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Conserved domains on  [gi|530407712|ref|XP_005255215|]
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protein-lysine N-methyltransferase EEF2KMT isoform X2 [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; ...
35-186 6.52e-18

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: 77.76  E-value: 6.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407712   35 GLVTWDAALYLAEW-----AIENPAV-FTNRTVLELGSGAGLTGLAICKMCRPRAYIFSDcHSRVLEQLRGNVLLNGLsl 108
Cdd:pfam10294  18 GGHVWDAAVVLSKYlemkiFKELGANnLSGLNVLELGSGTGLVGIAVALLLPGASVTITD-LEEALELLKKNIELNAL-- 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407712  109 eaditakldSPRVTVAQLDWDVATVHQLSAFQP-DVVIAADVLYCPEAIMSLVGVLRRLAacrehQRAPEVYVAFTVRN 186
Cdd:pfam10294  95 ---------SSKVVVKVLDWGENLPPDLFDGHPvDLILAADCVYNEDSFPLLEKTLKDLL-----GKESVILVAYKKRR 159
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
35-186 6.52e-18

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: 77.76  E-value: 6.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407712   35 GLVTWDAALYLAEW-----AIENPAV-FTNRTVLELGSGAGLTGLAICKMCRPRAYIFSDcHSRVLEQLRGNVLLNGLsl 108
Cdd:pfam10294  18 GGHVWDAAVVLSKYlemkiFKELGANnLSGLNVLELGSGTGLVGIAVALLLPGASVTITD-LEEALELLKKNIELNAL-- 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407712  109 eaditakldSPRVTVAQLDWDVATVHQLSAFQP-DVVIAADVLYCPEAIMSLVGVLRRLAacrehQRAPEVYVAFTVRN 186
Cdd:pfam10294  95 ---------SSKVVVKVLDWGENLPPDLFDGHPvDLILAADCVYNEDSFPLLEKTLKDLL-----GKESVILVAYKKRR 159
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
35-186 6.52e-18

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: 77.76  E-value: 6.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407712   35 GLVTWDAALYLAEW-----AIENPAV-FTNRTVLELGSGAGLTGLAICKMCRPRAYIFSDcHSRVLEQLRGNVLLNGLsl 108
Cdd:pfam10294  18 GGHVWDAAVVLSKYlemkiFKELGANnLSGLNVLELGSGTGLVGIAVALLLPGASVTITD-LEEALELLKKNIELNAL-- 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530407712  109 eaditakldSPRVTVAQLDWDVATVHQLSAFQP-DVVIAADVLYCPEAIMSLVGVLRRLAacrehQRAPEVYVAFTVRN 186
Cdd:pfam10294  95 ---------SSKVVVKVLDWGENLPPDLFDGHPvDLILAADCVYNEDSFPLLEKTLKDLL-----GKESVILVAYKKRR 159
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
62-168 2.39e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 36.19  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530407712   62 LELGSGAGLTGLAICKMCRPRAYIFSDCHSRVLEQLRGNVllnglsleaditakLDSPRVTVAQLDWDVATVHQLSAFQP 141
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERL--------------AALGLLNAVRVELFQLDLGELDPGSF 66
                          90       100
                  ....*....|....*....|....*..
gi 530407712  142 DVVIAADVLYCPEAIMSLVGVLRRLAA 168
Cdd:pfam08242  67 DVVVASNVLHHLADPRAVLRNIRRLLK 93
 
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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