SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.

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gi 26344560  72 IRRWTTKHVAVWLKDEGFFEYVDILCNKHRLDGITLLTLTEYDLRSPPLEIKVLGDIKRLMLSVRKLQK 140
Cdd:cd09515   1 VHEWTCEDVAKWLKKEGFSKYVDLLCNKHRIDGKVLLSLTEEDLRSPPLEIKVLGDIKRLWLAIRKLQR 69

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26344560  72 IRRWTTKHVAVWLKDEGFFEYVDILCNKHRLDGITLLTLTEYDLRSPPLEIKVLGDIKRLMLSVRKLQK 140
Cdd:cd09515   1 VHEWTCEDVAKWLKKEGFSKYVDLLCNKHRIDGKVLLSLTEEDLRSPPLEIKVLGDIKRLWLAIRKLQR 69

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 26344560    75 WTTKHVAVWLKDEGFFEYVDILcNKHRLDGITLLTLTEYDLRSppLEIKVLGDIKRLMLSVRKL 138
Cdd:pfam00536   3 WSVEDVGEWLESIGLGQYIDSF-RAGYIDGDALLQLTEDDLLK--LGVTLLGHRKKILYAIQRL 63

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26344560  72 IRRWTTKHVAVWLKDEGFFEYVDILCNKHRLDGITLLTLTEYDLRSPPLEIKVLGDIKRLMLSVRKLQK 140
Cdd:cd09515   1 VHEWTCEDVAKWLKKEGFSKYVDLLCNKHRIDGKVLLSLTEEDLRSPPLEIKVLGDIKRLWLAIRKLQR 69

SAM domain of sphingomyelin synthase; SAM (sterile alpha motif) domain of SGMS-1 (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. Sphingomyelin synthase 1 is a transmembrane protein with a SAM domain at the N-terminus and a catalytic domain at the C-terminus. Sphingomyelin synthase 1 is a Golgi-associated enzyme, and depending on the concentration of diacylglycerol and ceramide, can catalyze synthesis phosphocholine or sphingomyelin, respectively. It plays a central role in sphingolipid and glycerophospholipid metabolism.

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gi 26344560  72 IRRWTTKHVAVWLKDEGFFEYVDILcnkHRLDGITLLTLTEYDLRSPPLEiKVLGDIKRLML 133
Cdd:cd09514   4 VVQWSPKEVSDWLSEEGMQEYSEAL---RSFDGQALLNLTEEDFKKTPLS-LVSSDSGRQLL 61

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 26344560  80 VAVWLKDEGFFEYVDILcNKHRLDGITLLTLTEYDLRSppLEIKVLGDIKRLMLSVRK 137
Cdd:cd09487   2 VAEWLESLGLEQYADLF-RKNEIDGDALLLLTDEDLKE--LGITSPGHRKKILRAIQR 56

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).

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gi 26344560  73 RRWTTKHVAVWLKDEGFFEYVdilCNK---HRLDGITLLTLTEYDLRSppLEIKVLGDIKRLMLSVRKLQ 139
Cdd:cd09535   1 RSWSPEQVAEWLLSAGFDDSV---CEKfreNEITGDILLELDLEDLKE--LDIGSFGKRFKLWNEIKSLR 65

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 26344560     75 WTTKHVAVWLKDEGFFEYVDILcNKHRLDGITLLTLT-EYDLRSppLEIKVLGDIKRLMLSVRKLQK 140
Cdd:smart00454   4 WSPESVADWLESIGLEQYADNF-RKNGIDGALLLLLTsEEDLKE--LGITKLGHRKKILKAIQKLKE 67

SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases. The SAM domain is located at the C-terminus of two out of three isoforms of DGK-eta protein. DGK-eta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DCK-eta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-delta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it is responsible for sustained endosomal localization of the protein and resulted in negative regulation of DCK-eta catalytic activity.

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gi 26344560  72 IRRWTTKHVAVWLKDEGFFEYVDILCnKHRLDGITLLTLTEYDLRSppLEIKVLGDIKRLMLSVRKL 138
Cdd:cd09576   2 VQKWGTDEVAAWLDLLSLGEYKEIFI-RHDIRGSELLHLERRDLKD--LGIPKVGHMKRILQGIKEL 65

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 26344560  72 IRRWTTKHVAVWLKDEGFF-EYVDILCnKHRLDGITLLTLTEYDL 115
Cdd:cd09509   1 PSKWSVDDVAQFIKSLDGCaEYAEVFR-EQEIDGQALLLLTEDDL 44