second malignant brain tumor (MBT) repeat found in Polycomb protein sex comb on midleg homolog 1 (SCMH1) and similar proteins; SCMH1 is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. It contains two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023612099 162 PSHNFFKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPPG 236
Cdd:cd20108     1 PSQNFFKTGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRYDSRDIFPVGWCSLTGDNLQPPG 75

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023612099 565 GRDPSSWTVEDVMQFVREADPQ-LGPHADLFRKHEIDGKALLLLRSDMMMKYMGLKLGPALKLSYHIDRLKQ 635
Cdd:cd09578     1 SKDPSTWSVEDVVQFIKEADPQaLAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLKQ 72

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  233 QPPGTKVVIPKNPYPASDVNTEKPSiHSSTKTVLEHQPGqrgrkpGKKRGRTPktlishPISAPSKTAEPLKFPKKRGPK 312
Cdd:PHA03247  2822 ASPAGPLPPPTSAQPTAPPPPPGPP-PPSLPLGGSVAPG------GDVRRRPP------SRSPAAKPAAPARPPVRRLAR 2888

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2023612099  313 PGSKRKPRTLLNPPPASPTTSTPEPDTSTVPQDAATIPSSAMQAP 357
Cdd:PHA03247  2889 PAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPP 2933

second malignant brain tumor (MBT) repeat found in Polycomb protein sex comb on midleg homolog 1 (SCMH1) and similar proteins; SCMH1 is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. It contains two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023612099 162 PSHNFFKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPPG 236
Cdd:cd20108     1 PSQNFFKTGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRYDSRDIFPVGWCSLTGDNLQPPG 75

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023612099 565 GRDPSSWTVEDVMQFVREADPQ-LGPHADLFRKHEIDGKALLLLRSDMMMKYMGLKLGPALKLSYHIDRLKQ 635
Cdd:cd09578     1 SKDPSTWSVEDVVQFIKEADPQaLAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLKQ 72

Present in Drosophila Scm, l(3)mbt, and vertebrate SCML2; Present in Drosophila Scm, l(3)mbt, and vertebrate SCML2. These proteins are involved in transcriptional regulation.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  137 PMFLLKTlnGAEMAPIRIFHKEPPSPSHNFfKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDS 216
Cdd:smart00561   1 EDYLEET--GARAAPVELFKQPVDSPPNGF-KVGMKLEAVDPRNPSLICVATVVEVKGYRLLLHFDGWDDKYDFWCHADS 77

                           90
                   ....*....|....*....
gi 2023612099  217 RDIFPVGWCSLTGDNLQPP 235
Cdd:smart00561  78 PDIFPVGWCEKNGHPLQPP 96

mbt repeat; The function of this repeat is unknown, but is found in a number of nuclear proteins such as drosophila sex comb on midleg protein. The repeat is found in up to four copies as in Swiss:Q9UHJ3. The repeat contains a completely conserved glutamate at its amino terminus that may be important for function.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023612099  62 MKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDSAEIQPIGNCEKNGGMLQPPL 127
Cdd:pfam02820   1 MKLEAVDPLNPSLICVATVVKVLGGRLRLRFDGWDDSYDFWCHADSPDIHPVGWCEKNGHPLQPPK 66

RNA binding Region;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2023612099 271 GQRGRKPGkkRGRTPKTLiSHPISAPSKTA-----EPLKFPKKRGPKPGSKRKPRTLLN 324
Cdd:pfam17208   1 GQRGRKPG--RGKPPGST-SAPKKGSSPKNapakkEPIKIPKKRGPKPGSKRKPRPVLS 56

transcriptional regulator ICP4; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  173 LEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAfDYWCRFDSRDIFPVGWCSLTGDNLQPPGTkvviPKNPYPASDVN 252
Cdd:PHA03307    11 IEAAAEGGEFFPRPPATPGDAADDLLSGSQGQLVS-DSAELAAVTVVAGAAACDRFEPPTGPPPG----PGTEAPANESR 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  253 TeKPSIHSSTKTVL----EHQPGQRGRKPGKKRGRTPKTLiSHPISAPSKTAEPLKFPKKRGPKPGSKRKPRTLLNPPPA 328
Cdd:PHA03307    86 S-TPTWSLSTLAPAsparEGSPTPPGPSSPDPPPPTPPPA-SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVA 163

