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Conserved domains on  [gi|768811322|gb|AJV27926|]
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Set5p [Saccharomyces cerevisiae YJM1190]

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 ...
 352-429 6.61e-20

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: 85.51  E-value: 6.61e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768811322 352 NQYNGQVYHWISFINHDCEPNAYIEQVEEHEeLRLHARKPIKKGEQIRITYVNPLHGVRLRRRELRVNWGFLCQCDRC 429
Cdd:cd20071   46 NEIGVGLFPLASLLNHSCDPNAVVVFDGNGT-LRVRALRDIKAGEELTISYIDPLLPRTERRRELLEKYGFTCSCPRC 122
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 114-147 7.15e-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.


The actual alignment was detected with superfamily member cd10521:

Pssm-ID: 394802 [Multi-domain]  Cd Length: 282  Bit Score: 50.77  E-value: 7.15e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 768811322 114 VEVKFIDDEHGRGLFAKRDFSKGQIILKEnKPIV 147
Cdd:cd10521    2 VEVRFIDAAKGRGLFATRDFKKGDIIFEE-KPLV 34
 
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 ...
 352-429 6.61e-20

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: 85.51  E-value: 6.61e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768811322 352 NQYNGQVYHWISFINHDCEPNAYIEQVEEHEeLRLHARKPIKKGEQIRITYVNPLHGVRLRRRELRVNWGFLCQCDRC 429
Cdd:cd20071   46 NEIGVGLFPLASLLNHSCDPNAVVVFDGNGT-LRVRALRDIKAGEELTISYIDPLLPRTERRRELLEKYGFTCSCPRC 122
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 358-408 7.24e-10

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


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 56.96  E-value: 7.24e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 768811322   358 VYHWISFINHDCEPNAYIEQVEEHEELR--LHARKPIKKGEQIRITYVNPLHG 408
Cdd:smart00317  71 KGNLARFINHSCEPNCELLFVEVNGDDRivIFALRDIKPGEELTIDYGSDYAN 123
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 342-402 2.97e-09

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: 54.84  E-value: 2.97e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768811322  342 FLTMIGTFNINQYNGQVYHWISFINHDCEPNAY--IEQVEEHEELRLHARKPIKKGEQIRITY 402
Cdd:pfam00856  52 TLDEDSEYCIDARALYYGNWARFINHSCDPNCEvrVVYVNGGPRIVIFALRDIKPGEELTIDY 114
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
363-429 9.81e-08

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 51.12  E-value: 9.81e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768811322 363 SFINHDCEPNAYIEQVEEHeeLRLHARKPIKKGEQIRITYvnplhgvrlrrRELRVNWGFLCQCDRC 429
Cdd:COG2940   78 RFINHSCDPNCEADEEDGR--IFIVALRDIAAGEELTYDY-----------GLDYDEEEYPCRCPNC 131
SET_SMYD5 cd10521
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 114-147 7.15e-07

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 5 (SMYD5) and similar proteins; SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions. It plays an important role in chromosome integrity by regulating heterochromatin and repressing endogenous repetitive DNA elements during differentiation. In zebrafish embryogenesis, it plays pivotal roles in both primitive and definitive hematopoiesis.


Pssm-ID: 380919 [Multi-domain]  Cd Length: 282  Bit Score: 50.77  E-value: 7.15e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 768811322 114 VEVKFIDDEHGRGLFAKRDFSKGQIILKEnKPIV 147
Cdd:cd10521    2 VEVRFIDAAKGRGLFATRDFKKGDIIFEE-KPLV 34
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
113-139 7.20e-03

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 36.86  E-value: 7.20e-03
                         10        20
                 ....*....|....*....|....*..
gi 768811322 113 KVEVKfIDDEHGRGLFAKRDFSKGQII 139
Cdd:COG2940    7 RIEVR-PSPIHGRGVFATRDIPKGTLI 32
 
