGTVDKIIKgKKVNKMTAMP 97
Cdd:smart00856   1 APTSKLIDSICKSTD------YPDFCVSSLSSDPSSSAT-DPKDLAKIAIKVALSQATKTLSFISKLLK-KTKDPRLKAA 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237979     98 LRDCLQLYTDAIGSLNEALAGVKSRNYPTVKTVLSAAMDTPSTCETGFKER--KAPSPVTKENDNLYQMILIPLAF 171
Cdd:smart00856  73 LKDCLELYDDAVDSLEKALEELKSGDYDDVATWLSAALTDQDTCLDGFEENddKVKSPLTKRNDNLEKLTSNALAI 148
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 22-170 3.29e-26

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: 97.23  E-value: 3.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979    22 TLIRNSCKKATAtspkfkYNLCVTSLETNPQAKTAKdLAGLVMASTKNAVTKATTLKGTVDKIIKGKKVNKMTAMPLRDC 101
Cdd:pfam04043   1 SLIKTACKKTPY------PDLCVSSLSSDPASAASP-PKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDC 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237979   102 LQLYTDAIGSLNEALAGVKSRNYP--TVKTVLSAAMDTPSTCETGFKERKAP---SPVTKENDNLYQMILIPLA 170
Cdd:pfam04043  74 LELYDDAVDELNRALDALKAGDSSrdDAQTWLSAALTNQDTCEDGFKEAVKGqlkSSMKSPLRNLTKLTSNALA 147
PMEI_like cd14859
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ...
 40-174 6.37e-23

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: 88.64  E-value: 6.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979  40 YNLCVTSLETNPQAKTAkDLAGLVMASTKNAVTKATTLKGTVDKIIKGKKvNKMTAMPLRDCLQLYTDAIGSLNEALAGV 119
Cdd:cd14859   7 YKLCVSSLSSDPRSSTA-DLKGLANIALDAALANASDTQAFIAKLLKSTK-DPALKKALRDCADDYDDAVDDLEDAINAL 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15237979 120 KSRNYPTVKTVLSAAMDTPSTCETGFKER-KAPSPVTKENDNLYQMILIPLAFTNM 174
Cdd:cd14859  85 LSGDYDDAKTHVSAALDDADTCEEAFKESsGLPSPLTTRNDDLKRLCSIALAIILL 140
PMEI-like_1 cd15801
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 23-175 4.25e-22

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: 86.62  E-value: 4.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979  23 LIRNSCKKatatspKFKYNLCVTSLETNPQAKTAkDLAGLVMASTKNAVTKATTLKGTVDKIIKGKKvNKMTAMPLRDCL 102
Cdd:cd15801   1 LIEEACKK------TLDPDLCVSALSSDPESKKA-DLRGLAELALKAAAENATATASYVSELLNTAK-DPYVQQCLEDCS 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237979 103 QLYTDAIGSLNEALAGVKSRNYPTVKTVLSAAMDTPSTCETGFKERKA-PSPVTKENDNLYQMILIPLAFTNML 175
Cdd:cd15801  73 ENYEDAVEQLNDSLAALDSKAYGDVKTWVTAALADAETCEDAFKEKPGdKSPLTARNGDFSKLCSIALAIIKLL 146
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 21-175 6.79e-20

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: 80.87  E-value: 6.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979  21 QTLIRNSCKKATatSPKfkynLCVTSLeTNPQAKTAKDLAGLVMASTKNAVTKATTLKGTVDKIIKGKKVNKMTAMPLRD 100
Cdd:cd15800   1 DPSVKDICKKTD--YPA----LCLSTV-KPFLTKGKIDPVSALEAAIKALIAKTKQAKALAKKLAKSPSTSPEVKSALDV 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15237979 101 CLQLYTDAIGSLNEALAGVKSRNYPTVKTVLSAAMDTPSTCETGFKERKAPSPVTKENDNLYQMILIPLAFTNML 175
Cdd:cd15800  74 CKESYDDALDNLKKALKAIKSRDIGTLNSMLSAAITDYSTCDDAFAESGLVSPLAKINDLLKKLASNCLAIATLL 148
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 23-175 1.76e-19

