SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 154689858   298 EFLNCEGSGLFVLQSCCNHSCVPNAETSFPENN--FLLHVTALEDIKPGEEICISY 351
Cdd:smart00317  62 SDLCIDARRKGNLARFINHSCEPNCELLFVEVNgdDRIVIFALRDIKPGEELTIDY 117

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 154689858  314 CNHSCVPNAETSF--PENNFLLHVTALEDIKPGEEICISY 351
Cdd:pfam00856  75 INHSCDPNCEVRVvyVNGGPRIVIFALRDIKPGEELTIDY 114

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing protein, and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1-SYMD5. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154689858 298 EFLNCEGSGLFVLQSCCNHSCVPNAETSFpENNFLLHVTALEDIKPGEEICISYLDCCQRERSRHSRhkiLRENYLFVCS 377
Cdd:cd20071   43 DGLNEIGVGLFPLASLLNHSCDPNAVVVF-DGNGTLRVRALRDIKAGEELTISYIDPLLPRTERRRE---LLEKYGFTCS 118

                 ....
gi 154689858 378 CPKC 381
Cdd:cd20071  119 CPRC 122

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 (SMYD3) and similar proteins; SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. It is overexpressed in colorectal, breast, prostate, and hepatocellular tumors, and has been implicated as an oncogene in human malignancies. Methylation of MEKK2 by SMYD3 is important for regulation of the MEK/ERK pathway, suggesting the possibility of selectively targeting SMYD3 in RAS-driven cancers.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154689858 304 GSGLFVLQSCCNHSCVPNAETSFpeNNFLLHVTALEDIKPGEEICISYLDCCQrerSRHSRHKILRENYLFVCSCPKCL 382
Cdd:cd19203  136 GVGLYPSASLLNHSCDPNCVIVF--NGPHLLLRAIREIEVGEELTISYIDMLM---PSEERRKQLRDQYCFECDCFRCQ 209

SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, SMYD2, SMYD3 and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1, SMYD2 and SMYD3. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154689858 304 GSGLFVLQSCCNHSCVPNAETSFpeNNFLLHVTALEDIKPGEEICISYLDCCQRERSRHSRhkiLRENYLFVCSCPKCL 382
Cdd:cd19167  131 GVGIYPQAALLNHSCCPNCIVTF--NGPNIEVRAVQEIEPGEEVFHSYIDLLYPTEERRDQ---LRDQYFFLCQCADCQ 204

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 154689858  314 CNHSCVPNAETSF--PENNFLLHVTALEDIKPGEEICISY 351
Cdd:pfam00856  75 INHSCDPNCEVRVvyVNGGPRIVIFALRDIKPGEELTIDY 114

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains has been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154689858 304 GSGLFVLQS-----------CCNHSCVPNAETSFPENNFLLHV--TALEDIKPGEEICISY 351
Cdd:cd08161   11 GFGLFATRDipkgeviglarFINHSCEPNCEFEEVYVGGKPRVfiVALRDIKAGEELTVDY 71

SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing protein, and similar proteins; The family includes SET and MYND domain-containing proteins, SMYD1-SYMD5. SMYD1 (EC 2.1.1.43; also termed BOP) is a heart and muscle specific SET-MYND domain containing protein, which functions as a histone methyltransferase and regulates downstream gene transcription. It methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. SMYD2 (also termed HSKM-B, or lysine N-methyltransferase 3C (KMT3C)) functions as a histone methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. It specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). SMYD3 (also termed zinc finger MYND domain-containing protein 1) functions as a histone methyltransferase that specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation. It also methylates 'Lys-5' of histone H4. SMYD3 plays an important role in transcriptional activation as a member of an RNA polymerase complex. SMYD4 functions as a potential tumor suppressor that plays a critical role in breast carcinogenesis at least partly through inhibiting the expression of PDGFR-alpha. SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 154689858  24 EVRFVSSAKGKGLFATQLIRKGETIFVERPLVAAQF 59
Cdd:cd20071    1 EVRESEGSKGRGLVATRDIEPGELILVEKPLVSVPS 36

SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; Rubisco LSMT is a non-histone protein methyl transferase responsible for the trimethylation of lysine14 in the large subunit of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase). The family also includes SET domain-containing proteins, SETD3, SETD4 and SETD6, which belong to methyltransferase class VII that represents classical non-histone SET domain methyltransferases. Members in this family contain a SET domain and a C-terminal RubisCO LSMT substrate-binding (Rubis-subs-bind) domain.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 154689858 314 CNHS-CVPNAETSFPENNFLLHVTALEDIKPGEEICISY 351
Cdd:cd10527  183 LNHSpDAPNVRYEYDEDEGSFVLVATRDIAAGEEVFISY 221

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins; LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 154689858 315 NHSCVPNAETSFPENNFLLHVT--ALEDIKPGEEICISY 351
Cdd:cd10522   78 NHSDQPNLELIVRTLKGEQHIGfvAIRDIKPGEELFISY 116

SET domain-containing protein (function unknown) [General function prediction only];

                         10        20
                 ....*....|....*....|....*.
gi 154689858  23 VEVRfVSSAKGKGLFATQLIRKGETI 48
Cdd:COG2940    8 IEVR-PSPIHGRGVFATRDIPKGTLI 32

SET domain found in SET domain-containing protein 5 (SETD5), inactive histone-lysine N-methyltransferase 2E (KMT2E) and similar proteins; SETD5 is a probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. KMT2E (also termed inactive lysine N-methyltransferase 2E or myeloid/lymphoid or mixed-lineage leukemia protein 5 (MLL5)) associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription. The family also includes Saccharomyces cerevisiae SET domain-containing proteins, SET3 and SET4, and Schizosaccharomyces pombe SET3. Most of these family members contain a post-SET domain which harbors a zinc-binding site.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 154689858 316 HSCVPNAETS---FPENNFLLHVTALEDIKPGEEICISY 351
Cdd:cd10529   85 RSCRPNAELRhvvVSNGELRLFIFALKDIRKGTEITIPF 123

SET domain found in SET domain-containing protein 3 (SETD3) and similar proteins; SETD3 (EC 2.1.1.43) is a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me). It functions as a transcriptional activator that plays an important role in the transcriptional regulation of muscle cell differentiation via interaction with MYOD1.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 154689858 314 CNHsCVPNAETSFPENNFLLHVTALEDIKPGEEICISY 351
Cdd:cd19176  199 CNH-ANGKITTDYNLESDSLECVAMEDFKAGEQVFIFY 235