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 1717047087 180 PPENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPPGNS 256
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 1717047087 665 SKDPSTWSIEEVIRFVREADPQALAPHAELFRRHEIDGKALLLLRSDMVMKYMGLKLGPALKLCYHIERLKQ 736
Cdd:cd09578     1 SKDPSTWSVEDVVQFIKEADPQALAPHVDLFRKHEIDGKALLLLNSDMMMKYMGLKLGPALKLCYHIDKLKQ 72

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717047087 495 PYVGSAHSPLEYDKNKSAKEEIPESRNVKRFSQDSPPYTAPVSPKLARTEAHPSEAETLPAEENNTLKEHR--FSEETMD 572
Cdd:COG5233   282 PLAGVGQKPQLQKLGTTKRTEDPESHQVEQRGVEENFLPIPKPDTHRSEFAAKNFLSSLPLSFYGKKSEHKsgTQRAVTT 361

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1717047087 573 SALNSVNAPSPSLRNTTDYRISGNAAYYRSTLHPVSATSNSA 614
Cdd:COG5233   362 SYHEENGECPLCFKHEEKDRSSESSGEYTPLAPPPSLSSISS 403

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 1717047087 180 PPENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPPGNS 256
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 1717047087 665 SKDPSTWSIEEVIRFVREADPQALAPHAELFRRHEIDGKALLLLRSDMVMKYMGLKLGPALKLCYHIERLKQ 736
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 1717047087   49 EDYLRETGSISAPPHCFRQSKNPPSNDFKIGMKLEAHDPRNVTSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDI 128
Cdd:smart00561   1 EDYLEETGARAAPVELFKQPVDSPPNGFKVGMKLEAVDPRNPSLICVATVVEVKGYRLLLHFDGWDDKYDFWCHADSPDI 80

                           90
                   ....*....|....*.
gi 1717047087  129 QQIGTCEKKGDMLQPP 144
Cdd:smart00561  81 FPVGWCEKNGHPLQPP 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 1717047087  80 MKLEAHDPRNVTSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQQIGTCEKKGDMLQPPL 145
Cdd:pfam02820   1 MKLEAVDPLNPSLICVATVVKVLGGRLRLRFDGWDDSYDFWCHADSPDIHPVGWCEKNGHPLQPPK 66

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 1717047087  668 PSTWSIEEVIRFVREADpqaLAPHAELFRRHEIDGKALLLLRSDMVMKYMG-LKLGPALKLCYHIERLKQ 736
Cdd:smart00454   1 VSQWSPESVADWLESIG---LEQYADNFRKNGIDGALLLLLTSEEDLKELGiTKLGHRKKILKAIQKLKE 67

Peripheral Golgi membrane protein [Intracellular trafficking and secretion];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717047087 495 PYVGSAHSPLEYDKNKSAKEEIPESRNVKRFSQDSPPYTAPVSPKLARTEAHPSEAETLPAEENNTLKEHR--FSEETMD 572
Cdd:COG5233   282 PLAGVGQKPQLQKLGTTKRTEDPESHQVEQRGVEENFLPIPKPDTHRSEFAAKNFLSSLPLSFYGKKSEHKsgTQRAVTT 361

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1717047087 573 SALNSVNAPSPSLRNTTDYRISGNAAYYRSTLHPVSATSNSA 614
Cdd:COG5233   362 SYHEENGECPLCFKHEEKDRSSESSGEYTPLAPPPSLSSISS 403

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717047087  67 QSKNPPSNDFKIGMKLEAHDPRNVTSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQQIGTCEKKGDMLQPPLG 146
Cdd:cd20106     1 QSRIPPVNDFKVGMKLEARDPRNATSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPIGTCEKEGDMLQPPLG 80

                          90
                  ....*....|....*...
gi 1717047087 147 FQMNASSWPMFLLRTLNG 164
Cdd:cd20106    81 FQMNASSWPMFLLRTLNG 98

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 1717047087  67 QSKNPPSNDFKIGMKLEAHDPRNVTSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQQIGTCEKKGDMLQPPLG 146
Cdd:cd20107     1 QAQNPPKNEFKIGMKLEALDPRNVTSTCIATVVGVLGPRLRLRLDGSDNKNDFWRLVDSTEIHPIGHCEKNGGMLQPPLG 80

                          90
                  ....*....|....*....
gi 1717047087 147 FQMNASSWPMFLLRTLNGA 165
Cdd:cd20107    81 FRMNASSWPMFLLKTLNNA 99