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 ...
 352-429 6.61e-20

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: 85.51  E-value: 6.61e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768811322 352 NQYNGQVYHWISFINHDCEPNAYIEQVEEHEeLRLHARKPIKKGEQIRITYVNPLHGVRLRRRELRVNWGFLCQCDRC 429
Cdd:cd20071   46 NEIGVGLFPLASLLNHSCDPNAVVVFDGNGT-LRVRALRDIKAGEELTISYIDPLLPRTERRRELLEKYGFTCSCPRC 122
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 358-408 7.24e-10

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


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 56.96  E-value: 7.24e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 768811322   358 VYHWISFINHDCEPNAYIEQVEEHEELR--LHARKPIKKGEQIRITYVNPLHG 408
Cdd:smart00317  71 KGNLARFINHSCEPNCELLFVEVNGDDRivIFALRDIKPGEELTIDYGSDYAN 123
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 342-402 2.97e-09

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: 54.84  E-value: 2.97e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768811322  342 FLTMIGTFNINQYNGQVYHWISFINHDCEPNAY--IEQVEEHEELRLHARKPIKKGEQIRITY 402
Cdd:pfam00856  52 TLDEDSEYCIDARALYYGNWARFINHSCDPNCEvrVVYVNGGPRIVIFALRDIKPGEELTIDY 114
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 358-431 3.20e-09

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: 56.99  E-value: 3.20e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768811322 358 VYHWISFINHDCEPNAYIeqVEEHEELRLHARKPIKKGEQIRITYVNPLHGVRLRRRELRVNWGFLCQCDRCQN 431
Cdd:cd19203  139 LYPSASLLNHSCDPNCVI--VFNGPHLLLRAIREIEVGEELTISYIDMLMPSEERRKQLRDQYCFECDCFRCQD 210
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 364-402 5.36e-09

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: 52.64  E-value: 5.36e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 768811322 364 FINHDCEPNAYIEQVEEHEELR--LHARKPIKKGEQIRITY 402
Cdd:cd08161   31 FINHSCEPNCEFEEVYVGGKPRvfIVALRDIKAGEELTVDY 71
SET_SMYD1_2_3-like cd19167
SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, ...
 358-431 1.77e-08

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: 54.74  E-value: 1.77e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768811322 358 VYHWISFINHDCEPNAYIEQVEEHEELRlhARKPIKKGEQIRITYVNPLHGVRLRRRELRVNWGFLCQCDRCQN 431
Cdd:cd19167  134 IYPQAALLNHSCCPNCIVTFNGPNIEVR--AVQEIEPGEEVFHSYIDLLYPTEERRDQLRDQYFFLCQCADCQT 205
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
363-429 9.81e-08

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 51.12  E-value: 9.81e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768811322 363 SFINHDCEPNAYIEQVEEHeeLRLHARKPIKKGEQIRITYvnplhgvrlrrRELRVNWGFLCQCDRC 429
Cdd:COG2940   78 RFINHSCDPNCEADEEDGR--IFIVALRDIAAGEELTYDY-----------GLDYDEEEYPCRCPNC 131
SET_SMYD5 cd10521
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 114-147 7.15e-07

SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing protein 5 (SMYD5) and similar proteins; SMYD5 (also termed protein NN8-4AG, or retinoic acid-induced protein 15) functions as histone lysine methyltransferase that mediates H4K20me3 at heterochromatin regions. It plays an important role in chromosome integrity by regulating heterochromatin and repressing endogenous repetitive DNA elements during differentiation. In zebrafish embryogenesis, it plays pivotal roles in both primitive and definitive hematopoiesis.


