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 1731010437 237 VSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQ 290
Cdd:cd09487     2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55

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 1731010437 237 VSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQ 290
Cdd:cd09487     2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55

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 1731010437  232 NDTNVVSRWLEEVGFGKYAGVFEIHEVDEEALPLLTI-EDLKEIGVFSVGSRRKLYNAIQQLR 293
Cdd:smart00454   4 WSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66

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 1731010437 237 VSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQ 290
Cdd:cd09487     2 VAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQ 55

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 1731010437  232 NDTNVVSRWLEEVGFGKYAGVFEIHEVDEEALPLLTI-EDLKEIGVFSVGSRRKLYNAIQQLR 293
Cdd:smart00454   4 WSPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSeEDLKELGITKLGHRKKILKAIQKLK 66

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 1731010437 237 VSRWLEEVGFGKY-AGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQQLR 293
Cdd:cd09535     8 VAEWLLSAGFDDSvCEKFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEIKSLR 65

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.

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gi 1731010437 241 LEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQQLR 293
Cdd:cd09520    11 LAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAISELN 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 1731010437 237 VSRWLEEVGFGKYAGVF-EIHEVDEEALPLLTIEDLK----EIGVFsvGSRRKLYNAIQQLR 293
Cdd:cd09515     9 VAKWLKKEGFSKYVDLLcNKHRIDGKVLLSLTEEDLRspplEIKVL--GDIKRLWLAIRKLQ 68

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 1731010437 233 DTNVVSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQQL 292
Cdd:cd09506     6 TVDDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65

SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) group is a potential protein-protein interaction domain. Sec23ip proteins (also known as p125) contain an N-terminal proline-rich region, a central region containing a SAM domain and a C-terminal region with a predicted metal-binding domain. Sec23ip interacts with Sec23p/Sec24p part of COPII-coated vesicles complex involved in protein transport from the ER to the Golgi apparatus. The proline-rich region plays an essential role in this interaction. Overexpression of Sec23ip leads to disorganization of ER/Golgi intermediate compartment.

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gi 1731010437 230 EDNDTNVVSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVfSVGSRRKLYNAIQQ 291
Cdd:cd09584     5 EEEDVPSLQSVLEALSLSEYKSTFEKEKIDMESLLMCTVDDLKEMGI-PLGPRKKIANFVKE 65

SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) proteins, also known as LRSAM1 (Leucine-rich repeat and sterile alpha motif-containing) proteins, is a putative protein-protein interaction domain. Proteins of this subfamily participate in the regulation of retrovirus budding and receptor endocytosis. They show E3 ubiquitin ligase activity. Human TAL protein interacts with Tsg101 and TAL's C-terminal ring finger domain is essential for the multiple monoubiquitylation of Tsg101.

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gi 1731010437 230 EDNDTNVVSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQQLR 293
Cdd:cd09523     1 EAGVDPQLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQELL 64

SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a putative protein-protein interaction domain. This subfamily includes proteins related to human kinesin-like protein KIF24. SAM domain is located at the N-terminus followed by kinesin motor domain. Kinesins are proteins involved in a number of different cell processes including microtubule dynamics and axonal transport. Kinesins of this group belong to N-type; they drive microtubule plus end-directed transport. SAM apparently plays the role of adaptor or scaffold domain. In many cases SAM is known as a mediator of dimerization/oligomerization.

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gi 1731010437 235 NVVSRWLEEVGFGKYAGVFEIHEV-DEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQQLR 293
Cdd:cd09541     1 SVLYEWLEEAGLQHYYPAFAAGGVtSIEALAQLTMQDYASLGVQDMEDKQKLFRLIQTLK 60

SAM domain of liprin-beta1,2 proteins repeat 2; SAM (sterile alpha motif) domain repeat 2 of liprin-beta1,2 proteins is a protein-protein interaction domain. Liprin-beta proteins contain three copies (repeats) of SAM domain. They may form heterodimers with liprin-alpha proteins through their SAM domains. It was suggested based on bioinformatic approaches that the second SAM domain of liprin-beta potentially is able to form polymers. Liprins were originally identified as LAR (leukocyte common antigen-related) transmembrane protein-tyrosine phosphatase-interacting proteins. They participate in mammary gland development, in axon guidance, and in the maintenance of lymphatic vessel integrity.

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gi 1731010437 233 DTNVVSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQQLR 293
Cdd:cd09566     3 DTHWVLRWLDDIGLPQYKDAFSEAKVDGRMLHYLTVDDLLHLKVTSALHHASIRRGIQVLR 63

SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 interacting protein) subfamily is a potential protein-protein interaction domain. This group of proteins includes Sec23ip and DDHD2 proteins. All of them contain at least two domains: a SAM domain and a predicted metal-binding domain. For mammalian DDHD2 members of this group, phospholipase activity has been demonstrated. Sec23ip proteins of this group interact with Sec23 proteins via an N-terminal proline-rich region. Members of this subfamily are involved in organization of ER/Golgi intermediate compartment.

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gi 1731010437 241 LEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVfSVGSRRKLYNAIQQ 291
Cdd:cd09516    16 LEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGI-PMGPRKKLLGFLKD 65

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.

