The domain within your query sequence starts at position 22 and ends at position 99; the E-value for the R3H domain shown below is 3.06e-15.

ESRRKAREQAARLKKLQEQDKQQKVEFRKRDSGQVKKKFQPMNKIERSILHDVVEVAGLT
SFSFGEDDDCRYVMIFKK

R3H

Putative single-stranded nucleic acids-binding domain
R3H
SMART accession number:SM00393
Description: -
Interpro abstract (IPR001374):

The R3H domain is a conserved sequence motif found in proteins from a diverse range of organisms including eubacteria, green plants, fungi and various groups of metazoans, but not in archaea and Escherichia coli. The domain is named R3H because it contains an invariant arginine and a highly conserved histidine, that are separated by three residues. It also displays a conserved pattern of hydrophobic residues, prolines and glycines. It can be found alone, in association with AAA domain or with various DNA/RNA binding domains like DSRM, KH, G-patch, PHD, DEAD box, or RRM. The functions of these domains indicate that the R3H domain might be involved in polynucleotide-binding, including DNA, RNA and single-stranded DNA [(PUBMED:9787637)].

The 3D structure of the R3H domain has been solved. The fold presents a small motif, consisting of a three-stranded antiparallel beta-sheet, against which two alpha-helices pack from one side. This fold is related to the structures of the YhhP protein and the C-terminal domain of the translational initiation factor IF3. Three conserved basic residues cluster on the same face of the R3H domain and could play a role in nucleic acid recognition. An extended hydrophobic area at a different site of the molecular surface could act as a protein-binding site [(PUBMED:12547203)].

GO function:nucleic acid binding (GO:0003676)
Family alignment:
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There are 10310 R3H domains in 10308 proteins in SMART's nrdb database.

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