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91  structures 643  species 0  interactions 15751  sequences 224  architectures

Family: Myosin_tail_1 (PF01576)

Summary: Myosin tail

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

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.

Myosin tail Provide feedback

The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types [1]. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament [1]. The coiled-coil region provides the structural backbone the thick filament [1].

Literature references

  1. Strehler EE, Strehler-page M-A, Perriard JC, Periasamy M, Nadal-ginard B; , J MOL BIOL 1986;190:291-317.: Complete nucleotide and encoded amino acid sequence of a mammalian myosin heavy chain gene. Evidence against intron-dependent evolution of the rod. PUBMED:3783701 EPMC:3783701


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002928

Muscle contraction is caused by sliding between the thick and thin filaments of the myofibril. Myosin is a major component of thick filaments and exists as a hexamer of 2 heavy chains [ PUBMED:1939027 ], 2 alkali light chains, and 2 regulatory light chains. The heavy chain can be subdivided into the N-terminal globular head and the C-terminal coiled-coil rod-like tail [ PUBMED:11919279 ], although some forms have a globular region in their C-terminal. There are many cell-specific isoforms of myosin heavy chains, coded for by a multi-gene family [ PUBMED:2806546 ]. Myosin interacts with actin to convert chemical energy, in the form of ATP, to mechanical energy [ PUBMED:3540939 ]. The 3-D structure of the head portion of myosin has been determined [ PUBMED:8316857 ] and a model for actin-myosin complex has been constructed [ PUBMED:8316858 ].

This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament [ PUBMED:3783701 , PUBMED:26150528 ]. It contains skip residues that confers local relaxation surrounding them and allows the transition of the coiled-coil to a nonclose-packed structure [ PUBMED:26150528 ]. The coiled-coil region provides the structural backbone of the thick filament [ PUBMED:3783701 , PUBMED:26150528 ].

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
(12)
Full
(15751)
Representative proteomes UniProt
(25854)
RP15
(1944)
RP35
(4929)
RP55
(11938)
RP75
(15913)
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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
(12)
Full
(15751)
Representative proteomes UniProt
(25854)
RP15
(1944)
RP35
(4929)
RP55
(11938)
RP75
(15913)
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
(12)
Full
(15751)
Representative proteomes UniProt
(25854)
RP15
(1944)
RP35
(4929)
RP55
(11938)
RP75
(15913)
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_356 (release 4.1)
Previous IDs: Myosin_tail;
Type: Coiled-coil
Sequence Ontology: SO:0001080
Author: Bashton M , Bateman A
Number in seed: 12
Number in full: 15751
Average length of the domain: 746.4 aa
Average identity of full alignment: 36 %
Average coverage of the sequence by the domain: 51.29 %

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 38.1 38.1
Trusted cut-off 38.1 38.1
Noise cut-off 38.0 38.0
Model length: 1081
Family (HMM) version: 22
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_tail_1 domain has been found. There are 91 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
A0A044QLW3 View 3D Structure Click here
A0A044R6Q2 View 3D Structure Click here
A0A044S407 View 3D Structure Click here
A0A044TQH0 View 3D Structure Click here
A0A044TUC5 View 3D Structure Click here
A0A044UFP3 View 3D Structure Click here
A0A044UIR8 View 3D Structure Click here
A0A077Z422 View 3D Structure Click here
A0A077Z5K1 View 3D Structure Click here
A0A077Z6U9 View 3D Structure Click here
A0A077Z8E1 View 3D Structure Click here
A0A0G2JX91 View 3D Structure Click here
A0A0G2JY53 View 3D Structure Click here
A0A0G2L354 View 3D Structure Click here
A0A0G2L365 View 3D Structure Click here
A0A0J9XNP0 View 3D Structure Click here
A0A0K0DSA2 View 3D Structure Click here
A0A0K0DZH9 View 3D Structure Click here
A0A0K0E2W2 View 3D Structure Click here
A0A0K0E5X3 View 3D Structure Click here
A0A0K0EJG7 View 3D Structure Click here
A0A0K0ELR7 View 3D Structure Click here
A0A0K0ELW6 View 3D Structure Click here
A0A0K0EN49 View 3D Structure Click here
A0A0K0JD94 View 3D Structure Click here
A0A0N4STT5 View 3D Structure Click here
A0A0N4U0S1 View 3D Structure Click here
A0A0N4UBK4 View 3D Structure Click here
A0A0N4UK33 View 3D Structure Click here
A0A0N4UK34 View 3D Structure Click here
A0A0N4ULV5 View 3D Structure Click here
A0A0R4IJY6 View 3D Structure Click here
A0A0R4J7R2 View 3D Structure Click here
A0A158Q371 View 3D Structure Click here
A0A158Q5I3 View 3D Structure Click here
A0A175W8F9 View 3D Structure Click here
A0A2R8Q4J2 View 3D Structure Click here
A0A2R8Q7G9 View 3D Structure Click here
A0A2R8Q9M0 View 3D Structure Click here
A0A2R8QG07 View 3D Structure Click here