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Conserved domains on  [gi|15240603|ref|NP_199815|]
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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 ...
 24-166 3.42e-21

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: 84.34  E-value: 3.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240603     24 ASATTYIDAICQSVTDKAFCAKTLNAYPAAgSATSQFQAATATLNLAISYADKSAGFTGNAAK--ENPTLKTQFAASQDA 101
Cdd:smart00856   1 APTSKLIDSICKSTDYPDFCVSSLSSDPSS-SATDPKDLAKIAIKVALSQATKTLSFISKLLKktKDPRLKAALKDCLEL 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240603    102 FVTISKSLKSAASELK--ISPDTANYDVMVCSDSIATVKNLVEkNTDNSSKTVMTMTLMMEKLLTIA 166
Cdd:smart00856  80 YDDAVDSLEKALEELKsgDYDDVATWLSAALTDQDTCLDGFEE-NDDKVKSPLTKRNDNLEKLTSNA 145
 
Name Accession Description Interval E-value
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 24-166 3.42e-21

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: 84.34  E-value: 3.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240603     24 ASATTYIDAICQSVTDKAFCAKTLNAYPAAgSATSQFQAATATLNLAISYADKSAGFTGNAAK--ENPTLKTQFAASQDA 101
Cdd:smart00856   1 APTSKLIDSICKSTDYPDFCVSSLSSDPSS-SATDPKDLAKIAIKVALSQATKTLSFISKLLKktKDPRLKAALKDCLEL 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240603    102 FVTISKSLKSAASELK--ISPDTANYDVMVCSDSIATVKNLVEkNTDNSSKTVMTMTLMMEKLLTIA 166
Cdd:smart00856  80 YDDAVDSLEKALEELKsgDYDDVATWLSAALTDQDTCLDGFEE-NDDKVKSPLTKRNDNLEKLTSNA 145
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 30-136 2.39e-05

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: 42.35  E-value: 2.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240603  30 IDAICQSVTDKAFCAKTLNAYPAAGSATSQFQAATATLNLAISYADKSAGFTGNAAKENPT---LKTQFAASQDAFVTIS 106
Cdd:cd15795   3 KAAAGDPNVDYDFCVSSLQSDPRSRTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYpsdLKKALRDCLSLYSDAV 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 15240603 107 KSLKSAASELK-ISPDTANYDVMVCSDSIAT 136
Cdd:cd15795  83 DSLKSALDALKsGDYGDANYDLSAATDAPVT 113
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 28-156 3.99e-03

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: 35.99  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240603    28 TYIDAICQSVTDKAFCAKTLNAYPAAGSATSQfQAATATLNLAISYADKSAGFTGNAAKENPTLKTQFAASQD---AFVT 104
Cdd:pfam04043   1 SLIKTACKKTPYPDLCVSSLSSDPASAASPPK-GLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDcleLYDD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240603   105 ISKSLKSAASELKiSPDTANYDVMV-----------CSDSIA-TVKNLVEKNTDNSSKTVMTMT 156
Cdd:pfam04043  80 AVDELNRALDALK-AGDSSRDDAQTwlsaaltnqdtCEDGFKeAVKGQLKSSMKSPLRNLTKLT 142
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 7-117 6.95e-03

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: 35.47  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240603     7 YFFLVSLAVLLPFLIIFASATTYIDAICQSVTDKAFCAKTLNAYPaaGSATSQFQA-ATATLNLAISYADKSAGFTGNAA 85
Cdd:TIGR01614   9 LFLLLLSLVATSSSNSLNATQSLIKRICKKTEYPNFCISTLKSDP--SSAKADLQGlANISVSAALSNASDTLDHISKLL 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 15240603    86 KEN--PTLKTQFAASQDAFVTISKSLKSAASELK 117
Cdd:TIGR01614  87 LTKgdPRDKSALEDCVELYSDAVDALDKALASLK 120
 
Name Accession Description Interval E-value
PMEI smart00856
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 24-166 3.42e-21