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 1717047087 382 TVCVYVNKHGNSGPHLDKKKVLQLPDHFGPGPVDVVLQQAVQACVDCAYHSKIVFGFLKSGHHG-GEVITASFDGEKHAV 460
Cdd:pfam12140   1 TVCIYVNKNCFCGPHLDKKKIAELPDQFGPGPVSLVLKEVLQALIDCAYDPKQVLKLLKSGNGGrEEIITAKYEGKTHTV 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1717047087 461 NLPPVNSASYVLRFLEKLCHSLQ-CDNLFSSQ 491
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 1717047087 180 PPENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPPG 254
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 1717047087 665 SKDPSTWSIEEVIRFVREADPQALAPHAELFRRHEIDGKALLLLRSDMVMKYMGLKLGPALKLCYHIERLKQ 736
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 1717047087   49 EDYLRETGSISAPPHCFRQSKNPPSNDFKIGMKLEAHDPRNVTSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDI 128
Cdd:smart00561   1 EDYLEETGARAAPVELFKQPVDSPPNGFKVGMKLEAVDPRNPSLICVATVVEVKGYRLLLHFDGWDDKYDFWCHADSPDI 80

                           90
                   ....*....|....*.
gi 1717047087  129 QQIGTCEKKGDMLQPP 144
Cdd:smart00561  81 FPVGWCEKNGHPLQPP 96

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 1717047087 182 ENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPP 253
Cdd:cd20102     1 PHGFRVGMKLEAVDRKNPSLICVATVTDVIGNRFLVHFDGWDDSYDYWCDPDSPYIHPVGWCEENGKTLQPP 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717047087 185 FKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPP 253
Cdd:cd20100     3 FKVGMKLEAVDLMEPRLICVATVTRVVGRLLRVHFDGWDDEFDQWVDCDSPDIYPVGWCELVGYPLQPP 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717047087 180 PPENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPP 253
Cdd:cd20101     1 FNKNGFKVGMKLEGIDPKHPSLFCVLSVAEVRGYRLRLHFDGYSECYDFWVNADSPDIFPVGWCEKTGHKLQPP 74

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 1717047087 185 FKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWR-GAFDYWCKYDSRDIFPVGWCS 244
Cdd:cd20088     1 FKVGMKLEAVDPLNPSEICVATVVKVVGGRLLLHFDGWDpSRYDFWCDVDSPDIHPVGWCE 61

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 1717047087  71 PPSNDFKIGMKLEAHDPRNVTSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQQIGTCEKKGDMLQPPLGFQMN 150
Cdd:cd20101     1 FNKNGFKVGMKLEGIDPKHPSLFCVLSVAEVRGYRLRLHFDGYSECYDFWVNADSPDIFPVGWCEKTGHKLQPPKGYTSE 80

                          90       100
                  ....*....|....*....|...
gi 1717047087 151 ASSWPMFLLRTlnGAEMAPATIF 173
Cdd:cd20101    81 TFSWSAYLKLT--KAQAAPKHLF 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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717047087 180 PPENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPP 253
Cdd:cd20134     1 PPPLGFQVGMKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKPLTPP 74

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 1717047087  74 NDFKIGMKLEAHDPRNVTSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQQIGTCEKKGDMLQPPLGFQMNASS 153
Cdd:cd20132     4 NGFKVGMKLEGVDPEHQSMYCVLTVAEVCGYRIRLHFDGYSDCYDFWVNADSPDIHPVGWCEKTGHKLHPPKGYKEEEFN 83

                          90       100
                  ....*....|....*....|
gi 1717047087 154 WPMFLlrTLNGAEMAPATIF 173
Cdd:cd20132    84 WQSYL--KTCKAQAAPKSLF 101

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 1717047087 178 PKPPENyFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQ-PPGNS 256
Cdd:cd20139     3 LRPPHG-FQVNMKLEAVDKRNPILIRVATIVDKDDHRIKLHFDGWDHNYDFWVDADSPDIHPVGWCDKTGHALQvPLGAS 81

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 1717047087  73 SNDFKIGMKLEAHDPRNVTSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQQIGTCEKKGDMLQPPLGFQMNAS 152
Cdd:cd20102     1 PHGFRVGMKLEAVDRKNPSLICVATVTDVIGNRFLVHFDGWDDSYDYWCDPDSPYIHPVGWCEENGKTLQPPKGYSPGNF 80

                  ..
gi 1717047087 153 SW 154
Cdd:cd20102    81 SW 82

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 1717047087 185 FKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPP 253
Cdd:cd20129     3 FRVGMKLEAVDLMEPRLVCVATVTRIIHRLLRIHFDGWEDEYDQWVDCESPDLYPVGWCQLTGYQLQPP 71

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 1717047087 182 ENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPP 253
Cdd:cd20132     3 KNGFKVGMKLEGVDPEHQSMYCVLTVAEVCGYRIRLHFDGYSDCYDFWVNADSPDIHPVGWCEKTGHKLHPP 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 1717047087 182 ENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPP 253
Cdd:cd20133     3 RNGFKVGMRLEGIDPEHPSLFCVLSVAEVQGYRLRLHFDGYSECYDFWVNADSPDIHPVGWCEKTGHKLLPP 74

