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Conserved domains on  [gi|1907179602|ref|XP_036008833|]
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histone-lysine N-methyltransferase KMT5C isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SET_KMT5C cd19185
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) ...
 102-274 7.48e-108

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: 316.98  E-value: 7.48e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 102 PESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREEDEDLLRAGENDFSIMYSTRKRSAQLWLGPAAFI 181
Cdd:cd19185     1 PESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREEDEGLLRAGENDFSIMYSTRKRSAQLWLGPAAFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 182 NHDCKPNCKnpwtwvpgqvveldsscpalqarvlkgawpqFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCE 261
Cdd:cd19185    81 NHDCKPNCK-------------------------------FVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCE 129

                         170
                  ....*....|...
gi 1907179602 262 CYTCERKGEGAFR 274
Cdd:cd19185   130 CHTCERKGEGAFR 142
PHA02682 super family cl31817
ORF080 virion core protein; Provisional
 276-397 1.03e-04

ORF080 virion core protein; Provisional


The actual alignment was detected with superfamily member PHA02682:

Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 44.08  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 276 QPREPELRPKPLDKYELRETKRRLQQGLvSSQQSLMSRwaCSHLSPLRPDPFCAACQPSCLLPASPhmdyLPLWLQRAPQ 355
Cdd:PHA02682   39 APCPPDADVDPLDKYSVKEAGRYYQSRL-KANSACMQR--PSGQSPLAPSPACAAPAPACPACAPA----APAPAVTCPA 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907179602 356 PQPIVPPRKRHRRRRPRIRQASLPPVlrTACVPLHRwgGCGP 397
Cdd:PHA02682  112 PAPACPPATAPTCPPPAVCPAPARPA--PACPPSTR--QCPP 149
 
Name Accession Description Interval E-value
SET_KMT5C cd19185
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) ...
 102-274 7.48e-108

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: 316.98  E-value: 7.48e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 102 PESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREEDEDLLRAGENDFSIMYSTRKRSAQLWLGPAAFI 181
Cdd:cd19185     1 PESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREEDEGLLRAGENDFSIMYSTRKRSAQLWLGPAAFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 182 NHDCKPNCKnpwtwvpgqvveldsscpalqarvlkgawpqFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCE 261
Cdd:cd19185    81 NHDCKPNCK-------------------------------FVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCE 129

                         170
                  ....*....|...
gi 1907179602 262 CYTCERKGEGAFR 274
Cdd:cd19185   130 CHTCERKGEGAFR 142
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 120-255 1.69e-13

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: 66.97  E-value: 1.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602  120 GAKIVSTRAWKKNEKLELLVGCI---AELREEDEDLLRAGENDFSIMYSTRKRS--AQLWLGPAAFINHDCKPNCKNpwt 194
Cdd:smart00317  12 GWGVRATEDIPKGEFIGEYVGEIitsEEAEERPKAYDTDGAKAFYLFDIDSDLCidARRKGNLARFINHSCEPNCEL--- 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907179602  195 wvpgqvveldsscpalqarvlkgawpQFVPSDGNT-ACVKVLRDIEPGDEVTCFYGEGFFGE 255
Cdd:smart00317  89 --------------------------LFVEVNGDDrIVIFALRDIKPGEELTIDYGSDYANE 124
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 123-249 8.73e-10

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: 56.38  E-value: 8.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 123 IVSTRAWKKNEKLELLVGCI------AELREEDEDLLRAGENDFSIMYSTRKRS-------AQLWLGPAAFINHDCKPNC 189
Cdd:pfam00856   4 LFATEDIPKGEFIGEYVEVLlitkeeADKRELLYYDKLELRLWGPYLFTLDEDSeycidarALYYGNWARFINHSCDPNC 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 190 KNPWTWVPGqvveldsscpalqarvlkgawpqfvpsdGNTACVKVLRDIEPGDEVTCFYG 249
Cdd:pfam00856  84 EVRVVYVNG----------------------------GPRIVIFALRDIKPGEELTIDYG 115
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 276-397 1.03e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 44.08  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 276 QPREPELRPKPLDKYELRETKRRLQQGLvSSQQSLMSRwaCSHLSPLRPDPFCAACQPSCLLPASPhmdyLPLWLQRAPQ 355
Cdd:PHA02682   39 APCPPDADVDPLDKYSVKEAGRYYQSRL-KANSACMQR--PSGQSPLAPSPACAAPAPACPACAPA----APAPAVTCPA 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907179602 356 PQPIVPPRKRHRRRRPRIRQASLPPVlrTACVPLHRwgGCGP 397
Cdd:PHA02682  112 PAPACPPATAPTCPPPAVCPAPARPA--PACPPSTR--QCPP 149
 
Name Accession Description Interval E-value
SET_KMT5C cd19185
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5C (KMT5C) ...
 102-274 7.48e-108

