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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610808 401 VIPSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYPNV 480
Cdd:cd20135     1 VTPSGFRVGMKLEAVDKKNPSFICVATITDMVDNRLLIHFDNWDESYDYWCDASSPYIHPVGYCQEHGRTLTTPPGYKDP 80

                          90
                  ....*....|...
gi 2462610808 481 KHFSWDKYLEETN 493
Cdd:cd20135    81 KHFSWEKYLEETN 93

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 2462610808 740 VSKWSTDEVSEFIQSLPGCEEHGKVFKDEQIDGEAFLLMTQTDIVKIMSIKLGPALKIFNSILMFK 805
Cdd:cd09582     1 VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610808 401 VIPSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYPNV 480
Cdd:cd20135     1 VTPSGFRVGMKLEAVDKKNPSFICVATITDMVDNRLLIHFDNWDESYDYWCDASSPYIHPVGYCQEHGRTLTTPPGYKDP 80

                          90
                  ....*....|...
gi 2462610808 481 KHFSWDKYLEETN 493
Cdd:cd20135    81 KHFSWEKYLEETN 93

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 2462610808  271 SYLEEEKAVAVPAKLFKEHQSFPynKNGFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALD 350
Cdd:smart00561   2 DYLEETGARAAPVELFKQPVDSP--PNGFKVGMKLEAVDPRNPSLICVATVVEVKGYRLLLHFDGWDDKYDFWCHADSPD 79

                           90
                   ....*....|....*..
gi 2462610808  351 IHPVGWCEKTGHKLHPP 367
Cdd:smart00561  80 IFPVGWCEKNGHPLQPP 96

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 2462610808  486 DKYLEETNSLPAPARAFK---VKPPHGFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDI 562
Cdd:smart00561   1 EDYLEETGARAAPVELFKqpvDSPPNGFKVGMKLEAVDPRNPSLICVATVVEVKGYRLLLHFDGWDDKYDFWCHADSPDI 80

                           90
                   ....*....|....*.
gi 2462610808  563 HPVGWCSKTGHPLQPP 578
Cdd:smart00561  81 FPVGWCEKNGHPLQPP 96

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 2462610808  380 YLKTCKAQAAPKSLFeNQNITVIPSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIH 459
Cdd:smart00561   3 YLEETGARAAPVELF-KQPVDSPPNGFKVGMKLEAVDPRNPSLICVATVVEVKGYRLLLHFDGWDDKYDFWCHADSPDIF 81

                           90
                   ....*....|....*
gi 2462610808  460 PVGWCKEHRRTLITP 474
Cdd:smart00561  82 PVGWCEKNGHPLQPP 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 2462610808 410 MKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPP 475
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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462610808  740 VSKWSTDEVSEFIQSLpGCEEHGKVFKDEQIDGEAFL-LMTQTDIVKIMSIKLGPALKIFNSILMFKA 806
Cdd:smart00454   1 VSQWSPESVADWLESI-GLEQYADNFRKNGIDGALLLlLTSEEDLKELGITKLGHRKKILKAIQKLKE 67

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 2462610808 294 YNKNGFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPKGYKEE 373
Cdd:cd20101     1 FNKNGFKVGMKLEGIDPKHPSLFCVLSVAEVRGYRLRLHFDGYSECYDFWVNADSPDIFPVGWCEKTGHKLQPPKGYTSE 80

                          90       100
                  ....*....|....*....|.
gi 2462610808 374 EFNWQTYLKTCKAQAAPKSLF 394
Cdd:cd20101    81 TFSWSAYLKLTKAQAAPKHLF 101

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610808 401 VIPSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYPNV 480
Cdd:cd20135     1 VTPSGFRVGMKLEAVDKKNPSFICVATITDMVDNRLLIHFDNWDESYDYWCDASSPYIHPVGYCQEHGRTLTTPPGYKDP 80

                          90
                  ....*....|...
gi 2462610808 481 KHFSWDKYLEETN 493
Cdd:cd20135    81 KHFSWEKYLEETN 93

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 2462610808 403 PSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYPnVKH 482
Cdd:cd20102     1 PHGFRVGMKLEAVDRKNPSLICVATVTDVIGNRFLVHFDGWDDSYDYWCDPDSPYIHPVGWCEENGKTLQPPKGYS-PGN 79

                          90
                  ....*....|.
gi 2462610808 483 FSWDKYLEETN 493
Cdd:cd20102    80 FSWDKYLEETN 90

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462610808 502 FKVKPPHGFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPPL 579
Cdd:cd20138     1 FKVKPPHGFQKNMKLEVVDKRNPMLIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPAGWCAKTGHPLQPPL 78

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610808 402 IPSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYPNVK 481
Cdd:cd20136     1 MPKEFQVGMKLEAVDRKNPSLVCVATIADIVEDRLLVHFDNWDDSYDYWCDVNSPYIQPVGWCQENGRTLVAPQGYPNPE 80

