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Conserved domains on  [gi|2449489692|ref|XP_053665710|]
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SET domain-containing protein SmydA-8 [Anopheles marshallii]

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 ...
 244-326 1.73e-22

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: 92.83  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692 244 EENNHHEIILRGLYILGALMNHCCRPNVRYVFDDQLRMRVHASRPIKKGEQIMNNYSKILWGTQHRIIHLCFSKNFLCSC 323
Cdd:cd20071    40 SLTDGLNEIGVGLFPLASLLNHSCDPNAVVVFDGNGTLRVRALRDIKAGEELTISYIDPLLPRTERRRELLEKYGFTCSC 119


                  ...
gi 2449489692 324 DRC 326
Cdd:cd20071   120 PRC 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 ...
 244-326 1.73e-22

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: 92.83  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692 244 EENNHHEIILRGLYILGALMNHCCRPNVRYVFDDQLRMRVHASRPIKKGEQIMNNYSKILWGTQHRIIHLCFSKNFLCSC 323
Cdd:cd20071    40 SLTDGLNEIGVGLFPLASLLNHSCDPNAVVVFDGNGTLRVRALRDIKAGEELTISYIDPLLPRTERRRELLEKYGFTCSC 119


                  ...
gi 2449489692 324 DRC 326
Cdd:cd20071   120 PRC 122
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 262-299 1.34e-07

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: 50.21  E-value: 1.34e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2449489692 262 LMNHCCRPNVRYVFD---DQLRMRVHASRPIKKGEQIMNNY 299
Cdd:pfam00856  74 FINHSCDPNCEVRVVyvnGGPRIVIFALRDIKPGEELTIDY 114
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 259-306 1.23e-06

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: 47.71  E-value: 1.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2449489692  259 LGALMNHCCRPN--VRYVF-DDQLRMRVHASRPIKKGEQIMNNYSKILWGT 306
Cdd:smart00317  74 LARFINHSCEPNceLLFVEvNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
 
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 ...
 244-326 1.73e-22

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: 92.83  E-value: 1.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692 244 EENNHHEIILRGLYILGALMNHCCRPNVRYVFDDQLRMRVHASRPIKKGEQIMNNYSKILWGTQHRIIHLCFSKNFLCSC 323
Cdd:cd20071    40 SLTDGLNEIGVGLFPLASLLNHSCDPNAVVVFDGNGTLRVRALRDIKAGEELTISYIDPLLPRTERRRELLEKYGFTCSC 119


                  ...
gi 2449489692 324 DRC 326
Cdd:cd20071   120 PRC 122
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 73-326 5.61e-15

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: 73.87  E-value: 5.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692  73 GRGLVATRDIAVHELVFVDRP---VLVgPRVNNYEVIFcascccilrrlQLCTGgcrlpicsrcdysvgaasphaaecrl 149
Cdd:cd10536    17 GRFLVATRDIKAGEVLIVEKPyasVLL-PYSSDYRSVY-----------NLVTH-------------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692 150 IQSWQPKDagryskNILYALTSIrgFLLsdrdrsIVLQMEGHPPRKEMTTEIERLLKDGYFwnldgEGPAVRYLRQVV-N 228
Cdd:cd10536    59 TENRSPED------LFQRALTAV--FLA------KCLQLSGYFLLWEASTELNGEEPESIL-----GGLLLRHLQQLQcN 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692 229 VLNTNAFETSRIVADEENNHHEIILRGLYILGALMNHCCRPNVRYVF-DDQLRMRvhASRPIKKGEQIMNNYskilwgTQ 307
Cdd:cd10536   120 AHAITELQTTSSGSQVDTSKQVRIATAIYPTLSLLNHSCDPNTIRSFyGNTIVVR--ATRPIKKGEEITICY------GP 191

                         250       260
                  ....*....|....*....|....*..
gi 2449489692 308 HRIIH-----LCFSK---NFLCSCDRC 326
Cdd:cd10536   192 HFSRMkrserQRLLKeqyFFDCSCEAC 218
SET_SMYD1_2_3-like cd19167
SET domain (including post-SET domain) found in SET and MYND domain-containing proteins, SMYD1, ...
 155-326 1.25e-10