Pssm-ID: 380919 [Multi-domain]  Cd Length: 282  Bit Score: 50.77  E-value: 7.15e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 768811322 114 VEVKFIDDEHGRGLFAKRDFSKGQIILKEnKPIV 147
Cdd:cd10521    2 VEVRFIDAAKGRGLFATRDFKKGDIIFEE-KPLV 34
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
 362-431 2.13e-05

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: 45.48  E-value: 2.13e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811322 362 ISFINHDCEPNAYIeqVEEHEELRLHARKPIKKGEQIRITYVNPLHGVRLRRRELRVNWGFLCQCDRCQN 431
Cdd:cd10526  143 LCLVNHDCWPNCTV--IFNNGRIELRALGKISEGDELTVSYIDFLNTSEDRKEQLKKQYYFDCTCEHCTK 210
SET_LSMT cd10527
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; ...
 113-402 2.47e-05

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: 45.90  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811322 113 KVEVKfIDDEHGRGLFAKRDFSKGQIILKenkpiVyipPLDKLFLISNGKACARCGKALYDLtqhkIMVHYLDCEVCKAI 192
Cdd:cd10527    1 GVELA-ESPDGGRGLFATRDIAAGEVLLS-----V---PRSLLLTVETARESPLGGAALALL----ELDPELSWDVALAL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811322 193 WcsekckkahaslheLLYHswRSNRidilHAGNWKRFVNYCEKYCFTaafsvgliygSMLLDTTGEVKE-QWQKLASISQ 271
Cdd:cd10527   68 F--------------LLYE--RARG----PDSFWAPYLDSLPRPFED----------TPLFWSEEELDAlQGTPLLEAAA 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811322 272 RERIKLRDasgigstfsllngttvhteeesdngtkkgvekniddetVWEKCYELFCGAFPKAS-EEIDFEKFL---TMIG 347
Cdd:cd10527  118 AQRRRLRE--------------------------------------EYEALVEALPEALPAEPgEAFTLEEFLwalALVL 159

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768811322 348 T--FNINQYNGQ-VYH---WISFINHDCE-PNAYIEQVEEHEELRLHARKPIKKGEQIRITY 402
Cdd:cd10527  160 SraFSLPVPDGGgGLAlvpLADMLNHSPDaPNVRYEYDEDEGSFVLVATRDIAAGEEVFISY 221
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 363-402 1.14e-04

SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces pombe Set7 is a novel histone-lysine N-methyltransferase. The family also includes a viral histone H3 lysine 27 methyltransferase from Paramecium bursaria Chlorella virus 1 (PBCV-1).


Pssm-ID: 380938  Cd Length: 112  Bit Score: 41.47  E-value: 1.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 768811322 363 SFINHDCEPNAYIEQVEEHEELRLHARKPIKKGEQIRITY 402
Cdd:cd10540   67 SMFNHSYTPNAEYEIDFENQTIVFYALRDIEAGEELTINY 106
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 364-402 1.92e-04

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and similar proteins; SETD2 (also termed HIF-1, huntingtin yeast partner B, huntingtin-interacting protein 1 (HIP-1), huntingtin-interacting protein B, lysine N-methyltransferase 3A or protein-lysine N-methyltransferase SETD2) acts as histone-lysine N-methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. It has been shown that methylation is a posttranslational modification of dynamic microtubules and that SETD2 methylates alpha-tubulin at lysine 40, the same lysine that is marked by acetylation on microtubules. Methylation of microtubules occurs during mitosis and cytokinesis and can be ablated by SETD2 deletion, which causes mitotic spindle and cytokinesis defects, micronuclei, and polyploidy.


Pssm-ID: 380949 [Multi-domain]  Cd Length: 142  Bit Score: 41.80  E-value: 1.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 768811322 364 FINHDCEPNAYIEQVEEHEELR--LHARKPIKKGEQIRITY 402
Cdd:cd19172   78 FINHSCEPNCETQKWTVNGELRvgFFAKRDIPAGEELTFDY 118
SET_SETD1 cd19169
SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and ...
 364-406 2.08e-04

SET domain (including post-SET domain) found in SET domain-containing protein 1 (SETD1) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A) and SET domain-containing protein 1B (SETD1B). These proteins are histone-lysine N-methyltransferases that specifically methylate 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated.


