|SCOP2||1rvv / Telescopic / SUPFAM|
In molecular biology the
is a protein domain first discovered in the doublesex proteins of
and is also seen in
and mammalian proteins.
the doublesex gene controls somatic sexual differentiation by producing alternatively spliced mRNAs encoding related sexual activity-specific polypeptides.
These proteins are believed to office as transcription factors on downstream sex-determination genes, especially on neuroblast differentiation and yolk protein genes transcription.
The DM domain binds DNA as a dimer, allowing the recognition of pseudopalindromic sequences .
The NMR analysis of the DSX DM domain
revealed a novel zinc module containing ‘intertwined’ CCHC and HCCC zinc-binding sites. The recognition of the DNA requires the carboxy-last basic tail which contacts the small-scale groove of the target sequence.
Proteins with this domain
Proteins with the DM domain are found in many model organisms. Many
proteins comprise this domain, the best-known ane being mab-three.
Human proteins containing this domain include DMRT1, DMRT2, DMRT3, DMRTA1, DMRTA2, DMRTB1, and DMRTC2; each of these take a mouse homolog.
DMRT1 homologs have an additional mutual domain C-terminal to the DM domain. This domain is only constitute in bony vertebrates, and neither its structure nor role is unknown.
: species tree
Jpred predicts the man version of the department to be mostly coils; it also suggests a weak similarity to
DMRTA proteins have an boosted motif in their C-termina. This motif, ubiquitous in eukaryotes, has an unknown office. Information technology is similar in sequence to some ubiquitin-associated motifs.
Raymond CS, Shamu CE, Shen MM, Seifert KJ, Hirsch B, Hodgkin J, Zarkower D (February 1998). “Evidence for evolutionary conservation of sex-determining genes”.
(6668): 691–5. Bibcode:1998Natur.391..691R. doi:10.1038/35618. PMID 9490411. S2CID 11414843.
Erdman SE, Chen HJ, Burtis KC (December 1996). “Functional and genetic characterization of the oligomerization and DNA binding properties of the Drosophila doublesex proteins”.
(4): 1639–52. PMC1207715. PMID 8978051.
Burtis KC, Coschigano KT, Baker BS, Wensink PC (September 1991). “The doublesex proteins of Drosophila melanogaster demark directly to a sex-specific yolk protein cistron enhancer”.
(9): 2577–82. doi:10.1002/j.1460-2075.1991.tb07798.ten. PMC452955. PMID 1907913.
Shen MM, Hodgkin J (September 1988). “mab-three, a cistron required for sex-specific yolk poly peptide expression and a male-specific lineage in C. elegans”.
(vii): 1019–31. doi:10.1016/0092-8674(88)90117-1. PMID 3046751. S2CID 1386352.
Yi W, Zarkower D (February 1999). “Similarity of DNA binding and transcriptional regulation by Caenorhabditis elegans MAB-three and Drosophila melanogaster DSX suggests conservation of sex determining mechanisms”.
(5): 873–81. PMID 9927589.
Zhu Fifty, Wilken J, Phillips NB, Narendra U, Chan K, Stratton SM, Kent SB, Weiss MA (July 2000). “Sexual dimorphism in diverse metazoans is regulated by a novel course of intertwined zinc fingers”.
(14): 1750–64. PMC316782. PMID 10898790.
“Proteins matched: DM Dna-binding domain (IPR001275) filtered past species (Human being sapiens)”.
“Family: Dmrt1 (PF12374)”.
“Jpred results (MTECSGTSQPPPASVPTTAASEGRMVIQDIPAVTSRGHVENTPD)”.
www.compbio.dundee.ac.u.k.. Archived from the original on ten April 2019. Retrieved
“Species: DMRTA motif (IPR005173)”.