SAM domain of aveugle-like subfamily; SAM (sterile alpha motif) domain of SAM_aveugle-like subfamily is a protein-protein interaction domain. In Drosophila, the aveugle (AVE) protein (also known as HYP (Hyphen)) is involved in normal photoreceptor differentiation, and required for epidermal growth factor receptor (EGFR) signaling between ras and raf genes during eye development and wing vein formation. SAM domain of the HYP(AVE) protein interacts with SAM domain of CNK, the multidomain scaffold protein connector enhancer of kinase suppressor of ras. CNK/HYP(AVE) complex interacts with KSR (kinase suppressor of Ras) protein. This interaction leads to stimulation of Ras-dependent Raf activation. This subfamily also includes vertebrate AVE homologs - Samd10 and Samd12 proteins. Their exact function is unknown, but they may play a role in signal transduction during embryogenesis.

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gi 148675489 139 RPVVLWSQQDVCKWLKKHCPHNYLVYVEAFSQHAITGRALLRLNADKLQRMGLTQEAQRQEVLQQVLHLQVREEG 213
Cdd:cd09510    1 KPVYLWSVQDVCKWLKRHCPDYYLLYAELFLQHDITGRALLRLNDNKLERMGITDEDHRQDILREILKLRLKTEI 75

SAM domain of aveugle-like subfamily; SAM (sterile alpha motif) domain of SAM_aveugle-like subfamily is a protein-protein interaction domain. In Drosophila, the aveugle (AVE) protein (also known as HYP (Hyphen)) is involved in normal photoreceptor differentiation, and required for epidermal growth factor receptor (EGFR) signaling between ras and raf genes during eye development and wing vein formation. SAM domain of the HYP(AVE) protein interacts with SAM domain of CNK, the multidomain scaffold protein connector enhancer of kinase suppressor of ras. CNK/HYP(AVE) complex interacts with KSR (kinase suppressor of Ras) protein. This interaction leads to stimulation of Ras-dependent Raf activation. This subfamily also includes vertebrate AVE homologs - Samd10 and Samd12 proteins. Their exact function is unknown, but they may play a role in signal transduction during embryogenesis.

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gi 148675489 139 RPVVLWSQQDVCKWLKKHCPHNYLVYVEAFSQHAITGRALLRLNADKLQRMGLTQEAQRQEVLQQVLHLQVREEG 213
Cdd:cd09510    1 KPVYLWSVQDVCKWLKRHCPDYYLLYAELFLQHDITGRALLRLNDNKLERMGITDEDHRQDILREILKLRLKTEI 75

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 148675489   141 VVLWSQQDVCKWLKKHcphNYLVYVEAFSQHAITGRALLRL-NADKLQRMGLTQEAQRQEVLQQVLHLQ 208
Cdd:smart00454   1 VSQWSPESVADWLESI---GLEQYADNFRKNGIDGALLLLLtSEEDLKELGITKLGHRKKILKAIQKLK 66

SAM domain of aveugle-like subfamily; SAM (sterile alpha motif) domain of SAM_aveugle-like subfamily is a protein-protein interaction domain. In Drosophila, the aveugle (AVE) protein (also known as HYP (Hyphen)) is involved in normal photoreceptor differentiation, and required for epidermal growth factor receptor (EGFR) signaling between ras and raf genes during eye development and wing vein formation. SAM domain of the HYP(AVE) protein interacts with SAM domain of CNK, the multidomain scaffold protein connector enhancer of kinase suppressor of ras. CNK/HYP(AVE) complex interacts with KSR (kinase suppressor of Ras) protein. This interaction leads to stimulation of Ras-dependent Raf activation. This subfamily also includes vertebrate AVE homologs - Samd10 and Samd12 proteins. Their exact function is unknown, but they may play a role in signal transduction during embryogenesis.

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gi 148675489 139 RPVVLWSQQDVCKWLKKHCPHNYLVYVEAFSQHAITGRALLRLNADKLQRMGLTQEAQRQEVLQQVLHLQVREEG 213
Cdd:cd09510    1 KPVYLWSVQDVCKWLKRHCPDYYLLYAELFLQHDITGRALLRLNDNKLERMGITDEDHRQDILREILKLRLKTEI 75

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 148675489  144 WSQQDVCKWLKK-HCPHnylvYVEAFSQHAITGRALLRLNADKLQRMGLT 192
Cdd:pfam00536   3 WSVEDVGEWLESiGLGQ----YIDSFRAGYIDGDALLQLTEDDLLKLGVT 48

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.

