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Conserved domains on  [gi|308197129|sp|Q10CT5|]
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RecName: Full=Alpha N-terminal protein methyltransferase 1; AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1; Short=NTM1

Protein Classification

N-terminal Xaa-Pro-Lys N-methyltransferase 1( domain architecture ID 10531238)

N-terminal Xaa-Pro-Lys N-methyltransferase 1, also called alpha N-terminal protein methyltransferase 1, is a class I SAM-dependent methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 65-283 4.53e-137

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: 386.73  E-value: 4.53e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129   65 WYSKAIAYWQGVEASTEGVLGGYGCVNDVDVKGSDAFLRPLLAERFGAARRHLVALDCGSGIGRVTKNFLLRHFNEVDLV 144
Cdd:pfam05891   5 FYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRERLPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  145 EPVSHFLEAAQENLtecmevGEDTHKAANFYCVPLQDFTPDEGRYDVIWIQWCIGQLPDDDFISFFNRAKIGLKPNGFFV 224
Cdd:pfam05891  85 EPVEDFIEKAKEYL------AEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  225 LKENIARNGF-VLDKEDNSITRSDAYFKELFKKCGLYIHSIKDQSDLPKELFAVKMYALV 283
Cdd:pfam05891 159 VKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 65-283 4.53e-137

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: 386.73  E-value: 4.53e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129   65 WYSKAIAYWQGVEASTEGVLGGYGCVNDVDVKGSDAFLRPLLAERFGAARRHLVALDCGSGIGRVTKNFLLRHFNEVDLV 144
Cdd:pfam05891   5 FYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRERLPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  145 EPVSHFLEAAQENLtecmevGEDTHKAANFYCVPLQDFTPDEGRYDVIWIQWCIGQLPDDDFISFFNRAKIGLKPNGFFV 224
Cdd:pfam05891  85 EPVEDFIEKAKEYL------AEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  225 LKENIARNGF-VLDKEDNSITRSDAYFKELFKKCGLYIHSIKDQSDLPKELFAVKMYALV 283
Cdd:pfam05891 159 VKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 99-225 1.32e-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: 60.80  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  99 DAFLRPLLAERFGAARRhlvALDCGSGIGRVTKnFLLRHFNEVDLVEPVSHFLEAAQENLTECmevgedthkAANFYCVP 178
Cdd:COG2227   11 DRRLAALLARLLPAGGR---VLDVGCGTGRLAL-ALARRGADVTGVDISPEALEIARERAAEL---------NVDFVQGD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 308197129 179 LQDFTPDEGRYDVIWIQWCIGQLPDDDfiSFFNRAKIGLKPNGFFVL 225
Cdd:COG2227   78 LEDLPLEDGSFDLVICSEVLEHLPDPA--ALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 120-226 9.43e-04

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: 38.18  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129 120 LDCGSGIGRVTKNFLLRHFNEVDLVEPVSHFLEAAQENLTECMEVGedthkaANFYCVPLQDFTPDE-GRYDVIWIQWCI 198
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN------VEVLKGDAEELPPEAdESFDVIISDPPL 76

                         90       100
                 ....*....|....*....|....*...
gi 308197129 199 gQLPDDDFISFFNRAKIGLKPNGFFVLK 226
Cdd:cd02440   77 -HHLVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 65-283 4.53e-137

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: 386.73  E-value: 4.53e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129   65 WYSKAIAYWQGVEASTEGVLGGYGCVNDVDVKGSDAFLRPLLAERFGAARRHLVALDCGSGIGRVTKNFLLRHFNEVDLV 144
Cdd:pfam05891   5 FYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRERLPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  145 EPVSHFLEAAQENLtecmevGEDTHKAANFYCVPLQDFTPDEGRYDVIWIQWCIGQLPDDDFISFFNRAKIGLKPNGFFV 224
Cdd:pfam05891  85 EPVEDFIEKAKEYL------AEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  225 LKENIARNGF-VLDKEDNSITRSDAYFKELFKKCGLYIHSIKDQSDLPKELFAVKMYALV 283
Cdd:pfam05891 159 VKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 99-225 1.32e-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: 60.80  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  99 DAFLRPLLAERFGAARRhlvALDCGSGIGRVTKnFLLRHFNEVDLVEPVSHFLEAAQENLTECmevgedthkAANFYCVP 178
Cdd:COG2227   11 DRRLAALLARLLPAGGR---VLDVGCGTGRLAL-ALARRGADVTGVDISPEALEIARERAAEL---------NVDFVQGD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 308197129 179 LQDFTPDEGRYDVIWIQWCIGQLPDDDfiSFFNRAKIGLKPNGFFVL 225
Cdd:COG2227   78 LEDLPLEDGSFDLVICSEVLEHLPDPA--ALLRELARLLKPGGLLLL 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 120-221 1.72e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.80  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  120 LDCGSGIGRVTKNFLLRHFNEVDLVEPVSHFLEAAQENLtecmevgEDTHKAANFYCVPLQDFTPDEGRYDVIWIQWCIG 199
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERA-------AEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLH 74

