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Conserved domains on  [gi|568945336|ref|XP_006539835|]
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histone-lysine N-methyltransferase KMT5C isoform X1 [Mus musculus]

Protein Classification

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, ...
 196-279 1.87e-36

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 cd19185:

Pssm-ID: 394802  Cd Length: 142  Bit Score: 131.70  E-value: 1.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945336 196 LGPVRTTSASCTPPEKgvpscglaqlpsstmFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECYTCERKGE 275
Cdd:cd19185   74 LGPAAFINHDCKPNCK---------------FVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECHTCERKGE 138


                 ....
gi 568945336 276 GAFR 279
Cdd:cd19185  139 GAFR 142
PHA02682 super family cl31817
ORF080 virion core protein; Provisional
 281-346 3.55e-03

ORF080 virion core protein; Provisional


The actual alignment was detected with superfamily member PHA02682:

Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.46  E-value: 3.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568945336 281 QPREPELRPKPLDKYELRETKRRLQQGLVSSQQSLMSRwacSHLSPLRPDPFCAACQPSCLLPASP 346
Cdd:PHA02682  39 APCPPDADVDPLDKYSVKEAGRYYQSRLKANSACMQRP---SGQSPLAPSPACAAPAPACPACAPA 101
 
Name Accession Description Interval E-value
SET_KMT5C cd19185
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) ...
 196-279 1.87e-36

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) and similar proteins; KMT5C (also termed lysine N-methyltransferase 5C, lysine-specific methyltransferase 5C, suppressor of variegation 4-20 homolog 2, Su(var)4-20 homolog 2 or Suv4-20h2) is a histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 (H4K20me3). It plays a central role in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.


Pssm-ID: 380962  Cd Length: 142  Bit Score: 131.70  E-value: 1.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945336 196 LGPVRTTSASCTPPEKgvpscglaqlpsstmFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECYTCERKGE 275
Cdd:cd19185   74 LGPAAFINHDCKPNCK---------------FVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECHTCERKGE 138


                 ....
gi 568945336 276 GAFR 279
Cdd:cd19185  139 GAFR 142
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 281-346 3.55e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.46  E-value: 3.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568945336 281 QPREPELRPKPLDKYELRETKRRLQQGLVSSQQSLMSRwacSHLSPLRPDPFCAACQPSCLLPASP 346
Cdd:PHA02682  39 APCPPDADVDPLDKYSVKEAGRYYQSRLKANSACMQRP---SGQSPLAPSPACAAPAPACPACAPA 101
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 230-254 7.14e-03

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: 36.35  E-value: 7.14e-03
                          10        20
                  ....*....|....*....|....*
gi 568945336  230 SDGNTACVKVLRDIEPGDEVTCFYG 254
Cdd:pfam00856  91 NGGPRIVIFALRDIKPGEELTIDYG 115
 
Name Accession Description Interval E-value
SET_KMT5C cd19185
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) ...
 196-279 1.87e-36

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) and similar proteins; KMT5C (also termed lysine N-methyltransferase 5C, lysine-specific methyltransferase 5C, suppressor of variegation 4-20 homolog 2, Su(var)4-20 homolog 2 or Suv4-20h2) is a histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 (H4K20me3). It plays a central role in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.


Pssm-ID: 380962  Cd Length: 142  Bit Score: 131.70  E-value: 1.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945336 196 LGPVRTTSASCTPPEKgvpscglaqlpsstmFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECYTCERKGE 275
Cdd:cd19185   74 LGPAAFINHDCKPNCK---------------FVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECHTCERKGE 138


                 ....
gi 568945336 276 GAFR 279
Cdd:cd19185  139 GAFR 142
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 187-278 2.58e-27

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: 106.60  E-value: 2.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945336 187 SCVKR-MKTCLGPVRTTSASCTPpekgvpscglaqlpsSTMFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHC 265
Cdd:cd10524   64 SSRKKcSQLWLGPAAFINHDCRP---------------NCKFVPTGKSTACVKVLRDIEPGEEITVYYGDNYFGENNEEC 128

                         90
                 ....*....|...
gi 568945336 266 ECYTCERKGEGAF 278
Cdd:cd10524  129 ECETCERRGRGAF 141
SET_KMT5B cd19184
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5B (KMT5B) ...
 227-279 4.17e-23

SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5B (KMT5B) and similar proteins; KMT5B (also termed lysine N-methyltransferase 5B, lysine-specific methyltransferase 5B, suppressor of variegation 4-20 homolog 1, Su(var)4-20 homolog 1 or Suv4-20h1) is a histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4 (H4K20me3). It plays a central role in the establishment of constitutive heterochromatin in pericentric heterochromatin regions.


Pssm-ID: 380961  Cd Length: 144  Bit Score: 95.10  E-value: 4.17e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568945336 227 FVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECYTCERKGEGAFR 279
Cdd:cd19184   90 FVSTGRDTACVKALRDIEPGEEISCYYGDGFFGENNEFCECYTCERRGTGAFK 142
SET_Suv4-20 cd19186
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 227-278 6.16e-23

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.


Pssm-ID: 380963  Cd Length: 142  Bit Score: 94.44  E-value: 6.16e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568945336 227 FVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECYTCERKGEGAF 278
Cdd:cd19186   91 FVSTGRDTACVQVLRDIEPGEEITCFYGEDFFGDNNCYCECETCERRQTGAF 142
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 281-346 3.55e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.46  E-value: 3.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568945336 281 QPREPELRPKPLDKYELRETKRRLQQGLVSSQQSLMSRwacSHLSPLRPDPFCAACQPSCLLPASP 346
Cdd:PHA02682  39 APCPPDADVDPLDKYSVKEAGRYYQSRLKANSACMQRP---SGQSPLAPSPACAAPAPACPACAPA 101
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 230-254 7.14e-03

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: 36.35  E-value: 7.14e-03
                          10        20
                  ....*....|....*....|....*
gi 568945336  230 SDGNTACVKVLRDIEPGDEVTCFYG 254
Cdd:pfam00856  91 NGGPRIVIFALRDIKPGEELTIDYG 115
 
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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