The domain within your query sequence starts at position 1 and ends at position 504; the E-value for the Proteasom_PSMB domain shown below is 3.8e-199.
MAAQAVSLLREVARLEAPLEELRALQSVVQAVPLHELREQAAELRLRPLFSLLNQNNREQ TALCVSILERLLQAVEPIHLARNLRLDLQRGLTHPDDSVKTLTLSQIGRIVENSEAVTEI LNNAELLKQIVYCIGGENLSVAKAAIKSLSRISLTQAGLEALFESNLLDDLKNVMKTNDV VRYRVYELIIDISSVSSESLNYCTTSGLVTQLLKELTGEDVLVRATCIEMVTSLAYTHHG RQYLAQEGVIDQISNIIVGADSDPFSGFYLPGFVKFFGNLAVMDSPQQICERYPVFLEKV FEMADSQDPTMIGVAVDTVGILGSSVEGKQVLQKTGTRFERVLMRVGYQAKNASTELKIR CLDAVSSLLYLSPEQQTDDFLGMTESWFSSMSRDSLELFRGISNQPFPELHCAALKVFTA IADQPWAQRLMFNSPGFVEFVMDRSVEHDKASKDAKYELVKALANSKTVAEIFGNSNYLR LRAYLSEGPYYVKPVATTAVEGAD
Proteasom_PSMB |
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PFAM accession number: | PF10508 |
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Interpro abstract (IPR019538): | The 26S proteasome is an enzymatic complex that degrades ubiquitinated proteins in eukaryotic cells. 26S proteasome non-ATPase regulatory subunit 5 (PSMD5) is one of a number of chaperones that are involved in the assembly of the proteasome. The chaperones dissociate before 26S proteasome formation is complete [ (PUBMED:19490896) ]. TNF-alpha/NFkB inhibits 26S proteasome assembly via abnormal expression of PSMD5, establishing a link between inflammation and chronic neurodegenerative diseases with altered ubiquitin-proteasome system function [ (PUBMED:22921402) ]. |
GO process: | proteasome assembly (GO:0043248) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Proteasom_PSMB