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 1034673372 361 SKDPSTWSVDEVIQFMKHTDPQISGPLADLFRQHEIDGKALFLLKSDVMMKYMGLKLGPALKLCYYIEKLKE 432
Cdd:cd09578     1 SKDPSTWSVEDVVQFIKEADPQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLKQ 72

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 1034673372 361 SKDPSTWSVDEVIQFMKHTDPQISGPLADLFRQHEIDGKALFLLKSDVMMKYMGLKLGPALKLCYYIEKLKE 432
Cdd:cd09578     1 SKDPSTWSVEDVVQFIKEADPQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLKQ 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 1034673372  364 PSTWSVDEVIQFMKHTDPQisgPLADLFRQHEIDGKALFLLKSDVMMKYMG-LKLGPALKLCYYIEKLKE 432
Cdd:smart00454   1 VSQWSPESVADWLESIGLE---QYADNFRKNGIDGALLLLLTSEEDLKELGiTKLGHRKKILKAIQKLKE 67

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 1034673372 361 SKDPSTWSVDEVIQFMKHTDPQISGPLADLFRQHEIDGKALFLLKSDVMMKYMGLKLGPALKLCYYIEKLKE 432
Cdd:cd09578     1 SKDPSTWSVEDVVQFIKEADPQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLKQ 72

SAM domain of Ph (polyhomeotic) proteins of Polycomb group; SAM (sterile alpha motif) domain of Ph (polyhomeotic) proteins of Polycomb group is a protein-protein interaction domain. Ph1,2,3 proteins are members of PRC1 complex. This complex is involved in transcriptional repression of Hox (Homeobox) cluster genes. It is recruited through methylated H3Lys27 and supports the repression state by mediating monoubiquitination of histone H2A. Proteins of the Ph1,2,3 subfamily contribute to anterior-posterior neural tissue specification during embryogenesis. Additionally, the P2 protein of zebrafish is known to be involved in epiboly and tailbud formation. SAM domains of Ph proteins may interact with each other, forming homooligomers, as well as with SAM domains of other proteins, in particular with the SAM domain of Scm (sex comb on midleg) 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.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034673372 362 KDPSTWSVDEVIQFMKHTdPQISGpLADLFRQHEIDGKALFLLKSDVMMKYMGLKLGPALKLCYYIEKLKE 432
Cdd:cd09577     1 SNPSKWSVEDVYEFIRSL-PGCSD-YAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKICAKINSLKE 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 1034673372 364 PSTWSVDEVIQFMKHTD-PQisgpLADLFRQHEIDGKALFLLK-SDVMMKyMGLKLGPALKLCYYIEKL 430
Cdd:cd09583     1 PSNWSVEDVVQYFKTAGfPE----EANAFKEQEIDGKSLLLLTrSDVLTG-LSLKLGPALKIYEHVVKL 64

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 1034673372 365 STWSVDEVIQFMKHTDPqisGPLADLFRQHEIDGKALFLLKSDVMMKYMGLKLGPALKLCYYIEKLK 431
Cdd:pfam00536   1 DGWSVEDVGEWLESIGL---GQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 64

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 1034673372  364 PSTWSVDEVIQFMKHTDPQisgPLADLFRQHEIDGKALFLLKSDVMMKYMG-LKLGPALKLCYYIEKLKE 432
Cdd:smart00454   1 VSQWSPESVADWLESIGLE---QYADNFRKNGIDGALLLLLTSEEDLKELGiTKLGHRKKILKAIQKLKE 67

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 1034673372 365 STWSVDEVIQFMKHTDpqISGPLADLFRQHEIDGKALFLLKSDVMMKYMGLKLGPALKL 423
Cdd:cd09579     2 RKWTVDDVCSFIGSLP--GCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKI 58

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 1034673372 371 EVIQFMKHTDPqisGPLADLFRQHEIDGKALFLLkSDVMMKYMGLK-LGPALKLCYYIEK 429
Cdd:cd09487     1 DVAEWLESLGL---EQYADLFRKNEIDGDALLLL-TDEDLKELGITsPGHRKKILRAIQR 56

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 1034673372 366 TWSVDEVIQFMKHT--DPQIsgplADLFRQHEIDGKALFLLKSDvMMKYMGLK-LGPALKLCYYIEKLK 431
Cdd:cd09535     2 SWSPEQVAEWLLSAgfDDSV----CEKFRENEITGDILLELDLE-DLKELDIGsFGKRFKLWNEIKSLR 65

SAM / Pointed domain; A subfamily of the SAM domain

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                   ....*....|....*....|....*....|....*....|....*....
gi 1034673372  356 LKQGFSKDPSTWSVDEVIQFMKHTDPQISGPLADlFRQHEIDGKALFLL 404
Cdd:smart00251   9 KRLGIPADPQLWTEDHVLEWLEWAVKEFSLSPID-FSKFDMSGKELCSM 56