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749  structures 3310  species 0  interactions 38257  sequences 513  architectures

Family: COesterase (PF00135)

Summary: Carboxylesterase family

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Carboxylesterase family". More...

Carboxylesterase family Edit Wikipedia article

Carboxylesterase
PDB 1xlv EBI.jpg
Structure of ethylphosphorylated Butyrylcholinesterase.[1]
Identifiers
SymbolCOesterase
PfamPF00135
InterProIPR002018
PROSITEPDOC00112
SCOPe1acj / SUPFAM
OPM superfamily127
OPM protein1p0i
CDDcd00312

Carboxylesterase, type B is a family of evolutionarily related proteins.

Higher eukaryotes have many distinct esterases. The different types include those that act on carboxylic esters (EC 3.1.1). Carboxyl-esterases have been classified into three categories (A, B and C) on the basis of differential patterns of inhibition by organophosphates. The sequence of a number of type-B carboxylesterases indicates[2][3][4] that the majority are evolutionarily related. As is the case for lipases and serine proteases, the catalytic apparatus of esterases involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine. This family belongs to the superfamily of proteins with the Alpha/beta hydrolase fold.

Subfamilies

Examples

Human genes that encode proteins containing the carboxylesterase domain include:

See also

References

  1. ^ Nachon F, Asojo OA, Borgstahl GE, Masson P, Lockridge O (February 2005). "Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging". Biochemistry. 44 (4): 1154–62. CiteSeerX 10.1.1.529.7283. doi:10.1021/bi048238d. PMID 15667209.
  2. ^ Myers M, Richmond RC, Oakeshott JG (1988). "On the origins of esterases". Mol. Biol. Evol. 5 (2): 113–119. doi:10.1093/oxfordjournals.molbev.a040485. PMID 3163407.
  3. ^ Chatonnet A, Krejci E, Duval N, Vincens P, Massoulie J (1991). "Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid". Proc. Natl. Acad. Sci. U.S.A. 88 (15): 6647–6651. doi:10.1073/pnas.88.15.6647. PMC 52145. PMID 1862088.
  4. ^ Sussman JL, Cygler M, Harel M, Silman I, Schrag JD, Doctor BP, Gentry MK (1993). "Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins". Protein Sci. 2 (3): 366–382. doi:10.1002/pro.5560020309. PMC 2142374. PMID 8453375.

External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

Carboxylesterase family Provide feedback

No Pfam abstract.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002018

Higher eukaryotes have many distinct esterases. Among the different types are those which act on carboxylic esters ( EC ). Carboxyl-esterases have been classified into three categories (A, B and C) on the basis of differential patterns of inhibition by organophosphates. The sequence of a number of type-B carboxylesterases indicates [ PUBMED:3163407 , PUBMED:1862088 , PUBMED:8453375 ] that the majority are evolutionary related. As is the case for lipases and serine proteases, the catalytic apparatus of esterases involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.

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...

View options

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
(54)
Full
(38257)
Representative proteomes UniProt
(86078)
RP15
(7883)
RP35
(17899)
RP55
(31073)
RP75
(44914)
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HTML View             
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
(54)
Full
(38257)
Representative proteomes UniProt
(86078)
RP15
(7883)
RP35
(17899)
RP55
(31073)
RP75
(44914)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

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
(54)
Full
(38257)
Representative proteomes UniProt
(86078)
RP15
(7883)
RP35
(17899)
RP55
(31073)
RP75
(44914)
Raw Stockholm Download   Download   Download   Download   Download   Download    
Gzipped 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: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Sonnhammer ELL
Number in seed: 54
Number in full: 38257
Average length of the domain: 405.20 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 79.72 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 27.0 27.0
Noise cut-off 26.9 26.9
Model length: 515
Family (HMM) version: 31
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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 COesterase domain has been found. There are 749 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
A0A0B4K6L1 View 3D Structure Click here
A0A0B4K6V8 View 3D Structure Click here
A0A0B4LHM3 View 3D Structure Click here
A0A0G2K1L3 View 3D Structure Click here
A0A0G2KB83 View 3D Structure Click here
A0A0R4IJ74 View 3D Structure Click here
A0A0R4IPW5 View 3D Structure Click here
A0A0R4IYT8 View 3D Structure Click here
A0A1C3NSL8 View 3D Structure Click here
A0A1D6HZD9 View 3D Structure Click here
A0A1D6J2H6 View 3D Structure Click here
A0A2R8QP48 View 3D Structure Click here
A0A6H2EDS1 View 3D Structure Click here
A1ZA97 View 3D Structure Click here
A1ZA98 View 3D Structure Click here
A2BHL9 View 3D Structure Click here
B0F2B4 View 3D Structure Click here
B6VQ83 View 3D Structure Click here
D2X2F9 View 3D Structure Click here
D3Z298 View 3D Structure Click here
D3Z5G7 View 3D Structure Click here
D3ZP14 View 3D Structure Click here
D3ZXQ0 View 3D Structure Click here
D4AA05 View 3D Structure Click here
D4AE76 View 3D Structure Click here
E9PV38 View 3D Structure Click here
E9PYP1 View 3D Structure Click here
F1Q7W8 View 3D Structure Click here
F1QJV3 View 3D Structure Click here
F1QK81 View 3D Structure Click here
F1QX74 View 3D Structure Click here
F1R1T7 View 3D Structure Click here
F6P131 View 3D Structure Click here
F6Z9B9 View 3D Structure Click here
G3V7J5 View 3D Structure Click here
G5EC03 View 3D Structure Click here
G5EDJ7 View 3D Structure Click here
G5EDN1 View 3D Structure Click here
G5EDV9 View 3D Structure Click here
H2L0K7 View 3D Structure Click here