Pssm-ID: 380946  Cd Length: 148  Bit Score: 41.55  E-value: 2.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 768811322 364 FINHDCEPNAY--IEQVEEHEELRLHARKPIKKGEQIRITYVNPL 406
Cdd:cd19169   89 FINHSCNPNCYakIITVESQKKIVIYSKRPIAVNEEITYDYKFPI 133
SET_KMT2A_2B cd19170
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), ...
 364-406 2.72e-04

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B) and similar proteins; This family includes KMT2A and KMT2B. Both KMT2A (also termed ALL-1 or CXXC7 or MLL or MLL1 or TRX1 or HRX) and KMT2B (also termed MLL4 or TRX2) act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380947 [Multi-domain]  Cd Length: 152  Bit Score: 41.61  E-value: 2.72e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 768811322 364 FINHDCEPNAY--IEQVEEHEELRLHARKPIKKGEQIRITYVNPL 406
Cdd:cd19170   89 FINHSCEPNCYsrVVNIDGKKHIVIFALRRILRGEELTYDYKFPI 133
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 362-437 3.26e-04

SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of variegation 4-20 (Suv4-20) and similar proteins; Suv4-20 (also termed Su(var)4-20) is a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-20' of histone H4. It acts as a dominant suppressor of position-effect variegation. The family also includes Suv4-20 homologs, lysine N-methyltransferase 5B (KMT5B) and lysine N-methyltransferase 5C (KMT5C). Both KMT5B (also termed lysine-specific methyltransferase 5B, or suppressor of variegation 4-20 homolog 1, or Su(var)4-20 homolog 1, or Suv4-20h1) and KMT5C (also termed lysine-specific methyltransferase 5C, or suppressor of variegation 4-20 homolog 2, or Su(var)4-20 homolog 2, or Suv4-20h2) are histone methyltransferases that specifically trimethylate 'Lys-20' of histone H4 (H4K20me3). They play central roles in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.


Pssm-ID: 380922 [Multi-domain]  Cd Length: 141  Bit Score: 41.11  E-value: 3.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768811322 362 ISFINHDCEPNAYIEQVEEhEELRLHARKPIKKGEQIRITYVNPLHGVRLRRrelrvnwgflCQCDRCQNELSTFE 437
Cdd:cd10524   77 AAFINHDCRPNCKFVPTGK-STACVKVLRDIEPGEEITVYYGDNYFGENNEE----------CECETCERRGRGAF 141
SET_SETDB-like cd10538
SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) ...
 364-402 4.15e-04

SET domain (including pre-SET and post-SET domains) found in SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2, and similar proteins; The family includes SET domain bifurcated 1 (SETDB1) and 2 (SETDB2), suppressor of variegation 3-9 homologs, SUV39H1 and SUV39H2, euchromatic histone-lysine N-methyltransferase EHMT1 and EHMT2. SETDB1 (EC 2.1.1.43; also termed ERG-associated protein with SET domain (ESET), histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, or lysine N-methyltransferase 1E (KMT1E)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. SETDB2 (EC 2.1.1.43; also termed chronic lymphocytic leukemia deletion region gene 8 protein (CLLD8), or lysine N-methyltransferase 1F (KMT1F)) acts as a histone-lysine N-methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). It is involved in left-right axis specification in early development and mitosis. SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. EHMT1 (also termed Eu-HMTase1, G9a-like protein 1, GLP, GLP1, histone H3-K9 methyltransferase 5, H3-K9-HMTase 5, lysine N-methyltransferase 1D, or KMT1D) and EHMT2 (also termed Eu-HMTase2, HLA-B-associated transcript 8, histone H3-K9 methyltransferase 3, H3-K9-HMTase 3, lysine N-methyltransferase 1C, KMT1C, or protein G9a), both act as histone-lysine N-methyltransferases that specifically mono- and dimethylate 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. This family also includes the pre-SET domain, which is found in a number of histone methyltransferases (HMTase), N-terminal to the SET domain. Pre-SET domain is a zinc binding motif which contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilizing SET domains. Most family members, except for Arabidopsis thaliana SUVH9, contain a post-SET domain which harbors a zinc-binding site.