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: 316.98  E-value: 7.48e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 102 PESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREEDEDLLRAGENDFSIMYSTRKRSAQLWLGPAAFI 181
Cdd:cd19185     1 PESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREEDEGLLRAGENDFSIMYSTRKRSAQLWLGPAAFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 182 NHDCKPNCKnpwtwvpgqvveldsscpalqarvlkgawpqFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCE 261
Cdd:cd19185    81 NHDCKPNCK-------------------------------FVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCE 129

                         170
                  ....*....|...
gi 1907179602 262 CYTCERKGEGAFR 274
Cdd:cd19185   130 CHTCERKGEGAFR 142
SET_Suv4-20-like cd10524
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 104-273 8.06e-76

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: 234.87  E-value: 8.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 104 SGFTILPCTRYSME-TNGAKIVSTRAWKKNEKLELLVGCIAELREEDEDLLRAGENDFSIMYSTRKRSAQLWLGPAAFIN 182
Cdd:cd10524     2 SGFTICPCNRYSLEnHYGAKIIATKPIKKGEKIHELCGCIAELSEEEEALLRPGGNDFSVMYSSRKKCSQLWLGPAAFIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 183 HDCKPNCKnpwtwvpgqvveldsscpalqarvlkgawpqFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCEC 262
Cdd:cd10524    82 HDCRPNCK-------------------------------FVPTGKSTACVKVLRDIEPGEEITVYYGDNYFGENNEECEC 130

                         170
                  ....*....|.
gi 1907179602 263 YTCERKGEGAF 273
Cdd:cd10524   131 ETCERRGRGAF 141
SET_Suv4-20 cd19186
SET domain (including post-SET domain) found in Drosophila melanogaster suppressor of ...
 103-273 5.40e-74

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: 230.03  E-value: 5.40e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 103 ESGFTILPCTRYSMETN-GAKIVSTRAWKKNEKLELLVGCIAELREEDE-DLLRAGENDFSIMYSTRKRSAQLWLGPAAF 180
Cdd:cd19186     1 ESGFEIQPCHRYSLEGQmGAKIVATKKWKKNEKIPLLVGCIAELTEEEEaQLLRPGENDFSVMYSCRKNCAQLWLGPAAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 181 INHDCKPNCKnpwtwvpgqvveldsscpalqarvlkgawpqFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHC 260
Cdd:cd19186    81 INHDCRPNCK-------------------------------FVSTGRDTACVQVLRDIEPGEEITCFYGEDFFGDNNCYC 129

                         170
                  ....*....|...
gi 1907179602 261 ECYTCERKGEGAF 273
Cdd:cd19186   130 ECETCERRQTGAF 142
SET_KMT5B cd19184
SET domain (including post-SET domain) found in histone-lysine N-methyltransferase 5B (KMT5B) ...
 103-274 2.93e-70

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: 220.68  E-value: 2.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 103 ESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREEDED-LLRAGENDFSIMYSTRKRSAQLWLGPAAFI 181
Cdd:cd19184     1 DSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEENmLLRHGENDFSVMYSTRKNCAQLWLGPAAFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 182 NHDCKPNCKnpwtwvpgqvveldsscpalqarvlkgawpqFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCE 261
Cdd:cd19184    81 NHDCRPNCK-------------------------------FVSTGRDTACVKALRDIEPGEEISCYYGDGFFGENNEFCE 129

                         170
                  ....*....|...
gi 1907179602 262 CYTCERKGEGAFR 274
Cdd:cd19184   130 CYTCERRGTGAFK 142
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 120-255 1.69e-13

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: 66.97  E-value: 1.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602  120 GAKIVSTRAWKKNEKLELLVGCI---AELREEDEDLLRAGENDFSIMYSTRKRS--AQLWLGPAAFINHDCKPNCKNpwt 194
Cdd:smart00317  12 GWGVRATEDIPKGEFIGEYVGEIitsEEAEERPKAYDTDGAKAFYLFDIDSDLCidARRKGNLARFINHSCEPNCEL--- 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907179602  195 wvpgqvveldsscpalqarvlkgawpQFVPSDGNT-ACVKVLRDIEPGDEVTCFYGEGFFGE 255
Cdd:smart00317  89 --------------------------LFVEVNGDDrIVIFALRDIKPGEELTIDYGSDYANE 124
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 123-249 8.73e-10

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: 56.38  E-value: 8.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 123 IVSTRAWKKNEKLELLVGCI------AELREEDEDLLRAGENDFSIMYSTRKRS-------AQLWLGPAAFINHDCKPNC 189
Cdd:pfam00856   4 LFATEDIPKGEFIGEYVEVLlitkeeADKRELLYYDKLELRLWGPYLFTLDEDSeycidarALYYGNWARFINHSCDPNC 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 190 KNPWTWVPGqvveldsscpalqarvlkgawpqfvpsdGNTACVKVLRDIEPGDEVTCFYG 249
Cdd:pfam00856  84 EVRVVYVNG----------------------------GPRIVIFALRDIKPGEELTIDYG 115
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
 174-249 1.00e-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: 49.17  E-value: 1.00e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907179602 174 WLGPAAFINHDCKPNCknpwtwvpgqvveldsscpalqarvlkgaWPQFVPSDG-NTACVKVLRDIEPGDEVTCFYG 249
Cdd:cd08161    25 VIGLARFINHSCEPNC-----------------------------EFEEVYVGGkPRVFIVALRDIKAGEELTVDYG 72
SET_SMYD cd20071
SET domain (including SET domain and post-SET domain) found in SET and MYND domain-containing ...
 113-262 5.54e-05

