Tudor domain found in PHD finger protein 20-like protein 1 (PHF20L1) and similar proteins; PHF20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. In addition to the MBT domain, PHF20L1 also contains a Tudor domain, a plant homeodomain (PHD) finger and putative DNA-binding domains AT hook and C2H2-type zinc finger. 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 1034660523  86 DFKAGEEVLARWTDCRYYPAKIEAINKEGTFTVQFYDGVIRCLKRMHIKAMPEDAKGQ 143
Cdd:cd20454     1 DFKAGEEVLARWTDCRYYPAKIEAINKEGTYTVQFYDGVIRCLKRMHIKSMPEDAKGQ 58

PHD finger protein 20-like protein 1; PHD20L1_u1 is a region of natively unstructured but highly conserved sequence on a set of higher eukaryotic PHD finger protein 20-like protein 1 like proteins. The function is not known.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034660523 318 SQKKNEADISS--SANTQKPALLSSTLSSGKARSKKCKHESGDSSGCIKPPKSPLSPELIQVEDLTLV 383
Cdd:pfam16660   1 QEKKNEADIGSivPAESQKPALLSASASSGKARGKKCKHEPGDASGCIKNPKPPADLELHQEEDLTLV 68

Tudor domain found in PHD finger protein 20-like protein 1 (PHF20L1) and similar proteins; PHF20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. In addition to the MBT domain, PHF20L1 also contains a Tudor domain, a plant homeodomain (PHD) finger and putative DNA-binding domains AT hook and C2H2-type zinc finger. 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 1034660523  86 DFKAGEEVLARWTDCRYYPAKIEAINKEGTFTVQFYDGVIRCLKRMHIKAMPEDAKGQ 143
Cdd:cd20454     1 DFKAGEEVLARWTDCRYYPAKIEAINKEGTYTVQFYDGVIRCLKRMHIKSMPEDAKGQ 58

PHD finger protein 20-like protein 1; PHD20L1_u1 is a region of natively unstructured but highly conserved sequence on a set of higher eukaryotic PHD finger protein 20-like protein 1 like proteins. The function is not known.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034660523 318 SQKKNEADISS--SANTQKPALLSSTLSSGKARSKKCKHESGDSSGCIKPPKSPLSPELIQVEDLTLV 383
Cdd:pfam16660   1 QEKKNEADIGSivPAESQKPALLSASASSGKARGKKCKHEPGDASGCIKNPKPPADLELHQEEDLTLV 68

Protein of unknown function (DUF3776); This domain family is found in eukaryotes, and is approximately 100 amino acids in length.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660523 197 SNKDKDKDERKWFKVPSKKEETS-TCIATPDVEKKEDLPTSSETFGlhvenvPKMVFPQPESTLSNKRKNNQGNSFQAKR 275
Cdd:pfam12618   1 GKKEEEEKTLKSEKICSEKGKKSeKSLPKNESEEKENISPNEEYSG------DTQVDKKPESDIVKSRSKPQGNLCEPKR 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034660523 276 ARLNKITGLLASKAVGVDGAEKKEDYNETAPMLEQ 310
Cdd:pfam12618  75 KRLGKGAGCTELKAEGRPPSITPQQKVESSSQSLQ 109

Jumonji domain-containing protein 2A Tudor domain; This is the tudor domain found in histone demethylase Jumonji domain-containing protein 2A (JMJD2A). Structure and function analysis indicate that this domain can recognize equally well two unrelated histone peptides, H3K4me3 and H4K20me3, by means of two very different binding mechanisms. JMJD2 also known as KDM4, is a conserved iron (II)-dependent jumonji-domain demethylase subfamily that is essential during development. Vertebrate KDM4A-C proteins contain a conserved double tudor domain (DTD).

