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 270483848   7 MKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLYRVSSDNGQRLLDMIETLKMEHH 78
Cdd:cd09514    1 MKEVVQWSPKEVSDWLSEEGMQEYSEALRSFDGQALLNLTEEDFKKTPLSLVSSDSGRQLLEMIETLKIEHH 72

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 270483848   7 MKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLYRVSSDNGQRLLDMIETLKMEHH 78
Cdd:cd09514    1 MKEVVQWSPKEVSDWLSEEGMQEYSEALRSFDGQALLNLTEEDFKKTPLSLVSSDSGRQLLEMIETLKIEHH 72

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 270483848    10 VVYWSPKKVADWLLENAMPEYCEPLE--HFTGQDLINLTQEDFKK-----PPLYRvssdngQRLLDMIETLK 74
Cdd:smart00454   1 VSQWSPESVADWLESIGLEQYADNFRknGIDGALLLLLTSEEDLKelgitKLGHR------KKILKAIQKLK 66

PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 270483848 289 SGHTVMLTLTYLFIKEYSPRRLW--WYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYH 354
Cdd:cd01610   55 SGHAAFAFALALFLALLLPRRLLrlLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLVL 122

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 270483848   7 MKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLYRVSSDNGQRLLDMIETLKMEHH 78
Cdd:cd09514    1 MKEVVQWSPKEVSDWLSEEGMQEYSEALRSFDGQALLNLTEEDFKKTPLSLVSSDSGRQLLEMIETLKIEHH 72

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 270483848  13 WSPKKVADWLLENAMPEYCEPL---EHFTGQDLINLTQEDFKKPPL-YRVSSDNgQRLLDMIETLKME 76
Cdd:cd09515    4 WTCEDVAKWLKKEGFSKYVDLLcnkHRIDGKVLLSLTEEDLRSPPLeIKVLGDI-KRLWLAIRKLQRQ 70

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 270483848  18 VADWLLENAMPEYCEPLEH--FTGQDLINLTQEDFKKPPLyrVSSDNGQRLLDMIET 72
Cdd:cd09487    2 VAEWLESLGLEQYADLFRKneIDGDALLLLTDEDLKELGI--TSPGHRKKILRAIQR 56

SAM domain of CP2-like transcription factors; SAM (sterile alpha motif) domain of CP2-like transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and some also have a C-terminal dimerization domain. CP2-like family of transcriptional factors includes three subgroups: LBP1, TFCP2, and LBP9. Members of this family are involved in transcriptional regulation from early development to terminal differentiation. They play a role in regulation of expression of P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in placenta, and alpha-globin in erythroid cells. They are required for proper maturation of the dust (epithelial component of tubular organs) of kidney and salivary gland. Human LBP1 is known to be induced by HIV type I infection in lymphocytes; it represses HIV transcription by preventing the binding of TFIID to the virus promoter. Additionally, it has been suggested that UBP1 (LBP1) regulator might be a member of a blood pressure controlling network. LBP1 protein isoforms are able to form dimers apparently via SAM domain since SAM deletion or mutation resulted in a loss of this ability.

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                 ....*....|....*....|....*....|....*..
gi 270483848  14 SPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDF 50
Cdd:cd09537    1 SPQQTTQWLRKNRFGAYLRTFSNFSGADLLRLTRDDL 37

SAM domain of CNK1,2,3-suppressor subfamily; SAM (sterile alpha motif) domain of CNK (connector enhancer of kinase suppressor of ras (Ksr)) subfamily is a protein-protein interaction domain. CNK proteins are multidomain scaffold proteins containing a few protein-protein interaction domains and are required for connecting Rho and Ras signaling pathways. In Drosophila, the SAM domain of CNK is known to interact with the SAM domain of the aveugle protein, forming a heterodimer. Mutation of the SAM domain in human CNK1 abolishes the ability to cooperate with the Ras effector, supporting the idea that this interaction is necessary for proper Ras signal transduction.

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gi 270483848  13 WSPKKVADWL--LENAMPEYCEPLE--HFTGQDLINLTQED 49
Cdd:cd09511    4 WSPKQVTDWLkgLDDCLQQYIYTFEreKVTGEQLLNLSPQD 44

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 270483848   12 YWSPKKVADWLLENAMPEYCEPLEH--FTGQDLINLTQEDFKK----PPLYRvssdngQRLLDMIETLK 74
Cdd:pfam00536   2 GWSVEDVGEWLESIGLGQYIDSFRAgyIDGDALLQLTEDDLLKlgvtLLGHR------KKILYAIQRLK 64

Sterile alpha motif (SAM)/Pointed domain of ESE-like ETS transcriptional regulators; SAM Pointed domain of ESE-like (Epithelium-Specific ETS) subfamily of ETS transcriptional regulators is a putative protein-protein interaction domain. It can act as a major transactivator by providing a potential docking site for co-activators. ETS factors are important for cell differentiation. They can be involved in regulation of gene expression in different types of epithelial cells. They are expressed in salivary gland, intestine, stomach, pancreas, lungs, kidneys, colon, mammary gland, and prostate. Members of this group are proto-oncogenes. Expression profiles of these factors are altered in epithelial cancers, which makes them potential targets for cancer therapy.

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gi 270483848  12 YWSPKKVADWLL----ENAMPEYCEPLEHF---TGQDLINLTQEDFK 51
Cdd:cd08757    4 HWTKNDVLDWLLfvaeQNKIDAEEINFQKFdniDGQTLCSMSLEEFI 50

SAM domain of LBP9 transcriptional factors; SAM (sterile alpha motif) domain of LBP9 (also known as TFCP2L1 or CRTR-1 (CP2-Related Transcriptional Repressor-1)) transcription factor is a putative protein-protein interaction domain. Proteins of this group have an N-terminal DNA-binding CP2 domain, a central predicted SAM domain and a C-terminal dimerization domain. They are involved in transcriptional regulation from early development to terminal differentiation. In particular, they are required for proper maturation of the dust (epithelial component of tubular organs) of kidney and salivary gland as well as for regulation of P450scc (the cholesterol side-chain cleavage enzyme, cytochrome) in human placenta.

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                 ....*....|....*....|....*....|....*..
gi 270483848  14 SPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDF 50
Cdd:cd09590    1 SIQDAQQWLHRNRFSQFCRLFSSFSGADLLKMSRDDF 37