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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934785926  32 FIWDNYLKETGSIIAPSECFRQSEIPPTNDFKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDS 111
Cdd:cd20105     2 FSWDKYLKETGAVPAPVHCFKQSYTPPVNEFKIGMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDS 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1934785926 112 PDIQPIGTCEKEGDLLQPPLGYQMNVSSWPVFLLRTLSGSEMAPAALFKQ 161
Cdd:cd20105    82 SEIQPIGNCEKNGGMLQPPLGFRLNASSWPMFLLKTLNGAEMAPVRIFHK 131

SLED domain; The SLED (Scm-Like Embedded Domain) domain is a double-stranded DNA binding domain found in Scml2 which is a member of the Polycomb group of proteins involved in epigenetic gene silencing.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934785926 353 TVCVYVNKHGNPGPYLDQKKIQQLPDHFGPSPVNVVLRRTIQACVDCALQTKIVFGFLKPDNRG-GEVITASFDGENHSV 431
Cdd:pfam12140   1 TVCIYVNKNCFCGPHLDKKKIAELPDQFGPGPVSLVLKEVLQALIDCAYDPKQVLKLLKSGNGGrEEIITAKYEGKTHTV 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1934785926 432 QLPPVNSASFVLRFLEIFCHSLQ-CDNLLSSQ 462
Cdd:pfam12140  81 KLPIVNSASDVWRFLEKLCEKLGcCENLFSPQ 112

RNA binding Region;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1934785926 275 TQPIRKTSRIKPPGPTSVPKKGSSLKNPTA--------KNKGLNSGKKEKILPALC 322
Cdd:pfam17208   1 GQRGRKPGRGKPPGSTSAPKKGSSPKNAPAkkepikipKKRGPKPGSKRKPRPVLS 56

first malignant brain tumor (MBT) repeat found in Polycomb protein sex comb on midleg homolog 1; Sex comb on midleg homolog 1 (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 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 1934785926  32 FIWDNYLKETGSIIAPSECFRQSEIPPTNDFKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDS 111
Cdd:cd20105     2 FSWDKYLKETGAVPAPVHCFKQSYTPPVNEFKIGMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDS 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1934785926 112 PDIQPIGTCEKEGDLLQPPLGYQMNVSSWPVFLLRTLSGSEMAPAALFKQ 161
Cdd:cd20105    82 SEIQPIGNCEKNGGMLQPPLGFRLNASSWPMFLLKTLNGAEMAPVRIFHK 131

SLED domain; The SLED (Scm-Like Embedded Domain) domain is a double-stranded DNA binding domain found in Scml2 which is a member of the Polycomb group of proteins involved in epigenetic gene silencing.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934785926 353 TVCVYVNKHGNPGPYLDQKKIQQLPDHFGPSPVNVVLRRTIQACVDCALQTKIVFGFLKPDNRG-GEVITASFDGENHSV 431
Cdd:pfam12140   1 TVCIYVNKNCFCGPHLDKKKIAELPDQFGPGPVSLVLKEVLQALIDCAYDPKQVLKLLKSGNGGrEEIITAKYEGKTHTV 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1934785926 432 QLPPVNSASFVLRFLEIFCHSLQ-CDNLLSSQ 462
Cdd:pfam12140  81 KLPIVNSASDVWRFLEKLCEKLGcCENLFSPQ 112

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 1934785926 622 SKDPSSWSVDEVIQFMKHADPQTSASVADLFQQHEIDGKALLLLKTDVMMKYMGLKLGPALKLCHYVEKLKE 693
Cdd:cd09578     1 SKDPSTWSVEDVVQFIKEADPQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLKQ 72

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 1934785926 175 MKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPP 239
Cdd:pfam02820   1 MKLEAVDPLNPSLICVATVVKVLGGRLRLRFDGWDDSYDFWCHADSPDIHPVGWCEKNGHPLQPP 65

