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Conserved domains on  [gi|1720408604|ref|XP_017175676|]
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sterile alpha motif domain-containing protein 11 isoform X1 [Mus musculus]

Protein Classification

SAM domain-containing protein( domain architecture ID 81749)

SAM (sterile alpha motif) domain-containing protein may be involved in protein-protein interaction and in developmental regulation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SAM_superfamily super family cl15755
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
457-479 1.15e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


The actual alignment was detected with superfamily member cd09579:

Pssm-ID: 472832  Cd Length: 68  Bit Score: 45.90  E-value: 1.15e-06
                          10        20
                  ....*....|....*....|...
gi 1720408604 457 VNKWTVDDVCNFVGGLSGCGDST 479
Cdd:cd09579     1 IRKWTVDDVCSFIGSLPGCAEYA 23
 
Name Accession Description Interval E-value
SAM_Samd7,11 cd09579
SAM domain of Samd7,11 subfamily of Polycomb group; SAM (sterile alpha motif) domain is a ...
457-479 1.15e-06

SAM domain of Samd7,11 subfamily of Polycomb group; SAM (sterile alpha motif) domain is a protein-protein interaction domain. Phylogenetic analysis suggests that proteins of this subfamily are most closely related to SAM-Ph1,2,3 subfamily of Polycomb group. They are predicted transcriptional repressors in photoreceptor cells and pinealocytes of vertebrates. SAM domain containing protein 11 is also known as Mr-s (major retinal SAM) protein. In mouse, it is predominantly expressed in developing retinal photoreceptors and in adult pineal gland. The SAM domain is involved in homooligomerization of whole proteins (it was shown based on immunoprecipitation assay and mutagenesis), however its repression activity is not due to SAM/SAM interactions but to the C-terminal region.


Pssm-ID: 188978  Cd Length: 68  Bit Score: 45.90  E-value: 1.15e-06
                          10        20
                  ....*....|....*....|...
gi 1720408604 457 VNKWTVDDVCNFVGGLSGCGDST 479
Cdd:cd09579     1 IRKWTVDDVCSFIGSLPGCAEYA 23
 
Name Accession Description Interval E-value
SAM_Samd7,11 cd09579
SAM domain of Samd7,11 subfamily of Polycomb group; SAM (sterile alpha motif) domain is a ...
457-479 1.15e-06

SAM domain of Samd7,11 subfamily of Polycomb group; SAM (sterile alpha motif) domain is a protein-protein interaction domain. Phylogenetic analysis suggests that proteins of this subfamily are most closely related to SAM-Ph1,2,3 subfamily of Polycomb group. They are predicted transcriptional repressors in photoreceptor cells and pinealocytes of vertebrates. SAM domain containing protein 11 is also known as Mr-s (major retinal SAM) protein. In mouse, it is predominantly expressed in developing retinal photoreceptors and in adult pineal gland. The SAM domain is involved in homooligomerization of whole proteins (it was shown based on immunoprecipitation assay and mutagenesis), however its repression activity is not due to SAM/SAM interactions but to the C-terminal region.


Pssm-ID: 188978  Cd Length: 68  Bit Score: 45.90  E-value: 1.15e-06
                          10        20
                  ....*....|....*....|...
gi 1720408604 457 VNKWTVDDVCNFVGGLSGCGDST 479
Cdd:cd09579     1 IRKWTVDDVCSFIGSLPGCAEYA 23
SAM_Polycomb cd09509
SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a ...
457-477 2.04e-03

SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a protein-protein interaction domain. The Polycomb group includes transcriptional repressors which are involved in the regulation of some key regulatory genes during development in many organisms. They are best known for silencing Hox (Homeobox) genes. Polycomb proteins work together in large multimeric and chromatin-associated complexes. They organize chromatin of the target genes and maintain repressed states during many cell divisions. Polycomb proteins are classified based on their common function, but not on conserved domains and/or motifs; however many Polycomb proteins (members of PRC1 class complex) contain SAM domains which are more similar to each other inside of the Polycomb group than to SAM domains outside of it. Most information about structure and function of Polycomb SAM domains comes from studies of Ph (Polyhomeotic) and Scm (Sex comb on midleg) proteins. Polycomb SAM domains usually can be found at the C-terminus of the proteins. Some members of this group contain, in addition to the SAM domain, MTB repeats, Zn finger, and/or DUF3588 domains. Polycomb SAM domains can form homo- and/or heterooligomers through ML and EH surfaces. SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Polycomb proteins are known to be highly expressed in some cells years before their cancer pathology; thus they are attractive markers for early cancer therapy.


Pssm-ID: 188908  Cd Length: 64  Bit Score: 36.69  E-value: 2.04e-03
                          10        20
                  ....*....|....*....|.
gi 1720408604 457 VNKWTVDDVCNFVGGLSGCGD 477
Cdd:cd09509     1 PSKWSVDDVAQFIKSLDGCAE 21
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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