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Conserved domains on  [gi|1018614684|ref|NP_001309947|]
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SET domain-containing protein 9 isoform 3 [Homo sapiens]

Protein Classification

SET domain-containing protein 9( domain architecture ID 14410638)

SET domain-containing protein 9 (SETD9) is an uncharacterized protein that belongs to the class V-like SAM-binding methyltransferase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET_SETD9 cd10537
SET domain found in SET domain-containing protein 9 (SETD9) and similar proteins; SETD9 is an ...
 93-270 3.24e-79

SET domain found in SET domain-containing protein 9 (SETD9) and similar proteins; SETD9 is an uncharacterized protein that belongs to the class V-like SAM-binding methyltransferase superfamily.


:

Pssm-ID: 380935  Cd Length: 150  Bit Score: 235.93  E-value: 3.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018614684  93 TLGFSVAQATSSLISAGKGVFVTKGLVPKGAVVSMYPGTVYQKYEPIFFQSIGNPFIFRCLDGVLIDGNdkgiskvvyrs 172
Cdd:cd10537     1 VLGFTLHRKPSSIPDAGTGVFVEKGRVPPGTVVALYPGTVYLPYEPILFQSIGNPFLFRRYDGIIIDGN----------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018614684 173 cngrdrlgplkmsdstwltseihnPLAVGQYVNNCSNDRAANVCYQEFDVPAVFPIELKQYLPNIAYSYD-------KQS 245
Cdd:cd10537    70 ------------------------PLALGHYVNHPPKGTPPNVAYQEYDFPEDFPEELRRYIPNVYYSPDqvfnmtrGKR 125

                         170       180
                  ....*....|....*....|....*
gi 1018614684 246 PLRCVVLVALRDINQGEELFSNYYT 270
Cdd:cd10537   126 PLRGVVLVATRDIKDGEELFSNYRT 150
 
Name Accession Description Interval E-value
SET_SETD9 cd10537
SET domain found in SET domain-containing protein 9 (SETD9) and similar proteins; SETD9 is an ...
 93-270 3.24e-79

SET domain found in SET domain-containing protein 9 (SETD9) and similar proteins; SETD9 is an uncharacterized protein that belongs to the class V-like SAM-binding methyltransferase superfamily.


Pssm-ID: 380935  Cd Length: 150  Bit Score: 235.93  E-value: 3.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018614684  93 TLGFSVAQATSSLISAGKGVFVTKGLVPKGAVVSMYPGTVYQKYEPIFFQSIGNPFIFRCLDGVLIDGNdkgiskvvyrs 172
Cdd:cd10537     1 VLGFTLHRKPSSIPDAGTGVFVEKGRVPPGTVVALYPGTVYLPYEPILFQSIGNPFLFRRYDGIIIDGN----------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018614684 173 cngrdrlgplkmsdstwltseihnPLAVGQYVNNCSNDRAANVCYQEFDVPAVFPIELKQYLPNIAYSYD-------KQS 245
Cdd:cd10537    70 ------------------------PLALGHYVNHPPKGTPPNVAYQEYDFPEDFPEELRRYIPNVYYSPDqvfnmtrGKR 125

                         170       180
                  ....*....|....*....|....*
gi 1018614684 246 PLRCVVLVALRDINQGEELFSNYYT 270
Cdd:cd10537   126 PLRGVVLVATRDIKDGEELFSNYRT 150
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 235-268 7.88e-05

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.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 41.35  E-value: 7.88e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1018614684 235 PNIAYSYDKQSPLRCVVLVALRDINQGEELFSNY 268
Cdd:pfam00856  81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDY 114
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
108-271 1.02e-03

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 38.40  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018614684 108 AGKGVFVTKGLvPKGAVVSMYPGTVY---QKYEPIFFQSIGNPFIFRCLDGVLIDGNDKGiskvvyrsCNGRdrlgplkm 184
Cdd:COG2940    16 HGRGVFATRDI-PKGTLIGEYPGEVItwaEAERREPHKEPLHTYLFELDDDGVIDGALGG--------NPAR-------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018614684 185 sdstwltseihnplavgqYVNNCSNdraanvcyqefdvpavfpielkqylPNIAYSYDKQSplrcVVLVALRDINQGEEL 264
Cdd:COG2940    79 ------------------FINHSCD-------------------------PNCEADEEDGR----IFIVALRDIAAGEEL 111


