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Conserved domains on  [gi|557947974|ref|NP_001273730|]
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N-terminal Xaa-Pro-Lys N-methyltransferase 1 isoform b [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
Methyltransf_PK super family cl47937
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 8-118 3.37e-57

AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron PVT and in uterine cells in C. elegans [worm-base]. In Saccharomyces cerevisiae this is AdoMet dependent proline di-methyltransferase. This enzyme catalyzes the di-methylation of ribosomal proteins Rpl12 and Rps25 at N-terminal proline residues. The methyltransferases described here specifically recognize the N-terminal X-Pro-Lys sequence motif, and they may account for nearly all previously described eukaryotic protein N-terminal methylation reactions. A number of other yeast and human proteins also share the recognition motif and may be similarly modified. As with other methyltransferases, this family carries the characteriztic GxGxG motif.


The actual alignment was detected with superfamily member pfam05891:

Pssm-ID: 461771  Cd Length: 218  Bit Score: 177.18  E-value: 3.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947974    8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRE 86
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 557947974   87 VDMVDITEDFLVQAKTYLGEEGKRATS----PISTW 118
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEGKKKVGNffcvGLQDF 116
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 8-118 3.37e-57

AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron PVT and in uterine cells in C. elegans [worm-base]. In Saccharomyces cerevisiae this is AdoMet dependent proline di-methyltransferase. This enzyme catalyzes the di-methylation of ribosomal proteins Rpl12 and Rps25 at N-terminal proline residues. The methyltransferases described here specifically recognize the N-terminal X-Pro-Lys sequence motif, and they may account for nearly all previously described eukaryotic protein N-terminal methylation reactions. A number of other yeast and human proteins also share the recognition motif and may be similarly modified. As with other methyltransferases, this family carries the characteriztic GxGxG motif.


Pssm-ID: 461771  Cd Length: 218  Bit Score: 177.18  E-value: 3.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947974    8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRE 86
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 557947974   87 VDMVDITEDFLVQAKTYLGEEGKRATS----PISTW 118
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEGKKKVGNffcvGLQDF 116
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-112 4.89e-04

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 38.05  E-value: 4.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557947974  46 RKFLQRfLREGPNKTgtscALDCGAGIGRITkRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRAT 112
Cdd:COG2226   12 EALLAA-LGLRPGAR----VLDLGCGTGRLA-LALAERGARVTGVDISPEMLELARERAAEAGLNVE 72
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 66-101 6.97e-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: 34.33  E-value: 6.97e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 557947974  66 LDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAK 101
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELAR 38
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 8-118 3.37e-57

AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron PVT and in uterine cells in C. elegans [worm-base]. In Saccharomyces cerevisiae this is AdoMet dependent proline di-methyltransferase. This enzyme catalyzes the di-methylation of ribosomal proteins Rpl12 and Rps25 at N-terminal proline residues. The methyltransferases described here specifically recognize the N-terminal X-Pro-Lys sequence motif, and they may account for nearly all previously described eukaryotic protein N-terminal methylation reactions. A number of other yeast and human proteins also share the recognition motif and may be similarly modified. As with other methyltransferases, this family carries the characteriztic GxGxG motif.


Pssm-ID: 461771  Cd Length: 218  Bit Score: 177.18  E-value: 3.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557947974    8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRE 86
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 557947974   87 VDMVDITEDFLVQAKTYLGEEGKRATS----PISTW 118
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEGKKKVGNffcvGLQDF 116
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 66-112 1.20e-04

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 38.70  E-value: 1.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 557947974   66 LDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRAT 112
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVE 48
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-112 4.89e-04

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 38.05  E-value: 4.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557947974  46 RKFLQRfLREGPNKTgtscALDCGAGIGRITkRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRAT 112
Cdd:COG2226   12 EALLAA-LGLRPGAR----VLDLGCGTGRLA-LALAERGARVTGVDISPEMLELARERAAEAGLNVE 72
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 46-108 3.68e-03

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 35.38  E-value: 3.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557947974  46 RKFLQRFLREGPNKTGTscALDCGAGIGRITkRLLLPLFREVDMVDITEDFLVQAKTYLGEEG 108
Cdd:COG2227   11 DRRLAALLARLLPAGGR--VLDVGCGTGRLA-LALARRGADVTGVDISPEALEIARERAAELN 70
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
46-101 5.00e-03

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 35.36  E-value: 5.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557947974  46 RKFLQRFLREGPNKtgtscALDCGAGIGRITkRLLLPLFREVDMVDITEDFLVQAK 101
Cdd:COG4976   36 EELLARLPPGPFGR-----VLDLGCGTGLLG-EALRPRGYRLTGVDLSEEMLAKAR 85
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 66-101 6.97e-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: 34.33  E-value: 6.97e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 557947974  66 LDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAK 101
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELAR 38
 
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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