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Conserved domains on  [gi|13376109|ref|NP_079042|]
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calmodulin-lysine N-methyltransferase [Homo sapiens]

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; ...
 113-278 4.78e-14

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 pfam10294:

Pssm-ID: 473071  Cd Length: 172  Bit Score: 68.90  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376109   113 EDVLTSFDNTGNVC---IWPSEEVLAYYCLK------HNNIFRALAVCELGGGmTCLAGLMVAISADVKEVLLTDgneka 183
Cdd:pfam10294   4 NPGLRIEEDTGNGIgghVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSG-TGLVGIAVALLLPGASVTITD----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376109   184 IRNVQDIITRN-QKAGVfkTQKISSCVLRWDNETDVSQLEGH-FDIVMCADCLFLDQYRASLVDAIKRLLQPRGKAMVFA 261
Cdd:pfam10294  78 LEEALELLKKNiELNAL--SSKVVVKVLDWGENLPPDLFDGHpVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAY 155

                         170
                  ....*....|....*..
gi 13376109   262 PRRGNTLNQFCNLAEKA 278
Cdd:pfam10294 156 KKRREAEKKFFKLLERF 172
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 113-278 4.78e-14

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 68.90  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376109   113 EDVLTSFDNTGNVC---IWPSEEVLAYYCLK------HNNIFRALAVCELGGGmTCLAGLMVAISADVKEVLLTDgneka 183
Cdd:pfam10294   4 NPGLRIEEDTGNGIgghVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSG-TGLVGIAVALLLPGASVTITD----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376109   184 IRNVQDIITRN-QKAGVfkTQKISSCVLRWDNETDVSQLEGH-FDIVMCADCLFLDQYRASLVDAIKRLLQPRGKAMVFA 261
Cdd:pfam10294  78 LEEALELLKKNiELNAL--SSKVVVKVLDWGENLPPDLFDGHpVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAY 155

                         170
                  ....*....|....*..
gi 13376109   262 PRRGNTLNQFCNLAEKA 278
Cdd:pfam10294 156 KKRREAEKKFFKLLERF 172
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 150-259 5.53e-03

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: 35.87  E-value: 5.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376109 150 VCELGGGMTCLAglMVAISADVKEVLLTDGNEKAIRNVQDIITRNQKAGVFktqkisscVLRWDNETDVSQLEGHFDIVM 229
Cdd:cd02440   2 VLDLGCGTGALA--LALASGPGARVTGVDISPVALELARKAAAALLADNVE--------VLKGDAEELPPEADESFDVII 71

                        90       100       110
                ....*....|....*....|....*....|.
gi 13376109 230 CADCL-FLDQYRASLVDAIKRLLQPRGKAMV 259
Cdd:cd02440  72 SDPPLhHLVEDLARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 113-278 4.78e-14

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 68.90  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376109   113 EDVLTSFDNTGNVC---IWPSEEVLAYYCLK------HNNIFRALAVCELGGGmTCLAGLMVAISADVKEVLLTDgneka 183
Cdd:pfam10294   4 NPGLRIEEDTGNGIgghVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSG-TGLVGIAVALLLPGASVTITD----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376109   184 IRNVQDIITRN-QKAGVfkTQKISSCVLRWDNETDVSQLEGH-FDIVMCADCLFLDQYRASLVDAIKRLLQPRGKAMVFA 261
Cdd:pfam10294  78 LEEALELLKKNiELNAL--SSKVVVKVLDWGENLPPDLFDGHpVDLILAADCVYNEDSFPLLEKTLKDLLGKESVILVAY 155

                         170
                  ....*....|....*..
gi 13376109   262 PRRGNTLNQFCNLAEKA 278
Cdd:pfam10294 156 KKRREAEKKFFKLLERF 172
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 150-259 5.53e-03

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: 35.87  E-value: 5.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13376109 150 VCELGGGMTCLAglMVAISADVKEVLLTDGNEKAIRNVQDIITRNQKAGVFktqkisscVLRWDNETDVSQLEGHFDIVM 229
Cdd:cd02440   2 VLDLGCGTGALA--LALASGPGARVTGVDISPVALELARKAAAALLADNVE--------VLKGDAEELPPEADESFDVII 71

                        90       100       110
                ....*....|....*....|....*....|.
gi 13376109 230 CADCL-FLDQYRASLVDAIKRLLQPRGKAMV 259
Cdd:cd02440  72 SDPPLhHLVEDLARFLEEARRLLKPGGVLVL 102
 
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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