                          90
                  ....*....|.
gi 2462610808 482 HFSWDKYLEET 492
Cdd:cd20136    81 KFSWTEYLEAT 91

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462610808 506 PPHGFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPPL 579
Cdd:cd20137     1 PPHGFQVNMKLEAVDRRNPALIRVASVEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPPL 74

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 2462610808 740 VSKWSTDEVSEFIQSLPGCEEHGKVFKDEQIDGEAFLLMTQTDIVKIMSIKLGPALKIFNSILMFK 805
Cdd:cd09582     1 VLRWSVDEVAEFVQSLPGCEEHAKVFRDEQIDGEAFLLLTQSDLVKILGIKLGPALKIYNSILMLR 66

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 2462610808 514 MKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPPL 579
Cdd:pfam02820   1 MKLEAVDPLNPSLICVATVVKVLGGRLRLRFDGWDDSYDFWCHADSPDIHPVGWCEKNGHPLQPPK 66

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 2462610808 297 NGFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPKGYKEEEFN 376
Cdd:cd20102     2 HGFRVGMKLEAVDRKNPSLICVATVTDVIGNRFLVHFDGWDDSYDYWCDPDSPYIHPVGWCEENGKTLQPPKGYSPGNFS 81

                  ....*....
gi 2462610808 377 WQTYLKTCK 385
Cdd:cd20102    82 WDKYLEETN 90

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 2462610808 303 MKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPK 368
Cdd:pfam02820   1 MKLEAVDPLNPSLICVATVVKVLGGRLRLRFDGWDDSYDFWCHADSPDIHPVGWCEKNGHPLQPPK 66

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 2462610808 403 PSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYpNVKH 482
Cdd:cd20101     3 KNGFKVGMKLEGIDPKHPSLFCVLSVAEVRGYRLRLHFDGYSECYDFWVNADSPDIFPVGWCEKTGHKLQPPKGY-TSET 81

                          90       100
                  ....*....|....*....|
gi 2462610808 483 FSWDKYLEETNSLPAPARAF 502
Cdd:cd20101    82 FSWSAYLKLTKAQAAPKHLF 101

SAM domain of Polycomb group; SAM (sterile alpha motif) domain of Polycomb group is a protein-protein interaction domain. The Polycomb group includes transcriptional repressors which are involved in the regulation of some key regulatory genes during development in many organisms. They are best known for silencing Hox (Homeobox) genes. Polycomb proteins work together in large multimeric and chromatin-associated complexes. They organize chromatin of the target genes and maintain repressed states during many cell divisions. Polycomb proteins are classified based on their common function, but not on conserved domains and/or motifs; however many Polycomb proteins (members of PRC1 class complex) contain SAM domains which are more similar to each other inside of the Polycomb group than to SAM domains outside of it. Most information about structure and function of Polycomb SAM domains comes from studies of Ph (Polyhomeotic) and Scm (Sex comb on midleg) proteins. Polycomb SAM domains usually can be found at the C-terminus of the proteins. Some members of this group contain, in addition to the SAM domain, MTB repeats, Zn finger, and/or DUF3588 domains. Polycomb SAM domains can form homo- and/or heterooligomers through ML and EH surfaces. SAM/SAM oligomers apparently play a role in transcriptional repression through polymerization along the chromosome. Polycomb proteins are known to be highly expressed in some cells years before their cancer pathology; thus they are attractive markers for early cancer therapy.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462610808 740 VSKWSTDEVSEFIQSLPGCEEHGKVFKDEQIDGEAFLLMTQTDIVKIMSIKLGPALKIFNSILM 803
Cdd:cd09509     1 PSKWSVDDVAQFIKSLDGCAEYAEVFREQEIDGQALLLLTEDDLLKGMGLKLGPALKIYNHIVK 64

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462610808 510 FQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPP 578
Cdd:cd20092     6 FKVGMKLEAVDRKNPQLICPATVGDVDGDEIHISFDGWRGAFDYWCRYDSRDIFPVGWCKKTGHPLQPP 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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610808 299 FKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPKGYKE-EEFNW 377
Cdd:cd20136     5 FQVGMKLEAVDRKNPSLVCVATIADIVEDRLLVHFDNWDDSYDYWCDVNSPYIQPVGWCQENGRTLVAPQGYPNpEKFSW 84

                  ....*
gi 2462610808 378 QTYLK 382
Cdd:cd20136    85 TEYLE 89

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610808 507 PHGFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPP-------- 578
Cdd:cd20136     2 PKEFQVGMKLEAVDRKNPSLVCVATIADIVEDRLLVHFDNWDDSYDYWCDVNSPYIQPVGWCQENGRTLVAPqgypnpek 81

                          90
                  ....*....|.
gi 2462610808 579 LSPLELMEASE 589
Cdd:cd20136    82 FSWTEYLEATQ 92

