The domain within your query sequence starts at position 16 and ends at position 140; the E-value for the PAX domain shown below is 9.7e-91.
GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYET GSIKPGVIGGSKPKVATPKVVDKIAEYKRQNPTMFAWEIRDRLLAEGICDNDTVPSVSSI NRIIR
PAX |
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PFAM accession number: | PF00292 |
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Interpro abstract (IPR001523): | The paired domain is an approximately 126 amino acid DNA-binding domain, which is found in eukaryotic transcription regulatory proteins involved in embryogenesis. The domain was originally described as the 'paired box' in the Drosophila protein paired (prd) [ (PUBMED:2877747) (PUBMED:3123319) ]. The paired domain is generally located in the N-terminal part. An octapeptide [ (PUBMED:10811620) ] and/or a homeodomain can occur C-terminal to the paired domain, as well as a Pro-Ser-Thr-rich C terminus. Paired domain proteins can function as transcription repressors or activators. The paired domain contains three subdomains, which show functional differences in DNA-binding. The crystal structures of prd and Pax proteins show that the DNA-bound paired domain is bipartite, consisting of an N-terminal subdomain (PAI or NTD) and a C-terminal subdomain (RED or CTD), connected by a linker. PAI and RED each form a three-helical fold, with the most C-terminal helices comprising a helix-turn-helix (HTH) motif that binds the DNA major groove. In addition, the PAI subdomain encompasses an N-terminal beta-turn and beta-hairpin, also named 'wing', participating in DNA-binding. The linker can bind into the DNA minor groove. Different Pax proteins and their alternatively spliced isoforms use different (sub)domains for DNA-binding to mediate the specificity of sequence recognition [ (PUBMED:11103953) (PUBMED:15148315) ]. Some proteins known to contain a paired domain:
The Pax proteins:
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GO process: | regulation of transcription, DNA-templated (GO:0006355) |
GO function: | DNA binding (GO:0003677) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry PAX