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934785926 626 SSWSVDEVIQFMKHADPQtsaSVADLFQQHEIDGKALLLLKTDVMMKYMGLKLGPALKLCHYVEKLK 692
Cdd:pfam00536   1 DGWSVEDVGEWLESIGLG---QYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRLK 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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934785926  625 PSSWSVDEVIQFMKHADPQtsaSVADLFQQHEIDGKALLLLKTDVMMKYMG-LKLGPALKLCHYVEKLKE 693
Cdd:smart00454   1 VSQWSPESVADWLESIGLE---QYADNFRKNGIDGALLLLLTSEEDLKELGiTKLGHRKKILKAIQKLKE 67

first malignant brain tumor (MBT) repeat found in Polycomb protein sex comb on midleg homolog 1; Sex comb on midleg homolog 1 (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 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 1934785926  32 FIWDNYLKETGSIIAPSECFRQSEIPPTNDFKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDS 111
Cdd:cd20105     2 FSWDKYLKETGAVPAPVHCFKQSYTPPVNEFKIGMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDS 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1934785926 112 PDIQPIGTCEKEGDLLQPPLGYQMNVSSWPVFLLRTLSGSEMAPAALFKQ 161
Cdd:cd20105    82 SEIQPIGNCEKNGGMLQPPLGFRLNASSWPMFLLKTLNGAEMAPVRIFHK 131

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 1934785926  53 QSEIPPTNDFKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDSPDIQPIGTCEKEGDLLQPPLG 132
Cdd:cd20091     1 QSPIPPVNEFKVGMKLEAQDPRNLTSTCIATVVGIQGPRLRLRLDGSDNKNDFWRLVDSSDIHPVGWCEKNGGLLQPPLG 80

                          90
                  ....*....|....*.
gi 1934785926 133 YQMNVSSWPVFLLRTL 148
Cdd:cd20091    81 FRMNPSSWPMFLQKTL 96

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 1934785926 166 PALNNFKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPPGNN 242
Cdd:cd20109     1 PPLNNFKVGMKLEAIDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCRLTGDVLQPPGNS 77

SLED domain; The SLED (Scm-Like Embedded Domain) domain is a double-stranded DNA binding domain found in Scml2 which is a member of the Polycomb group of proteins involved in epigenetic gene silencing.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934785926 353 TVCVYVNKHGNPGPYLDQKKIQQLPDHFGPSPVNVVLRRTIQACVDCALQTKIVFGFLKPDNRG-GEVITASFDGENHSV 431
Cdd:pfam12140   1 TVCIYVNKNCFCGPHLDKKKIAELPDQFGPGPVSLVLKEVLQALIDCAYDPKQVLKLLKSGNGGrEEIITAKYEGKTHTV 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1934785926 432 QLPPVNSASFVLRFLEIFCHSLQ-CDNLLSSQ 462
Cdd:pfam12140  81 KLPIVNSASDVWRFLEKLCEKLGcCENLFSPQ 112

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 1934785926 166 PALNNFKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPPG 240
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 1934785926 622 SKDPSSWSVDEVIQFMKHADPQTSASVADLFQQHEIDGKALLLLKTDVMMKYMGLKLGPALKLCHYVEKLKE 693
Cdd:cd09578     1 SKDPSTWSVEDVVQFIKEADPQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLKQ 72

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934785926 169 NNFKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPP 239
Cdd:cd20102     2 HGFRVGMKLEAVDRKNPSLICVATVTDVIGNRFLVHFDGWDDSYDYWCDPDSPYIHPVGWCEENGKTLQPP 72

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934785926 169 NNFKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPP 239
Cdd:cd20100     1 HGFKVGMKLEAVDLMEPRLICVATVTRVVGRLLRVHFDGWDDEFDQWVDCDSPDIYPVGWCELVGYPLQPP 71

first 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 first MBT repeat that contains the semi-aromatic cage and may bind methylated lysine residues.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934785926  57 PPTNDFKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDSPDIQPIGTCEKEGDLLQPPLGYQMN 136
Cdd:cd20101     1 FNKNGFKVGMKLEGIDPKHPSLFCVLSVAEVRGYRLRLHFDGYSECYDFWVNADSPDIFPVGWCEKTGHKLQPPKGYTSE 80

