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Conserved domains on  [gi|15240961|ref|NP_198677|]
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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 ...
 30-189 3.14e-49

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: 156.76  E-value: 3.14e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961  30 CKSCAAKSTIFDYNFCVSSLNNSPIAlPSPTNLSSLALVPMLQALDNATATASTIQQLLISDDDGSFRSACLRDCLELYE 109
Cdd:cd15795   1 CKKAAAGDPNVDYDFCVSSLQSDPRS-RTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKALRDCLSLYS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961 110 DATDRLEEAVRVFITRKeLGTVNVMVSAAMESAVTCENGFRERddgdgggggvTTWTSPIGDENHKLFEFGQIALCIFNM 189
Cdd:cd15795  80 DAVDSLKSALDALKSGD-YGDANYDLSAATDAPVTCEDAFKEA----------KIVVSPLTKENDELFQLALIALAITSM 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 ...
 30-189 3.14e-49

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: 156.76  E-value: 3.14e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961  30 CKSCAAKSTIFDYNFCVSSLNNSPIAlPSPTNLSSLALVPMLQALDNATATASTIQQLLISDDDGSFRSACLRDCLELYE 109
Cdd:cd15795   1 CKKAAAGDPNVDYDFCVSSLQSDPRS-RTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKALRDCLSLYS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961 110 DATDRLEEAVRVFITRKeLGTVNVMVSAAMESAVTCENGFRERddgdgggggvTTWTSPIGDENHKLFEFGQIALCIFNM 189
Cdd:cd15795  80 DAVDSLKSALDALKSGD-YGDANYDLSAATDAPVTCEDAFKEA----------KIVVSPLTKENDELFQLALIALAITSM 148
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 20-186 1.26e-24

Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences, suggesting that both PMEs and their inhibitors are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.


Pssm-ID: 214860 [Multi-domain]  Cd Length: 148  Bit Score: 93.97  E-value: 1.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961     20 KSTSDMIDQTCKScaakstIFDYNFCVSSLNNSPIalPSPTNLSSLALVPMLQALDNATATASTIQQLLISDDDgSFRSA 99
Cdd:smart00856   1 APTSKLIDSICKS------TDYPDFCVSSLSSDPS--SSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTKD-PRLKA 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961    100 CLRDCLELYEDATDRLEEAVRvFITRKELGTVNVMVSAAMESAVTCENGFRERDdgdgggggvTTWTSPIGDENHKLFEF 179
Cdd:smart00856  72 ALKDCLELYDDAVDSLEKALE-ELKSGDYDDVATWLSAALTDQDTCLDGFEEND---------DKVKSPLTKRNDNLEKL 141


                   ....*..
gi 15240961    180 GQIALCI 186
Cdd:smart00856 142 TSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 1-191 1.92e-24

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: 94.41  E-value: 1.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961     1 MKLSQVFYIIFLFFLVS------QVKSTSDMIDQTCKSCAakstifDYNFCVSSLNNSPIAlpSPTNLSSLALVPMLQAL 74
Cdd:TIGR01614   1 MASSLSLLLFLLLLSLVatsssnSLNATQSLIKRICKKTE------YPNFCISTLKSDPSS--AKADLQGLANISVSAAL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961    75 DNATATASTIQQLLISDDDGSFRSAcLRDCLELYEDATDRLEEAVRVFITRKeLGTVNVMVSAAMESAVTCENGFRERDD 154
Cdd:TIGR01614  73 SNASDTLDHISKLLLTKGDPRDKSA-LEDCVELYSDAVDALDKALASLKSKD-YSDAETWLSSALTDPSTCEDGFEELGG 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 15240961   155 GDgggggvttwTSPIGDENHKLFEFGQIALCIFNMLS 191
Cdd:TIGR01614 151 IV---------KSPLTKRNNNVKKLSSITLAIIKMLT 178
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 24-186 5.06e-23

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: 89.91  E-value: 5.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961    24 DMIDQTCKSCaakstiFDYNFCVSSLNNSPIALPSPtnLSSLALVPMLQALDNATATASTIQQLLISDDDGSFRSACLRD 103
Cdd:pfam04043   1 SLIKTACKKT------PYPDLCVSSLSSDPASAASP--PKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALED 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961   104 CLELYEDATDRLEEAVRVF-ITRKELGTVNVMVSAAMESAVTCENGFRERDDGDGGgggvttwtSPIGDENHKLFEFGQI 182
Cdd:pfam04043  73 CLELYDDAVDELNRALDALkAGDSSRDDAQTWLSAALTNQDTCEDGFKEAVKGQLK--------SSMKSPLRNLTKLTSN 144


