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Conserved domains on  [gi|442615898|ref|NP_001259436|]
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SET and MYND domain containing, arthropod-specific, member 4, isoform C [Drosophila melanogaster]

Protein Classification

SET domain-containing protein( domain architecture ID 14448404)

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain-containing protein may function as a protein-lysine N-methyltransferase, catalyzing the S-adenosyl-L-methionine (SAM)-dependent methylation at specific lysine residues of target proteins such as histones

CATH:  2.170.270.10
EC:  2.1.1.-
Gene Ontology:  GO:0005515|GO:0008168|GO:1904047
PubMed:  12372294|17013555|16086857

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 67-156 5.89e-17

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.


:

Pssm-ID: 380997 [Multi-domain]  Cd Length: 122  Bit Score: 76.26  E-value: 5.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615898  67 ILDVNCFEI-GQNGAKARTLYPSAFLLAHDCTPNTAHTDDPSsFEILLRTSRRVREREALTLSYAYTLQGTLKRRAFMHE 145
Cdd:cd20071   33 SVPSNSFSLtDGLNEIGVGLFPLASLLNHSCDPNAVVVFDGN-GTLRVRALRDIKAGEELTISYIDPLLPRTERRRELLE 111

                         90
                 ....*....|.
gi 442615898 146 GKLFWCCCRRC 156
Cdd:cd20071  112 KYGFTCSCPRC 122
 
Name Accession Description Interval E-value
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 67-156 5.89e-17

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.


Pssm-ID: 380997 [Multi-domain]  Cd Length: 122  Bit Score: 76.26  E-value: 5.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615898  67 ILDVNCFEI-GQNGAKARTLYPSAFLLAHDCTPNTAHTDDPSsFEILLRTSRRVREREALTLSYAYTLQGTLKRRAFMHE 145
Cdd:cd20071   33 SVPSNSFSLtDGLNEIGVGLFPLASLLNHSCDPNAVVVFDGN-GTLRVRALRDIKAGEELTISYIDPLLPRTERRRELLE 111

                         90
                 ....*....|.
gi 442615898 146 GKLFWCCCRRC 156
Cdd:cd20071  112 KYGFTCSCPRC 122
 
Name Accession Description Interval E-value
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 67-156 5.89e-17

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.


Pssm-ID: 380997 [Multi-domain]  Cd Length: 122  Bit Score: 76.26  E-value: 5.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615898  67 ILDVNCFEI-GQNGAKARTLYPSAFLLAHDCTPNTAHTDDPSsFEILLRTSRRVREREALTLSYAYTLQGTLKRRAFMHE 145
Cdd:cd20071   33 SVPSNSFSLtDGLNEIGVGLFPLASLLNHSCDPNAVVVFDGN-GTLRVRALRDIKAGEELTISYIDPLLPRTERRRELLE 111

                         90
                 ....*....|.
gi 442615898 146 GKLFWCCCRRC 156
Cdd:cd20071  112 KYGFTCSCPRC 122
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 27-158 8.98e-10

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.


Pssm-ID: 380980 [Multi-domain]  Cd Length: 210  Bit Score: 58.14  E-value: 8.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615898  27 EERRQNAVLWRHYEEKVVQRLRvtwQLEDleAEQVHEVCGILDVNCFEI--GQNGAKARTLYPSAFLLAHDCTPNTAHTD 104
Cdd:cd19203   84 EGLRQLAMVLQHYLREEIQDAS---QLPP--AFDIFELFAKVTCNSFTIcdAEMQEVGVGLYPSASLLNHSCDPNCVIVF 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442615898 105 DpsSFEILLRTSRRVREREALTLSYAYTLQGTLKRRAFMHEGKLFWCCCRRCSD 158
Cdd:cd19203  159 N--GPHLLLRAIREIEVGEELTISYIDMLMPSEERRKQLRDQYCFECDCFRCQD 210
SET_SMYD1_2_3-like cd19167
SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, ...
 18-156 4.18e-07

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.


Pssm-ID: 380944 [Multi-domain]  Cd Length: 205  Bit Score: 50.12  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615898  18 LIARMESHTEE-----RRQNAVLWRHYEEkvvqrlrvtwQLEDLEAEQVHEVCGILDVNCFEIGQNGAK--ARTLYPSAF 90
Cdd:cd19167   70 LESHVEKLDEEkkdglRSDVATLHQFMSK----------DLQLPDAAYLVELFGKVNCNGFTISDEELQhvGVGIYPQAA 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615898  91 LLAHDCTPNTAHT-DDPssfEILLRTSRRVREREALTLSYAYTLQGTLKRRAFMHEGKLFWCCCRRC 156
Cdd:cd19167  140 LLNHSCCPNCIVTfNGP---NIEVRAVQEIEPGEEVFHSYIDLLYPTEERRDQLRDQYFFLCQCADC 203
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
 59-157 1.23e-06

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 (SMYD1) and similar proteins; 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. SMYD1 plays a critical role in cardiomyocyte differentiation, cardiac morphogenesis and myofibril organization, as well as in the regulation of endothelial cells (ECs). It is expressed in vascular endothelial cells, it has beenshown that knockdown of SMYD1 in endothelial cells impairs EC migration and tube formation.


Pssm-ID: 380924 [Multi-domain]  Cd Length: 210  Bit Score: 48.57  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615898  59 EQVHEVCGILDVNCFEIG-QNGAKAR--TLYPSAFLLAHDCTPN-TAHTDDPssfEILLRTSRRVREREALTLSYAYTLQ 134
Cdd:cd10526  110 EYISHIFGVINCNGFTLSdQRGLQAVgvGIFPNLCLVNHDCWPNcTVIFNNG---RIELRALGKISEGDELTVSYIDFLN 186

                         90       100
                 ....*....|....*....|...
gi 442615898 135 GTLKRRAFMHEGKLFWCCCRRCS 157
Cdd:cd10526  187 TSEDRKEQLKKQYYFDCTCEHCT 209
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 82-156 1.64e-04

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 4 (SMYD4) and similar proteins; 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. In zebrafish, SMYD4 is ubiquitously expressed in early embryos and becomes enriched in the developing heart; mutants show a strong defect in cardiomyocyte proliferation, which lead to a severe cardiac malformation.


Pssm-ID: 380934 [Multi-domain]  Cd Length: 218  Bit Score: 42.29  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615898  82 ARTLYPSAFLLAHDCTPNTAHtddpsSFE---ILLRTSRRVREREALTLSYAYT-LQGTLK-RRAFMHEGKLFWCCCRRC 156
Cdd:cd10536  144 ATAIYPTLSLLNHSCDPNTIR-----SFYgntIVVRATRPIKKGEEITICYGPHfSRMKRSeRQRLLKEQYFFDCSCEAC 218
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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