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: 79.77  E-value: 1.76e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979  23 LIRNSCKKAtatspkFKYNLCVTSLETNPQAKTA--KDLAGLVMASTKNAVTKATTLkgtVDKIIKGKKvNKMTAMPLRD 100
Cdd:cd15797   4 LIDTICKKT------ENPSFCLQILNSDPRSASAdlVGLAQIAIDLAQSNATNTLKL---IQSLIKSTT-DPKLKNRYES 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237979 101 CLQLYTDAIGSLNEALAGVKSRNYPTVKTVLSAAMDTPSTCETGFK-ERKAPSPVTKENDNLYQMILIPLAFTNML 175
Cdd:cd15797  74 CSKNYNDAIDALEEAKKSLSSGDYDGLNKAASAALDAVSTCEDELSkPPKDPSPLAKYNRDVEDLCDIILVISDLL 149
CIF_like cd15796
Cell-wall inhibitor of beta fructosidase and similar proteins; Cell-wall invertases (CWIs) are ...
 23-175 5.55e-16

Cell-wall inhibitor of beta fructosidase and similar proteins; Cell-wall invertases (CWIs) are secreted apoplastic enzymes belonging to the glycoside hydrolase family 32 (EC 3.2.1.26) that catalyze the hydrolytic cleavage of the disaccharide sucrose into glucose and fructose. Their activity is tightly regulated by compartment-specific inhibitor proteins at transcriptional and post-transcriptional levels. 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). Interaction of invertase inhibitor Nt-CIF (Nicotiana tabacum cell-wall inhibitor of beta-fructosidase) with CWI is strictly pH-dependent, 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: 275440 [Multi-domain]  Cd Length: 148  Bit Score: 70.86  E-value: 5.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979  23 LIRNSCKKAtatspkFKYNLCVTSLETNPQAKTAKDLAGLVMASTKNAVTKATTlkgTVDKIIKGKKVNKMTA--MPLRD 100
Cdd:cd15796   3 LIDETCKKT------PNYDLCVSILRSDPRSTTAADVKGLALIMLDAVLAKAND---TLRKIGELLKKTTDPAlkRALSS 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237979 101 CLQLYTDAIGS-LNEALAGVKSRNYPTVKTVLSAAMDTPSTCETGFKERKApSPVTKENDNLYQMILIPLAFTNML 175
Cdd:cd15796  74 CAEEYGVIVEDdLPQAIEALKKGDYKAAKDSMYDAGKEADSCEEQFKGSSS-SPLTDRNKAVHDLAVVAAAIVRQL 148
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 42-175 1.32e-13

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: 64.77  E-value: 1.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979  42 LCVTSLETNPQAKTAkDLAGLVMASTKNAVTKATTLKGTVDKIIKGKKVNKMTAMPLRDCLQLYTDAIGSLNEALAGVKS 121
Cdd:cd15798  11 LCKSSLSSYASSSST-DPKELAKAALNAALDEAKKALALLSSLLKSSGSNPREKAALEDCLELLDDAVDDLNRSLSELNS 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15237979 122 -------RNYPTVKTVLSAAMDTPSTCETGFKERKAPSP--VTKENDNLYQMILIPLAFTNML 175
Cdd:cd15798  90 lskdkfsERVDDVQTWLSAALTNQDTCLDGFEETGSTVKkeLRASLKNVSKLTSNALALVNAL 152
PMEI-like_4 cd15799
plant invertase/pectin methylesterase inhibitor domain-containing protein; This subfamily ...
 42-149 7.14e-07

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: 46.63  E-value: 7.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979  42 LCVTSLETNPQAKTAKDLAGLVMASTKNAVTKATTLKGTVDKIIKGKKVNKmTAMPLRDCLQLYTDAIGSLNEALAGVKS 121
Cdd:cd15799  14 PSVSSSANALSAQCLKVPLDVFLAALKTTVDRIQSALSMVSKLRNGSDDPR-LSNALSDCLELLDFSADRLSWSLSALQN 92

                        90       100       110
                ....*....|....*....|....*....|.
gi 15237979 122 RNYPT---VKTVLSAAMDTPSTCETGFKERK 149
Cdd:cd15799  93 PKGDSgsdARTWLSAALTNHDTCLDGLEETG 123
PLN02484 PLN02484
probable pectinesterase/pectinesterase inhibitor
 41-147 1.10e-05

