Summary: Thymopoietin protein
Thymopoietin protein Provide feedback
Short protein of 49 amino acid isolated from bovine spleen cells . 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 .
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
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
This tab holds annotation information from the InterPro database.
InterPro entry IPR013146
The LEM (LAP2, emerin, MAN1) domain 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.
All LAP2 isoforms also share an N-terminal segment composed of a LEM domain that is connected to a highly divergent LEM-like domain by a highly flexible 60- residue linker. The LEM-like globular domain has the same size and structural fold as the LEM domain, but has been shown to bind directly to DNA [PUBMED:10671519, PUBMED:11500367, PUBMED:11435115].
This entry represents the LEM-like domain.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||DNA binding (GO:0003677)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
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- the UniProt description of the protein sequence
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We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
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- alignment generated by searching the NCBI sequence database using the family HMM
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Curation and family details
|Seed source:||Short protein clustering|
|Number in seed:||17|
|Number in full:||127|
|Average length of the domain:||47.90 aa|
|Average identity of full alignment:||73 %|
|Average coverage of the sequence by the domain:||11.37 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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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