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212  structures 5002  species 5  interactions 13986  sequences 56  architectures

Clan: PELOTA (CL0101)

Summary

Pelota - RNA ribose binding superfamily Add an annotation

The members of this clan are all involved in binding to ribose sugar of RNA[1]. Indeed, the key RNA binding residues are conserved across the different families [1]. Members of this clan form mixed alpha-helical and beta-sheet structures [1][2].

This clan contains 5 families and the total number of domains in the clan is 13986. The clan was built by RD Finn.

Literature references

  1. Anantharaman V, Koonin EV, Aravind L;, Nucleic Acids Res. 2002;30:1427-1464.: Comparative genomics and evolution of proteins involved in RNA metabolism. PUBMED:11917006 EPMC:11917006
  2. Michel G, Sauve V, Larocque R, Li Y, Matte A, Cygler M; , Structure (Camb) 2002;10:1303-1315.: The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot. PUBMED:12377117 EPMC:12377117

Members

This clan contains the following 5 member families:

eRF1_3 PELOTA_1 Ribosomal_L7Ae RNase_P_pop3 SpoU_sub_bind

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures from this clan. More...

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Alignments

The table below shows the number of occurrences of each domain throughout the sequence database. More...

Pfam family Num. domains Alignment
SpoU_sub_bind (PF08032) 7167 (51.2%) View
Ribosomal_L7Ae (PF01248) 5260 (37.6%) View
eRF1_3 (PF03465) 1128 (8.1%) View
PELOTA_1 (PF15608) 343 (2.5%) View
RNase_P_pop3 (PF08228) 88 (0.6%) View
Total: 5 Total: 13986 Clan alignment
 

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Family relationships

This diagram shows the relationships between members of this clan. More...

Species distribution

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This tree shows the occurrence of the domains in this clan across different species. More...

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Interactions

There are 5 interactions for this clan. More...

Interacting families
A B
eRF1_3 eRF1_1
eRF1_2
SpoU_sub_bind SpoU_methylase
Ribosomal_L7Ae Ribosomal_L7Ae
SBP_bac_1

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.

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