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353  structures 1577  species 0  interactions 9407  sequences 270  architectures

Family: Tyrosinase (PF00264)

Summary: Common central domain of tyrosinase

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 "Tyrosinase". More...

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.

Common central domain of tyrosinase Provide feedback

This family also contains polyphenol oxidases and some hemocyanins. Binds two copper ions via two sets of three histidines. This family is related to PF00372.

Literature references

  1. Volbeda A, Hol WG; , J Mol Biol 1989;209:249-279.: Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution. PUBMED:2585484 EPMC:2585484


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002227

Tyrosinase ( EC ) [ PUBMED:3130643 ] is a copper monooxygenases that catalyzes the hydroxylation of monophenols and the oxidation of o-diphenols to o-quinols. This enzyme, found in prokaryotes as well as in eukaryotes, is involved in the formation of pigments such as melanins and other polyphenolic compounds. Tyrosinase binds two copper ions (CuA and CuB). Each of the two copper ions has been shown [ PUBMED:1901488 ] to be bound by three conserved histidines residues. The regions around these copper-binding ligands are well conserved and also shared by some hemocyanins, which are copper-containing oxygen carriers from the hemolymph of many molluscs and arthropods [ PUBMED:2664531 , PUBMED:1898774 ]. At least two proteins related to tyrosinase are known to exist in mammals, and include TRP-1 (TYRP1) [ PUBMED:7813420 ], which is responsible for the conversion of 5,6-dihydro-xyindole-2-carboxylic acid (DHICA) to indole-5,6-quinone-2-carboxylic acid; and TRP-2 (TYRP2) [ PUBMED:1537334 ], which is the melanogenic enzyme DOPAchrome tautomerase ( EC ) that catalyzes the conversion of DOPAchrome to DHICA. TRP-2 differs from tyrosinases and TRP-1 in that it binds two zinc ions instead of copper [ PUBMED:7980602 ]. Other proteins that belong to this family are plant polyphenol oxidases (PPO) ( EC ), which catalyze the oxidation of mono- and o-diphenols to o-diquinones [ PUBMED:1391768 ]; and Caenorhabditis elegans hypothetical protein C02C2.1.

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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Pfam Clan

This family is a member of clan Di-copper (CL0205), which has the following description:

This superfamily includes tyrosinases and hemocyanins that share a di-copper centre [1].

The clan contains the following 2 members:

Hemocyanin_M Tyrosinase

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
(120)
Full
(9407)
Representative proteomes UniProt
(23268)
RP15
(1998)
RP35
(4587)
RP55
(7663)
RP75
(10690)
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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
(120)
Full
(9407)
Representative proteomes UniProt
(23268)
RP15
(1998)
RP35
(4587)
RP55
(7663)
RP75
(10690)
Alignment:
Format:
Order:
Sequence:
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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
(120)
Full
(9407)
Representative proteomes UniProt
(23268)
RP15
(1998)
RP35
(4587)
RP55
(7663)
RP75
(10690)
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: Prosite
Previous IDs: tyrosinase;
Type: Domain
Sequence Ontology: SO:0000417
Author: Sonnhammer ELL , Griffiths-Jones SR
Number in seed: 120
Number in full: 9407
Average length of the domain: 202.50 aa
Average identity of full alignment: 21 %
Average coverage of the sequence by the domain: 43.95 %

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 22.6 22.6
Trusted cut-off 22.6 22.6
Noise cut-off 22.5 22.5
Model length: 222
Family (HMM) version: 22
Download: download the raw HMM for this family

Species distribution

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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 Tyrosinase domain has been found. There are 353 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
A0A0P0WF38 View 3D Structure Click here
A0A0P0WFB1 View 3D Structure Click here
A0A0R0G762 View 3D Structure Click here
A0A0R0G762 View 3D Structure Click here
A0A0R0G896 View 3D Structure Click here
A0A0R0GQB4 View 3D Structure Click here
A0A0R0GYN5 View 3D Structure Click here
A0A0R0JBC8 View 3D Structure Click here
A0A0R0JCW2 View 3D Structure Click here
A0A0R0LHN0 View 3D Structure Click here
A0A1D6JCC2 View 3D Structure Click here
A0A1D6JET7 View 3D Structure Click here
A0A1D6N9K8 View 3D Structure Click here
A0A1X7YDI6 View 3D Structure Click here
A0A368UH97 View 3D Structure Click here
A2ZYK9 View 3D Structure Click here
B7ZZ57 View 3D Structure Click here
C7IXC9 View 3D Structure Click here
D3ZH71 View 3D Structure Click here
D4A9G4 View 3D Structure Click here
F1QDZ4 View 3D Structure Click here
F1QEC9 View 3D Structure Click here
F1QRR2 View 3D Structure Click here
I1KEH4 View 3D Structure Click here
I1KLG6 View 3D Structure Click here
I1M285 View 3D Structure Click here
I1MEE6 View 3D Structure Click here
I1N3I2 View 3D Structure Click here
K7KJM5 View 3D Structure Click here
K7L2P1 View 3D Structure Click here
K7M1M4 View 3D Structure Click here
K7MU36 View 3D Structure Click here
K7VJ76 View 3D Structure Click here
O01497 View 3D Structure Click here
O76708 View 3D Structure Click here
P07147 View 3D Structure Click here
P11344 View 3D Structure Click here
P14679 View 3D Structure Click here
P17643 View 3D Structure Click here
P29812 View 3D Structure Click here
P34269 View 3D Structure Click here
P40126 View 3D Structure Click here
Q0J9Z1 View 3D Structure Click here
Q19673 View 3D Structure Click here
Q54QT0 View 3D Structure Click here
Q54QT1 View 3D Structure Click here
Q6DGE4 View 3D Structure Click here
Q95XC6 View 3D Structure Click here
Q9XUS8 View 3D Structure Click here