                  ....*..
gi 1018614684 265 FSNYYTI 271
Cdd:COG2940   112 TYDYGLD 118
 
Name Accession Description Interval E-value
SET_SETD9 cd10537
SET domain found in SET domain-containing protein 9 (SETD9) and similar proteins; SETD9 is an ...
 93-270 3.24e-79

SET domain found in SET domain-containing protein 9 (SETD9) and similar proteins; SETD9 is an uncharacterized protein that belongs to the class V-like SAM-binding methyltransferase superfamily.


Pssm-ID: 380935  Cd Length: 150  Bit Score: 235.93  E-value: 3.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018614684  93 TLGFSVAQATSSLISAGKGVFVTKGLVPKGAVVSMYPGTVYQKYEPIFFQSIGNPFIFRCLDGVLIDGNdkgiskvvyrs 172
Cdd:cd10537     1 VLGFTLHRKPSSIPDAGTGVFVEKGRVPPGTVVALYPGTVYLPYEPILFQSIGNPFLFRRYDGIIIDGN----------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018614684 173 cngrdrlgplkmsdstwltseihnPLAVGQYVNNCSNDRAANVCYQEFDVPAVFPIELKQYLPNIAYSYD-------KQS 245
Cdd:cd10537    70 ------------------------PLALGHYVNHPPKGTPPNVAYQEYDFPEDFPEELRRYIPNVYYSPDqvfnmtrGKR 125

                         170       180
                  ....*....|....*....|....*
gi 1018614684 246 PLRCVVLVALRDINQGEELFSNYYT 270
Cdd:cd10537   126 PLRGVVLVATRDIKDGEELFSNYRT 150
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 235-269 6.09e-07

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.


Pssm-ID: 380914 [Multi-domain]  Cd Length: 72  Bit Score: 46.09  E-value: 6.09e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1018614684 235 PNIAYSYDKQSPLRCVVLVALRDINQGEELFSNYY 269
Cdd:cd08161    38 PNCEFEEVYVGGKPRVFIVALRDIKAGEELTVDYG 72
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 235-268 7.88e-05

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.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 41.35  E-value: 7.88e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1018614684 235 PNIAYSYDKQSPLRCVVLVALRDINQGEELFSNY 268
Cdd:pfam00856  81 PNCEVRVVYVNGGPRIVIFALRDIKPGEELTIDY 114
SET_LSMT cd10527
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; ...
 235-268 5.42e-04

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.


Pssm-ID: 380925 [Multi-domain]  Cd Length: 236  Bit Score: 40.51  E-value: 5.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1018614684 235 PNIAYSYDkqSPLRCVVLVALRDINQGEELFSNY 268
Cdd:cd10527   190 PNVRYEYD--EDEGSFVLVATRDIAAGEEVFISY 221
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 235-268 6.21e-04

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: 38.90  E-value: 6.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1018614684 235 PNIAYSYDkqsPLRCVVLVALRDINQGEELFSNY 268
Cdd:cd20071    65 PNAVVVFD---GNGTLRVRALRDIKAGEELTISY 95
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
108-271 1.02e-03

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 38.40  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018614684 108 AGKGVFVTKGLvPKGAVVSMYPGTVY---QKYEPIFFQSIGNPFIFRCLDGVLIDGNDKGiskvvyrsCNGRdrlgplkm 184
Cdd:COG2940    16 HGRGVFATRDI-PKGTLIGEYPGEVItwaEAERREPHKEPLHTYLFELDDDGVIDGALGG--------NPAR-------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018614684 185 sdstwltseihnplavgqYVNNCSNdraanvcyqefdvpavfpielkqylPNIAYSYDKQSplrcVVLVALRDINQGEEL 264
Cdd:COG2940    79 ------------------FINHSCD-------------------------PNCEADEEDGR----IFIVALRDIAAGEEL 111


                  ....*..
gi 1018614684 265 FSNYYTI 271
Cdd:COG2940   112 TYDYGLD 118
 
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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