                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034660523  90 GEEVLARWTDCRYYPAKIEAINKEGTFTVQFYDG 123
Cdd:pfam18104   1 GQDVIARWTDGRYYLGKFIGIHTQTFYEVEFEDG 34

Tudor domain found in PHD finger protein 20-like protein 1 (PHF20L1) and similar proteins; PHF20L1 is an active malignant brain tumor (MBT) domain-containing protein that binds to monomethylated lysine 142 on DNA (cytosine-5) Methyltransferase 1 (DNMT1) (DNMT1K142me1) and colocalizes at the perinucleolar space in a SET7-dependent manner. Its MBT domain reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 proteasomal degradation. In addition to the MBT domain, PHF20L1 also contains a Tudor domain, a plant homeodomain (PHD) finger and putative DNA-binding domains AT hook and C2H2-type zinc finger. 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 1034660523  86 DFKAGEEVLARWTDCRYYPAKIEAINKEGTFTVQFYDGVIRCLKRMHIKAMPEDAKGQ 143
Cdd:cd20454     1 DFKAGEEVLARWTDCRYYPAKIEAINKEGTYTVQFYDGVIRCLKRMHIKSMPEDAKGQ 58

PHD finger protein 20-like protein 1; PHD20L1_u1 is a region of natively unstructured but highly conserved sequence on a set of higher eukaryotic PHD finger protein 20-like protein 1 like proteins. The function is not known.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034660523 318 SQKKNEADISS--SANTQKPALLSSTLSSGKARSKKCKHESGDSSGCIKPPKSPLSPELIQVEDLTLV 383
Cdd:pfam16660   1 QEKKNEADIGSivPAESQKPALLSASASSGKARGKKCKHEPGDASGCIKNPKPPADLELHQEEDLTLV 68

Tudor domain found in PHD finger protein 20 (PHF20) and similar proteins; PHF20, also called Glioma-expressed antigen 2, hepatocellular carcinoma-associated antigen 58, novel zinc finger protein, or transcription factor TZP (referring to Tudor and zinc finger domain containing protein), is a regulator of NF-kappaB activation by disrupting recruitment of PP2A to p65. It also functions as a transcription factor that binds to Akt and plays a role in Akt cell survival/growth signaling. Moreover, it transcriptionally regulates p53. The phosphorylation of PHF20 on Ser291 mediated by protein kinase B (PKB) is essential in tumorigenesis via the regulation of p53-mediated signaling. PHF20 contains an N-terminal malignant brain tumor (MBT) domain, a Tudor domain, a plant homeodomain (PHD) finger and putative DNA-binding domains AT hook and C2H2-type zinc finger. 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 1034660523  87 FKAGEEVLARWTDCRYYPAKIEAINKEGTFTVQFYDGVIRCLKRMHIKAMPED 139
Cdd:cd20453     1 FQVNEQVLACWSDCRFYPAKVTAVNKDGTYTVKFYDGVVQTVKHIHVKAFSKD 53

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1034660523  90 GEEVLARWT-DCRYYPAKIEAINKEGTFTVQFYDGVIRCLKRMHIK 134
Cdd:cd04508     1 GDRVEAKWSdDGQWYPATVVAVNDDGKYTVLFDDGNEEEVSEDDIR 46

Protein of unknown function (DUF3776); This domain family is found in eukaryotes, and is approximately 100 amino acids in length.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034660523 197 SNKDKDKDERKWFKVPSKKEETS-TCIATPDVEKKEDLPTSSETFGlhvenvPKMVFPQPESTLSNKRKNNQGNSFQAKR 275
Cdd:pfam12618   1 GKKEEEEKTLKSEKICSEKGKKSeKSLPKNESEEKENISPNEEYSG------DTQVDKKPESDIVKSRSKPQGNLCEPKR 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034660523 276 ARLNKITGLLASKAVGVDGAEKKEDYNETAPMLEQ 310
Cdd:pfam12618  75 KRLGKGAGCTELKAEGRPPSITPQQKVESSSQSLQ 109

Jumonji domain-containing protein 2A Tudor domain; This is the tudor domain found in histone demethylase Jumonji domain-containing protein 2A (JMJD2A). Structure and function analysis indicate that this domain can recognize equally well two unrelated histone peptides, H3K4me3 and H4K20me3, by means of two very different binding mechanisms. JMJD2 also known as KDM4, is a conserved iron (II)-dependent jumonji-domain demethylase subfamily that is essential during development. Vertebrate KDM4A-C proteins contain a conserved double tudor domain (DTD).

