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Conserved domains on  [gi|767908507|ref|XP_011507534|]
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N-terminal Xaa-Pro-Lys N-methyltransferase 2 isoform X1 [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 ...
 2-212 3.49e-89

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: 261.54  E-value: 3.49e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507    2 QFYARAKLFYQEVPATEEGMMGNFIELSSPDIQASQKFLRKFV--GGPGRAGTDCALDCGSGIGRVSKHVLLPVFNSVEL 79
Cdd:pfam05891   4 IFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLreRLPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507   80 VDMMESFLLEAQNYLQVKGDKVESYHCYSLQEFTPPFRRYDVIWIQWVSGHLTDKDLLAFLSRCRDGLKENGIIILKDNV 159
Cdd:pfam05891  84 VEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKENV 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767908507  160 AREG-CILDLSDSSVTRDMDILRSLIRKSGLVVLGQEKQDGFPEQCIPVWMFAL 212
Cdd:pfam05891 164 TQNGfDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYAL 217
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 2-212 3.49e-89

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: 261.54  E-value: 3.49e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507    2 QFYARAKLFYQEVPATEEGMMGNFIELSSPDIQASQKFLRKFV--GGPGRAGTDCALDCGSGIGRVSKHVLLPVFNSVEL 79
Cdd:pfam05891   4 IFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLreRLPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507   80 VDMMESFLLEAQNYLQVKGDKVESYHCYSLQEFTPPFRRYDVIWIQWVSGHLTDKDLLAFLSRCRDGLKENGIIILKDNV 159
Cdd:pfam05891  84 VEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKENV 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767908507  160 AREG-CILDLSDSSVTRDMDILRSLIRKSGLVVLGQEKQDGFPEQCIPVWMFAL 212
Cdd:pfam05891 164 TQNGfDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYAL 217
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 37-155 2.40e-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: 53.48  E-value: 2.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507  37 QKFLRKFVGGPGRAgtdcaLDCGSGIGRVSKHvLLPVFNSVELVDMMESFLLEAQNYLqvKGDKVEsYHCYSLQEFTPPF 116
Cdd:COG2227   15 AALLARLLPAGGRV-----LDVGCGTGRLALA-LARRGADVTGVDISPEALEIARERA--AELNVD-FVQGDLEDLPLED 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767908507 117 RRYDVIWIQWVSGHLTdkDLLAFLSRCRDGLKENGIIIL 155
Cdd:COG2227   86 GSFDLVICSEVLEHLP--DPAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-156 7.05e-07

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: 46.27  E-value: 7.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507  56 LDCGSGIGRVSKHVLLPVFNSVELVDMMESFLLEA-QNYLQVKGDKVESYHCYSLQEFTPPFRRYDVIwIQWVSGHLTDK 134
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELArKAAAALLADNVEVLKGDAEELPPEADESFDVI-ISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|..
gi 767908507 135 DLLAFLSRCRDGLKENGIIILK 156
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 ...
 2-212 3.49e-89

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: 261.54  E-value: 3.49e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507    2 QFYARAKLFYQEVPATEEGMMGNFIELSSPDIQASQKFLRKFV--GGPGRAGTDCALDCGSGIGRVSKHVLLPVFNSVEL 79
Cdd:pfam05891   4 IFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLreRLPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507   80 VDMMESFLLEAQNYLQVKGDKVESYHCYSLQEFTPPFRRYDVIWIQWVSGHLTDKDLLAFLSRCRDGLKENGIIILKDNV 159
Cdd:pfam05891  84 VEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKENV 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767908507  160 AREG-CILDLSDSSVTRDMDILRSLIRKSGLVVLGQEKQDGFPEQCIPVWMFAL 212
Cdd:pfam05891 164 TQNGfDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYAL 217
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 56-151 7.28e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.80  E-value: 7.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507   56 LDCGSGIGRVSKHVLLPVFNSVELVDMMESFLLEAQNYLQVKGDKVEsYHCYSLQEFTPPFRRYDVIWIQWVSGHLTDKD 135
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVE-FVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 767908507  136 LLAFLSRCRDGLKENG 151
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 37-155 2.40e-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: 53.48  E-value: 2.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507  37 QKFLRKFVGGPGRAgtdcaLDCGSGIGRVSKHvLLPVFNSVELVDMMESFLLEAQNYLqvKGDKVEsYHCYSLQEFTPPF 116
Cdd:COG2227   15 AALLARLLPAGGRV-----LDVGCGTGRLALA-LARRGADVTGVDISPEALEIARERA--AELNVD-FVQGDLEDLPLED 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767908507 117 RRYDVIWIQWVSGHLTdkDLLAFLSRCRDGLKENGIIIL 155
Cdd:COG2227   86 GSFDLVICSEVLEHLP--DPAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-156 7.05e-07

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: 46.27  E-value: 7.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507  56 LDCGSGIGRVSKHVLLPVFNSVELVDMMESFLLEA-QNYLQVKGDKVESYHCYSLQEFTPPFRRYDVIwIQWVSGHLTDK 134
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELArKAAAALLADNVEVLKGDAEELPPEADESFDVI-ISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|..
gi 767908507 135 DLLAFLSRCRDGLKENGIIILK 156
Cdd:cd02440   82 DLARFLEEARRLLKPGGVLVLT 103
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 37-167 1.59e-05

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: 43.44  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507  37 QKFLRKFVGGPGragtDCALDCGSGIGRVSKHvLLPVFNSVELVDMMESFLLEAQNYLQVKGDKVEsYHCYSLQEFtpPF 116
Cdd:COG2226   12 EALLAALGLRPG----ARVLDLGCGTGRLALA-LAERGARVTGVDISPEMLELARERAAEAGLNVE-FVVGDAEDL--PF 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767908507 117 R--RYDVIWIQWVSGHLTDKDllAFLSRCRDGLKENGIIILKDNVAREGCILD 167
Cdd:COG2226   84 PdgSFDLVISSFVLHHLPDPE--RALAEIARVLKPGGRLVVVDFSPPDLAELE 134
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 54-164 3.48e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 40.28  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507  54 CALDCGSGIGRVSkHVLLPVFNS-VELVDMMESFLLEAQNYLQVKG-DKVEsYHCYSLQEFTP-PFRRYDVIWIQWVSGH 130
Cdd:COG0500   29 RVLDLGCGTGRNL-LALAARFGGrVIGIDLSPEAIALARARAAKAGlGNVE-FLVADLAELDPlPAESFDLVVAFGVLHH 106

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767908507 131 LTDKDLLAFLSRCRDGLKENGIIILKDNVAREGC 164
Cdd:COG0500  107 LPPEEREALLRELARALKPGGVLLLSASDAAAAL 140
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-155 5.79e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.64  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767908507   56 LDCGSGIGRVSKHvLLPVFNSVELVDMMESFLLEAQnylQVKGDKVESYHCYSLQEFtpPFR--RYDVIWIQWVSGHLtd 133
Cdd:pfam08241   1 LDVGCGTGLLTEL-LARLGARVTGVDISPEMLELAR---EKAPREGLTFVVGDAEDL--PFPdnSFDLVLSSEVLHHV-- 72

                          90       100
                  ....*....|....*....|..
gi 767908507  134 KDLLAFLSRCRDGLKENGIIIL 155
Cdd:pfam08241  73 EDPERALREIARVLKPGGILII 94
 
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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