                  ....
gi 15240961   183 ALCI 186
Cdd:pfam04043 145 ALAI 148
PLN02484 PLN02484
probable pectinesterase/pectinesterase inhibitor
 43-151 1.12e-05

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178102 [Multi-domain]  Cd Length: 587  Bit Score: 45.29  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961   43 NFCVSSLNNSPIAL-PSPTNLSSLALVPMLQALDNATATASTIQQLlisDDDGSFRSAcLRDCLELYEDATDRLEEAVRV 121
Cdd:PLN02484  87 NLCVDSLLDFPGSLtASESDLIHISFNMTLQHFSKALYLSSTISYV---QMPPRVRSA-YDSCLELLDDSVDALSRALSS 162

                         90       100       110
                 ....*....|....*....|....*....|...
gi 15240961  122 FITRKELGT---VNVMVSAAMESAVTCENGFRE 151
Cdd:PLN02484 163 VVPSSGGGSpqdVVTWLSAALTNHDTCTEGFDG 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 ...
 30-189 3.14e-49

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: 156.76  E-value: 3.14e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961  30 CKSCAAKSTIFDYNFCVSSLNNSPIAlPSPTNLSSLALVPMLQALDNATATASTIQQLLISDDDGSFRSACLRDCLELYE 109
Cdd:cd15795   1 CKKAAAGDPNVDYDFCVSSLQSDPRS-RTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYPSDLKKALRDCLSLYS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961 110 DATDRLEEAVRVFITRKeLGTVNVMVSAAMESAVTCENGFRERddgdgggggvTTWTSPIGDENHKLFEFGQIALCIFNM 189
Cdd:cd15795  80 DAVDSLKSALDALKSGD-YGDANYDLSAATDAPVTCEDAFKEA----------KIVVSPLTKENDELFQLALIALAITSM 148
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 20-186 1.26e-24

Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein. It is also found at the N-termini of PMEs predicted from DNA sequences, suggesting that both PMEs and their inhibitors are expressed as a single polyprotein and subsequently processed. It has two disulphide bridges and is mainly alpha-helical.


Pssm-ID: 214860 [Multi-domain]  Cd Length: 148  Bit Score: 93.97  E-value: 1.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961     20 KSTSDMIDQTCKScaakstIFDYNFCVSSLNNSPIalPSPTNLSSLALVPMLQALDNATATASTIQQLLISDDDgSFRSA 99
Cdd:smart00856   1 APTSKLIDSICKS------TDYPDFCVSSLSSDPS--SSATDPKDLAKIAIKVALSQATKTLSFISKLLKKTKD-PRLKA 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961    100 CLRDCLELYEDATDRLEEAVRvFITRKELGTVNVMVSAAMESAVTCENGFRERDdgdgggggvTTWTSPIGDENHKLFEF 179
Cdd:smart00856  72 ALKDCLELYDDAVDSLEKALE-ELKSGDYDDVATWLSAALTDQDTCLDGFEEND---------DKVKSPLTKRNDNLEKL 141


                   ....*..
gi 15240961    180 GQIALCI 186
Cdd:smart00856 142 TSNALAI 148
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 1-191 1.92e-24

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: 94.41  E-value: 1.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961     1 MKLSQVFYIIFLFFLVS------QVKSTSDMIDQTCKSCAakstifDYNFCVSSLNNSPIAlpSPTNLSSLALVPMLQAL 74
Cdd:TIGR01614   1 MASSLSLLLFLLLLSLVatsssnSLNATQSLIKRICKKTE------YPNFCISTLKSDPSS--AKADLQGLANISVSAAL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961    75 DNATATASTIQQLLISDDDGSFRSAcLRDCLELYEDATDRLEEAVRVFITRKeLGTVNVMVSAAMESAVTCENGFRERDD 154
Cdd:TIGR01614  73 SNASDTLDHISKLLLTKGDPRDKSA-LEDCVELYSDAVDALDKALASLKSKD-YSDAETWLSSALTDPSTCEDGFEELGG 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 15240961   155 GDgggggvttwTSPIGDENHKLFEFGQIALCIFNMLS 191
Cdd:TIGR01614 151 IV---------KSPLTKRNNNVKKLSSITLAIIKMLT 178
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 24-186 5.06e-23

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: 89.91  E-value: 5.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961    24 DMIDQTCKSCaakstiFDYNFCVSSLNNSPIALPSPtnLSSLALVPMLQALDNATATASTIQQLLISDDDGSFRSACLRD 103
Cdd:pfam04043   1 SLIKTACKKT------PYPDLCVSSLSSDPASAASP--PKGLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALED 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961   104 CLELYEDATDRLEEAVRVF-ITRKELGTVNVMVSAAMESAVTCENGFRERDDGDGGgggvttwtSPIGDENHKLFEFGQI 182
Cdd:pfam04043  73 CLELYDDAVDELNRALDALkAGDSSRDDAQTWLSAALTNQDTCEDGFKEAVKGQLK--------SSMKSPLRNLTKLTSN 144


