4  structures 464  species 1  interaction 1184  sequences 5  architectures

Family: CRS1_YhbY (PF01985)

Summary

CRS1 / YhbY (CRM) domain Add an annotation

Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants [4]. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing [5]. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes [4]. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome [1].


Literature references

  1. Ostheimer GJ, Barkan A, Matthews BW; , Structure (Camb) 2002;10:1593-1601.: Crystal structure of E. coli YhbY: a representative of a novel class of RNA binding proteins. PUBMED:12429100

  2. Willis MA, Krajewski W, Chalamasetty VR, Reddy P, Howard A, Herzberg O; , Proteins 2002;49:423-426.: Structure of HI1333 (YhbY), a putative RNA-binding protein from Haemophilus influenzae. PUBMED:12360533

  3. Till B, Schmitz-Linneweber C, Williams-Carrier R, Barkan A; , RNA 2001;7:1227-1238.: CRS1 is a novel group II intron splicing factor that was derived from a domain of ancient origin. PUBMED:11565746

  4. Barkan A, Klipcan L, Ostersetzer O, Kawamura T, Asakura Y, Watkins KP; , RNA. 2007;13:55-64.: The CRM domain: an RNA binding module derived from an ancient ribosome-associated protein. PUBMED:17105995

  5. Asakura Y, Barkan A; , Plant Cell. 2007;19:3864-3875.: A CRM domain protein functions dually in group I and group II intron splicing in land plant chloroplasts. PUBMED:18065687


InterPro entry IPR001890

The CRM domain is an ~100-amino acid RNA-binding domain. The name chloroplast RNA splicing and ribosome maturation (CRM) has been suggested to reflect the functions established for the four characterised members of the family: Zea mays (Maize) CRS1 (), CAF1 () and CAF2 () proteins and the Escherichia coli protein YhbY (). The CRM domain is found in eubacteria, archaea, and plants. The CRM domain is represented as a stand-alone protein in archaea and bacteria, and in single- and multi-domain proteins in plants. It has been suggested that prokaryotic CRM proteins existed as ribosome-associated proteins prior to the divergence of archaea and bacteria, and that they were co-opted in the plant lineage as RNA binding modules by incorporation into diverse protein contexts. Plant CRM domains are predicted to reside not only in the chloroplast, but also in the mitochondrion and the nucleo/cytoplasmic compartment. The diversity of the CRM domain family in plants suggests a diverse set of RNA targets PUBMED:12881426, PUBMED:17105995.

The CRM domain is a compact alpha/beta domain consisting of a four-stranded beta sheet and three alpha helices with an alpha-beta-alpha-beta-alpha-beta-beta topology. The beta sheet face is basic, consistent with a role in RNA binding. Proximal to the basic beta sheet face is another moiety that could contribute to nucleic acid recognition. Connecting strand beta1 and helix alpha2 is a loop with a six amino acid motif, GxxG flanked by large aliphatic residues, within which one 'x' is typically a basic residue PUBMED:12429100.

Escherichia coli YhbY is associated with pre-50S ribosomal subunits, which implies a function in ribosome assembly. GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants PUBMED:17105995. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing PUBMED:18065687. In vitro experiments with an isolated maize CRM domain have shown it to have RNA binding activity. These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes PUBMED:17105995. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome PUBMED:11565746.

Gene Ontology

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

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Trees

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Enright A
Previous IDs: UPF0044;
Type: Domain
Author: Enright A, Ouzounis C, Bateman A
Number in seed: 155
Number in full: 1184
Average length of the domain: 83.80 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 34.05 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.8 20.8
Trusted cut-off 21.3 21.6
Noise cut-off 19.9 20.0
Model length: 84
Family (HMM) version: 14
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Species distribution

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Interactions

There is 1 interaction for this family. More...

CRS1_YhbY

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 sequences and three-dimensional protein structures. The table below shows the structures on which the CRS1_YhbY domain has been found.

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