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Conserved domains on  [gi|1046880275|ref|XP_017447369|]
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N-terminal Xaa-Pro-Lys N-methyltransferase 1 isoform X4 [Rattus norvegicus]

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 ...
 1-135 1.13e-77

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: 228.80  E-value: 1.13e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880275   1 MVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPSSYDVIWIQWVIGHLTDQHLAEFLRRCRRGLRPNGIIVIKDN 80
Cdd:pfam05891  83 LVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKEN 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046880275  81 MAQEGV-ILDDVDSSVCRDLEVVRRIIRSAGLSLLAEERQENLPDEIYHVYSFALR 135
Cdd:pfam05891 163 VTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 1-135 1.13e-77

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: 228.80  E-value: 1.13e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880275   1 MVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPSSYDVIWIQWVIGHLTDQHLAEFLRRCRRGLRPNGIIVIKDN 80
Cdd:pfam05891  83 LVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKEN 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046880275  81 MAQEGV-ILDDVDSSVCRDLEVVRRIIRSAGLSLLAEERQENLPDEIYHVYSFALR 135
Cdd:pfam05891 163 VTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 2-77 5.44e-11

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: 55.79  E-value: 5.44e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046880275   2 VDVTEDFLAKAKTYLGEEGKRvrnYFCCGLQDFSPEPSSYDVIWIQWVIGHLTDqhLAEFLRRCRRGLRPNGIIVI 77
Cdd:COG2227    52 VDISPEALEIARERAAELNVD---FVQGDLEDLPLEDGSFDLVICSEVLEHLPD--PAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 1-78 9.50e-06

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: 9.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046880275   1 MVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSP-EPSSYDVIWIQWVIGHLtDQHLAEFLRRCRRGLRPNGIIVIK 78
Cdd:cd02440    26 GVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLVLT 103
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 2-84 3.55e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 36.10  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880275   2 VDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFsPEpSSYDVIWIQWVIGHLTDQHLAEFLRRCRRGLRPNGIIVIKDNM 81
Cdd:PTZ00098   81 VDICEKMVNIAKLRNSDKNKIEFEANDILKKDF-PE-NTFDMIYSRDAILHLSYADKKKLFEKCYKWLKPNGILLITDYC 158


                  ...
gi 1046880275  82 AQE 84
Cdd:PTZ00098  159 ADK 161
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 1-135 1.13e-77

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: 228.80  E-value: 1.13e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880275   1 MVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPSSYDVIWIQWVIGHLTDQHLAEFLRRCRRGLRPNGIIVIKDN 80
Cdd:pfam05891  83 LVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKEN 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046880275  81 MAQEGV-ILDDVDSSVCRDLEVVRRIIRSAGLSLLAEERQENLPDEIYHVYSFALR 135
Cdd:pfam05891 163 VTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 2-73 1.70e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 1.70e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046880275   2 VDVTEDFLAKAKTYLGEEGKRVRnYFCCGLQDFSPEPSSYDVIWIQWVIGHLTDQHLAEFLRRCRRGLRPNG 73
Cdd:pfam13649  26 VDLSPEMLERARERAAEAGLNVE-FVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 2-77 5.44e-11

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: 55.79  E-value: 5.44e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046880275   2 VDVTEDFLAKAKTYLGEEGKRvrnYFCCGLQDFSPEPSSYDVIWIQWVIGHLTDqhLAEFLRRCRRGLRPNGIIVI 77
Cdd:COG2227    52 VDISPEALEIARERAAELNVD---FVQGDLEDLPLEDGSFDLVICSEVLEHLPD--PAALLRELARLLKPGGLLLL 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 2-112 2.06e-09

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: 52.30  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880275   2 VDVTEDFLAKAKTYLGEEGKRVRnyFCCG-LQDFSPEPSSYDVIWIQWVIGHLTDqhLAEFLRRCRRGLRPNGIIVIKDN 80
Cdd:COG2226    50 VDISPEMLELARERAAEAGLNVE--FVVGdAEDLPFPDGSFDLVISSFVLHHLPD--PERALAEIARVLKPGGRLVVVDF 125

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1046880275  81 MAqegvilddvdssvcRDLEVVRRIIRSAGLS 112
Cdd:COG2226   126 SP--------------PDLAELEELLAEAGFE 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 2-77 7.46e-08

