The domain within your query sequence starts at position 34 and ends at position 67; the E-value for the CHCH domain shown below is 2.5e-9.

CAASHFAVQECMAQHQDWRQCQPQVQAFRDCMSA

CHCH

CHCH
PFAM accession number:PF06747
Interpro abstract (IPR010625):

A conserved motif was identified in the LOC118487 protein was called the CHCH motif. Alignment of this protein with related members showed the presence of three subgroups of proteins, which are called the S (Small), N (N-terminal extended) and C (C-terminal extended) subgroups. All three sub-groups of proteins have in common that they contain a predicted conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2] domain (CHCH domain). Within each helix of the CHCH domain, there are two cysteines present in a C-X9-C motif. The N-group contains an additional double helix domain, and each helix contains the C-X9-C motif. This family contains a number of characterised proteins: Cox19 protein - a nuclear gene of Saccharomyces cerevisiae, codes for an 11kDa protein (Cox19p) required for expression of cytochrome oxidase. Because cox19 mutants are able to synthesise the mitochondrial and nuclear gene products of cytochrome oxidase, Cox19p probably functions post-translationally during assembly of the enzyme. Cox19p is present in the cytoplasm and mitochondria, where it exists as a soluble intermembrane protein. This dual location is similar to what was previously reported for Cox17p, a low molecular weight copper protein thought to be required for maturation of the CuA centre of subunit 2 of cytochrome oxidase. Cox19p have four conserved potential metal ligands, these are three cysteines and one histidine. Mrp10 - belongs to the class of yeast mitochondrial ribosomal proteins that are essential for translation [ (PUBMED:9065385) ]. Eukaryotic NADH-ubiquinone oxidoreductase 19kDa (NDUFA8) subunit [ (PUBMED:9860297) ]. The CHCH domain was previously called DUF657 [ (PUBMED:15177562) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry CHCH