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Conserved domains on  [gi|302423991|ref|XP_003009822|]
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histone-lysine N-methyltransferase [Verticillium alfalfae VaMs.102]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 285-487 9.21e-94

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


The actual alignment was detected with superfamily member pfam08123:

Pssm-ID: 473071  Cd Length: 205  Bit Score: 283.04  E-value: 9.21e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302423991  285 YDRTVSPDVEKLKQYTNGTDNVYGELNYVFISKILQeKTRMTSDQVFVDLGSGVGNVVLQAALEIGCE-SWGCEMMDNPC 363
Cdd:pfam08123   1 YSRSVSPDANKLNHYKAFSNEVYGELLPEFLSDVLD-KCNLGPQDVFVDLGSGVGNCVLQAALEFGCKlSFGCEIMDNAS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302423991  364 DFAEAQKKEFAKRCRLWGLAPGKVNLVRGDFLQETSVHDVLKRADVVLVNNQAFTPQLNDKLVSLFLDLKKGCKIVSLKS 443
Cdd:pfam08123  80 NLAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIIPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 302423991  444 FL---YDQGVRSINDVaSNILQVEDHTYPEGHVSWTNAGGTFCISTR 487
Cdd:pfam08123 160 FVplnYRINFRNLSDI-FNILKVEELKLPEGSVSWTSRGVEYYISTV 205
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 285-487 9.21e-94

Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating histone H3. H3 methylation by DOT1 has been shown to be required for the DNA damage checkpoint in yeast.


Pssm-ID: 149273  Cd Length: 205  Bit Score: 283.04  E-value: 9.21e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302423991  285 YDRTVSPDVEKLKQYTNGTDNVYGELNYVFISKILQeKTRMTSDQVFVDLGSGVGNVVLQAALEIGCE-SWGCEMMDNPC 363
Cdd:pfam08123   1 YSRSVSPDANKLNHYKAFSNEVYGELLPEFLSDVLD-KCNLGPQDVFVDLGSGVGNCVLQAALEFGCKlSFGCEIMDNAS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302423991  364 DFAEAQKKEFAKRCRLWGLAPGKVNLVRGDFLQETSVHDVLKRADVVLVNNQAFTPQLNDKLVSLFLDLKKGCKIVSLKS 443
Cdd:pfam08123  80 NLAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIIPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 302423991  444 FL---YDQGVRSINDVaSNILQVEDHTYPEGHVSWTNAGGTFCISTR 487
Cdd:pfam08123 160 FVplnYRINFRNLSDI-FNILKVEELKLPEGSVSWTSRGVEYYISTV 205
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 331-439 1.64e-04

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 40.88  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302423991 331 FVDLGSGVGNVVLQAALEIGCESWGCEMmdNPCDFAEAQKKEFAKRcrlwglaPGKVNLVRGDFLQETSVHDvlKRADVV 410
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDI--SPVALELARKAAAALL-------ADNVEVLKGDAEELPPEAD--ESFDVI 70

                         90       100       110
                 ....*....|....*....|....*....|..
gi 302423991 411 LVNNqAFTPQLND--KLVSLFLD-LKKGCKIV 439
Cdd:cd02440   71 ISDP-PLHHLVEDlaRFLEEARRlLKPGGVLV 101
 
Name Accession Description Interval E-value
DOT1 pfam08123
Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating ...
 285-487 9.21e-94

Histone methylation protein DOT1; The DOT1 domain regulates gene expression by methylating histone H3. H3 methylation by DOT1 has been shown to be required for the DNA damage checkpoint in yeast.


Pssm-ID: 149273  Cd Length: 205  Bit Score: 283.04  E-value: 9.21e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302423991  285 YDRTVSPDVEKLKQYTNGTDNVYGELNYVFISKILQeKTRMTSDQVFVDLGSGVGNVVLQAALEIGCE-SWGCEMMDNPC 363
Cdd:pfam08123   1 YSRSVSPDANKLNHYKAFSNEVYGELLPEFLSDVLD-KCNLGPQDVFVDLGSGVGNCVLQAALEFGCKlSFGCEIMDNAS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302423991  364 DFAEAQKKEFAKRCRLWGLAPGKVNLVRGDFLQETSVHDVLKRADVVLVNNQAFTPQLNDKLVSLFLDLKKGCKIVSLKS 443
Cdd:pfam08123  80 NLAELQDEEFKKRCKLFGKKLGKIEFIRGSFLDNERVEEIIPEADVILVNNFAFDPELNLQLKEMLQDLKDGCKIISLKS 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 302423991  444 FL---YDQGVRSINDVaSNILQVEDHTYPEGHVSWTNAGGTFCISTR 487
Cdd:pfam08123 160 FVplnYRINFRNLSDI-FNILKVEELKLPEGSVSWTSRGVEYYISTV 205
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 331-439 1.64e-04

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 40.88  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302423991 331 FVDLGSGVGNVVLQAALEIGCESWGCEMmdNPCDFAEAQKKEFAKRcrlwglaPGKVNLVRGDFLQETSVHDvlKRADVV 410
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDI--SPVALELARKAAAALL-------ADNVEVLKGDAEELPPEAD--ESFDVI 70

                         90       100       110
                 ....*....|....*....|....*....|..
gi 302423991 411 LVNNqAFTPQLND--KLVSLFLD-LKKGCKIV 439
Cdd:cd02440   71 ISDP-PLHHLVEDlaRFLEEARRlLKPGGVLV 101
 
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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