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31  structures 1351  species 0  interactions 7673  sequences 499  architectures

Family: DHC_N1 (PF08385)

Summary: Dynein heavy chain, N-terminal region 1

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 "Dynein". More...

Dynein Edit Wikipedia article

Dyenin can be divided into two groups:

Cytoplasmic dynein and Axonemal dynein.

The Axonomal dynein acts to activate a sliding within flagellar microtubules, wherease the Cytoplasmic dynein is implcated in moving toward the negative end of a microtubule.

See also:

Kinesin How Cilia and Flagella Work (Axonomal Dynein) Microtubule Based Movement (Cytoplasmic dynein)

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.

Dynein heavy chain, N-terminal region 1 Provide feedback

Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit [1]. The region featured in this family includes the sequences implicated in mediating these interactions [2]. It is thought to be flexible and not to adopt a rigid conformation [1].

Literature references

  1. King SM; , J Cell Sci 2000;113:2521-2526.: AAA domains and organization of the dynein motor unit. PUBMED:10862709 EPMC:10862709

  2. Habura A, Tikhonenko I, Chisholm RL, Koonce MP; , J Biol Chem 1999;274:15447-15453.: Interaction mapping of a dynein heavy chain. Identification of dimerization and intermediate-chain binding domains. PUBMED:10336435 EPMC:10336435

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR013594

Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit [ PUBMED:10862709 ]. The region featured in this family includes the sequences implicated in mediating these interactions [ PUBMED:10336435 ]. It is thought to be flexible and not to adopt a rigid conformation [ PUBMED:10862709 ].

Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. Dyneins generally contain one to three heavy chains, which belong to the AAA+ superfamily of mechanochemical enzymes [ PUBMED:9927482 ]. Each heavy chain consists of a flexible N-terminal tail known as the cargo-binding domain [ PUBMED:15661525 ] and a motor domain which consists of an ATP-hydrolysing AAA+ ring, a flexible microtubule-binding stalk, a linker and a C-sequence [ PUBMED:22398446 ]. The stalk has an ATP-sensitive microtubule-binding site (MTBD) at its tip [ PUBMED:9403697 , PUBMED:9242627 ], whereas the linker has been suggested to function as a mechanical element for generating dynein's power stroke [ PUBMED:12610617 , PUBMED:19203583 , PUBMED:15880123 ].

The two categories of dyneins are the axonemal dyneins, which produce the bending motions that propagate along cilia and flagella, and the cytosolic dyneins, which drive a variety of fundamental cellular processes including nuclear migration, organisation of the mitotic spindle, chromosome separation during mitosis, and the positioning and function of many intracellular organelles. Cytoplasmic dyneins contain several accessory subunits ranging from light to intermediate chains.

Domain organisation

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

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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.

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

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

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Representative proteomes UniProt

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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.

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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...


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_3094 (release 18.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Fenech M
Number in seed: 195
Number in full: 7673
Average length of the domain: 436.7 aa
Average identity of full alignment: 19 %
Average coverage of the sequence by the domain: 14.13 %

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 28.3 28.3
Trusted cut-off 28.3 28.3
Noise cut-off 28.1 28.2
Model length: 562
Family (HMM) version: 15
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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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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The tree shows the occurrence of this domain across different species. More...


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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 DHC_N1 domain has been found. There are 31 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
A0A0R4IUQ6 View 3D Structure Click here
A0A158Q610 View 3D Structure Click here
A0A3P7E2W2 View 3D Structure Click here
A1ZAD3 View 3D Structure Click here
Q4CPG2 View 3D Structure Click here
Q4DEV6 View 3D Structure Click here
Q4DKP5 View 3D Structure Click here