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717047087  65 FRQSKNPP--SNDFKIGMKLEAHDPRNVTSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQQIGTCEKKGDMLQ 142
Cdd:cd20131     1 FQDSQAVThnKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQ 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1717047087 143 PPLGFQMNASSWPMFLLRTlnGAEMAPATIF 173
Cdd:cd20131    81 PPKGYKEEEFSWSQYLRST--RAQAAPKHLF 109

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 1717047087 176 EPPKPPENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPP 253
Cdd:cd20106     1 QSRIPPVNDFKVGMKLEARDPRNATSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPIGTCEKEGDMLQPP 78

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 1717047087 153 SWPMFLLRTlnGAEMAPATIFKKEPpKPPENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKY 232
Cdd:cd20105     3 SWDKYLKET--GAVPAPVHCFKQSY-TPPVNEFKIGMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1717047087 233 DSRDIFPVGWCSLTGDALQPP-GNSVSitktntntPSSPPKAIRRSMQSAQKSPI 286
Cdd:cd20105    80 DSSEIQPIGNCEKNGGMLQPPlGFRLN--------ASSWPMFLLKTLNGAEMAPV 126

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 1717047087 185 FKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRG-AFDYWCKYDSRDIFPVGWCSLTGDALQPP 253
Cdd:cd20096     1 FERGMKLEAVNPENPNQICVATITKVVGPLLWLHLDSEKKlSPNIIVDVESTDIFPVGWCESNGYPLVTP 70

SAM domain of Scm-like-3MBT3,4 proteins of Polycomb group; SAM (sterile alpha motif) domain of Scm-like-3MBT3,4 (Sex comb on midleg, Malignant brain tumor) subfamily proteins (also known as L3mbtl3,4 proteins) is a putative protein-protein interaction domain. Proteins of this subfamily are predicted transcriptional regulators belonging to Polycomb group. The majority of them are multidomain proteins: in addition to the C-terminal SAM domain, they contain three MBT repeats and Zn finger domain. Murine L3mbtl3 protein of this subfamily is essential for maturation of myeloid progenitor cells during differentiation. Human L3mbtl4 is a potential tumor suppressor gene in breast cancer, while deregulation of L3MBTL3 is associated with neuroblastoma.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717047087 668 PSTWSIEEVIRFVrEADPqALAPHAELFRRHEIDGKALLLLRSDMVMKYMGLKLGPALKLCYHIERLK 735
Cdd:cd09582     1 VLRWSVDEVAEFV-QSLP-GCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66

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 1717047087  74 NDFKIGMKLEAHDPRNVTSVCIATVIGITGARLRLRLDG--SDNKNDFWRLVDSSDIQQIGTCEKKGDMLQPPLGFQMNA 151
Cdd:cd20093     2 SGFKPGMKLEVPNKNNPDTYWVATVVMTCGPLLRLRYVGyeDDRSADFWCDLSSGDVHPIGWCAQNGKPLQPPADIKEKE 81

                          90
                  ....*....|...
gi 1717047087 152 SSWPMFLLRTLNG 164
Cdd:cd20093    82 LDWAEFLIKELTG 94

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 1717047087 180 PPENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGWRGAFDYWCKYDSRDIFPVGWCSLTGDALQPP 253
Cdd:cd20107     5 PPKNEFKIGMKLEALDPRNVTSTCIATVVGVLGPRLRLRLDGSDNKNDFWRLVDSTEIHPIGHCEKNGGMLQPP 78

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 1717047087  72 PSNDFKIGMKLEAHDPRNVTSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQQIGTCEKKGDMLQPPLG 146
Cdd:cd20139     5 PPHGFQVNMKLEAVDKRNPILIRVATIVDKDDHRIKLHFDGWDHNYDFWVDADSPDIHPVGWCDKTGHALQVPLG 79

second 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 second MBT repeat that does not seem to contain a semi-aromatic cage and may not bind methylated lysine residues.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717047087 185 FKVGMKLEAVDKKNPYLICPATIGDVKGDEVFIT-FDGWRGAFDYWCKYDSRDIFPVGWCSLTG 247
Cdd:cd20098    15 FKVGMRLEVVDKMCISRTRVAVVEEVVGGRLRLQyVDSEDDDDDFWCHMKSPLIHPVGWSQAVG 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717047087 182 ENYFKVGMKLEAVDKKNPYLICPATIGDVKGDEVFITFDGW--RGAFDYWCKYDSRDIFPVGWCSLTGDALQPP 253
Cdd:cd20093     1 QSGFKPGMKLEVPNKNNPDTYWVATVVMTCGPLLRLRYVGYedDRSADFWCDLSSGDVHPIGWCAQNGKPLQPP 74