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.

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gi 1878247266 704 VTKWTVDDVCSFVGGLSGCGEYTRVFREQGIDGETLPLLTEEHLLTNMGLKLGPALKIRAQVARRLGR 771
Cdd:cd09579     1 IRKWTVDDVCSFIGSLPGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKIRSQVAKRLGR 68

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.

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gi 1878247266 704 VTKWTVDDVCSFVGGLSGCGEYTRVFREQGIDGETLPLLTEEHLLTNMGLKLGPALKIRAQVARRLGR 771
Cdd:cd09579     1 IRKWTVDDVCSFIGSLPGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKIRSQVAKRLGR 68

SAND domain;

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gi 1878247266  114 PCIEVECGANRALLYVRKLCQGSKGPSIRHRGEWLTPNEFQFVSGRETAKDWKRSIRHKGKSLKTLMSKGILQ 186
Cdd:smart00258   1 SELPVTCGTVKGILYKKKFKCGISVKCIQYEDKWFTPKEFEIEGGKGKSKDWKRSIRCGGSSLRTLMENGTLD 73

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.

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gi 1878247266 706 KWTVDDVCSFVGGLsGCGEYTRVFREQGIDGETLPLLTEEHLLTNMGLKLGPALKI 761
Cdd:pfam00536   2 GWSVEDVGEWLESI-GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKI 56

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.

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gi 1878247266 704 VTKWTVDDVCSFVGGLSGCGEYTRVFREQGIDGETLPLLTEEHLLTNMGLKLGPALKIRAQVARRLGR 771
Cdd:cd09579     1 IRKWTVDDVCSFIGSLPGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKIRSQVAKRLGR 68

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.

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gi 1878247266 704 VTKWTVDDVCSFVGGLSGCGEYTRVFREQGIDGETLPLLTEEHLLTNMGLKLGPALKIRAQVAR 767
Cdd:cd09509     1 PSKWSVDDVAQFIKSLDGCAEYAEVFREQEIDGQALLLLTEDDLLKGMGLKLGPALKIYNHIVK 64

SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain of Ph (polyhomeotic) proteins of Polycomb group is a protein-protein interaction domain. Ph1,2,3 proteins are members of PRC1 complex. This complex is involved in transcriptional repression of Hox (Homeobox) cluster genes. It is recruited through methylated H3Lys27 and supports the repression state by mediating monoubiquitination of histone H2A. Proteins of the Ph1,2,3 subfamily contribute to anterior-posterior neural tissue specification during embryogenesis. Additionally, the P2 protein of zebrafish is known to be involved in epiboly and tailbud formation. SAM domains of Ph proteins may interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with the SAM domain of Scm (sex comb on midleg) proteins, forming heterooligomers. Homooligomers are similar to the ones formed by SAM Pointed domains of the TEL proteins. Such SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome.

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gi 1878247266 703 DVTKWTVDDVCSFVGGLSGCGEYTRVFREQGIDGETLPLLTEEHLLTNMGLKLGPALKIRAQV 765
Cdd:cd09577     2 NPSKWSVEDVYEFIRSLPGCSDYAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKI 64

SAM domain of Atherin/Atherin-like subfamily; SAM (sterile alpha motif) domain of SAM_Atherin and Atherin-like subfamily proteins is a putative protein-protein and/or protein-lipid interaction domain. In addition to the C-terminal SAM domain, the majority of proteins belonging to this group also have PHD (or Zn finger) domain. As potential members of the polycomb group, these proteins may be involved in regulation of some key regulatory genes during development. Atherin can be recruited by Ruk/CIN85 kinase-binding proteins via its SH3 domains thus participating in the signal transferring kinase cascades. Also, atherin was found associated with low density lipids (LDL) in atherosclerotic lesions in human. It was suggested that atherin plays an essential role in atherogenesis via immobilization of LDL in the arterial wall. SAM domains of atherins are predicted to form polymers. Inhibition of polymer formation could be a potential antiatherosclerotic therapy.

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gi 1878247266 704 VTKWTVDDVCSFVGGlSGCGEYTRVFREQGIDGETLPLLTEEHLLTNMGLKLGPALKIRAQVAR 767
Cdd:cd09583     1 PSNWSVEDVVQYFKT-AGFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVK 63

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.