                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034660523  90 GEEVLARWTDCRYYPAKIEAINKEGTFTVQFYDG 123
Cdd:pfam18104   1 GQDVIARWTDGRYYLGKFIGIHTQTFYEVEFEDG 34

Tudor domain found in Schizosaccharomyces pombe splicing factor spf30 (SpSPF30) and similar proteins; SpSPF30, also called survival of motor neuron-related-splicing factor 30, is necessary for spliceosome assembly. It contains one 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 1034660523  87 FKAGEEVLARWT--DCRYYPAKIEAINKEGT---FTVQFYD-GVIRCLKRMHIKAM 136
Cdd:cd20446     1 FKPGEVVMARWKsgDGKFYPARITSITGSSInpiYTVKFLDyGEIDTVYLKDIRPL 56

third malignant brain tumor (MBT) repeat found in the Lethal(3)malignant brain tumor-like protein 1 (L3MBTL1)-like family; The L3MBTL1-like family includes L3MBTL1, L3MBTL3, and L3MBTL4. L3MBTL1, also called L(3)mbt-like, or L(3)mbt protein homolog, is a Polycomb group (PcG) protein that functions as a 'reader' of a network of post-translational modifications by specifically recognizing and binding mono- and dimethyllysine residues on target proteins. It acts as a chromatin compaction factor by binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condensed chromatin and repressed transcription. L3MBTL3, also called L(3)mbt-like protein 3, or MBT-1, is a PcG protein that recognizes mono- and dimethylated lysine residues on histone tails. It also acts as a methyl-binding protein that binds the K142-methylated DNMT1 and recruits a novel CRL4(DCAF5) ubiquitin ligase to degrade DNMT1. L3MBTL4, also called L(3)mbt-like protein 4, or L3mbt-like 4, is a PcG protein that may act as a tumor suppressor. Members of this family contain three MBT (malignant brain tumor) repeats. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the third MBT repeat that contains the semi-aromatic cage that may bind methylated lysine residues.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034660523   9 PGITFEIGARLEALDylqKWYPSRIEK---IDYEEGKMLVHFERWSHRYDEWIYWDSNRLRP 67
Cdd:cd20103     1 PPHGFEVGMKLEAVD---KRNPRLIRVatvADVEDYRVKLHFDGWPDIYDFWVDDDSPDIHP 59

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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034660523  13 FEIGARLEALDYLQKWY--PSRIEKIdyeEGKML-VHFERWSHRYDEWIYWDSNRLRP 67
Cdd:cd20100     3 FKVGMKLEAVDLMEPRLicVATVTRV---VGRLLrVHFDGWDDEFDQWVDCDSPDIYP 57

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034660523   9 PGITFEIGARLEALDylqKWYPSRIEK---IDYEEGKMLVHFERWSHRYDEWIYWDSNRLRP 67
Cdd:cd20137     1 PPHGFQVNMKLEAVD---RRNPALIRVasvEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHP 59

