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 17555656   7 FEVGENVACIYK-GKPYDAKITDIktnSDGKELYCVHFKGWNNRYDEKIPVGEEkdRIFK 65
Cdd:cd20104   1 FKVGDRVDALDGeGKWYEAKIVEV---DEEENKVLVHYDGWSSRYDEWIDRDSE--RLRP 55

malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and similar domains; PHF20L1 associates with SOX2, antagonizes SOX2 ubiquitination and the sequential degradation induced by MLL1/WDR5 complexes. It binds both monomethylated Lys-42 and Lys-117 in SOX2 and thereby prevents SOX2 proteolysis. PHF20L1 also reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 degradation. PHF20L1 contains one MBT (malignant brain tumor) repeat. 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 MBT repeat of PHF20L1 and similar domains that contains the semi-aromatic cage that may bind methylated lysine residues.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555656   7 FEVGENVACIYK-GKPYDAKITDIktnSDGKELYCVHFKGWNNRYDEKIPVGEEkdRIFK 65
Cdd:cd20104   1 FKVGDRVDALDGeGKWYEAKIVEV---DEEENKVLVHYDGWSSRYDEWIDRDSE--RLRP 55

RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is required for binding to RNA. The know influences the loop conformation of the helical turn Ht2 - residues 61-6 3- that is located at the side opposite the knot in the tudor domain-chromodomain; stabilization of Ht2 is essential for RNA binding.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 17555656     7 FEVGENVACI-YKGKPYDAKITDIKTNSDGKELYcVHFKGWNNRYDEKIPVgeekDRI 63
Cdd:pfam11717   1 IEIGCKVLVRkRDGEWRLAEILSIRPKKGKYEYY-VHYVGFNKRLDEWVPE----DRI 53

malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and similar domains; PHF20L1 associates with SOX2, antagonizes SOX2 ubiquitination and the sequential degradation induced by MLL1/WDR5 complexes. It binds both monomethylated Lys-42 and Lys-117 in SOX2 and thereby prevents SOX2 proteolysis. PHF20L1 also reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 degradation. PHF20L1 contains one MBT (malignant brain tumor) repeat. 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 MBT repeat of PHF20L1 and similar domains that contains the semi-aromatic cage that may bind methylated lysine residues.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17555656   7 FEVGENVACIYK-GKPYDAKITDIktnSDGKELYCVHFKGWNNRYDEKIPVGEEkdRIFK 65
Cdd:cd20104   1 FKVGDRVDALDGeGKWYEAKIVEV---DEEENKVLVHYDGWSSRYDEWIDRDSE--RLRP 55

Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. ERCC6L2 gene mutations have been associated with bone marrow failure that includes developmental delay and microcephaly. It contains an N-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 17555656  15 CIYKGKPYDAKITDIKTNSDGKELYCVHFKGWNNRYDEKIPVGE 58
Cdd:cd20400  11 YSGDGKLYEAVIKSISTDENGKSFAVVKFLGYESDEDEKVPVSK 54

Chromatin organization modifier domain;

                           10        20
                   ....*....|....*....|....*....
gi 17555656     24 AKITDIKTNSDGKELYCVHFKGWNNRYDE 52
Cdd:smart00298   5 EKILDHRWKKKGELEYLVKWKGYSYSEDT 33

chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the chromo barrel domains found in human Tat-interactive protein 60 (TIP60, (also known as KAT5 or HTATIP), Drosophila melanogaster males-absent on the first (MOF) protein, human male-specific lethal (MSL) complex subunit 3 (MSL3), and retinoblastoma binding protein 1. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. The chromobarrel domains include a MOF-like subgroup which may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.

                        10        20        30
                ....*....|....*....|....*....|....*.
gi 17555656  19 GKPYDAKITDIKTNSDGK--ELYCVHFKGWNNRYDE 52
Cdd:cd18643  13 RVLYDAKILSVITGKDGRapPEYLVHYVGWNRRLDE 48