This family contains a number of hypothetical proteins of about 450 residues in length. Their function is unknown, and most are bacterial. However, structurally this family is part of the 6 hairpin glycosidase superfamily, suggesting a glycosyl hydrolase function.
This family includes proteins from bacteria and fungi. It was originally identified as a protein of unknown function from Schizosaccharomyces pombe, which was isolated from a screen to identify novel genes required for meiosis [ (PUBMED:16303567) ]. Members of this family have since been characterised from Streptococcus pneumoniae (A0A0H2URZ6) and Clostridium perfringens (Q8XNB2), and represent a new glycoside hydrolase family, also known as GH125. This family is the first characterized metal-independent alpha-mannosidase family [ (PUBMED:21388958) ]. Proteins in this family have been reported to be strict exo-alpha-1,6-mannosidases that operate via a metal-independent inverting catalytic mechanism [ (PUBMED:21388958) ].
Family alignment:
There are 3685 DUF1237 domains in 3685 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing DUF1237 domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with DUF1237 domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing DUF1237 domain in the selected taxonomic class.
Analysis of a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Streptococcus pneumoniae SP_2144 apo-structure
Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 1-deoxymannojirimycin complex
Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Streptococcus pneumoniae SP_2144 non-productive substrate complex with alpha-1,6-mannobiose
Analysis of a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Clostridium perfringens CPE0426 apo-structure
Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose