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1  structure 1372  species 0  interactions 6506  sequences 129  architectures

Family: Myosin_TH1 (PF06017)

Summary: Unconventional myosin tail, actin- and lipid-binding

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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.

Unconventional myosin tail, actin- and lipid-binding Provide feedback

Unconventional myosins, ie those that are not found in muscle, have the common, classical-type head domain, sometimes a neck with the IQ calmodulin-binding motifs, and then non-standard tails. These tails determine the subcellular localisation of the unconventional myosins and also help determine their individual functions. The family carries several different unconventional myosins, eg. Myo1f is expressed mainly in immune cells as well as in the inner ear where it can be associated with deafness, Myo1d has a lipid-binding module in their tail and is implicated in endosome vesicle recycling in epithelial cells. Myo1a, b, c and g from various eukaryotes are also found in this family.

Literature references

  1. Kim SV, Mehal WZ, Dong X, Heinrich V, Pypaert M, Mellman I, Dembo M, Mooseker MS, Wu D, Flavell RA;, Science. 2006;314:136-139.: Modulation of cell adhesion and motility in the immune system by Myo1f. PUBMED:17023661 EPMC:17023661

  2. Zadro C, Alemanno MS, Bellacchio E, Ficarella R, Donaudy F, Melchionda S, Zelante L, Rabionet R, Hilgert N, Estivill X, Van Camp G, Gasparini P, Carella M;, Biochim Biophys Acta. 2009;1792:27-32.: Are MYO1C and MYO1F associated with hearing loss?. PUBMED:19027848 EPMC:19027848

  3. Hartman MA, Finan D, Sivaramakrishnan S, Spudich JA;, Annu Rev Cell Dev Biol. 2011;27:133-155.: Principles of unconventional myosin function and targeting. PUBMED:21639800 EPMC:21639800


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR010926

Class I myosins (Myo1s) are widely expressed in eukaryotic cells. Myo1s exist as monomers and can sense cellular mechanical forces and function as tension- sensitive anchors or transporters. Each Myo1 contains from N terminus to C terminus, a motor domain, a neck region consisting of several calmodulin (CaM)-binding IQ motifs and a tail region. All Myo1s contain a tail homology (TH1) domain featuring an embedded pleckstrin-homology (PH) domain capable of binding to lipid membranes. In addition, Myo1s with long tails also contain a TH2 (or GPA) domain and a C-terminal TH3 (or SH3) domain, the latter of which may be responsible for binding to cargos. All Myo1s are capable of bridging actin cytoskeletons with lipid membranes by using their motor heads and tail TH1 domains.

The TH1 domain is an extended PH domain capable of binding to lipids [ PUBMED:25437912 , PUBMED:20071333 ].

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
(167)
Full
(6506)
Representative proteomes UniProt
(9896)
RP15
(839)
RP35
(1989)
RP55
(4799)
RP75
(6616)
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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
(167)
Full
(6506)
Representative proteomes UniProt
(9896)
RP15
(839)
RP35
(1989)
RP55
(4799)
RP75
(6616)
Alignment:
Format:
Order:
Sequence:
Gaps:
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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
(167)
Full
(6506)
Representative proteomes UniProt
(9896)
RP15
(839)
RP35
(1989)
RP55
(4799)
RP75
(6616)
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: Pfam-B_12631 (release 8.0)
Previous IDs: M_tail; Myosin_tail_2;
Type: Domain
Sequence Ontology: SO:0000417
Author: Yeats C
Number in seed: 167
Number in full: 6506
Average length of the domain: 183.10 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 18.34 %

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 31.1 31.1
Trusted cut-off 31.1 31.1
Noise cut-off 30.8 31.0
Model length: 189
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
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 Myosin_TH1 domain has been found. There are 1 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
A0A0G2K6E3 View 3D Structure Click here
A0A0R0GRY4 View 3D Structure Click here
A0A1D6JG05 View 3D Structure Click here
A0A286Y9H2 View 3D Structure Click here
A0A286YBP3 View 3D Structure Click here
A1C4A5 View 3D Structure Click here
A1DBH2 View 3D Structure Click here
A2R5J1 View 3D Structure Click here
A3LYL7 View 3D Structure Click here
A4RE77 View 3D Structure Click here
A5DKH0 View 3D Structure Click here
A5E4A8 View 3D Structure Click here
A5PF48 View 3D Structure Click here
A7EK16 View 3D Structure Click here
A7TDZ8 View 3D Structure Click here
A8N2Y6 View 3D Structure Click here
A8PWF6 View 3D Structure Click here
B0CRJ3 View 3D Structure Click here
B0I1T2 View 3D Structure Click here
B0S6F2 View 3D Structure Click here
D4A7X9 View 3D Structure Click here
E7F9L8 View 3D Structure Click here
E7FDV0 View 3D Structure Click here
E7FGI1 View 3D Structure Click here
E9Q634 View 3D Structure Click here
F1PRN2 View 3D Structure Click here
F1QJK0 View 3D Structure Click here
F1R617 View 3D Structure Click here
G5ECZ0 View 3D Structure Click here
I1JYV7 View 3D Structure Click here
I1KAM1 View 3D Structure Click here
M0R829 View 3D Structure Click here
O00159 View 3D Structure Click here
O00160 View 3D Structure Click here
O43795 View 3D Structure Click here
O88329 View 3D Structure Click here
O94832 View 3D Structure Click here
P0CP00 View 3D Structure Click here
P10568 View 3D Structure Click here
P22467 View 3D Structure Click here