Pssm-ID: 380936 [Multi-domain]  Cd Length: 217  Bit Score: 41.97  E-value: 4.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 768811322 364 FINHDCEPNAYIEQVE-EHEELRLH-----ARKPIKKGEQIRITY 402
Cdd:cd10538  172 FINHSCDPNLFPFNVViDHDDLRYPrialfATRDILPGEELTFDY 216
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 361-402 8.02e-04

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.


Pssm-ID: 380920 [Multi-domain]  Cd Length: 122  Bit Score: 39.25  E-value: 8.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 768811322 361 WISFINHDCEPNAYIEQVEEHEELRLHAR--KPIKKGEQIRITY 402
Cdd:cd10522   73 LTRFINHSDQPNLELIVRTLKGEQHIGFVaiRDIKPGEELFISY 116
SET_SETD4 cd19177
SET domain found in SET domain-containing protein 4 (SETD4) and similar proteins; SETD4 is a ...
 120-402 2.64e-03

SET domain found in SET domain-containing protein 4 (SETD4) and similar proteins; SETD4 is a cytosolic and nuclear functional lysine methyltransferase that plays a crucial role in breast carcinogenesis. However, its specific substrates and modification sites remain to be disclosed.


Pssm-ID: 380954 [Multi-domain]  Cd Length: 245  Bit Score: 39.59  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811322 120 DDEHGRGLFAKRDFskgqiilKENKPIVYIPpldKLFLIsNGKACARCGKALY------DLTQHKIMVHYLdcevckaiw 193
Cdd:cd19177   10 FPDTGRGLVATKDI-------KPGELIISIP---ESLLI-NTTTVLSSLLGSLikrvkpKLSSLQLLALFL--------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811322 194 CSEKCKKAHASlhellyhswrsnridilhagnWKRFVNycekyCFTAAF-SVGLIYGSMLLDTTG-----EVKEQWQKla 267
Cdd:cd19177   70 ALEKRRGENSF---------------------WAPYLD-----SLPKSFdTHPLYWSLEELSLLPpslleAVRKLLDK-- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811322 268 sisQRERIKlrdasgigstfsllngttvhteeesdngtkkgvekniDDETVWEKCYELFCGAFPkaSEEIDFEKFLtmIG 347
Cdd:cd19177  122 ---QKKRFE-------------------------------------SDWEIISSVLKSLPSLFD--SEIFTLEEFR--WA 157

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768811322 348 TFNINQ----YNGQVYHWIS-------------FINHDCEPNAYIEQVEEHEELRLHARKPIKKGEQIRITY 402
Cdd:cd19177  158 WLCVNTrcvyYKLPLSDYLSssednialapfldLLNHSPDVNVKAGFNKSGKCYEIRTGTDYKKGEEVFISY 229
SET_SETD1-like cd10518
SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), ...
 364-402 4.15e-03

SET domain (including post-SET domain) found in SET domain-containing proteins (SETD1A/SETD1B), histone-lysine N-methyltransferases (KMT2A/KMT2B/KMT2C/KMT2D) and similar proteins; This family includes SET domain-containing protein 1A (SETD1A), 1B (SETD1B), as well as histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B), 2C (KMT2C), 2D (KMT2D). These proteins are histone-lysine N-methyltransferases (EC 2.1.1.43) that specifically methylate 'Lys-4' of histone H3 (H3K4me).


Pssm-ID: 380916  Cd Length: 150  Bit Score: 37.96  E-value: 4.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 768811322 364 FINHDCEPNAYIEQVEEHEELR--LHARKPIKKGEQirITY 402
Cdd:cd10518   90 FINHSCDPNCYAKIITVDGEKHivIFAKRDIAPGEE--LTY 128
SET_SETD2-like cd10531
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), ...
 363-402 4.88e-03

SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2), ASH1-like protein (ASH1L) and similar proteins; This family includes SET domain-containing protein 2 (SETD2), nuclear SETD2 (NSD2) and ASH1-like protein (ASH1L), which function as histone-lysine N-methyltransferases. SETD2 specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using demethylated 'Lys-36' (H3K36me2) as substrate. NSD2 shows histone H3 'Lys-27' (H3K27me) methyltransferase activity. ASH1L specifically methylates 'Lys-36' of histone H3 (H3K36me). The family also includes Arabidopsis thaliana ASH1-related protein 3 (ASHR3) and similar proteins.