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gi 148675489 139 RPVVLWSQQDVCKWLKKHcphNYLVYVEAFSQHAITGRALLRLNADKLQRMGLT 192
Cdd:cd09512    2 RPVSEWSVQQVCQWLMGL---GLEQYIPEFTANNIDGQQLLQLDSSKLKALGIT 52

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 148675489 144 WSQQDVCKWLKKH-CPHnylvYVEAFSQHAITGRALLRLNADKLQRMGLT 192
Cdd:cd09534    1 WDEEFVEEWLNELnCGQ----YLDIFEKNLITGDLLLELDKEALKELGIT 46

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 148675489 144 WSQQDVCKWLKK--HCPHnylvYVEAFSQHAITGRALLRLNADKLQR-MGL 191
Cdd:cd09509    4 WSVDDVAQFIKSldGCAE----YAEVFREQEIDGQALLLLTEDDLLKgMGL 50

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 148675489 140 PVVLWSQQDVCKWLKKHcphNYLVYVEAFSQHAITGRALLRLNADKLQRMGLTQEAQRQ 198
Cdd:cd09506    1 PVHEWTVDDVGDWLESL---NLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRM 56

SAM domain of MLTK subfamily; SAM (sterile alpha motif) domain of MLTK subfamily is a protein-protein interaction domain. Besides SAM domain, these proteins have N-terminal protein tyrosine kinase domain and leucine-zipper motif. Proteins of this group act as mitogen-activated protein triple kinase in a number of MAPK cascades. They can be activated by autophosphorylation in response to stress signals. MLTK-alpha is known to phosphorylate histone H3. In mammals, MLTKs participate in the activation of the JNK/SAPK, p38, ERK5 pathways, the transcriptional factor NF-kB, in the regulation of the cell cycle checkpoint, and in the induction of apoptosis in a hepatoma cell line. Some members of this subfamily are proto-oncogenes, thus MLTK-alpha is involved in neoplasmic cell transformation and/or skin cancer development in athymic nude mice. Based on in vivo coprecipitation experiments in mammalian cells, it has been demonstrated that MLTK proteins might form homodimers/oligomers via their SAM domains.

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gi 148675489 144 WSQQDVCKWLKKH-----CPHNYLVYVEAFSQHAITGRALLRLNADKLQRMGLTQEAQRqevlqqvLHLQ 208
Cdd:cd09529    2 WTEEDVHFWMQQLvrkggHPSELSQYADLFKENHITGKRLLLLTEEDLRDMGIGSKGHI-------IHLK 64

SAM domain of Samd3 subfamily; SAM (sterile alpha motif) domain of the Samd3 subfamily is a putative protein-protein interaction domain. Proteins of this subfamily have a SAM domain at the N-terminus. SAM is a widespread domain in signaling and regulatory proteins. In many cases SAM mediates dimerization/oligomerization. Exact function of proteins belonging to this subfamily is unknown.

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gi 148675489 144 WSQQDVCKWLKKhcpHNYLVYVEAFSQHAITGRALLRLNADKLQRmgLTQEAQRQEVLQQVL 205
Cdd:cd09526    4 WSVEQVCNWLVE---KNLGELVPRFQEEEVSGAALLALNDRMVQQ--LVKKIGHQAVLMDLI 60

SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta.

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gi 148675489 140 PVVLWSQQDVCKWLKKHCphnYLVYVEAFSQHAITGRALLRLNADKLQRMGLTQEAQRQEVLQQVLHL 207
Cdd:cd09575    1 PVHLWGTEEVAAWLEHLS---LCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65

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 148675489 144 WSQQDVCKWLKK--HCPhnylvYVEAF-SQHAITGRALLRLNADKLQRMGL 191
Cdd:cd09515    4 WTCEDVAKWLKKegFSK-----YVDLLcNKHRIDGKVLLSLTEEDLRSPPL 49