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Conserved domains on  [gi|221139873|ref|NP_001137428|]
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N-terminal Xaa-Pro-Lys N-methyltransferase 2 [Mus musculus]

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 ...
 63-277 2.36e-87

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: 259.62  E-value: 2.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873   63 DGEmQFYARAKLFYQEVPATEEGMMGNFIELSNPDIQASREFLRKFV--GGPGRAGTGCALDCGSGIGRVSKHVLLPVFS 140
Cdd:pfam05891   1 DEE-IFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLreRLPGKNRHLVALDCGAGIGRVTKNLLLPLFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873  141 SVELVDMMESFLLEAQSYLQVNEDKVESYHCYSLQEFTPHLGRYDVIWIQWVSGYLTDKDLLAFLSRCRDGLKENGVIIL 220
Cdd:pfam05891  80 KVDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221139873  221 KDNVAREG-CIFDLSDSSVTRDMDILRSLIRKSGLVVLGQEKQEGFPEQCVPVWMFAL 277
Cdd:pfam05891 160 KENVTQNGfDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYAL 217
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 63-277 2.36e-87

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: 259.62  E-value: 2.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873   63 DGEmQFYARAKLFYQEVPATEEGMMGNFIELSNPDIQASREFLRKFV--GGPGRAGTGCALDCGSGIGRVSKHVLLPVFS 140
Cdd:pfam05891   1 DEE-IFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLreRLPGKNRHLVALDCGAGIGRVTKNLLLPLFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873  141 SVELVDMMESFLLEAQSYLQVNEDKVESYHCYSLQEFTPHLGRYDVIWIQWVSGYLTDKDLLAFLSRCRDGLKENGVIIL 220
Cdd:pfam05891  80 KVDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221139873  221 KDNVAREG-CIFDLSDSSVTRDMDILRSLIRKSGLVVLGQEKQEGFPEQCVPVWMFAL 277
Cdd:pfam05891 160 KENVTQNGfDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYAL 217
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 102-220 2.34e-09

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: 54.25  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873 102 REFLRKFVGGPGRAgtgcaLDCGSGIGRVSKHvLLPVFSSVELVDMMESFLLEAQSYLQvnEDKVEsYHCYSLQEFTPHL 181
Cdd:COG2227   15 AALLARLLPAGGRV-----LDVGCGTGRLALA-LARRGADVTGVDISPEALEIARERAA--ELNVD-FVQGDLEDLPLED 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 221139873 182 GRYDVIW----IQWVSgyltdkDLLAFLSRCRDGLKENGVIIL 220
Cdd:COG2227   86 GSFDLVIcsevLEHLP------DPAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 121-221 4.74e-05

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: 41.65  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873 121 LDCGSGIGRVSKHVLLPVFSSVELVDMMESFLLEAQSY-LQVNEDKVESYHCYSLQEFTPHLGRYDVIWIQWVSGYLTDk 199
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAaAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLVE- 81

                         90       100
                 ....*....|....*....|..
gi 221139873 200 DLLAFLSRCRDGLKENGVIILK 221
Cdd:cd02440   82 DLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 63-277 2.36e-87

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: 259.62  E-value: 2.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873   63 DGEmQFYARAKLFYQEVPATEEGMMGNFIELSNPDIQASREFLRKFV--GGPGRAGTGCALDCGSGIGRVSKHVLLPVFS 140
Cdd:pfam05891   1 DEE-IFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLreRLPGKNRHLVALDCGAGIGRVTKNLLLPLFS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873  141 SVELVDMMESFLLEAQSYLQVNEDKVESYHCYSLQEFTPHLGRYDVIWIQWVSGYLTDKDLLAFLSRCRDGLKENGVIIL 220
Cdd:pfam05891  80 KVDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 221139873  221 KDNVAREG-CIFDLSDSSVTRDMDILRSLIRKSGLVVLGQEKQEGFPEQCVPVWMFAL 277
Cdd:pfam05891 160 KENVTQNGfDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYAL 217
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 121-216 3.90e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 55.65  E-value: 3.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873  121 LDCGSGIGRVSKHVLLPVFSSVELVDMMESFLLEAQSYLQVNEDKVEsYHCYSLQEFTPHLGRYDVIWIQWVSGYLTDKD 200
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVE-FVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 221139873  201 LLAFLSRCRDGLKENG 216
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 102-220 2.34e-09

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: 54.25  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873 102 REFLRKFVGGPGRAgtgcaLDCGSGIGRVSKHvLLPVFSSVELVDMMESFLLEAQSYLQvnEDKVEsYHCYSLQEFTPHL 181
Cdd:COG2227   15 AALLARLLPAGGRV-----LDVGCGTGRLALA-LARRGADVTGVDISPEALEIARERAA--ELNVD-FVQGDLEDLPLED 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 221139873 182 GRYDVIW----IQWVSgyltdkDLLAFLSRCRDGLKENGVIIL 220
Cdd:COG2227   86 GSFDLVIcsevLEHLP------DPAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 121-221 4.74e-05

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: 41.65  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873 121 LDCGSGIGRVSKHVLLPVFSSVELVDMMESFLLEAQSY-LQVNEDKVESYHCYSLQEFTPHLGRYDVIWIQWVSGYLTDk 199
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAaAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLVE- 81

                         90       100
                 ....*....|....*....|..
gi 221139873 200 DLLAFLSRCRDGLKENGVIILK 221
Cdd:cd02440   82 DLARFLEEARRLLKPGGVLVLT 103
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
102-220 1.39e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 38.83  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873 102 REFLRKFVGGPGRAgtgcALDCGSGIGRVSKHvLLPVFSSVELVDMMESFLLEAQsylqvnEDKVE-SYHCYSLQEFTPH 180
Cdd:COG4976   36 EELLARLPPGPFGR----VLDLGCGTGLLGEA-LRPRGYRLTGVDLSEEMLAKAR------EKGVYdRLLVADLADLAEP 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 221139873 181 LGRYDVIWIQWVSGYLTdkDLLAFLSRCRDGLKENGVIIL 220
Cdd:COG4976  105 DGRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFIF 142
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 102-222 1.95e-03

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: 37.67  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873 102 REFLRKFVGGPGRAgtgcALDCGSGIGRVSKHvLLPVFSSVELVDMMESFLLEAQSYLQVNEDKVEsYHCYSLQEFTPHL 181
Cdd:COG2226   12 EALLAALGLRPGAR----VLDLGCGTGRLALA-LAERGARVTGVDISPEMLELARERAAEAGLNVE-FVVGDAEDLPFPD 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 221139873 182 GRYDVIWIQWVSGYLTDKDllAFLSRCRDGLKENGVIILKD 222
Cdd:COG2226   86 GSFDLVISSFVLHHLPDPE--RALAEIARVLKPGGRLVVVD 124
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 94-229 2.59e-03

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.97  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221139873  94 SNPDIQASREFLRKFVGGPGRAGTGCALDCGSGIGRVSKHVLLPVFSSVELVDMMESFLLEAQSYLQVNE-DKVEsYHCY 172
Cdd:COG0500    4 SYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGlGNVE-FLVA 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221139873 173 SLQEFTP-HLGRYDVIW----IQWVSgyltDKDLLAFLSRCRDGLKENGVIILKDNVAREGC 229
Cdd:COG0500   83 DLAELDPlPAESFDLVVafgvLHHLP----PEEREALLRELARALKPGGVLLLSASDAAAAL 140
 
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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