Pssm-ID: 380929  Cd Length: 136  Bit Score: 37.62  E-value: 4.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 768811322 363 SFINHDCEPNAYIEQ--VEEHEELRLHARKPIKKGEQIRITY 402
Cdd:cd10531   75 RFINHSCEPNCETQKwiVNGEYRIGIFALRDIPAGEELTFDY 116
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 362-429 6.68e-03

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: 38.05  E-value: 6.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768811322 362 ISFINHDCEPNA---YIEQVeeheeLRLHARKPIKKGEQIRITYvNPLHGVRLRR---RELRVNWGFLCQCDRC 429
Cdd:cd10536  151 LSLLNHSCDPNTirsFYGNT-----IVVRATRPIKKGEEITICY-GPHFSRMKRSerqRLLKEQYFFDCSCEAC 218
SET_SUV39H cd10542
SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 ...
 353-404 6.70e-03

SET domain (including pre-SET and post-SET domains) found in suppressor of variegation 3-9 homologs, SUV39H1, SUV39H2 and similar proteins; This family includes SUV39H1 (also termed histone H3-K9 methyltransferase 1, H3-K9-HMTase 1, lysine N-methyltransferase 1A, KMT1A, position-effect variegation 3-9 homolog, SUV39H, or Su(var)3-9 homolog 1) and SUV39H2 (also termed histone H3-K9 methyltransferase 2, H3-K9-HMTase 2, lysine N-methyltransferase 1B, KMT1B, or Su(var)3-9 homolog 2), both act as histone-lysine N-methyltransferases that specifically trimethylate 'Lys-9' of histone H3 (H3K9me3) using monomethylated H3 'Lys-9' as substrate. They mainly function in heterochromatin regions, thereby playing central roles in the establishment of constitutive heterochromatin at pericentric and telomere regions. Also included are Schizosaccharomyces pombe H3K9 methyltransferase Clr4 (SUV39H homolog) and Neurospora crassa DIM-5, both of which also methylate 'Lys-9' of histone H3.


Pssm-ID: 380940 [Multi-domain]  Cd Length: 245  Bit Score: 38.43  E-value: 6.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768811322 353 QYNGQVYHwisFINHDCEPN-----AYIEQVEEHE-ELRLHARKPIKKGEQIRITYVN 404
Cdd:cd10542  159 AYYGNISH---FINHSCDPNlavyaVWINHLDPRLpRIAFFAKRDIKAGEELTFDYLM 213
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
113-139 7.20e-03

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 36.86  E-value: 7.20e-03
                         10        20
                 ....*....|....*....|....*..
gi 768811322 113 KVEVKfIDDEHGRGLFAKRDFSKGQII 139
Cdd:COG2940    7 RIEVR-PSPIHGRGVFATRDIPKGTLI 32
SET_SETD1B cd19205
SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and ...
 364-406 7.97e-03

SET domain (including post-SET domain) found in SET domain-containing protein 1B (SETD1B) and similar proteins; SETD1B (EC2.1.1.43), also termed lysine N-methyltransferase 2G, is a histone-lysine N-methyltransferase that specifically methylates 'Lys-4' of histone H3 (H3K4me) when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. Loss of SETD1B occurs in up to half the gastric and colorectal cancers, most commonly via SETD1B mutations, while de novo variants in SETD1B are associated with intellectual disability, epilepsy and autism.


Pssm-ID: 380982 [Multi-domain]  Cd Length: 153  Bit Score: 37.34  E-value: 7.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 768811322 364 FINHDCEPNAYIE--QVEEHEELRLHARKPIKKGEQIRITYVNPL 406
Cdd:cd19205   90 FINHSCNPNCYAKviTVESQKKIVIYSKQHINVNEEITYDYKFPI 134
 
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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