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Conserved domains on  [gi|330443625|ref|NP_012663|]
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protein-lysine N-methyltransferase [Saccharomyces cerevisiae S288C]

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; ...
137-286 8.17e-17

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: 76.99  E-value: 8.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443625  137 WEAALYMGDFLIHKPLQELAPVQGQDdgkkkLNVLEVGAGTGIVSLVIlqKYHEFVNKMYVTDGDsNLVETqLKRNFELN 216
Cdd:pfam10294  22 WDAAVVLSKYLEMKIFKELGANNLSG-----LNVLELGSGTGLVGIAV--ALLLPGASVTITDLE-EALEL-LKKNIELN 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330443625  217 NevreNEPDIKLQRLWWGSD-----RVPEDIDLVVGADVTYDPTILPDLCECLAECLALDRCklCLLSATIRSES 286
Cdd:pfam10294  93 A----LSSKVVVKVLDWGENlppdlFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESV--ILVAYKKRREA 161
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
137-286 8.17e-17

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: 76.99  E-value: 8.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443625  137 WEAALYMGDFLIHKPLQELAPVQGQDdgkkkLNVLEVGAGTGIVSLVIlqKYHEFVNKMYVTDGDsNLVETqLKRNFELN 216
Cdd:pfam10294  22 WDAAVVLSKYLEMKIFKELGANNLSG-----LNVLELGSGTGLVGIAV--ALLLPGASVTITDLE-EALEL-LKKNIELN 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330443625  217 NevreNEPDIKLQRLWWGSD-----RVPEDIDLVVGADVTYDPTILPDLCECLAECLALDRCklCLLSATIRSES 286
Cdd:pfam10294  93 A----LSSKVVVKVLDWGENlppdlFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESV--ILVAYKKRREA 161
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
137-269 1.03e-07

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 51.81  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443625 137 WEAALYMGDFLIHKPlqELApvqgqddGKKklnVLEVGAGTGIVSLVILQKyheFVNKMYVTDGDSnLVETQLKRNFELN 216
Cdd:COG3897   53 WPSGQALARYLLDHP--EVA-------GKR---VLELGCGLGLVGIAAAKA---GAADVTATDYDP-EALAALRLNAALN 116
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 330443625 217 NEvrenepDIKLQRLWWGSDRVPEDIDLVVGADVTYDPTILPDLCECLAECLA 269
Cdd:COG3897  117 GV------AITTRLGDWRDPPAAGGFDLILGGDVLYERDLAEPLLPFLDRLAA 163
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
137-286 8.17e-17

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: 76.99  E-value: 8.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443625  137 WEAALYMGDFLIHKPLQELAPVQGQDdgkkkLNVLEVGAGTGIVSLVIlqKYHEFVNKMYVTDGDsNLVETqLKRNFELN 216
Cdd:pfam10294  22 WDAAVVLSKYLEMKIFKELGANNLSG-----LNVLELGSGTGLVGIAV--ALLLPGASVTITDLE-EALEL-LKKNIELN 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330443625  217 NevreNEPDIKLQRLWWGSD-----RVPEDIDLVVGADVTYDPTILPDLCECLAECLALDRCklCLLSATIRSES 286
Cdd:pfam10294  93 A----LSSKVVVKVLDWGENlppdlFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESV--ILVAYKKRREA 161
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
137-269 1.03e-07

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 51.81  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443625 137 WEAALYMGDFLIHKPlqELApvqgqddGKKklnVLEVGAGTGIVSLVILQKyheFVNKMYVTDGDSnLVETQLKRNFELN 216
Cdd:COG3897   53 WPSGQALARYLLDHP--EVA-------GKR---VLELGCGLGLVGIAAAKA---GAADVTATDYDP-EALAALRLNAALN 116
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 330443625 217 NEvrenepDIKLQRLWWGSDRVPEDIDLVVGADVTYDPTILPDLCECLAECLA 269
Cdd:COG3897  117 GV------AITTRLGDWRDPPAAGGFDLILGGDVLYERDLAEPLLPFLDRLAA 163
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
165-246 5.80e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 40.90  E-value: 5.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443625 165 KKKLNVLEVGAGTGIVSLVILQKYHE-FVnkmyvtDG---DSNLVEtQLKRNFELNN-----EVRENepDIKLqrlwWGS 235
Cdd:COG4123   36 KKGGRVLDLGTGTGVIALMLAQRSPGaRI------TGveiQPEAAE-LARRNVALNGledriTVIHG--DLKE----FAA 102
                         90
                 ....*....|.
gi 330443625 236 DRVPEDIDLVV 246
Cdd:COG4123  103 ELPPGSFDLVV 113
 
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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