                          90       100
                  ....*....|....*....|..
gi 308197129  200 QLPDDDFISFFNRAKIGLKPNG 221
Cdd:pfam13649  75 HLPDPDLEAALREIARVLKPGG 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
90-259 1.16e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 48.07  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  90 VNDVDVKGSDAFLRPLLAERFGAARRHlvALDCGSGIGRVTKnFLLRHFNEVDLVEPVSHFLEAAQENLTEcmevgedth 169
Cdd:COG4976   23 VEDLGYEAPALLAEELLARLPPGPFGR--VLDLGCGTGLLGE-ALRPRGYRLTGVDLSEEMLAKAREKGVY--------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129 170 kaANFYCVPLQDFTPDEGRYDVIWIQWCIGQLpdDDFISFFNRAKIGLKPNGFFVlkeniarngFVLDKEDNSI--TRSD 247
Cdd:COG4976   91 --DRLLVADLADLAEPDGRFDLIVAADVLTYL--GDLAAVFAGVARALKPGGLFI---------FSVEDADGSGryAHSL 157

                        170
                 ....*....|..
gi 308197129 248 AYFKELFKKCGL 259
Cdd:COG4976  158 DYVRDLLAAAGF 169
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 102-238 3.92e-06

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: 45.76  E-value: 3.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129 102 LRPLLAERFGAARRHLVaLDCGSGIGRVTKnFLLRHFNEVDLVEPVSHFLEAAQENLTEcmEVGEDTHKAANFYCVPLQD 181
Cdd:COG2226   10 GREALLAALGLRPGARV-LDLGCGTGRLAL-ALAERGARVTGVDISPEMLELARERAAE--AGLNVEFVVGDAEDLPFPD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 308197129 182 ftpdeGRYDVIWIQWCIGQLPD-DDFISFFNRAkigLKPNGFFVLKENIARNGFVLDK 238
Cdd:COG2226   86 -----GSFDLVISSFVLHHLPDpERALAEIARV---LKPGGRLVVVDFSPPDLAELEE 135
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 120-225 2.24e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 42.27  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  120 LDCGSGIGRVTKnFLLRHFNEVDLVEPVSHFLEAAQENLTecmEVGEDTHKaANFYCVPLQDftpdeGRYDVIWIQWCIG 199
Cdd:pfam08241   1 LDVGCGTGLLTE-LLARLGARVTGVDISPEMLELAREKAP---REGLTFVV-GDAEDLPFPD-----NSFDLVLSSEVLH 70

                          90       100
                  ....*....|....*....|....*..
gi 308197129  200 QLPD-DDFISFFNRAkigLKPNGFFVL 225
Cdd:pfam08241  71 HVEDpERALREIARV---LKPGGILII 94
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 96-225 6.98e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.98  E-value: 6.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129  96 KGSDAFLRPLLAERFGAARR---HLVALDCGSGIGRVTkNFLLRHFNE-VDLVEPVSHFLEAAQENLTEcmevgeDTHKA 171
Cdd:COG0500    4 SYYSDELLPGLAALLALLERlpkGGRVLDLGCGTGRNL-LALAARFGGrVIGIDLSPEAIALARARAAK------AGLGN 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 308197129 172 ANFYCVPLQDFTP-DEGRYDVIWIQWCIGQLPDDDFISFFNRAKIGLKPNGFFVL 225
Cdd:COG0500   77 VEFLVADLAELDPlPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 120-226 9.43e-04

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: 38.18  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129 120 LDCGSGIGRVTKNFLLRHFNEVDLVEPVSHFLEAAQENLTECMEVGedthkaANFYCVPLQDFTPDE-GRYDVIWIQWCI 198
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN------VEVLKGDAEELPPEAdESFDVIISDPPL 76

                         90       100
                 ....*....|....*....|....*...
gi 308197129 199 gQLPDDDFISFFNRAKIGLKPNGFFVLK 226
Cdd:cd02440   77 -HHLVEDLARFLEEARRLLKPGGVLVLT 103
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 120-225 1.85e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 38.37  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308197129 120 LDCGSGIGRVTKnFLLRHFN-EVDLVEPVSHFLEAAQENLTEcmevgEDTHKAANFYCVPLQDFTPDeGRYDVIwiqWCI 198
Cdd:COG2230   56 LDIGCGWGGLAL-YLARRYGvRVTGVTLSPEQLEYARERAAE-----AGLADRVEVRLADYRDLPAD-GQFDAI---VSI 125

                         90       100       110
                 ....*....|....*....|....*....|
gi 308197129 199 G---QLPDDDFISFFNRAKIGLKPNGFFVL 225
Cdd:COG2230  126 GmfeHVGPENYPAYFAKVARLLKPGGRLLL 155
 
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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