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 2462610808 403 PSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGY 477
Cdd:cd20139     6 PHGFQVNMKLEAVDKRNPILIRVATIVDKDDHRIKLHFDGWDHNYDFWVDADSPDIHPVGWCDKTGHALQVPLGA 80

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 2462610808 508 HGFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPP 578
Cdd:cd20100     1 HGFKVGMKLEAVDLMEPRLICVATVTRVVGRLLRVHFDGWDDEFDQWVDCDSPDIYPVGWCELVGYPLQPP 71

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 2462610808 288 EHQSFPYNKngFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPP 367
Cdd:cd20091     1 QSPIPPVNE--FKVGMKLEAQDPRNLTSTCIATVVGIQGPRLRLRLDGSDNKNDFWRLVDSSDIHPVGWCEKNGGLLQPP 78

                          90
                  ....*....|....*
gi 2462610808 368 KGYKEEEFNWQTYLK 382
Cdd:cd20091    79 LGFRMNPSSWPMFLQ 93

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 2462610808 510 FQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNN-CYDYWIDADSPDIHPVGWCS 569
Cdd:cd20088     1 FKVGMKLEAVDPLNPSEICVATVVKVVGGRLLLHFDGWDPsRYDFWCDVDSPDIHPVGWCE 61

third 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 third 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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610808 406 FRVGMKLEAVDKKNPSFICVATVTDMVDNRFLV----HFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYPNvK 481
Cdd:cd20099     1 FKVGMKLEAVDPLNLSSICVATVRKVLRFGYLVigidGPSADDGSDWFCCHASSPFIFPVGFAEKNGIELTPPRGYES-K 79

                          90
                  ....*....|..
gi 2462610808 482 HFSWDKYLEETN 493
Cdd:cd20099    80 PFDWEEYLEETG 91

third 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 third 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 2462610808 406 FRVGMKLEAVDKKNPSFICVATVTDMVDNR-FLVHFDN----WDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYPNv 480
Cdd:cd20095     1 FKVGMKLEALHPKNPSTICPATVTKVFNEYyFLVEIDDlrpeESEKITFVCHANSPGIFPVGWCAKNGLRLTPPPGYPK- 79

                          90
                  ....*....|...
gi 2462610808 481 KHFSWDKYLEETN 493
Cdd:cd20095    80 SEFDWDSYLKLCG 92

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462610808 296 KNGFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPK 368
Cdd:cd20092     3 KNMFKVGMKLEAVDRKNPQLICPATVGDVDGDEIHISFDGWRGAFDYWCRYDSRDIFPVGWCKKTGHPLQPPG 75

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610808 298 GFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPKGYKE-EEFN 376
Cdd:cd20134     5 GFQVGMKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDpDNFS 84

                  ....*.
gi 2462610808 377 WQTYLK 382
Cdd:cd20134    85 WEKYLE 90

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462610808 298 GFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPKGYKE-EEFN 376
Cdd:cd20135     5 GFRVGMKLEAVDKKNPSFICVATITDMVDNRLLIHFDNWDESYDYWCDASSPYIHPVGYCQEHGRTLTTPPGYKDpKHFS 84

                  ....*
gi 2462610808 377 WQTYL 381
Cdd:cd20135    85 WEKYL 89

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462610808 297 NGFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPP 367
Cdd:cd20138     7 HGFQKNMKLEVVDKRNPMLIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPAGWCAKTGHPLQPP 77

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 2462610808 500 RAFKVKPPH--GFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQP 577
Cdd:cd20131     2 QDSQAVTHNknGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQP 81

                  .
gi 2462610808 578 P 578
Cdd:cd20131    82 P 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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462610808 508 HGFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPP 578
Cdd:cd20129     1 HGFRVGMKLEAVDLMEPRLVCVATVTRIIHRLLRIHFDGWEDEYDQWVDCESPDLYPVGWCQLTGYQLQPP 71

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462610808 506 PPHGFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPPL 579
Cdd:cd20091     6 PVNEFKVGMKLEAQDPRNLTSTCIATVVGIQGPRLRLRLDGSDNKNDFWRLVDSSDIHPVGWCEKNGGLLQPPL 79

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 2462610808 290 QSFPYNKNGFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPKG 369
Cdd:cd20107     1 QAQNPPKNEFKIGMKLEALDPRNVTSTCIATVVGVLGPRLRLRLDGSDNKNDFWRLVDSTEIHPIGHCEKNGGMLQPPLG 80

                          90
                  ....*....|..
gi 2462610808 370 YKEEEFNWQTYL 381
Cdd:cd20107    81 FRMNASSWPMFL 92

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 2462610808 297 NGFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPKGYKEEEFN 376
Cdd:cd20106     8 NDFKVGMKLEARDPRNATSVCIATVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPIGTCEKEGDMLQPPLGFQMNASS 87

                  ....*
gi 2462610808 377 WQTYL 381
Cdd:cd20106    88 WPMFL 92