                  ....
gi 15240961   183 ALCI 186
Cdd:pfam04043 145 ALAI 148
PMEI-like_1 cd15801
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 25-190 1.13e-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: 88.93  E-value: 1.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961  25 MIDQTCKscaaksTIFDYNFCVSSLNNSPIALPS-PTNLSSLALVpmlQALDNATATASTIQQLLISDDDGSFrSACLRD 103
Cdd:cd15801   1 LIEEACK------KTLDPDLCVSALSSDPESKKAdLRGLAELALK---AAAENATATASYVSELLNTAKDPYV-QQCLED 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961 104 CLELYEDATDRLEEAVRVFITRKeLGTVNVMVSAAMESAVTCENGFRERDDGdgggggvttwTSPIGDENHKLFEFGQIA 183
Cdd:cd15801  71 CSENYEDAVEQLNDSLAALDSKA-YGDVKTWVTAALADAETCEDAFKEKPGD----------KSPLTARNGDFSKLCSIA 139


                ....*..
gi 15240961 184 LCIFNML 190
Cdd:cd15801 140 LAIIKLL 146
PMEI_like cd14859
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ...
 41-189 5.24e-18

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: 76.70  E-value: 5.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961  41 DYNFCVSSLNNSPIAlpSPTNLSSLALVPMLQALDNATATASTIQQLLISDDDGSFRsACLRDCLELYEDATDRLEEAVR 120
Cdd:cd14859   6 YYKLCVSSLSSDPRS--STADLKGLANIALDAALANASDTQAFIAKLLKSTKDPALK-KALRDCADDYDDAVDDLEDAIN 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240961 121 VFITrKELGTVNVMVSAAMESAVTCENGFRERDDGdgggggvttwTSPIGDENHKLFEFGQIALCIFNM 189
Cdd:cd14859  83 ALLS-GDYDDAKTHVSAALDDADTCEEAFKESSGL----------PSPLTTRNDDLKRLCSIALAIILL 140
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 22-190 1.67e-16

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: 72.84  E-value: 1.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961  22 TSDMIDQTCKSCaakstiFDYNFCVSSLNNSPIAlpSPTNLSSLALVPMLQALDNATATASTIQQLLISDDDGSFRSAcL 101
Cdd:cd15797   1 TEELIDTICKKT------ENPSFCLQILNSDPRS--ASADLVGLAQIAIDLAQSNATNTLKLIQSLIKSTTDPKLKNR-Y 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961 102 RDCLELYEDATDRLEEAVRVFiTRKELGTVNVMVSAAMESAVTCENGFRERDDGdgggggvttwTSPIGDENHKLFEFGQ 181
Cdd:cd15797  72 ESCSKNYNDAIDALEEAKKSL-SSGDYDGLNKAASAALDAVSTCEDELSKPPKD----------PSPLAKYNRDVEDLCD 140


                ....*....
gi 15240961 182 IALCIFNML 190
Cdd:cd15797 141 IILVISDLL 149
CIF_like cd15796
Cell-wall inhibitor of beta fructosidase and similar proteins; Cell-wall invertases (CWIs) are ...
 23-190 1.03e-15

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: 1.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961  23 SDMIDQTCKScaakstIFDYNFCVSSLNNSPIALpSPTNLSSLALVpMLQA-LDNATATASTIQQLLISDDDGSFRSAcL 101
Cdd:cd15796   1 ADLIDETCKK------TPNYDLCVSILRSDPRST-TAADVKGLALI-MLDAvLAKANDTLRKIGELLKKTTDPALKRA-L 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961 102 RDCLELYEDATDRLEEAVRVFITRKELGTV-NVMVSAAMEsAVTCENGFRerddgdgggggvTTWTSPIGDENHKLFEFG 180
Cdd:cd15796  72 SSCAEEYGVIVEDDLPQAIEALKKGDYKAAkDSMYDAGKE-ADSCEEQFK------------GSSSSPLTDRNKAVHDLA 138

                       170
                ....*....|
gi 15240961 181 QIALCIFNML 190
Cdd:cd15796 139 VVAAAIVRQL 148
PMEI-like_2 cd15800
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitors; This subfamily ...
 45-190 5.73e-11