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2023612099  329 SPTTSTPEP-DTSTVPQDAATIPSSAMQAPTV 359
Cdd:PHA03307   164 SDAASSRQAaLPLSSPEETARAPSSPPAEPPP 195

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  233 QPPGTKVVIPKNPYPASDVNTEKPSiHSSTKTVLEHQPGqrgrkpGKKRGRTPktlishPISAPSKTAEPLKFPKKRGPK 312
Cdd:PHA03247  2822 ASPAGPLPPPTSAQPTAPPPPPGPP-PPSLPLGGSVAPG------GDVRRRPP------SRSPAAKPAAPARPPVRRLAR 2888

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2023612099  313 PGSKRKPRTLLNPPPASPTTSTPEPDTSTVPQDAATIPSSAMQAP 357
Cdd:PHA03247  2889 PAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPP 2933

first malignant brain tumor (MBT) repeat found in the sex comb on midleg family; The sex comb on midleg (Scm) family of Polycomb proteins includes Drosophila melanogaster Scm protein, as well as two vertebrate homologs of Scm, sex comb on midleg homolog 1 (SCMH1) and sex comb on midleg-like protein 2 (SCML2). Scm is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Both SCMH1 and SCML2 are components of PRC1, which acts as an E3 ubiquitin ligase both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. Members of this family contain two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  49 QSYTPPSNEFKISMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDSAEIQPIGNCEKNGGMLQPPLG 128
Cdd:cd20091     1 QSPIPPVNEFKVGMKLEAQDPRNLTSTCIATVVGIQGPRLRLRLDGSDNKNDFWRLVDSSDIHPVGWCEKNGGLLQPPLG 80

                          90
                  ....*....|....*..
gi 2023612099 129 FRLNASSWPMFLLKTLN 145
Cdd:cd20091    81 FRMNPSSWPMFLQKTLN 97

first malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein sex comb on midleg and similar proteins; Sex comb on midleg (Scm) is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Scm contains two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  49 QSYTPPSNEFKISMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDSAEIQPIGNCEKNGGMLQPPLG 128
Cdd:cd20107     1 QAQNPPKNEFKIGMKLEALDPRNVTSTCIATVVGVLGPRLRLRLDGSDNKNDFWRLVDSTEIHPIGHCEKNGGMLQPPLG 80

                          90
                  ....*....|....*....
gi 2023612099 129 FRLNASSWPMFLLKTLNGA 147
Cdd:cd20107    81 FRMNASSWPMFLLKTLNNA 99

second malignant brain tumor (MBT) repeat found in the Polycomb protein sex comb on midleg family; The Sex comb on midleg (Scm) family of Polycomb proteins includes Drosophila melanogaster Scm protein, as well as two vertebrate homologs of Scm, Polycomb protein sex comb on midleg homolog 1 (SCMH1) and sex comb on midleg-like protein 2 (SCML2). Scm is a putative zinc finger protein that functions as a transcriptional regulator which represses multiple homeotic genes during embryonic stages. It coordinates Polycomb group (PcG) complexes, PRC1 (PcG-repressive complex 1) or PRC2 (PcG-repressive complex 2), and polymerizes to produce broad domains of PcG silencing. Both SCMH1 and SCML2 are components of PRC1, which acts as an E3 ubiquitin ligase both for histone H2A to silence transcription and for geminin to regulate its stability. SCMH1 provides the complex with an interaction domain for geminin. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. Members of this family contain two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023612099 162 PSHNFFKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPPG 236
Cdd:cd20092     1 PEKNMFKVGMKLEAVDRKNPQLICPATVGDVDGDEIHISFDGWRGAFDYWCRYDSRDIFPVGWCKKTGHPLQPPG 75

second malignant brain tumor (MBT) repeat found in sex comb on midleg-like protein 2 (SCML2) and similar proteins; SCML2 is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. SCML2 contains two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023612099 162 PSHNFFKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPPGTK 238
Cdd:cd20109     1 PPLNNFKVGMKLEAIDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCRLTGDVLQPPGNS 77

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023612099 565 GRDPSSWTVEDVMQFVREADPQ-LGPHADLFRKHEIDGKALLLLRSDMMMKYMGLKLGPALKLSYHIDRLKQ 635
Cdd:cd09578     1 SKDPSTWSVEDVVQFIKEADPQaLAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLKQ 72