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gi 1731010437 232 NDTNVVSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQQLR 293
Cdd:cd09497     2 PDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQ 63

SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential protein-protein interaction domain. DDHD2 proteins contain at least two domains:a SAM domain and a predicted metal-binding domain. Phospholipase A1 activity was demonstrated for the mammalian DDHD2 protein. Mutation of the putative catalytic serine resulted in elimination of activity. Unlike SEC23IP, DDHD2 proteins do not have an N-terminal proline-rich region and correspondingly they are not able to interact with Sec23p/Sec24p complex. Overexpression of DDHD2 is the cause of dispersion of ER/Golgi intermediate compartment and dispersion of tethering proteins located in the Golgi region, leading to aggregation in the endoplasmic reticulum.

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gi 1731010437 233 DTNVVSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVfSVGSRRKLYNAIQQLR 293
Cdd:cd09585     8 DTPTLEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGI-PLGPRKKILNYIRRRF 67

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 1731010437 234 TNVVSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQQL 292
Cdd:cd09575     7 TEEVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65

SAM domain of EPH family of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH (erythropoietin-producing hepatocyte) family of receptor tyrosine kinases is a C-terminal signal transduction module located in the cytoplasmic region of these receptors. SAM appears to mediate cell-cell initiated signal transduction via binding proteins to a conserved tyrosine that is phosphorylated. In some cases the SAM domain mediates homodimerization/oligomerization and plays a role in the clustering process necessary for signaling. EPH kinases are the largest family of receptor tyrosine kinases. They are classified into two groups based on their abilities to bind ephrin-A and ephrin-B ligands. The EPH receptors are involved in regulation of cell movement, shape, and attachment during embryonic development; they control cell-cell interactions in the vascular, nervous, epithelial, and immune systems, and in many tumors. They are potential molecular markers for cancer diagnostics and potential targets for cancer therapy.

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gi 1731010437 237 VSRWLEEVGFGKYAGVFEIHEVDE-EALPLLTIEDLKEIGVFSVGSRRKLYNAIQQL 292
Cdd:cd09488     5 VGEWLESIKMGRYKENFTAAGYTSlDAVAQMTAEDLTRLGVTLVGHQKKILNSIQAL 61

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 1731010437 234 TNVVSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQQL 292
Cdd:cd09576     7 TDEVAAWLDLLSLGEYKEIFIRHDIRGSELLHLERRDLKDLGIPKVGHMKRILQGIKEL 65

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 1731010437 237 VSRWLEEVGFGKYAGVFEIHEVDEEALPLLTIEDLKE-IGVFSVGSRRKLYNAIQQLR 293
Cdd:cd09501     9 VQTWLKQIGFEDYAEKFSESQVDGDLLLQLTEDELKQdLGMSSGLLRKRFLRELVELK 66

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 1731010437 233 DTNVVSRWLEEVGF--GKYAGVFEIHEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQQLR 293
Cdd:cd09508     6 DPEDVCQFLRGNGFgePELLEIFRENEITGAHLPDLTESRLEKLGVSSLGERLKLLKCLQKLS 68

SAM domain of EPH-B6 subfamily of tyrosine kinase receptors; SAM (sterile alpha motif) domain of EPH-B6 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-B6 receptors and appears to mediate cell-cell initiated signal transduction. Receptors of this type are highly expressed in embryo and adult nervous system, in thymus and also in T-cells. They are involved in regulation of cell adhesion and migration. (EPH-B6 receptor is unusual; it fails to show catalytic activity due to alteration in kinase domain). EPH-B6 may be considered as a biomarker in some types of tumors; EPH-B6 activates MAP kinase signaling in lung adenocarcinoma, suppresses metastasis formation in non-small cell lung cancer, and slows invasiveness in some breast cancer cell lines.

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gi 1731010437 240 WLEEVGFGKY------AGVFEIHEVDEealplLTIEDLKEIGVFSVGSRRKLYNAIQQLR 293
Cdd:cd09555    12 WLSAIGLECYqdnfskFGLCTFSDVAQ-----LSLEDLPALGITLAGHQKKLLHHIQLLQ 66

SAM domain of VTS1 RNA-binding proteins; SAM (sterile alpha motif) domain of VTS1 subfamily proteins is RNA binding domain located in the C-terminal region. SAM interacts with stem-loop structures of mRNA. Proteins of this subfamily participate in regulation of transcript stability and degradation, and also may be involved in vacuolar protein transport regulation. VTS1 protein of S.cerevisiae induces mRNA degradation via the major deadenylation-dependent mRNA decay pathway; VTS1 recruits CCR4/POP2/NOT deadenylase complex to target mRNA. The recruitment is the initial step resulting in poly(A) tail removal transcripts. Potentially SAM domain may be responsible not only for RNA binding but also for deadenylase binding.

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gi 1731010437 237 VSRWLEEVGFGKYAGVFEihEVDEEALPLLTIEDLKEIGVFSVGSRRKLYNAIQQLR 293
Cdd:cd09556     9 IPAWLRSLRLHKYTDNLK--DLSWKELIELDDEDLEDKGVSALGARRKLLKAFEIVR 63