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Conserved domains on  [gi|15222837|ref|NP_176006|]
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Plant invertase/pectin methylesterase inhibitor superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PMEI_like super family cl04375
pectin methylesterase inhibitor and related proteins; Pectin methylesterase (PME; ...
 21-74 1.67e-10

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.


The actual alignment was detected with superfamily member cd15797:

Pssm-ID: 471005 [Multi-domain]  Cd Length: 149  Bit Score: 57.43  E-value: 1.67e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222837  21 EKDLMKEECHNAQVPTICMQCLESDPTSVHADRVGIAEIIIHCLDSRLDIITKQ 74
Cdd:cd15797   1 TEELIDTICKKTENPSFCLQILNSDPRSASADLVGLAQIAIDLAQSNATNTLKL 54
 
Name Accession Description Interval E-value
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 21-74 1.67e-10

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: 57.43  E-value: 1.67e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222837  21 EKDLMKEECHNAQVPTICMQCLESDPTSVHADRVGIAEIIIHCLDSRLDIITKQ 74
Cdd:cd15797   1 TEELIDTICKKTENPSFCLQILNSDPRSASADLVGLAQIAIDLAQSNATNTLKL 54
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 1-77 1.47e-06

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: 47.03  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222837     1 MTIMIKFLLLALLVIS---PICAEKDLMKEECHNAQVPTICMQCLESDPTSVHADRVGIAEIIIHCLDSR----LDIITK 73
Cdd:TIGR01614   5 LSLLLFLLLLSLVATSssnSLNATQSLIKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSNasdtLDHISK 84


                  ....
gi 15222837    74 QKGE 77
Cdd:TIGR01614  85 LLLT 88
 
Name Accession Description Interval E-value
PMEI cd15797
Pectin methylesterase inhibitor; Pectin methylesterase (PME; Pectinesterase; EC 3.1.1.11; CAZy ...
 21-74 1.67e-10

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: 57.43  E-value: 1.67e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15222837  21 EKDLMKEECHNAQVPTICMQCLESDPTSVHADRVGIAEIIIHCLDSRLDIITKQ 74
Cdd:cd15797   1 TEELIDTICKKTENPSFCLQILNSDPRSASADLVGLAQIAIDLAQSNATNTLKL 54
PME_inhib TIGR01614
pectinesterase inhibitor domain; This model describes a plant domain of about 200 amino acids, ...
 1-77 1.47e-06

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: 47.03  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222837     1 MTIMIKFLLLALLVIS---PICAEKDLMKEECHNAQVPTICMQCLESDPTSVHADRVGIAEIIIHCLDSR----LDIITK 73
Cdd:TIGR01614   5 LSLLLFLLLLSLVATSssnSLNATQSLIKRICKKTEYPNFCISTLKSDPSSAKADLQGLANISVSAALSNasdtLDHISK 84


                  ....
gi 15222837    74 QKGE 77
Cdd:TIGR01614  85 LLLT 88
 
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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