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gi 1878247266  704 VTKWTVDDVCSFVGGLsGCGEYTRVFREQGIDGETLPLLTEEHLLTNMG-LKLGPALKI 761
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLLLTSEEDLKELGiTKLGHRKKI 58

SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-4MBT1,2 (Sex comb on midleg, Malignant Brain Tumor) subfamily proteins (also known as Sfmbt1,2 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain four MBT repeats and DUF5388 domain. The MBT repeats of the human sfmbt1 protein are responsible for association with the nuclear matrix and for selective binding of H3 histone N-terminal tails, while the exact function of the SAM domain is unclear.

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gi 1878247266 706 KWTVDDVCSFVGgLSGCGEYTRVFREQGIDGETLPLLTEEHLLTNMGLKLGPALKIRAQVAR 767
Cdd:cd09581    14 FWSVDDVVRFIK-STDCAPLAKIFKDQEIDGQALLLLTLPTVQECMELKLGPAIKLCHHIER 74

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.

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gi 1878247266 711 DVCSFVGGLsGCGEYTRVFREQGIDGETLPLLTEEHLLTNMGLKLGPALKI 761
Cdd:cd09487     1 DVAEWLESL-GLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKI 50

SAM domain of Samd9/Samd9L subfamily; SAM (sterile alpha motif) domain of Samd9/Samd9L subfamily is a putative protein-protein interaction domain. SAM is a widespread domain in signaling proteins. Samd9 is a tumor suppressor gene. It is involved in death signaling of malignant glioblastoma. Samd9 suppression blocks cancer cell death induced by HVJ-E or IFN-beta treatment. Deleterious mutations in Samd9 lead to normophosphatemic familial tumoral calcinosis, a cutaneous disorder characterized by cutaneous calcification or ossification.

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gi 1878247266 706 KWTVDDVCSFVGGLSGCGEYTRVFREQGIDGETLPLLTEEHLLtNMGLKLGPALKI 761
Cdd:cd09528     2 DWTKEHVKQWLIEDLIDKKYAEILYEEEVTGAVLKELTEEDLV-DMGLPHGPALLI 56

SAM domain of HD-phosphohydrolase; SAM (sterile alpha motif) domain of SAM_HD subfamily proteins is a putative protein-protein interaction domain. Proteins of this group, additionally to the SAM domain, contain a HD hydrolase domain. Human SAM-HD1 is a nuclear protein involved in innate immune response and may act as a negative regulator of the cell-intrinsic antiviral response. Mutations in this gene lead to Aicardi-Goutieres syndrome (symptoms include cerebral atrophy, leukoencephalopathy, hepatosplenomegaly, and increased production of alpha-interferon).

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gi 1878247266 703 DVTKWTVDDVCSFV--GGLSGcGEYTRVFREQGIDGETLPLLTEEHlLTNMG 752
Cdd:cd09508     1 DFRSWDPEDVCQFLrgNGFGE-PELLEIFRENEITGAHLPDLTESR-LEKLG 50

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.

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gi 1878247266 707 WTVDDVCSFVGGLsGCGEYTRVFREQGIDGETLPLLTEEHlLTNMGL-KLGPALKIRAQV 765
Cdd:cd09534     1 WDEEFVEEWLNEL-NCGQYLDIFEKNLITGDLLLELDKEA-LKELGItKVGDRIRLLRAI 58

SAM domain of Ste50 fungal subfamily; SAM (sterile alpha motif) domain of Ste50 fungal subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and Ras-associated UBQ superfamily domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response, and contribute to cell wall integrity in vegetative cells. Ste50 of S.cerevisiae acts as an adaptor protein between G protein and MAP triple kinase Ste11. Ste50 proteins are able to form homooligomers, binding each other via their SAM domains, as well as heterodimers and heterogeneous complexes with SAM domain or SAM homodimers of MAPKKK Ste11 protein kinase.

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gi 1878247266 702 EDVTKWTVDDVCSFVGGLSGCGEYTRVF---REQGIDGETLPLLTEEHL--LTNMGLKLGPALKI 761
Cdd:cd09536     1 EEFNEWSTDEVVKWCISSLGLDDGDPLCdrlRENNITGSLLSELTLEDCkeLCDNDLSLAIRLKL 65

Ste50p, sterile alpha motif; The fungal Ste50p SAM domain consists of five helices, which form a compact, globular fold. It is required for mediation of homodimerization and heterodimerization (and in some cases oligomerization) of the protein.

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gi 1878247266 702 EDVTKWTVDDVCSFVGGLSGCGE----YTRVfREQGIDGETLPLLT 743
Cdd:pfam09235   1 SGFNEWSTDEVCKWCKAELGLTEgdplILRI-RENKITGSTLSELT 45