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: 60.90  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692 155 PKDAGRYSKNILYAL----TSIRGFLLSDRDRSIVLQMEGHPPRKEMTTEIERLLKdgyFWNLDGEGPAVRYLRQVVNVL 230
Cdd:cd19167    39 PPEHVRLTGRILYKQhirkTRTSGKLLSVYDLESHVEKLDEEKKDGLRSDVATLHQ---FMSKDLQLPDAAYLVELFGKV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692 231 NTNAFETSrivaDEENNHheiILRGLYILGALMNHCCRPNVRYVFDDQLrMRVHASRPIKKGEQIMNNYSKILWGTQHRI 310
Cdd:cd19167   116 NCNGFTIS----DEELQH---VGVGIYPQAALLNHSCCPNCIVTFNGPN-IEVRAVQEIEPGEEVFHSYIDLLYPTEERR 187

                         170
                  ....*....|....*.
gi 2449489692 311 IHLCFSKNFLCSCDRC 326
Cdd:cd19167   188 DQLRDQYFFLCQCADC 203
SET_SMYD3 cd19203
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 3 ...
 255-328 1.76e-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: 57.76  E-value: 1.76e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2449489692 255 GLYILGALMNHCCRPNVRYVFDDqLRMRVHASRPIKKGEQIMNNYSKILWGTQHRIIHLCFSKNFLCSCDRCKD 328
Cdd:cd19203   138 GLYPSASLLNHSCDPNCVIVFNG-PHLLLRAIREIEVGEELTISYIDMLMPSEERRKQLRDQYCFECDCFRCQD 210
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 262-299 1.34e-07

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: 50.21  E-value: 1.34e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2449489692 262 LMNHCCRPNVRYVFD---DQLRMRVHASRPIKKGEQIMNNY 299
Cdd:pfam00856  74 FINHSCDPNCEVRVVyvnGGPRIVIFALRDIKPGEELTIDY 114
SET_SpSet7-like cd10540
SET domain found in Schizossacharomyces pombe Set7 and similar proteins; Schizosaccharomyces ...
 259-304 2.90e-07

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: 49.17  E-value: 2.90e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2449489692 259 LGALMNHCCRPNVRYVFD-DQLRMRVHASRPIKKGEQIMNNYSKILW 304
Cdd:cd10540    65 YGSMFNHSYTPNAEYEIDfENQTIVFYALRDIEAGEELTINYGDDLW 111
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 258-299 3.01e-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: 47.63  E-value: 3.01e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2449489692 258 ILGALMNHCCRPNVRYVFDDQ---LRMRVHASRPIKKGEQIMNNY 299
Cdd:cd08161    27 GLARFINHSCEPNCEFEEVYVggkPRVFIVALRDIKAGEELTVDY 71
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 261-327 4.30e-07

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: 49.20  E-value: 4.30e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2449489692 261 ALMNHCCRPNVRYVFDDQLRMRVHASRPIKKGEQIMNNYSKILWGTqhriihlcfsKNFLCSCDRCK 327
Cdd:cd10524    78 AFINHDCRPNCKFVPTGKSTACVKVLRDIEPGEEITVYYGDNYFGE----------NNEECECETCE 134
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 259-306 1.23e-06

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: 47.71  E-value: 1.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2449489692  259 LGALMNHCCRPN--VRYVF-DDQLRMRVHASRPIKKGEQIMNNYSKILWGT 306
Cdd:smart00317  74 LARFINHSCEPNceLLFVEvNGDDRIVIFALRDIKPGEELTIDYGSDYANE 124
SET_SMYD2 cd19202
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 ...
 230-326 2.10e-05

SET domain (including post-SET domain) found in SET and MYND domain-containing protein 2 (SMYD2) and similar proteins; SMYD2 (also termed HSKM-B, 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). It plays a role in myofilament organization in both skeletal and cardiac muscles via Hsp90 methylation. SMYD2 overexpression is associated with tumor cell proliferation and a worse outcome in human papillomavirus-unrelated nonmultiple head and neck carcinomas. It regulates leukemia cell growth such that diminished SMYD2 expression upregulates SET7/9, thereby possibly shifting leukemia cells from growth to quiescence state associated with resistance to DNA damage associated with Acute Myeloid Leukemia (AML).


Pssm-ID: 380979 [Multi-domain]  Cd Length: 206  Bit Score: 45.58  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692 230 LNTNAFetsrIVADEENNHheiilRGLYILG--ALMNHCCRPNVRYVFDDQLrMRVHASRPIKKGEQIMNNYSKILWGTQ 307
Cdd:cd19202   116 VNCNGF----TIEDEELSH-----LGSAIFPdvALMNHSCCPNVIVTYKGTL-AEVRAVQEIKPGEEVFTSYIDLLYPTE 185