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178102 [Multi-domain]  Cd Length: 587  Bit Score: 44.52  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979   41 NLCVTSLETNPQAKTA--KDLAGLVMASTKNAVTKATTLKGTVdkiikgkkvnKMTAMPLR------DCLQLYTDAIGSL 112
Cdd:PLN02484  87 NLCVDSLLDFPGSLTAseSDLIHISFNMTLQHFSKALYLSSTI----------SYVQMPPRvrsaydSCLELLDDSVDAL 156

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 15237979  113 NEALAGVKS----RNYPTVKTVLSAAMDTPSTCETGFKE 147
Cdd:PLN02484 157 SRALSSVVPssggGSPQDVVTWLSAALTNHDTCTEGFDG 195
PLN02933 PLN02933
Probable pectinesterase/pectinesterase inhibitor
 100-160 1.87e-03

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178521 [Multi-domain]  Cd Length: 530  Bit Score: 38.06  E-value: 1.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15237979  100 DCLQLYTDAIGSLNEALAGVKSRN--YPTVKTVLSAAMDTPSTCETGFKerkapspvTKENDN 160
Cdd:PLN02933  94 DCLGLLDDTISDLTTAISKLRSSSpeFNDVSMLLSNAMTNQDTCLDGFS--------TSDNEN 148
PLN02506 PLN02506
putative pectinesterase/pectinesterase inhibitor
 19-149 2.76e-03

putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 215280 [Multi-domain]  Cd Length: 537  Bit Score: 37.60  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979   19 NGQTLIRNSCKKATAtspkfkYNLCVTSLETNPQAKTAKDLAGLVMASTKNAVTKAttlKGTVDKIikgKKVNKMTA--- 95
Cdd:PLN02506  32 NFQALIAQACQFVEN------HSSCVSNIQAELKKSGPRTPHSVLSAALKATLDEA---RLAIDMI---TKFNALSIsyr 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237979   96 --MPLRDCLQLYTDAIGSL-------NEALAGVKSRNYP-TVKTVLSAAMDTPSTCETGFK--ERK 149
Cdd:PLN02506 100 eqVAIEDCKELLDFSVSELawsllemNKIRAGHDNVAYEgNLKAWLSAALSNQDTCLEGFEgtDRH 165
PLN02468 PLN02468
putative pectinesterase/pectinesterase inhibitor
 22-149 4.40e-03

putative pectinesterase/pectinesterase inhibitor


Pssm-ID: 178087 [Multi-domain]  Cd Length: 565  Bit Score: 36.78  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979   22 TLIRNSCKKATATSPKfkynlcvtSLETNPQaktakDLAGLVMASTKNAVTKAttlkgtVDKIIKGKKV----NKMTAMP 97
Cdd:PLN02468  74 TLYKDSCYETLAPAPK--------ASQLQPE-----ELFKYAVKVAINELSKA------SQAFSNSEGFlgvkDNMTNAA 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15237979   98 LRDCLQLYTDAIGSLNEALAGVKSRNYPTV----KTVLSAAMDTPSTCETGFKERK 149
Cdd:PLN02468 135 LNACQELLDLAIDNLNNSLTSSGGVSVLDNvddlRTWLSSAGTYQETCIDGLAEPN 190
PLN02314 PLN02314
pectinesterase
 43-147 9.56e-03

pectinesterase


Pssm-ID: 215179 [Multi-domain]  Cd Length: 586  Bit Score: 35.96  E-value: 9.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237979   43 CVTSLETNPQAKTAkDLAGLVMASTKNAVTKATTLKGTVDKIIKGKKVNKMTAmPLRDCLQLYTDAIGSLNEALAGVKSR 122
Cdd:PLN02314  86 CISSISSLPTSNTT-DPETLFKLSLKVAIDELSKLSDLPQKLINETNDERLKS-ALRVCETLFDDAIDRLNDSISSMQVG 163

                         90       100       110
                 ....*....|....*....|....*....|....
gi 15237979  123 NYPTV---------KTVLSAAMDTPSTCETGFKE 147
Cdd:PLN02314 164 EGEKIlssskiddlKTWLSATITDQETCIDALQE 197
 
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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