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: 84.34  E-value: 3.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240603     24 ASATTYIDAICQSVTDKAFCAKTLNAYPAAgSATSQFQAATATLNLAISYADKSAGFTGNAAK--ENPTLKTQFAASQDA 101
Cdd:smart00856   1 APTSKLIDSICKSTDYPDFCVSSLSSDPSS-SATDPKDLAKIAIKVALSQATKTLSFISKLLKktKDPRLKAALKDCLEL 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240603    102 FVTISKSLKSAASELK--ISPDTANYDVMVCSDSIATVKNLVEkNTDNSSKTVMTMTLMMEKLLTIA 166
Cdd:smart00856  80 YDDAVDSLEKALEELKsgDYDDVATWLSAALTDQDTCLDGFEE-NDDKVKSPLTKRNDNLEKLTSNA 145
PMEI-Pla_a_1_like cd15795
Pollen allergen Pla a 1 and similar plant proteins; The major Platanus acerifolia pollen ...
 30-136 2.39e-05

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: 42.35  E-value: 2.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240603  30 IDAICQSVTDKAFCAKTLNAYPAAGSATSQFQAATATLNLAISYADKSAGFTGNAAKENPT---LKTQFAASQDAFVTIS 106
Cdd:cd15795   3 KAAAGDPNVDYDFCVSSLQSDPRSRTAADLKGLAVIATKLAIANATATKAKIEKLLKSKKYpsdLKKALRDCLSLYSDAV 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 15240603 107 KSLKSAASELK-ISPDTANYDVMVCSDSIAT 136
Cdd:cd15795  83 DSLKSALDALKsGDYGDANYDLSAATDAPVT 113
PMEI-like_3 cd15798
Uncharacterized subfamily of plant invertase/pectin methylesterase inhibitor domains; This ...
 32-156 2.64e-03

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: 36.65  E-value: 2.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240603  32 AICQSVTDKAFCAKTLNAYPAAGSATSQfQAATATLNLAISYADKSAGFTGNAAKENPTLKTQFAASQDAFVTISKS--- 108
Cdd:cd15798   1 AICSSTPYPDLCKSSLSSYASSSSTDPK-ELAKAALNAALDEAKKALALLSSLLKSSGSNPREKAALEDCLELLDDAvdd 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240603 109 LKSAASELKISPDTANYDVMV---------------CSDSIATVKNLVEKNTDNSSKTVMTMT 156
Cdd:cd15798  80 LNRSLSELNSLSKDKFSERVDdvqtwlsaaltnqdtCLDGFEETGSTVKKELRASLKNVSKLT 142
PMEI pfam04043
Plant invertase/pectin methylesterase inhibitor; This domain inhibits pectin methylesterases ...
 28-156 3.99e-03

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: 35.99  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240603    28 TYIDAICQSVTDKAFCAKTLNAYPAAGSATSQfQAATATLNLAISYADKSAGFTGNAAKENPTLKTQFAASQD---AFVT 104
Cdd:pfam04043   1 SLIKTACKKTPYPDLCVSSLSSDPASAASPPK-GLAKAAVNVALSNATSALSFISKLLKKSKKSAKDKAALEDcleLYDD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240603   105 ISKSLKSAASELKiSPDTANYDVMV-----------CSDSIA-TVKNLVEKNTDNSSKTVMTMT 156
Cdd:pfam04043  80 AVDELNRALDALK-AGDSSRDDAQTwlsaaltnqdtCEDGFKeAVKGQLKSSMKSPLRNLTKLT 142
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 7-117 6.95e-03

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: 35.47  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240603     7 YFFLVSLAVLLPFLIIFASATTYIDAICQSVTDKAFCAKTLNAYPaaGSATSQFQA-ATATLNLAISYADKSAGFTGNAA 85
Cdd:TIGR01614   9 LFLLLLSLVATSSSNSLNATQSLIKRICKKTEYPNFCISTLKSDP--SSAKADLQGlANISVSAALSNASDTLDHISKLL 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 15240603    86 KEN--PTLKTQFAASQDAFVTISKSLKSAASELK 117
Cdd:TIGR01614  87 LTKgdPRDKSALEDCVELYSDAVDALDKALASLK 120
 
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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