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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3BS7_A       1 KAVYLWTVSDVLKWYRRHCGE-YTQYEQLFAQHDITGRALLRITDSSLQRMGVTDNRDREAIWREIVKQRLKTDI 74
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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3BS7_A       1 KAVYLWTVSDVLKWYRRHCGE-YTQYEQLFAQHDITGRALLRITDSSLQRMGVTDNRDREAIWREIVKQRLKTDI 74
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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3BS7_A          3 VYLWTVSDVLKWYRRHcgEYTQYEQLFAQHDITGRALLRITDSS-LQRMGVTDNRDREAIWREIvkQRLKTD 73
Cdd:smart00454  1 VSQWSPESVADWLESI--GLEQYADNFRKNGIDGALLLLLTSEEdLKELGITKLGHRKKILKAI--QKLKEQ 68

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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3BS7_A       1 KAVYLWTVSDVLKWYRRHCGE-YTQYEQLFAQHDITGRALLRITDSSLQRMGVTDNRDREAIWREIVKQRLKTDI 74
Cdd:cd09510  1 KPVYLWSVQDVCKWLKRHCPDyYLLYAELFLQHDITGRALLRLNDNKLERMGITDEDHRQDILREILKLRLKTEI 75

SAM domain (Sterile alpha motif);

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3BS7_A         6 WTVSDVLKWYRRHcgEYTQYEQLFAQHDITG-RALLRITDSSLQRMGVTDNRDREAIWREIvkQRLK 71
Cdd:pfam07647  4 WSLESVADWLRSI--GLEQYTDNFRDQGITGaELLLRLTLEDLKRLGITSVGHRRKILKKI--QELK 66

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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3BS7_A         6 WTVSDVLKWYRRHcgEYTQYEQLFAQHDITGRALLRITDSSLQRMGVTDNRDREAIWREIvkQRLK 71
Cdd:pfam00536  3 WSVEDVGEWLESI--GLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAI--QRLK 64

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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3BS7_A       6 WTVSDVLKWYRRH------CGEYTQYEQLFAQHDITGRALLRITDSSLQRMGVT 53
Cdd:cd09529  2 WTEEDVHFWMQQLvrkgghPSELSQYADLFKENHITGKRLLLLTEEDLRDMGIG 55

SAM domain of STIM-1,2-like proteins; SAM (sterile alpha motif) domain of STIM-1,2-like (Stromal interaction molecule) proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM1 and STIM2 are involved in opposite regulation of store operated channels in plasma membrane.

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3BS7_A       3 VYLWTVSDVLKWYRrHCGEYTQYEQLFAQHDITGRALLRITDSSLQRM----GVTDNRDREAI 61
Cdd:cd09504  2 VHNWTVEDTVEWLV-NSVELPQYVEAFKENGVDGSALPRLAVNNPSFLtsvlGIKDPIHRQKL 63

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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3BS7_A       6 WTVSDVLKWYrrHCGEYTQYEQLFAQHDITGRALLRITDSSLQRMGVTDNRDreaiwREIVKQRLK 71
Cdd:cd09512  7 WSVQQVCQWL--MGLGLEQYIPEFTANNIDGQQLLQLDSSKLKALGITSSSD-----RSLLKKKLK 65

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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3BS7_A       3 VYLWTVSDVLKWYRRHCgeYTQYEQLFAQHDITGRALLRITDSSLQRMGVT 53
Cdd:cd09575  2 VHLWGTEEVAAWLEHLS--LCEYKDIFTRHDVRGSELLHLERRDLKDLGVT 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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3BS7_A       3 VYLWTVSDVLKWYRR-HCGEYTQyeqLFAQHDITGRALLRITDSSLQRMGVTDNRDREAIWREI 65
Cdd:cd09506  2 VHEWTVDDVGDWLESlNLGEHRE---RFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERAL 62

SAM domain of STIM2 subfamily proteins; SAM (sterile alpha motif) domain of STIM2 (Stromal interaction molecule) subfamily proteins is a putative protein-protein interaction domain. STIM1 and STIM2 human proteins are type I transmembrane proteins. The N-terminal part of them includes "hidden" EF-hand and SAM domains. This region is responsible for sensing changes in store-operated and basal cytoplasmic Ca2+ levels and initiates oligomerization. "Hidden" EF hand and SAM domains have a stable intramolecular association, and the SAM domain is a component that regulates stability within STIM proteins. Destabilization of the EF-SAM association during Ca2+ depletion leads to partial unfolding and aggregation (homooligomerization), thus activating the store-operated Ca2+ entry. Immunoprecipitation analysis indicates that STIM1 and STIM2 can form co-precipitable oligomeric associations in vivo. It was suggested that STIM2 protein is an inhibitor of store operated channels in plasma membrane.

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3BS7_A       3 VYLWTVSDVLKWYRRHCgEYTQYEQLFAQHDITGRALLRITDSS----LQRMGVTDNRDRE 59
Cdd:cd09574  2 VHNWTMEDTLQWLKEFV-ELPQYEKNFRDNNVKGTTLPRIAVNEpsfmISQLKILDRSHRQ 61

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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3BS7_A       5 LWTVSDVLKWYRRHCGEYTQYEQLFAQHDITGRALLRITDSSLQRMGV 52
Cdd:cd09508  4 SWDPEDVCQFLRGNGFGEPELLEIFRENEITGAHLPDLTESRLEKLGV 51

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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3BS7_A       6 WTVSDVLKWYRrhCGEYTQYEQLFA-QHDITGRALLRITDSSL 47
Cdd:cd09515  4 WTCEDVAKWLK--KEGFSKYVDLLCnKHRIDGKVLLSLTEEDL 44

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.

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3BS7_A      28 LFAQHDITGRALLRITDSSLQRMGVTDNRDREAI 61
Cdd:cd09521 23 LFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKI 56