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 1785359810  30 PAHWAVDDVVNYFKTAGFEEQASAFKEQEIDGKSLLLMTRNDVLTGLSLKLGPALKIYEYHVKPLQTQH 98
Cdd:cd09583     1 PSNWSVEDVVQYFKTAGFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQQSH 69

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 1785359810  30 PAHWAVDDVVNYFKTAGFEEQASAFKEQEIDGKSLLLMTRNDVLTGLSLKLGPALKIYEYHVKPLQTQH 98
Cdd:cd09583     1 PSNWSVEDVVQYFKTAGFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQQSH 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 1785359810  32 HWAVDDVVNYFKTAGFEEQASAFKEQEIDGKSLLLMTRNDvLTGLS-LKLGPALKIY 87
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDD-LLKLGvTLLGHRKKIL 57

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 1785359810  30 PAHWAVDDVVNYFKTAGFEEQASAFKEQEIDGKSLLLMTRNDVLTGLSLKLGPALKIYEYHVKPLQTQH 98
Cdd:cd09583     1 PSNWSVEDVVQYFKTAGFPEEANAFKEQEIDGKSLLLLTRSDVLTGLSLKLGPALKIYEHVVKLQQQSH 69

SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-3MBT3,4 (Sex comb on midleg, Malignant brain tumor) subfamily proteins (also known as L3mbtl3,4 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are predicted transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain three MBT repeats and Zn finger domain. Murine L3mbtl3 protein of this subfamily is essential for maturation of myeloid progenitor cells during differentiation. Human L3mbtl4 is a potential tumor suppressor gene in breast cancer, while deregulation of L3MBTL3 is associated with neuroblastoma.

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gi 1785359810  30 PAHWAVDDVVNYFKT-AGFEEQASAFKEQEIDGKSLLLMTRNDVLTGLSLKLGPALKIY 87
Cdd:cd09582     1 VLRWSVDEVAEFVQSlPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIY 59

SAM domain of Scm proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm (Sex comb on midleg) subfamily of Polycomb group is a protein-protein interaction domain. Proteins of this subfamily are transcriptional repressors associated with PRC1 complex. This group includes invertebrate Scm protein and chordate Scm homolog 1 and Scm-like 1, 2, 3 proteins. Most have a SAM domain, two MBT repeats, and a DUF3588 domain, except Scm-like 4 proteins which do not have MBT repeats. Originally the Scm protein was described in Drosophila as a regulator required for proper spatial expression of homeotic genes. It plays a major role during early embryogenesis. SAM domains of Scm proteins can interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with SAM domains of Ph (polyhomeotic) 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. Mammalian Scmh1 protein is known be indispensible member of PRC1 complex; it plays a regulatory role for the complex during meiotic prophase of male sperm cells, and is particularly involved in regulation of chromatin modification at the XY chromatin domain of the pachytene spermatocytes.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785359810  29 DPAHWAVDDVVNYFKTAgfEEQASA-----FKEQEIDGKSLLLMTRNDVLTGLSLKLGPALKIYeYHVKPLQ 95
Cdd:cd09578     3 DPSTWSVEDVVQFIKEA--DPQALAphvdlFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLC-YHIDKLK 71

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 1785359810  33 WAVDDVVNYFKT-AGFEEQASAFKEQEIDGKSLLLMTRNDVLTGLSLKLGPALKI 86
Cdd:cd09579     4 WTVDDVCSFIGSlPGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKI 58

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 1785359810   30 PAHWAVDDVVNYFKTAGFEEQASAFKEQEIDGKSLLLMTRNDVLTGL-SLKLGPALKI 86
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELgITKLGHRKKI 58

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 1785359810  33 WAVDDVVNYFKTAGFEEQ-ASAFKEQEIDGKSLLLMTRND 71
Cdd:cd09535     3 WSPEQVAEWLLSAGFDDSvCEKFRENEITGDILLELDLED 42

SAM domain ot SARM1-like proteins, repeat 1; SAM (sterile alpha motif) domain repeat 1 of SARM1-like adaptor proteins is a protein-protein interaction domain. SARM1-like proteins contain two tandem SAM domains. SARM1-like proteins are involved in TLR (Toll-like receptor) signaling. They are responsible for targeted localization of the whole protein to post-synaptic regions of axons. In humans SARM1 expression is detected in kidney and liver.

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                  ....*....|....*....|....*....|....*....|....*....
gi 1785359810  33 WAVDDVVNYFKTAGFEEQASAFKEQEIDGKSLLLMTRNDVLTGLSLKLG 81
Cdd:cd09501     4 WSVADVQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQDLGMSSG 52

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.

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gi 1785359810  33 WAVDDVVNYFKTAGFEEQASAFKEQEIDGKSLLLMTRNDvLTGLSLK 79
Cdd:cd09506     5 WTVDDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKED-LTELGVT 50

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 1785359810  30 PAHWAVDDVVNYFKTAGFEEQASAF-KEQEIDGKSLLLMTRNDV 72
Cdd:cd09515     1 VHEWTCEDVAKWLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDL 44

SAM domain (Sterile alpha motif);

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                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785359810  33 WAVDDVVNYFKTAGFEEQASAFKEQEIDGKSLLL-MTRNDvLTGLS-LKLGPALKI 86
Cdd:pfam07647   4 WSLESVADWLRSIGLEQYTDNFRDQGITGAELLLrLTLED-LKRLGiTSVGHRRKI 58

SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

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                  ....*....|....*....|....*....|....*....|.
gi 1785359810  46 GFEEQASAFKEQEIDGKSLLLMTRNDvLTGLSLKLGPALKI 86
Cdd:cd09517    13 HLEEYLPVFEREKIDLEALMLLTDED-LQSLKLPLGPRRKL 52