Summary: Proteasome subunit A N-terminal signature
Proteasome subunit A N-terminal signature Provide feedback
This domain is conserved in the A subunits of the proteasome complex proteins.
Internal database links
|SCOOP:||Nup160 Nbas_N PD40|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000426
The proteasome (or macropain) (EC) [PUBMED:7682410, PUBMED:2643381, PUBMED:1317508, PUBMED:7697118, PUBMED:8882582] is a eukaryotic and archaeal multicatalytic proteinase complex that seems to be involved in an ATP/ubiquitin-dependent nonlysosomal proteolytic pathway. In eukaryotes the proteasome is composed of about 28 distinct subunits which form a highly ordered ring-shaped structure (20S ring) of about 700 kDa. Most proteasome subunits can be classified on the basis of sequence similarities into two groups, alpha (A) and beta (B).
Subunits that belong to the A group are proteins of from 210 to 290 amino acids. They are classified as non-peptidase homologues in MEROPS peptidase family T1 (clan PB(T)).
This entry represents an N-terminal domain conserved in the A subunits of the proteasome complex.
|Cellular component||proteasome core complex, alpha-subunit complex (GO:0019773)|
|Molecular function||endopeptidase activity (GO:0004175)|
|Biological process||ubiquitin-dependent protein catabolic process (GO:0006511)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
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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
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
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- an HTML-based viewer that uses DAS to retrieve alignment fragments on request
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Key: available, not generated, — not available.
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Curation and family details
|Author:||Finn R, Coggill P|
|Number in seed:||74|
|Number in full:||2896|
|Average length of the domain:||22.80 aa|
|Average identity of full alignment:||63 %|
|Average coverage of the sequence by the domain:||9.05 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||4|
|Download:||download the raw HMM for this family|
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The tree shows the occurrence of this domain across different species. More...
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There are 2 interactions 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 Proteasome_A_N domain has been found. There are 763 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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