                          90
                  ....*....|....*....
gi 2449489692 308 HRIIHLCFSKNFLCSCDRC 326
Cdd:cd19202   186 DRNDRLRDSYFFTCECQEC 204
SET_SMYD1 cd10526
SET domain (including post-SET domain) found in SET and MYND domain-containing protein 1 ...
 200-327 2.18e-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: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692 200 EIERLLKDGY----FWNLDGEGPAVRYLRQVVNVLNTNAFETSrivaDEennhheiilRGLYILG-------ALMNHCCR 268
Cdd:cd10526    85 EKKDLREDVHsfldYWPYQSQQFSMEYISHIFGVINCNGFTLS----DQ---------RGLQAVGvgifpnlCLVNHDCW 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2449489692 269 PNVRYVFDDQlRMRVHASRPIKKGEQIMNNYSKILWGTQHRIIHLCFSKNFLCSCDRCK 327
Cdd:cd10526   152 PNCTVIFNNG-RIELRALGKISEGDELTVSYIDFLNTSEDRKEQLKKQYYFDCTCEHCT 209
SET_SETD2 cd19172
SET domain (including post-SET domain) found in SET domain-containing protein 2 (SETD2) and ...
 229-299 5.26e-05

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: 43.34  E-value: 5.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692 229 VLNTNAFETSRIVADEENNHH---------EII---LRGlyILGALMNHCCRPNV---RYVFDDQLRMRVHASRPIKKGE 293
Cdd:cd19172    35 VLDEKEFKRRMKEYAREGNRHyyfmalksdEIIdatKKG--NLSRFINHSCEPNCetqKWTVNGELRVGFFAKRDIPAGE 112


                  ....*.
gi 2449489692 294 QIMNNY 299
Cdd:cd19172   113 ELTFDY 118
SET_LSMT cd10527
SET domain found in Rubisco large subunit methyltransferase (LSMT) and similar proteins; ...
 262-299 3.24e-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: 42.44  E-value: 3.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2449489692 262 LMNHC-CRPNVRYVFDDQ-LRMRVHASRPIKKGEQIMNNY 299
Cdd:cd10527   182 MLNHSpDAPNVRYEYDEDeGSFVLVATRDIAAGEEVFISY 221
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 264-304 8.30e-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: 8.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2449489692 264 NHCCRPNVRYVF---DDQLRMRVHASRPIKKGEQIMNNYSKILW 304
Cdd:cd10522    78 NHSDQPNLELIVrtlKGEQHIGFVAIRDIKPGEELFISYGPKYW 121
SET_SETD6 cd19178
SET domain found in SET domain-containing protein 6 (SETD6) and similar proteins; SETD6 is a ...
 262-299 1.51e-03

SET domain found in SET domain-containing protein 6 (SETD6) and similar proteins; SETD6 is a lysine N-methyltransferase that monomethylates 'Lys-310' of the RELA subunit of NF-kappa-B complex, leading to down-regulate NF-kappa-B transcription factor activity. It also monomethylates 'Lys-8' of H2AZ (H2AZK8me1).


Pssm-ID: 380955 [Multi-domain]  Cd Length: 250  Bit Score: 40.37  E-value: 1.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2449489692 262 LMNHCCRPNVRYVFDDQ-LRMRvhASRPIKKGEQIMNNY 299
Cdd:cd19178   197 MLNHIANNNARLEFDPDcLRMI--ATRDIKKGEEIFNTY 233
SET_KMT2C_2D cd19171
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), ...
 263-318 2.24e-03

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 2C (KMT2C), 2D (KMT2D) and similar proteins; This family includes KMT2C and KMT2D. Both, KMT2C (also termed HALR or MLL3) and KMT2D (also termed ALR or MLL2), act as histone methyltransferases that methylate 'Lys-4' of histone H3 (H3K4me). They are subunits of MLL2/3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation.


Pssm-ID: 380948 [Multi-domain]  Cd Length: 153  Bit Score: 38.95  E-value: 2.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2449489692 263 MNHCCRPN-VRYV--FDDQLRMRVHASRPIKKGEQIMNNYSKILWGTQHRIIHLCFSKN 318
Cdd:cd19171    90 INHSCNPNcVAEVvtFDKEKKIIIISNRRIAKGEELTYDYKFDFEDDQHKIPCLCGAPN 148
SET_SMYD5 cd10521
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
 255-326 6.71e-03

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: 38.44  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489692 255 GLYILGALMNHCCRPNVRYVFDD-QLRMRVHASRPIKKGEQIMNNY-----SKILWGTQHRIIhlcfSKNFL--CSCDRC 326
Cdd:cd10521   204 GLYLLQSCCNHSCVPNAEITFPEnNFTLSLKALRDIQEGEEICISYldecqRERSRHSRQKIL----RENYLfiCNCPKC 279
 
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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