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Conserved domains on  [gi|442627894|ref|NP_001260462|]
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down and out, isoform B [Drosophila melanogaster]

Protein Classification

SET domain-containing protein( domain architecture ID 1562517)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
459-657 2.16e-14

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 cd10536:

Pssm-ID: 394802 [Multi-domain]  Cd Length: 218  Bit Score: 73.10  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627894 459 YSAVLRLERLKEERPTDTVIALALAAHILSIYLSKcTTFFDQLEKSLptasRMSSAEWELLCAALLMRHIGQLRhrslta 538
Cdd:cd10536   49 YRSVYNLVTHTENRSPEDLFQRALTAVFLAKCLQL-SGYFLLWEAST----ELNGEEPESILGGLLLRHLQQLQ------ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627894 539 CRSFvlpadphvfsPLNEFQLWAAPMRLQEGHlhllageVAVVSYSVYPdTLNLCRHSCSSTICAKFSGRTVTALALLDL 618
Cdd:cd10536  118 CNAH----------AITELQTTSSGSQVDTSK-------QVRIATAIYP-TLSLLNHSCDPNTIRSFYGNTIVVRATRPI 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 442627894 619 PAGSGIYNCFaGGNFQQLPREERTKQLLES-GIRCHCNAC 657
Cdd:cd10536  180 KKGEEITICY-GPHFSRMKRSERQRLLKEQyFFDCSCEAC 218
 
Name Accession Description Interval E-value
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
459-657 2.16e-14

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: 73.10  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627894 459 YSAVLRLERLKEERPTDTVIALALAAHILSIYLSKcTTFFDQLEKSLptasRMSSAEWELLCAALLMRHIGQLRhrslta 538
Cdd:cd10536   49 YRSVYNLVTHTENRSPEDLFQRALTAVFLAKCLQL-SGYFLLWEAST----ELNGEEPESILGGLLLRHLQQLQ------ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627894 539 CRSFvlpadphvfsPLNEFQLWAAPMRLQEGHlhllageVAVVSYSVYPdTLNLCRHSCSSTICAKFSGRTVTALALLDL 618
Cdd:cd10536  118 CNAH----------AITELQTTSSGSQVDTSK-------QVRIATAIYP-TLSLLNHSCDPNTIRSFYGNTIVVRATRPI 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 442627894 619 PAGSGIYNCFaGGNFQQLPREERTKQLLES-GIRCHCNAC 657
Cdd:cd10536  180 KKGEEITICY-GPHFSRMKRSERQRLLKEQyFFDCSCEAC 218
 
Name Accession Description Interval E-value
SET_SMYD4 cd10536
SET domain (including iSET domain and post-SET domain) found in SET and MYND domain-containing ...
459-657 2.16e-14

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: 73.10  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627894 459 YSAVLRLERLKEERPTDTVIALALAAHILSIYLSKcTTFFDQLEKSLptasRMSSAEWELLCAALLMRHIGQLRhrslta 538
Cdd:cd10536   49 YRSVYNLVTHTENRSPEDLFQRALTAVFLAKCLQL-SGYFLLWEAST----ELNGEEPESILGGLLLRHLQQLQ------ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627894 539 CRSFvlpadphvfsPLNEFQLWAAPMRLQEGHlhllageVAVVSYSVYPdTLNLCRHSCSSTICAKFSGRTVTALALLDL 618
Cdd:cd10536  118 CNAH----------AITELQTTSSGSQVDTSK-------QVRIATAIYP-TLSLLNHSCDPNTIRSFYGNTIVVRATRPI 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 442627894 619 PAGSGIYNCFaGGNFQQLPREERTKQLLES-GIRCHCNAC 657
Cdd:cd10536  180 KKGEEITICY-GPHFSRMKRSERQRLLKEQyFFDCSCEAC 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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