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
                ....*....|....*....|....*....|....*....|....*..
gi 71992950 439 GKPYDAYIVDIItdtDGKDFYCVHFKGWNSRYDEKIPVGEEqgRLFK 485
Cdd:cd20104  14 GKWYEAKIVEVD---EEENKVLVHYDGWSSRYDEWIDRDSE--RLRP 55

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
                ....*....|....*....|....*....|....*....|....*....
gi 71992950  11 FAIGEDITCVYKTHP-YDATIIGIEnnrEGKECYCVHFKGWNCRYDEKI 58
Cdd:cd20104   1 FKVGDRVDALDGEGKwYEAKIVEVD---EEENKVLVHYDGWSSRYDEWI 46

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
                ....*....|....*....|....*....|....*....|....*..
gi 71992950 439 GKPYDAYIVDIItdtDGKDFYCVHFKGWNSRYDEKIPVGEEqgRLFK 485
Cdd:cd20104  14 GKWYEAKIVEVD---EEENKVLVHYDGWSSRYDEWIDRDSE--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
                ....*....|....*....|....*....|....*....|....*....
gi 71992950  11 FAIGEDITCVYKTHP-YDATIIGIEnnrEGKECYCVHFKGWNCRYDEKI 58
Cdd:cd20104   1 FKVGDRVDALDGEGKwYEAKIVEVD---EEENKVLVHYDGWSSRYDEWI 46

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 71992950   427 FIIGEQVTCT-QNGKPYDAYIVDIITDTDGKDFYcVHFKGWNSRYDEKIPV 476
Cdd:pfam11717   1 IEIGCKVLVRkRDGEWRLAEILSIRPKKGKYEYY-VHYVGFNKRLDEWVPE 50

Chromatin organization modifier domain;

                           10        20
                   ....*....|....*....|....*..
gi 71992950    446 IVDIITDTDGKDFYCVHFKGWNSRYDE 472
Cdd:smart00298   7 ILDHRWKKKGELEYLVKWKGYSYSEDT 33

chromo barrel domain of human male-specific lethal complex subunit 3, and similar proteins; This subgroup includes human male-specific lethal (MSL) complex subunit 3 (MSL3, also known as MSL3L1). The MSL3 chromodomain specifically recognizes the H4K20 monomethyl mark, in a DNA-dependent manner, and may be involved in chromosomal targeting of the MSL complex. Also included is MORF-related gene on chromosome 15 (MRG15, also known as MORF4L1) which specifically binds to Lys36-methylated histone H3 and plays a role in transcriptional regulation and in DNA repair. This subgroup also includes Arabidopsis thaliana Morf Related Gene 2 (MRG2) which acts as a H3K4me3/H3K36me3 reader involved in the regulation of Arabidopsis flowering. 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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71992950 329 ELVACTYKGKVYDAVITDIKPDKDGKEcYCIHFKGWNNRYDEQIPigeeTDRIFK 383
Cdd:cd18983   1 ERVLCFHGPLLYEAKILDVIPDKKEWK-YFIHYNGWNKSWDEWVP----EDRVLK 50

MAEBL; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992950    77 KKSHKTVVTAVVAGKQKQTASSSADSNGTSSGATEKAAKAPAATMRKSAKKVDESSSEAADPKAKAEESSQNALKVDPPL 156
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992950   157 TTRKSSRTTTEATGAMKRLTVAQETEDEAPKETVQK------KARIEPVDSAEESKAKGSTAPMRKSAKKVGESNSEATD 230
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkadeaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992950   231 PEAKAKE---SSQSALKVEPPLTTHNSSRKTVEATGAMKRLTVAKETE--DEALKSQKKARIEPVEDASKAKGSAAPKSA 305
Cdd:PTZ00121 1475 AKKKAEEakkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkaDEAKKAEEAKKADEAKKAEEKKKADELKKA 1554