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: 58.14  E-value: 5.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961  45 CVSSLnnSPIALPSPTNLSSlALVPMLQALDNATATASTIQQLLISDDDGS-FRSACLRDCLELYEDATDRLEEAVRVFI 123
Cdd:cd15800  17 CLSTV--KPFLTKGKIDPVS-ALEAAIKALIAKTKQAKALAKKLAKSPSTSpEVKSALDVCKESYDDALDNLKKALKAIK 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240961 124 TRkELGTVNVMVSAAMESAVTCENGFRERDDgdgggggvttwTSPIGDENHKLFEFGQIALCIFNML 190
Cdd:cd15800  94 SR-DIGTLNSMLSAAITDYSTCDDAFAESGL-----------VSPLAKINDLLKKLASNCLAIATLL 148
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 44-151 4.32e-09

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: 53.21  E-value: 4.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961  44 FCVSSLNNSPIAlpSPTNLSSLALVPMLQALDNATATASTIQQLLISDDDGSFRSACLRDCLELYEDATDRLEEAVR--- 120
Cdd:cd15798  11 LCKSSLSSYASS--SSTDPKELAKAALNAALDEAKKALALLSSLLKSSGSNPREKAALEDCLELLDDAVDDLNRSLSeln 88

                        90       100       110
                ....*....|....*....|....*....|....
gi 15240961 121 ---VFITRKELGTVNVMVSAAMESAVTCENGFRE 151
Cdd:cd15798  89 slsKDKFSERVDDVQTWLSAALTNQDTCLDGFEE 122
PLN02484 PLN02484
probable pectinesterase/pectinesterase inhibitor
 43-151 1.12e-05

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178102 [Multi-domain]  Cd Length: 587  Bit Score: 45.29  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961   43 NFCVSSLNNSPIAL-PSPTNLSSLALVPMLQALDNATATASTIQQLlisDDDGSFRSAcLRDCLELYEDATDRLEEAVRV 121
Cdd:PLN02484  87 NLCVDSLLDFPGSLtASESDLIHISFNMTLQHFSKALYLSSTISYV---QMPPRVRSA-YDSCLELLDDSVDALSRALSS 162

                         90       100       110
                 ....*....|....*....|....*....|...
gi 15240961  122 FITRKELGT---VNVMVSAAMESAVTCENGFRE 151
Cdd:PLN02484 163 VVPSSGGGSpqdVVTWLSAALTNHDTCTEGFDG 195
PLN02314 PLN02314
pectinesterase
 45-151 6.12e-04

pectinesterase


Pssm-ID: 215179 [Multi-domain]  Cd Length: 586  Bit Score: 39.81  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961   45 CVSSLNNSPIAlpSPTNLSSLALVPMLQALDNATATASTIQQLLISDDDGSFRSAcLRDCLELYEDATDRLEEAV----- 119
Cdd:PLN02314  86 CISSISSLPTS--NTTDPETLFKLSLKVAIDELSKLSDLPQKLINETNDERLKSA-LRVCETLFDDAIDRLNDSIssmqv 162

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15240961  120 ----RVFITRKeLGTVNVMVSAAMESAVTCENGFRE 151
Cdd:PLN02314 163 gegeKILSSSK-IDDLKTWLSATITDQETCIDALQE 197
PMEI-like_4 cd15799
plant invertase/pectin methylesterase inhibitor domain-containing protein; This subfamily ...
 45-151 2.17e-03

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: 37.00  E-value: 2.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961  45 CVSSLNNSPIALPSPTNLSSL--ALVPMLQALDNAtatASTIQQLLISDDDGSFRSAcLRDCLELYEDATDRLEEAVR-- 120
Cdd:cd15799  15 SVSSSANALSAQCLKVPLDVFlaALKTTVDRIQSA---LSMVSKLRNGSDDPRLSNA-LSDCLELLDFSADRLSWSLSal 90

                        90       100       110
                ....*....|....*....|....*....|.
gi 15240961 121 VFITRKELGTVNVMVSAAMESAVTCENGFRE 151
Cdd:cd15799  91 QNPKGDSGSDARTWLSAALTNHDTCLDGLEE 121
PLN02933 PLN02933
Probable pectinesterase/pectinesterase inhibitor
 3-149 3.87e-03

Probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 178521 [Multi-domain]  Cd Length: 530  Bit Score: 37.29  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240961    3 LSQVFYIIFLfflvSQVKSTSDMIDQTCKSCAAKSTIFDYNFCVSSLNNSPialpSPTNLSSlalvpmlqaldnatATAS 82
Cdd:PLN02933  17 LSLIFFLIFL----STVVSSQSPSYTTHKTQRLTETKTIPELIIADLNLTI----LKVNLAS--------------SNFS 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240961   83 TIQQLLISDDdgSFRSAC-LRDCLELYEDATDRLEEAV-RVFITRKELGTVNVMVSAAMESAVTCENGF 149
Cdd:PLN02933  75 DLQTRLGPNL--THRERCaFEDCLGLLDDTISDLTTAIsKLRSSSPEFNDVSMLLSNAMTNQDTCLDGF 141
 
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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