Present in Drosophila Scm, l(3)mbt, and vertebrate SCML2; Present in Drosophila Scm, l(3)mbt, and vertebrate SCML2. These proteins are involved in transcriptional regulation.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  137 PMFLLKTlnGAEMAPIRIFHKEPPSPSHNFfKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDS 216
Cdd:smart00561   1 EDYLEET--GARAAPVELFKQPVDSPPNGF-KVGMKLEAVDPRNPSLICVATVVEVKGYRLLLHFDGWDDKYDFWCHADS 77

                           90
                   ....*....|....*....
gi 2023612099  217 RDIFPVGWCSLTGDNLQPP 235
Cdd:smart00561  78 PDIFPVGWCEKNGHPLQPP 96

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023612099 568 PSSWTVEDVMQFVREAdPQLGPHADLFRKHEIDGKALLLLRSDMMMKYMGLKLGPALKLSYHIDR 632
Cdd:cd09509     1 PSKWSVDDVAQFIKSL-DGCAEYAEVFREQEIDGQALLLLTEDDLLKGMGLKLGPALKIYNHIVK 64

fourth malignant brain tumor (MBT) repeat found in the Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt)-like family; The dSfmbt-like family includes Drosophila melanogaster Scm-like with four MBT domain-containing protein 1 (dSfmbt), as well as its two vertebrate homologs, MBT domain-containing protein 1 (MBTD1) and Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2). dSfmbt is a Polycomb group (PcG) repressor involved in epigenetic regulation of gene expression. MBTD1 and L3MBTL2, also called L(3)mbt-like protein 2, are putative PcG proteins that specifically bind to monomethylated and dimethylated 'Lys-20' on histone H4. L3MBTL2 also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. Members of this family contain four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the fourth MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023612099 167 FKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPP 235
Cdd:cd20100     3 FKVGMKLEAVDLMEPRLICVATVTRVVGRLLRVHFDGWDDEFDQWVDCDSPDIYPVGWCELVGYPLQPP 71

third malignant brain tumor (MBT) repeat found in the Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1)-like family; The L3MBTL1-like family includes L3MBTL1, L3MBTL3, and L3MBTL4. L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a PcG protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a PcG protein that may act as a tumor suppressor. Members of this family contain three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023612099 167 FKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPP 235
Cdd:cd20103     5 FEVGMKLEAVDKRNPRLIRVATVADVEDYRVKLHFDGWPDIYDFWVDDDSPDIHPPGWCSKTGHPLEPP 73

malignant brain tumor (MBT) repeat; The MBT repeat is a protein module that recognizes methylated lysine residues on histones and are thought to affect a variety of chromatin processes, including transcription. It exists as tandem repeats and is found in a number of nuclear proteins such as Drosophila sex comb on midleg protein. In the human genome, there are at least 9 MBT repeat proteins, each containing two, three or four MBT repeats. MBT repeat proteins use a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine (monomethyllysine and/or dimethyllysine).

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023612099 167 FKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWR-GAFDYWCRFDSRDIFPVGWCS 226
Cdd:cd20088     1 FKVGMKLEAVDPLNPSEICVATVVKVVGGRLLLHFDGWDpSRYDFWCDVDSPDIHPVGWCE 61

second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 4 (L3MBTL4); L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a Polycomb group (PcG) protein that may act as a tumor suppressor. L3MBTL4 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099 167 FKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCsltgdnlQPPGTKVVIPKNpY 246
Cdd:cd20136     5 FQVGMKLEAVDRKNPSLVCVATIADIVEDRLLVHFDNWDDSYDYWCDVNSPYIQPVGWC-------QENGRTLVAPQG-Y 76

                  ....
gi 2023612099 247 PASD 250
Cdd:cd20136    77 PNPE 80

third malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1); L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL1 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023612099 162 PSHNFfKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPP 235
Cdd:cd20137     1 PPHGF-QVNMKLEAVDRRNPALIRVASVEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPP 73

first malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 3 (L3MBTL3); L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a Polycomb group (PcG) protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL3 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  56 NEFKISMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDSAEIQPIGNCEKNGGMLQPPLGFRLNASS 135
Cdd:cd20132     4 NGFKVGMKLEGVDPEHQSMYCVLTVAEVCGYRIRLHFDGYSDCYDFWVNADSPDIHPVGWCEKTGHKLHPPKGYKEEEFN 83

                          90       100
                  ....*....|....*....|
gi 2023612099 136 WPMFLlkTLNGAEMAPIRIF 155
Cdd:cd20132    84 WQSYL--KTCKAQAAPKSLF 101

third malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 3 (L3MBTL3); L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a Polycomb group (PcG) protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL3 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023612099 162 PSHNFFKmGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPP 235
Cdd:cd20138     5 PPHGFQK-NMKLEVVDKRNPMLIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPAGWCAKTGHPLQPP 77

second malignant brain tumor (MBT) repeat found in the Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1)-like family; The L3MBTL1-like family includes L3MBTL1, L3MBTL3, and L3MBTL4. L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a PcG protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a PcG protein that may act as a tumor suppressor. Members of this family contain three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  55 SNEFKISMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDSAEIQPIGNCEKNGGMLQPPLGFRLNAS 134
Cdd:cd20102     1 PHGFRVGMKLEAVDRKNPSLICVATVTDVIGNRFLVHFDGWDDSYDYWCDPDSPYIHPVGWCEENGKTLQPPKGYSPGNF 80

                  ....*....
gi 2023612099 135 SWPMFLLKT 143
Cdd:cd20102    81 SWDKYLEET 89

fourth malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 2 (L3MBTL2); L3MBTL2, also called L(3)mbt-like protein 2, is a putative Polycomb group (PcG) protein that binds to monomethylated and dimethylated 'Lys-20' on histone H4 and also binds histone H3 peptides which are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'. L3MBTL2 orchestrates ubiquitin signalling by dictating the sequential recruitment of RNF8 and RNF168 after DNA damage. It is an integral component of the polycomb repressive complex 1.6 (PRC1.6) and has been implicated in transcriptional repression and chromatin compaction. L3MBTL2 contains four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the fourth MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023612099 162 PSHNFfKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPP 235
Cdd:cd20130     2 PNHGF-KVGMKLEAVDLMEPRLICVATVKRVVHRLLSIHFDGWDSEYDQWVDCESPDIYPVGWCELTGYQLQPP 74

fourth malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 4 (L3MBTL4); L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a Polycomb group (PcG) protein that may act as a tumor suppressor. L3MBTL4 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023612099 160 PSPSHNFfKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQ-PPGT 237
Cdd:cd20139     3 LRPPHGF-QVNMKLEAVDKRNPILIRVATIVDKDDHRIKLHFDGWDHNYDFWVDADSPDIHPVGWCDKTGHALQvPLGA 80

first malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 4 (L3MBTL4); L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a Polycomb group (PcG) protein that may act as a tumor suppressor. L3MBTL4 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023612099 163 SHNFFKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPP 235
Cdd:cd20133     2 SRNGFKVGMRLEGIDPEHPSLFCVLSVAEVQGYRLRLHFDGYSECYDFWVNADSPDIHPVGWCEKTGHKLLPP 74

third malignant brain tumor (MBT) repeat found in the Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1)-like family; The L3MBTL1-like family includes L3MBTL1, L3MBTL3, and L3MBTL4. L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a PcG protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a PcG protein that may act as a tumor suppressor. Members of this family contain three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023612099  54 PSNEFKISMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDSAEIQPIGNCEKNGGMLQPP 126
Cdd:cd20103     1 PPHGFEVGMKLEAVDKRNPRLIRVATVADVEDYRVKLHFDGWPDIYDFWVDDDSPDIHPPGWCSKTGHPLEPP 73

second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 4 (L3MBTL4); L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a Polycomb group (PcG) protein that may act as a tumor suppressor. L3MBTL4 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  55 SNEFKISMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDSAEIQPIGNCEKNGGMLQPPLGF-RLNA 133
Cdd:cd20136     2 PKEFQVGMKLEAVDRKNPSLVCVATIADIVEDRLLVHFDNWDDSYDYWCDVNSPYIQPVGWCQENGRTLVAPQGYpNPEK 81

                          90
                  ....*....|
gi 2023612099 134 SSWPMFLLKT 143
Cdd:cd20136    82 FSWTEYLEAT 91

SAM domain of Scm-like-4MBT proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-4MBT (Sex comb on midleg like, Malignant Brain Tumor) subfamily proteins of the polycomb group is a putative protein-protein interaction domain. Additionally to the SAM domain, most of the proteins of this subfamily have 4 MBT repeats. In Drosophila SAM-Scm-like-4MBT protein (known as dSfmbt) is a member of Pho repressive complex (PhoRC). Additionally to dSfmbt, the PhoRC complex includes Pho or Pho-like proteins. This complex is responsible for HOX (Homeobox) gene silencing: Pho or Pho-like proteins bind DNA and dSmbt binds methylated histones. dSmbt can interact with mono- and di-methylated histones H3 and H4 (however this activity has been shown for the MBT repeats, while exact function of the SAM domain is unclear). Besides interaction with histones, dSmbt can interact with Scm (a member of PRC complex), but this interaction also seems to be SAM domain independent.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023612099 568 PSSWTVEDVMQFVREADpqLGPHADLFRKHEIDGKALLLLRSDMMMKYMGLKLGPALKLSYHIDRLK 634
Cdd:cd09580     1 PSTWGVKDVSQFLREND--CGAYCECFCRQNIDGKRLLSLTKEQIMTLTGMKVGPSLKIYDLIQQLK 65

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023612099 568 PSSWTVEDVMQFVREAD-PQlgpHADLFRKHEIDGKALLLL-RSDMMMKyMGLKLGPALKLSYHIDRLKQGK 637
Cdd:cd09583     1 PSNWSVEDVVQYFKTAGfPE---EANAFKEQEIDGKSLLLLtRSDVLTG-LSLKLGPALKIYEHVVKLQQQS 68

first malignant brain tumor (MBT) repeat found in sex comb on midleg-like protein 2; Sex comb on midleg-like protein 2 (SCML2) is a homolog of Drosophila Sex comb on midleg (Scm). It is a component of PRC1 (Polycomb repressive complex 1), which acts as an E3 ubiquitin ligase, both for histone H2A to silence transcription and for geminin to regulate its stability. SCML2 is a germline-specific Polycomb protein that acts as a critical regulator of heterochromatin organization in spermatogenesis. SCML2 contains two MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the first MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023612099 158 EPPSPSHNFFKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPP 235
Cdd:cd20106     1 QSRIPPVNDFKVGMKLEARDPRNATSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPIGTCEKEGDMLQPP 78

fourth malignant brain tumor (MBT) repeat found in the Scm-like with four MBT domains protein (SFMBT) family; The SFMBT family includes SFMBT1 and SFMBT2. SFMBT1, also called renal ubiquitous protein 1, is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3 and functions as a chromatin reader in regulating epigenetic silencing and the myogenic gene program. It mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. SFMBT2, also called Scm-like with 4 MBT domains protein 2, is a transcriptional repressor of the HOXB13 gene. It is required for trophoblast maintenance and placenta development. It also negatively regulates cell migration and invasion in prostate cancer cells. Members of this family contain four MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the fourth MBT repeat that does not contain a semi-aromatic cage and may not bind methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023612099 167 FKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWrgafDYWCRF-----DSRDIFPVGWCSLTGDNLQPP 235
Cdd:cd20096     1 FERGMKLEAVNPENPNQICVATITKVVGPLLWLHLDSE----KKLSPNiivdvESTDIFPVGWCESNGYPLVTP 70

fourth malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 4 (L3MBTL4); L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a Polycomb group (PcG) protein that may act as a tumor suppressor. L3MBTL4 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023612099  54 PSNEFKISMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDSAEIQPIGNCEKNGGMLQPPLG 128
Cdd:cd20139     5 PPHGFQVNMKLEAVDKRNPILIRVATIVDKDDHRIKLHFDGWDHNYDFWVDADSPDIHPVGWCDKTGHALQVPLG 79

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023612099 569 SSWTVEDVMQFVREAdPQLGPHADLFRKHEIDGKALLLLRSDMMMKYMGLKLGPALKLSYHIDR 632
Cdd:cd09579     2 RKWTVDDVCSFIGSL-PGCAEYAQVFREHSIDGETLPLLTEEHLLNTMGLKLGPALKIRSQVAK 64

second malignant brain tumor (MBT) repeat found in Lethal(3)malignant brain tumor-like protein 3 (L3MBTL3); L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a Polycomb group (PcG) protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL3 contains three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023612099  54 PSNeFKISMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDSAEIQPIGNCEKNGGMLQPPLGFR-LN 132
Cdd:cd20135     3 PSG-FRVGMKLEAVDKKNPSFICVATITDMVDNRLLIHFDNWDESYDYWCDASSPYIHPVGYCQEHGRTLTTPPGYKdPK 81

                          90
                  ....*....|.
gi 2023612099 133 ASSWPMFLLKT 143
Cdd:cd20135    82 HFSWEKYLEET 92