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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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Amos Bairoch

PROSITE documentation PDOC51165
THUMP domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51165

Description

The THUMP (after thiouridine synthases, RNA methylases and pseudouridine synthases) domain is a module of 100-110 amino acid residues which is involved RNA metabolism. It is shared by enzymes that are predicted to carry out at least three unrelated types of RNA-modification, namely methylation, pseudouridylation and thiouridylation. The THUMP domain can occur in stand-alone form or in association with a variety of catalytic domains, like methylase, pseudo U-synthase or rhodanese (see <PDOC00322>). THUMP is an ancient domain with predicted RNA-binding capacity that probably functions by delivering a variety of RNA modification enzymes to their targets. The THUMP domain apparently evolved prior to the divergence of the primary divisions of life [1].

The THUMP domain has been predicted to adopt an α/β fold similar to that found in the C-terminal domain of translation initiation factor 3 and ribosomal protein S8 [1].

Some proteins known to contain a THUMP domain are listed below:

  • Bacterial and archaeal thiI-like 4-thiouridine synthases.
  • Bacterial, archaeal and eukaryotic RNA methylases.
  • Archaeal pseudouridine synthases (PSUSs).
  • Several uncharacterized proteins.

The profile we developed covers the entire THUMP domain.

Last update:

November 2005 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

THUMP, PS51165; THUMP domain profile  (MATRIX)


Reference

1AuthorsAravind L. Koonin E.V.
TitleTHUMP - a predicted RNA-binding domain shared by 4-thiouridine, pseudouridine synthases and RNA methylases.
SourceTrends Biochem. Sci. 26:215-217(2001).
PubMed ID11295541



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