second Tudor domain found in Jumonji domain-containing protein 2 (JMJD2) family of histone demethylases; JMJD2 proteins, also called lysine-specific demethylase 4 histone demethylases (KDM4), have been implicated in various cellular processes including DNA damage response, transcription, cell cycle regulation, cellular differentiation, senescence, and carcinogenesis. They selectively catalyze the demethylation of di- and trimethylated H3K9 and H3K36. This model contains only three JMJD2 proteins, JMJD2A-C, which all contain jmjN and jmjC domains in the N-terminal region, followed by a canonical PHD domain, a noncanonical extended PHD domain, and tandem Tudor domains. The model corresponds to the second 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. JMJD2D is not included in this model, since it lacks both the PHD and Tudor domains and has a different substrate specificity. JMJD2A-C are required for efficient cancer cell growth.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1034660523  88 KAGEEVLARWTDCRYYPAKIEAINKEGTFTVQFYDGVIRCLKRMHI 133
Cdd:cd20392     3 EVGDPVKVKWTDGELYDAKFVGSSIVIMYTVEFEDGSVLTLKREDV 48

Tudor domain found in polycomb repressive complex 2 (PRC2)-associated polycomb-like (PCL) family proteins; The PCL family includes PHD finger protein1 (PHF1) and its homologs, metal-response element-binding transcription factor 2 (MTF2/PCL2) and PHF19/PCL3, which are accessory components of the Polycomb repressive complex 2 (PRC2) core complex. Members contain an N-terminal Tudor domain followed by two PHD domains, and a C-terminal MTF2 domain. PCL proteins specifically recognize tri-methylated H3K36 (H3K36me3) through their N-terminal Tudor domains. The interaction between their Tudor domains and H3K36me3 is critical for both the targeting and spreading of PRC2 into active chromatin regions and for the maintenance of optimal repression of poised developmental genes where PCL proteins, H3K36me3, and H3K27me3 coexist. Moreover, unlike other PHD domain-containing proteins, the first PHD domains of PCL proteins do not display histone H3K4 binding affinity and they do not affect the binding of the Tudor domain to histones.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1034660523  86 DFKAGEEVLARWTDCRYYPAKIEAINKE-GTFTVQFYD 122
Cdd:cd20385     1 KFAEGQDVLARWTDGLFYLGTIKKVDSAkEKCLVIFED 38

Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing 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. Members of this group contain a single 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
                  ....*....|....*....|....*....|....*
gi 1034660523  90 GEEVLARWT-DCRYYPAKIEAINKEGTFTVQFYDG 123
Cdd:cd21182     1 GDKCLAPYSdDGKYYEATIEEITEESDTATVVFDG 35

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 1034660523   9 PGITFEIGARLEALDYLQkwyPSRI---EKIDYEEGKMLVHFERWSHRYDEW----------IYWDSNRLRPLERPalrk 75
Cdd:cd20134     2 PPLGFQVGMKLEAVDRMN---PSLVcvaSVTDVVDSRFLVHFDNWDDTYDYWcdpsspyihpVGWCQKQGKPLTPP---- 74

                  ....*....
gi 1034660523  76 EGLKDEEDF 84
Cdd:cd20134    75 QDYPDPDNF 83

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 1034660523  13 FEIGARLEALDylqKWYPSRI---EKIDYEEGKMLVHFERWSHRYDEWIYWDSNRLRPL------ERPALRKEGLKDEED 83
Cdd:cd20136     5 FQVGMKLEAVD---RKNPSLVcvaTIADIVEDRLLVHFDNWDDSYDYWCDVNSPYIQPVgwcqenGRTLVAPQGYPNPEK 81

                  .
gi 1034660523  84 F 84
Cdd:cd20136    82 F 82

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 1034660523  13 FEIGARLEALDYLQKWYPSRIEKIDYEEGKM--LVHFERWSHRYDEWIywDSNRLR 66
Cdd:pfam11717   1 IEIGCKVLVRKRDGEWRLAEILSIRPKKGKYeyYVHYVGFNKRLDEWV--PEDRID 54

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 1034660523  26 QKWYPSRIEKIDYEEGKM--LVHFERWSHRYDEWI 58
Cdd:cd18641    13 QKIYEASIKSTEIDDGEVlyLVHYYGWNVRYDEWV 47