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: 42.75  E-value: 5.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 113 RYSMETNGAKIVSTRAWKKNEKLellvgciaeLREEDedLLRAGENDFSIMYSTRKRSAQLWLGpAAFINHDCKPNCknp 192
Cdd:cd20071     3 RESEGSKGRGLVATRDIEPGELI---------LVEKP--LVSVPSNSFSLTDGLNEIGVGLFPL-ASLLNHSCDPNA--- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 193 wtwvpgqvveldsscpalqarvlkgawpQFVPSDGNTACVKVLRDIEPGDEVTCFYGEGFFGEKNE----------HCEC 262
Cdd:cd20071    68 ----------------------------VVVFDGNGTLRVRALRDIKAGEELTISYIDPLLPRTERrrellekygfTCSC 119
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 276-397 1.03e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 44.08  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 276 QPREPELRPKPLDKYELRETKRRLQQGLvSSQQSLMSRwaCSHLSPLRPDPFCAACQPSCLLPASPhmdyLPLWLQRAPQ 355
Cdd:PHA02682   39 APCPPDADVDPLDKYSVKEAGRYYQSRL-KANSACMQR--PSGQSPLAPSPACAAPAPACPACAPA----APAPAVTCPA 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907179602 356 PQPIVPPRKRHRRRRPRIRQASLPPVlrTACVPLHRwgGCGP 397
Cdd:PHA02682  112 PAPACPPATAPTCPPPAVCPAPARPA--PACPPSTR--QCPP 149
SET_NSD2 cd19211
SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) ...
 120-194 9.31e-04

SET domain (including post-SET domain) found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; NSD2 (EC 2.1.1.43; also termed multiple myeloma SET domain-containing protein (MMSET), protein trithorax-5 (TRX5), or wolf-Hirschhorn syndrome candidate 1 protein (WHSC1)) acts as histone-lysine N-methyltransferase with histone H3 'Lys-36' (H3K36me) methyltransferase activity. NSD2 has been shown to mediate di- and trimethylation of H3K36 and dimethylation of H4K20 in different systems, and has been characterized as a transcriptional repressor interacting with histone deacetylase HDAC1 and histone demethylase LSD1. NSD2 mediates constitutive NF-kappaB signaling for cancer cell proliferation, survival and tumor growth. It is highly overexpressed in several types of human cancers, including small-cell lung cancers, neuroblastoma, carcinomas of stomach and colon, and bladder cancers, and its overexpression tends to be associated with tumor aggressiveness. WHSC1 is frequently deleted in Wolf-Hirschhorn syndrome (WHS).


Pssm-ID: 380988 [Multi-domain]  Cd Length: 142  Bit Score: 39.59  E-value: 9.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 120 GAKIVSTRAWKKNEKLELLVGciaELREEDEDLLR---AGENDFSIMYS-TRKRSAQLWLGP----AAFINHDCKPNCKN 191
Cdd:cd19211    13 GWGLIAKRDIKKGEFVNEYVG---ELIDEEECMARikhAHENDITHFYMlTIDKDRIIDAGPkgnySRFMNHSCQPNCET 89


                  ....
gi 1907179602 192 -PWT 194
Cdd:cd19211    90 qKWT 93
SET_SETMAR cd10544
SET domain (including pre-SET and post-SET domains) found in SET domain and mariner ...
 180-269 3.23e-03

SET domain (including pre-SET and post-SET domains) found in SET domain and mariner transposase fusion protein (SETMAR) and similar proteins; SETMAR (also termed metnase) is a DNA-binding protein that is indirectly recruited to sites of DNA damage through protein-protein interactions. It has a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. SETMAR also acts as a histone-lysine N-methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3. It specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining.


Pssm-ID: 380942 [Multi-domain]  Cd Length: 254  Bit Score: 39.20  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907179602 180 FINHDCKPNCknpwTWVPgqvVELDSSCPALqarvlkgawpqfvpsdgntaCVKVLRDIEPGDEVTCFYGEGFFGEKNEH 259
Cdd:cd10544   172 FLNHSCEPNL----FMVP---VRVDSMVPKL--------------------ALFAARDIVAGEELSFDYSGEFSNSVESV 224

                          90
                  ....*....|
gi 1907179602 260 CECYTCERKG 269
Cdd:cd10544   225 TLARQDESKS 234
 
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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