Why Can’t I Dm On Domain_10

Protein family

DM domain

Drosophila melanogaster doublesex (dsx), nmr, 18 structures

Identifiers
Symbol DM
Pfam PF00751
InterPro IPR001275
SMART SM00718
SCOP2 1rvv / Telescopic / SUPFAM
Available poly peptide structures:
Pfam structures / ECOD
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In molecular biology the
DM domain
is a protein domain first discovered in the doublesex proteins of
Drosophila melanogaster
and is also seen in
C. elegans
and mammalian proteins.[1]
In
D. melanogaster
the doublesex gene controls somatic sexual differentiation by producing alternatively spliced mRNAs encoding related sexual activity-specific polypeptides.[2]
These proteins are believed to office as transcription factors on downstream sex-determination genes, especially on neuroblast differentiation and yolk protein genes transcription.[3]
[4]

The DM domain binds DNA as a dimer, allowing the recognition of pseudopalindromic sequences .[2]
[5]
[half dozen]
The NMR analysis of the DSX DM domain
[half-dozen]
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

[edit]

Proteins with the DM domain are found in many model organisms. Many
C. elegans
Mab
proteins comprise this domain, the best-known ane being mab-three.[1]
Human proteins containing this domain include DMRT1, DMRT2, DMRT3, DMRTA1, DMRTA2, DMRTB1, and DMRTC2; each of these take a mouse homolog.[7]

Dmrt1-specific
Identifiers
Symbol Dmrt1
Pfam PF12374
InterPro IPR022114
Available protein structures:
Pfam structures / ECOD
PDB RCSB PDB; PDBe; PDBj
PDBsum construction summary

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.[8]

: species tree

Jpred predicts the man version of the department to be mostly coils; it also suggests a weak similarity to
PDB: 6BO4​ by BLAST.[9]

DMRTA motif
Identifiers
Symbol DMA
Pfam PF03474
InterPro IPR005173
Bachelor protein structures:
Pfam structures / ECOD
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

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.[10]

References

[edit]

  1. ^


    a




    b




    Raymond CS, Shamu CE, Shen MM, Seifert KJ, Hirsch B, Hodgkin J, Zarkower D (February 1998). “Evidence for evolutionary conservation of sex-determining genes”.
    Nature.
    391
    (6668): 691–5. Bibcode:1998Natur.391..691R. doi:10.1038/35618. PMID 9490411. S2CID 11414843.


  2. ^


    a




    b




    Erdman SE, Chen HJ, Burtis KC (December 1996). “Functional and genetic characterization of the oligomerization and DNA binding properties of the Drosophila doublesex proteins”.
    Genetics.
    144
    (4): 1639–52. PMC1207715. PMID 8978051.



  3. ^


    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”.
    EMBO J.
    10
    (9): 2577–82. doi:10.1002/j.1460-2075.1991.tb07798.ten. PMC452955. PMID 1907913.



  4. ^


    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”.
    Prison cell.
    54
    (vii): 1019–31. doi:10.1016/0092-8674(88)90117-1. PMID 3046751. S2CID 1386352.



  5. ^


    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”.
    Evolution.
    126
    (5): 873–81. PMID 9927589.


  6. ^


    a




    b




    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”.
    Genes Dev.
    xiv
    (14): 1750–64. PMC316782. PMID 10898790.



  7. ^


    “Proteins matched: DM Dna-binding domain (IPR001275) filtered past species (Human being sapiens)”.
    InterPro.



  8. ^


    “Family: Dmrt1 (PF12374)”.
    Pfam.



  9. ^


    “Jpred results (MTECSGTSQPPPASVPTTAASEGRMVIQDIPAVTSRGHVENTPD)”.
    www.compbio.dundee.ac.u.k.. Archived from the original on ten April 2019. Retrieved
    ten April
    2019
    .



  10. ^


    “Species: DMRTA motif (IPR005173)”.
    InterPro
    . Retrieved
    10 April
    2019
    .




Source: https://en.wikipedia.org/wiki/DM_domain