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
                ....*....|....*....|....*....|....*....|....*....
gi 71992950  11 FAIGEDITCVYKTHP-YDATIIGIEnnrEGKECYCVHFKGWNCRYDEKI 58
Cdd:cd20104   1 FKVGDRVDALDGEGKwYEAKIVEVD---EEENKVLVHYDGWSSRYDEWI 46

chromo barrel domain of retinoblastoma binding protein 1, and similar proteins; Retinoblastoma-binding protein 1 (RBP1), also termed AT-rich interaction domain 4A, is a ubiquitously expressed nuclear protein. RBP1 is a tumor and leukemia suppressor that binds both methylated histone tails and DNA, and is involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndromes. The chromo barrel domain of RBP1 has been reported to recognize histone H4K20me3 weakly, and this binding is enhanced by the simultaneous binding of DNA. RBP1 binds directly, with several other proteins, to retinoblastoma protein (pRB) which regulates cell proliferation; pRB represses transcription by recruiting RBP1. 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 chromodomain.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71992950 337 GKVYDAVITDIKPDkDGKECYCIHFKGWNNRYDEQIPigeeTDRIFKGIADG 388
Cdd:cd18641  13 QKIYEASIKSTEID-DGEVLYLVHYYGWNVRYDEWVK----ADRIIWPLDKG 59

chromo barrel domain of retinoblastoma binding protein 1, and similar proteins; Retinoblastoma-binding protein 1 (RBP1), also termed AT-rich interaction domain 4A, is a ubiquitously expressed nuclear protein. RBP1 is a tumor and leukemia suppressor that binds both methylated histone tails and DNA, and is involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndromes. The chromo barrel domain of RBP1 has been reported to recognize histone H4K20me3 weakly, and this binding is enhanced by the simultaneous binding of DNA. RBP1 binds directly, with several other proteins, to retinoblastoma protein (pRB) which regulates cell proliferation; pRB represses transcription by recruiting RBP1. 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 chromodomain.

                        10        20        30
                ....*....|....*....|....*....|....*....
gi 71992950 437 QNGKPYDAYIVDIITDtDGKDFYCVHFKGWNSRYDEKIP 475
Cdd:cd18641  11 KTQKIYEASIKSTEID-DGEVLYLVHYYGWNVRYDEWVK 48

MAEBL; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992950    53 RYDEKIVIGEEKDRIFKGTVEDYYKKSHKTVVTAVVAGKQKQTASSSADSNGTSSGATEKAAKAPAATMRKSAKKVDESS 132
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK 1328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992950   133 SEAADPKAKAEESSQ--NALKVDPPLTTRKSSRTTTEATGAMKRLTVAQETEDEAPKETVQKKARIEPVDSAEESKAKGS 210
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992950   211 TAPMRKSAKKVGESNSEATDPEAKAKESSQSALKVEPPLTTHNSSRKTVEATGAMKRLTVAKETEDEALKSQKKARIEPV 290
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488

                         250       260       270
                  ....*....|....*....|....*....|...
gi 71992950   291 E---DASKAKGSAAPKSASSRAEDGESSSTNDA 320
Cdd:PTZ00121 1489 KkkaEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521

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        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 71992950 327 IGE--LVACTYKGKVYDAVITDIKPDKDGKECYCIHFKGWNNRYDEQIPIGE 376
Cdd:cd20400   3 VGDrcLAPYSGDGKLYEAVIKSISTDENGKSFAVVKFLGYESDEDEKVPVSK 54

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        40
                ....*....|....*....|....*....|....*....|....*...
gi 71992950 431 EQVTCTQN----GKPYDAYIVDIITDTDGK--DFYCVHFKGWNSRYDE 472
Cdd:cd18643   1 EKVLVFEPdpkaRVLYDAKILSVITGKDGRapPEYLVHYVGWNRRLDE 48

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        40
                ....*....|....*....|....*....|....*....|....*...
gi 71992950 337 GKVYDAVITDIKPDKDGKEC--YCIHFKGWNNRYDEQIpigeETDRIF 382
Cdd:cd18643  13 RVLYDAKILSVITGKDGRAPpeYLVHYVGWNRRLDEWV----AEDRVL 56

Chromatin organization modifier domain;

                           10        20
                   ....*....|....*....|....*..
gi 71992950    446 IVDIITDTDGKDFYCVHFKGWNSRYDE 472
Cdd:smart00298   7 ILDHRWKKKGELEYLVKWKGYSYSEDT 33

Chromatin organization modifier domain;

                           10        20
                   ....*....|....*....|....*..
gi 71992950     30 IIGIENNREGKECYCVHFKGWNCRYDE 56
Cdd:smart00298   7 ILDHRWKKKGELEYLVKWKGYSYSEDT 33