                          90       100
                  ....*....|....*....|...
gi 1934785926 137 VSSWPVFLLRTlsGSEMAPAALF 159
Cdd:cd20101    81 TFSWSAYLKLT--KAQAAPKHLF 101

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 1934785926  66 MKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDSPDIQPIGTCEKEGDLLQPPL 131
Cdd:pfam02820   1 MKLEAVDPLNPSLICVATVVKVLGGRLRLRFDGWDDSYDFWCHADSPDIHPVGWCEKNGHPLQPPK 66

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934785926 171 FKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPP 239
Cdd:cd20136     5 FQVGMKLEAVDRKNPSLVCVATIADIVEDRLLVHFDNWDDSYDYWCDVNSPYIQPVGWCQENGRTLVAP 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 1934785926  60 NDFKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDSPDIQPIGTCEKEGDLLQPPLGYQMNVSS 139
Cdd:cd20132     4 NGFKVGMKLEGVDPEHQSMYCVLTVAEVCGYRIRLHFDGYSDCYDFWVNADSPDIHPVGWCEKTGHKLHPPKGYKEEEFN 83

                          90       100
                  ....*....|....*....|
gi 1934785926 140 WPVFLlrTLSGSEMAPAALF 159
Cdd:cd20132    84 WQSYL--KTCKAQAAPKSLF 101

second 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 second MBT repeat that contains the semi-aromatic cage that binds methylated lysine residues.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934785926 171 FKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPP 239
Cdd:cd20134     6 FQVGMKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKPLTPP 74

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 1934785926  59 TNDFKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDSPDIQPIGTCEKEGDLLQPPLGYQMNVS 138
Cdd:cd20102     1 PHGFRVGMKLEAVDRKNPSLICVATVTDVIGNRFLVHFDGWDDSYDYWCDPDSPYIHPVGWCEENGKTLQPPKGYSPGNF 80

                  ....*.
gi 1934785926 139 SWPVFL 144
Cdd:cd20102    81 SWDKYL 86

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934785926 159 FKQEPPrpalNNFKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQP 238
Cdd:cd20138     1 FKVKPP----HGFQKNMKLEVVDKRNPMLIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPAGWCAKTGHPLQP 76

                  .
gi 1934785926 239 P 239
Cdd:cd20138    77 P 77

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934785926 159 FKQEPPrpalNNFKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQ- 237
Cdd:cd20139     1 FKLRPP----HGFQVNMKLEAVDKRNPILIRVATIVDKDDHRIKLHFDGWDHNYDFWVDADSPDIHPVGWCDKTGHALQv 76

                  ....*
gi 1934785926 238 PPGNN 242
Cdd:cd20139    77 PLGAS 81

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 1934785926  58 PTNDFKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDSPDIQPIGTCEKEGDLLQPP 130
Cdd:cd20103     1 PPHGFEVGMKLEAVDKRNPRLIRVATVADVEDYRVKLHFDGWPDIYDFWVDDDSPDIHPPGWCSKTGHPLEPP 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934785926 169 NNFKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPP 239
Cdd:cd20132     4 NGFKVGMKLEGVDPEHQSMYCVLTVAEVCGYRIRLHFDGYSDCYDFWVNADSPDIHPVGWCEKTGHKLHPP 74

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 1934785926 169 NNFKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPP 239
Cdd:cd20133     4 NGFKVGMRLEGIDPEHPSLFCVLSVAEVQGYRLRLHFDGYSECYDFWVNADSPDIHPVGWCEKTGHKLLPP 74

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934785926  61 DFKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDSPDIQPIGTCEKEGDLLQPPLGY 133
Cdd:cd20136     4 EFQVGMKLEAVDRKNPSLVCVATIADIVEDRLLVHFDNWDDSYDYWCDVNSPYIQPVGWCQENGRTLVAPQGY 76

