Summary: Thymopoietin protein
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Thymopoietin protein Provide feedback
Short protein of 49 amino acid isolated from bovine spleen cells [1]. Thymopoietins (TMPOs) are a group of ubiquitously expressed nuclear proteins. They are suggested to play an important role in nuclear envelope organisation and cell cycle control [2].
Literature references
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Audhya T, Schlesinger DH, Goldstein G; , Biochemistry 1981;20:6195-6200.: Complete amino acid sequences of bovine thymopoietins I, II, and III: closely homologous polypeptides. PUBMED:7306506 EPMC:7306506
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Weber PJ, Eckhard CP, Gonser S, Otto H, Folkers G, Beck-Sickinger AG; , Biol Chem 1999;380:653-660.: On the role of thymopoietins in cell proliferation. Immunochemical evidence for new members of the human thymopoietin family. PUBMED:10430029 EPMC:10430029
External database links
| PANDIT: | PF08198 |
| Pseudofam: | PF08198 |
| SYSTERS: | Thymopoietin |
This tab holds annotation information from the InterPro database.
InterPro entry IPR013146
This entry included thymopoietins; short proteins of 49 amino acid isolated from bovine spleen cells [PUBMED:7306506]. Thymopoietins (TMPOs) are a group of ubiquitously expressed nuclear proteins. They are suggested to play an important role in nuclear envelope organisation and cell cycle control [PUBMED:10430029].
Thymopoietins are characterised by LEM (LAP2, emerin, MAN1) domain, this is a globular module of approximately 40 amino acids, which is mostly found in the nucleoplasmic portions of metazoan inner nuclear membrane proteins. The LEM domain has been shown to mediate binding to BAF (barrier-to-autointegration factor) and BAF-DNA complexes. BAF dimers bind to double-stranded DNA non-specifically and thereby bridge DNA molecules to form a large, discrete nucleoprotein complex [PUBMED:14618255, PUBMED:10671519].
The resolution of the solution structure of the LEM domain reveals that it is composed of a three-residue N-terminal helical turn and two large parallel alpha helices interacting through a set of conserved hydrophobic amino acids. The two helices, which are connected by a long loop are oriented at an angle of ~45 degree [PUBMED:11435115].
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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics 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 (7) |
Full (109) |
Representative proteomes | NCBI (92) |
Meta (0) |
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| RP15 (6) |
RP35 (10) |
RP55 (23) |
RP75 (42) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
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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.
| Seed (7) |
Full (109) |
Representative proteomes | NCBI (92) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (6) |
RP35 (10) |
RP55 (23) |
RP75 (42) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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
| Seed source: | Short protein clustering |
| Previous IDs: | none |
| Type: | Family |
| Author: | Rossi R |
| Number in seed: | 7 |
| Number in full: | 109 |
| Average length of the domain: | 48.90 aa |
| Average identity of full alignment: | 74 % |
| Average coverage of the sequence by the domain: | 11.69 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 49 | ||||||||||||
| Family (HMM) version: | 6 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
LEMStructures
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 Thymopoietin domain has been found. There are 2 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 seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence