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25  structures 139  species 0  interactions 12597  sequences 173  architectures

Family: PMEI (PF04043)

Summary: Plant invertase/pectin methylesterase inhibitor

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The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Plant invertase/pectin methylesterase inhibitor Provide feedback

This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex [1]. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension (see [2]). It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein [1]. 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 [2].

Literature references

  1. Giovane A, Balestrieri C, Quagliuolo L, Castaldo D, Servillo L; , Eur J Biochem 1995;233:926-929.: A glycoprotein inhibitor of pectin methylesterase in kiwi fruit. Purification by affinity chromatography and evidence of a ripening-related precursor. PUBMED:8521860 EPMC:8521860

  2. Camardella L, Carratore V, Ciardiello MA, Servillo L, Balestrieri C, Giovane A; , Eur J Biochem 2000;267:4561-4565.: Kiwi protein inhibitor of pectin methylesterase amino-acid sequence and structural importance of two disulfide bridges. PUBMED:10880981 EPMC:10880981


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006501

This domain inhibits pectin methylesterases (PMEs) and invertases through formation of a non-covalent 1:1 complex [ PUBMED:8521860 ]. It has been implicated in the regulation of fruit development, carbohydrate metabolism and cell wall extension [ PUBMED:10880981 ]. It may also be involved in inhibiting microbial pathogen PMEs. It has been observed that it is often expressed as a large inactive preprotein [ PUBMED:8521860 ]. It is also found at the N-termini of PMEs, 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 [ PUBMED:10880981 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(629)
Full
(12597)
Representative proteomes UniProt
(18319)
RP15
(1046)
RP35
(6690)
RP55
(10379)
RP75
(14057)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(629)
Full
(12597)
Representative proteomes UniProt
(18319)
RP15
(1046)
RP35
(6690)
RP55
(10379)
RP75
(14057)
Alignment:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(629)
Full
(12597)
Representative proteomes UniProt
(18319)
RP15
(1046)
RP35
(6690)
RP55
(10379)
RP75
(14057)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Yeats C, McQueen A
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Yeats C
Number in seed: 629
Number in full: 12597
Average length of the domain: 145.00 aa
Average identity of full alignment: 18 %
Average coverage of the sequence by the domain: 41.84 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 26.7 26.7
Trusted cut-off 26.7 26.7
Noise cut-off 26.6 26.6
Model length: 154
Family (HMM) version: 17
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PMEI domain has been found. There are 25 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0N7KN71 View 3D Structure Click here
A0A0N7KSJ9 View 3D Structure Click here
A0A0P0UXK1 View 3D Structure Click here
A0A0P0V0P1 View 3D Structure Click here
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A0A0P0V2N2 View 3D Structure Click here
A0A0P0VJX3 View 3D Structure Click here
A0A0P0VN51 View 3D Structure Click here
A0A0P0WEA4 View 3D Structure Click here
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A0A0R0E613 View 3D Structure Click here
A0A0R0E619 View 3D Structure Click here
A0A0R0E753 View 3D Structure Click here
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A0A0R0ERW6 View 3D Structure Click here
A0A0R0FDV5 View 3D Structure Click here
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A0A0R0G197 View 3D Structure Click here
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A0A0R0GYI7 View 3D Structure Click here
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A0A0R0HT91 View 3D Structure Click here
A0A0R0I8X6 View 3D Structure Click here
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A0A0R0J590 View 3D Structure Click here
A0A0R0J7M3 View 3D Structure Click here
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A0A0R0JHD5 View 3D Structure Click here
A0A0R0JNR4 View 3D Structure Click here
A0A0R0K417 View 3D Structure Click here
A0A0R0K417 View 3D Structure Click here
A0A0R0KGZ7 View 3D Structure Click here
A0A0R0KN67 View 3D Structure Click here
A0A0R0KQL0 View 3D Structure Click here
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A0A1D6E1Q3 View 3D Structure Click here
A0A1D6E975 View 3D Structure Click here
A0A1D6EQT6 View 3D Structure Click here
A0A1D6FC44 View 3D Structure Click here
A0A1D6FNG9 View 3D Structure Click here
A0A1D6GXX4 View 3D Structure Click here
A0A1D6H4M1 View 3D Structure Click here
A0A1D6H8D8 View 3D Structure Click here
A0A1D6HA44 View 3D Structure Click here
A0A1D6HA45 View 3D Structure Click here
A0A1D6HWK3 View 3D Structure Click here
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A0A1D6HWK6 View 3D Structure Click here
A0A1D6HWN4 View 3D Structure Click here
A0A1D6I4U1 View 3D Structure Click here
A0A1D6IN03 View 3D Structure Click here
A0A1D6IP48 View 3D Structure Click here
A0A1D6J2Q2 View 3D Structure Click here
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A0A1D6K988 View 3D Structure Click here
A0A1D6KD80 View 3D Structure Click here
A0A1D6KNK0 View 3D Structure Click here
A0A1D6KR50 View 3D Structure Click here
A0A1D6LAI1 View 3D Structure Click here
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A0A1D6M0U7 View 3D Structure Click here
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A0A1D6MX92 View 3D Structure Click here
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A0A1D6P829 View 3D Structure Click here
A0A1D6PZP0 View 3D Structure Click here
A0A1D6Q782 View 3D Structure Click here
A0A1I9LNH8 View 3D Structure Click here
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A0A1P8AP64 View 3D Structure Click here
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I1MI21 View 3D Structure Click here
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I1MK76 View 3D Structure Click here
I1MP45 View 3D Structure Click here
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Q0D9K6 View 3D Structure Click here
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Q10MP6 View 3D Structure Click here
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Q1G390 View 3D Structure Click here
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Q1PEC0 View 3D Structure Click here
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