SAM domain of Scm-like-4MBT1,2 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-4MBT1,2 (Sex comb on midleg, Malignant Brain Tumor) subfamily proteins (also known as Sfmbt1,2 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain four MBT repeats and DUF5388 domain. The MBT repeats of the human sfmbt1 protein are responsible for association with the nuclear matrix and for selective binding of H3 histone N-terminal tails, while the exact function of the SAM domain is unclear.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934785926 624 DPSSWSVDEVIQFMKHADpqtSASVADLFQQHEIDGKALLLLKTDVMMKYMGLKLGPALKLCHYVEKLK 692
Cdd:cd09581    11 NPLFWSVDDVVRFIKSTD---CAPLAKIFKDQEIDGQALLLLTLPTVQECMELKLGPAIKLCHHIERVK 76

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 1934785926  58 PTNDFKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDSPDIQPIGTCEKEGDLLQPPLGY 133
Cdd:cd20139     5 PPHGFQVNMKLEAVDKRNPILIRVATIVDKDDHRIKLHFDGWDHNYDFWVDADSPDIHPVGWCDKTGHALQVPLGA 80

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 1934785926 162 EPPRPALNNFKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPP 239
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 1934785926 171 FKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSG-AFDYWCKYDSRDIFPVGWCQLTGDILQPP 239
Cdd:cd20096     1 FERGMKLEAVNPENPNQICVATITKVVGPLLWLHLDSEKKlSPNIIVDVESTDIFPVGWCESNGYPLVTP 70

fourth malignant brain tumor (MBT) repeat found in Drosophila melanogaster Polycomb protein Sfmbt (dSfmbt); dSfmbt, also called Scm-like with four MBT domain-containing protein 1, is a Polycomb group repressor involved in epigenetic regulation of gene expression. dSfmbt 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 1934785926 169 NNFKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPP 239
Cdd:cd20128     1 HGFEVGMSLECADLMDPRLVCVATVARVVGRLLKVHFDGWTDEYDQWLDCESADIYPVGWCVLVNHKLEGP 71

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 1934785926  62 FKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDSPDIQPIGTCEKEGDLLQPP 130
Cdd:cd20100     3 FKVGMKLEAVDLMEPRLICVATVTRVVGRLLRVHFDGWDDEFDQWVDCDSPDIYPVGWCELVGYPLQPP 71

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934785926 161 QEPPRpalNNFKVGMKLEAVDRKNPYLICPATIGDVKGDAVHITFDGWSGAFDYWCKYDSRDIFPVGWCQLTGDILQPP 239
Cdd:cd20107     3 QNPPK---NEFKIGMKLEALDPRNVTSTCIATVVGVLGPRLRLRLDGSDNKNDFWRLVDSTEIHPIGHCEKNGGMLQPP 78

first 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 first MBT repeat that contains a partially conserved semi-aromatic cage.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934785926  60 NDFKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDG--SDNQNDFWRLVDSPDIQPIGTCEKEGDLLQPPLGYQMNV 137
Cdd:cd20093     2 SGFKPGMKLEVPNKNNPDTYWVATVVMTCGPLLRLRYVGyeDDRSADFWCDLSSGDVHPIGWCAQNGKPLQPPADIKEKE 81

                          90
                  ....*....|...
gi 1934785926 138 SSWPVFLLRTLSG 150
Cdd:cd20093    82 LDWAEFLIKELTG 94

fourth malignant brain tumor (MBT) repeat found in MBT domain-containing protein 1 (MBTD1); MBTD1 is a putative Polycomb group (PcG) protein that specifically binds to monomethylated and dimethylated 'Lys-20' on histone H4. MBTD1 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934785926  62 FKVGMKLEAHDPRNVTSVCIATVVGITGARLRLRLDGSDNQNDFWRLVDSPDIQPIGTCEKEGDLLQPP 130
Cdd:cd20129     3 FRVGMKLEAVDLMEPRLVCVATVTRIIHRLLRIHFDGWEDEYDQWVDCESPDLYPVGWCQLTGYQLQPP 71