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 46.89  E-value: 7.46e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046880275   2 VDVTEDFLAKAKTYLGEEGKrvrNYFCCGLQDFSPEPSSYDVIWIQWVIGHLTDqhLAEFLRRCRRGLRPNGIIVI 77
Cdd:pfam08241  24 VDISPEMLELAREKAPREGL---TFVVGDAEDLPFPDNSFDLVLSSEVLHHVED--PERALREIARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
2-77 9.19e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 46.74  E-value: 9.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046880275   2 VDVTEDFLAKAKTYLGeegkRVRnyFCCG-LQDFSPEPSsYDVIWIQWVIGHLTDQhlAEFLRRCRRGLRPNGIIVI 77
Cdd:COG4106    31 VDLSPEMLARARARLP----NVR--FVVAdLRDLDPPEP-FDLVVSNAALHWLPDH--AALLARLAAALAPGGVLAV 98
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 2-75 9.78e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 44.28  E-value: 9.78e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046880275   2 VDVTEDFLAKAKTYLGEEGKRVR---NYFCcgLQDFSPEPSSYDVIWIQWVIGHLTDqhLAEFLRRCRRGLRPNGII 75
Cdd:pfam08242  26 LDISPAALEAARERLAALGLLNAvrvELFQ--LDLGELDPGSFDVVVASNVLHHLAD--PRAVLRNIRRLLKPGGVL 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 2-77 4.62e-06

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 43.38  E-value: 4.62e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046880275   2 VDVTEDFLAKAKTYLGEEG--KRVRnYFCCGLQDFsPEPSSYDVIWIQWVIGHLTDQHLAEFLRRCRRGLRPNGIIVI 77
Cdd:COG2230    80 VTLSPEQLEYARERAAEAGlaDRVE-VRLADYRDL-PADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 1-78 9.50e-06

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: 9.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046880275   1 MVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSP-EPSSYDVIWIQWVIGHLtDQHLAEFLRRCRRGLRPNGIIVIK 78
Cdd:cd02440    26 GVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLVLT 103
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 2-86 1.04e-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: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880275   2 VDVTEDFLAKAKTYLGEEG-KRVRnYFCCGLQDFSPEPS-SYDVIWIQWVIGHLTDQHLAEFLRRCRRGLRPNGIIVIKD 79
Cdd:COG0500    55 IDLSPEAIALARARAAKAGlGNVE-FLVADLAELDPLPAeSFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSA 133


                  ....*..
gi 1046880275  80 NMAQEGV 86
Cdd:COG0500   134 SDAAAAL 140
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
37-77 1.53e-03

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 36.38  E-value: 1.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1046880275  37 EPSSYDVIWIQWVIGHLTDQHLAEFLRRCRRGLRPNGIIVI 77
Cdd:COG4627    43 PDNSVDAIYSSHVLEHLDYEEAPLALKECYRVLKPGGILRI 83
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 10-85 2.14e-03

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 36.61  E-value: 2.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046880275  10 AKAKTYLgEEGKRVRNYFCCGlqDFSPEP-SSYDVIWIQWVIGHLTDQHLAEFLRRCRRGLRPNGIIVIKDNMAQEG 85
Cdd:pfam00891  97 EAAPTHF-SAGEEPRVTFHGG--DFFKDSlPEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGKVILVESLLGAD 170
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 2-89 3.13e-03

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 35.55  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880275   2 VDVTEDFLAKAKTYLGEEG--KRVRnyFCCG-----LQDFSPEPssYDVIWIqwvighltD---QHLAEFLRRCRRGLRP 71
Cdd:COG4122    47 IEIDPERAAIARENFARAGlaDRIR--LILGdalevLPRLADGP--FDLVFI--------DadkSNYPDYLELALPLLRP 114

                          90
                  ....*....|....*...
gi 1046880275  72 NGIIVIkDNMAQEGVILD 89
Cdd:COG4122   115 GGLIVA-DNVLWHGRVAD 131
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 2-84 3.55e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 36.10  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880275   2 VDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFsPEpSSYDVIWIQWVIGHLTDQHLAEFLRRCRRGLRPNGIIVIKDNM 81
Cdd:PTZ00098   81 VDICEKMVNIAKLRNSDKNKIEFEANDILKKDF-PE-NTFDMIYSRDAILHLSYADKKKLFEKCYKWLKPNGILLITDYC 158


                  ...
gi 1046880275  82 AQE 84
Cdd:PTZ00098  159 ADK 161
 
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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