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Conserved domains on  [gi|6319738|ref|NP_009820|]
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N-terminal protein methyltransferase [Saccharomyces cerevisiae S288C]

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 ...
 6-228 5.56e-129

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: 362.85  E-value: 5.56e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738      6 DSHIKYEDAIDYWTDVDATVDGVLGGYGegtVVPTMDVLGSNNFLRKLKSRMLPQENNVKYAVDIGAGIGRVSKTMLHKH 85
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYG---HVSDIDVNGSRNFLRRLLRERLPGKNRHLVALDCGAGIGRVTKNLLLPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738     86 AAKIDLVEPVKPFIEQMHVELAElkDKGQIGQIYEVGMQDWTPDAGKYWLIWCQWCVGHLPDAELVAFLKRCIVGLQPNG 165
Cdd:pfam05891  78 FSKVDLVEPVEDFIEKAKEYLAE--GKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNG 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319738    166 TIVVKENNTPTDTDDFDETDSSVTRSDAKFRQIFEEAGLKLIASERQRGLPRELYPVRMYALK 228
Cdd:pfam05891 156 FIVVKENVTQNGFDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 6-228 5.56e-129

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: 362.85  E-value: 5.56e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738      6 DSHIKYEDAIDYWTDVDATVDGVLGGYGegtVVPTMDVLGSNNFLRKLKSRMLPQENNVKYAVDIGAGIGRVSKTMLHKH 85
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYG---HVSDIDVNGSRNFLRRLLRERLPGKNRHLVALDCGAGIGRVTKNLLLPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738     86 AAKIDLVEPVKPFIEQMHVELAElkDKGQIGQIYEVGMQDWTPDAGKYWLIWCQWCVGHLPDAELVAFLKRCIVGLQPNG 165
Cdd:pfam05891  78 FSKVDLVEPVEDFIEKAKEYLAE--GKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNG 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319738    166 TIVVKENNTPTDTDDFDETDSSVTRSDAKFRQIFEEAGLKLIASERQRGLPRELYPVRMYALK 228
Cdd:pfam05891 156 FIVVKENVTQNGFDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 47-169 2.38e-06

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: 45.39  E-value: 2.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738   47 NNFLRKLKSRMLPQENNVkyaVDIGAGIGRVSKtMLHKHAAKIDLVEPVKPFIEQMHVELAELKdkgqiGQIYEVGMQDW 126
Cdd:COG2227  11 DRRLAALLARLLPAGGRV---LDVGCGTGRLAL-ALARRGADVTGVDISPEALEIARERAAELN-----VDFVQGDLEDL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6319738  127 TPDAGKYWLIWCQWCVGHLPDAElvAFLKRCIVGLQPNGTIVV 169
Cdd:COG2227  82 PLEDGSFDLVICSEVLEHLPDPA--ALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 68-170 4.07e-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: 35.87  E-value: 4.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738   68 VDIGAGIGRVSKTMLHKHAAKIDLVEPVKPFIEQMHVELAELKDKGqiGQIYEVGMQDWTPDAGKYW-LIWCQWCVGHLP 146
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN--VEVLKGDAEELPPEADESFdVIISDPPLHHLV 80

                        90       100
                ....*....|....*....|....
gi 6319738  147 DaELVAFLKRCIVGLQPNGTIVVK 170
Cdd:cd02440  81 E-DLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 6-228 5.56e-129

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: 362.85  E-value: 5.56e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738      6 DSHIKYEDAIDYWTDVDATVDGVLGGYGegtVVPTMDVLGSNNFLRKLKSRMLPQENNVKYAVDIGAGIGRVSKTMLHKH 85
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYG---HVSDIDVNGSRNFLRRLLRERLPGKNRHLVALDCGAGIGRVTKNLLLPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738     86 AAKIDLVEPVKPFIEQMHVELAElkDKGQIGQIYEVGMQDWTPDAGKYWLIWCQWCVGHLPDAELVAFLKRCIVGLQPNG 165
Cdd:pfam05891  78 FSKVDLVEPVEDFIEKAKEYLAE--GKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNG 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6319738    166 TIVVKENNTPTDTDDFDETDSSVTRSDAKFRQIFEEAGLKLIASERQRGLPRELYPVRMYALK 228
Cdd:pfam05891 156 FIVVKENVTQNGFDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 69-165 1.19e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 48.33  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738     69 DIGAGIGRVSKTMLHKHAAKIDLVEPVKPFIEQMHvelAELKDKGQIGQIYEVGMQDWTPDAGKYWLIWCQWCVGHLPDA 148
Cdd:pfam13649   3 DLGCGTGRLTLALARRGGARVTGVDLSPEMLERAR---ERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 6319738    149 ELVAFLKRCIVGLQPNG 165
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 47-169 2.38e-06

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: 45.39  E-value: 2.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738   47 NNFLRKLKSRMLPQENNVkyaVDIGAGIGRVSKtMLHKHAAKIDLVEPVKPFIEQMHVELAELKdkgqiGQIYEVGMQDW 126
Cdd:COG2227  11 DRRLAALLARLLPAGGRV---LDVGCGTGRLAL-ALARRGADVTGVDISPEALEIARERAAELN-----VDFVQGDLEDL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6319738  127 TPDAGKYWLIWCQWCVGHLPDAElvAFLKRCIVGLQPNGTIVV 169
Cdd:COG2227  82 PLEDGSFDLVICSEVLEHLPDPA--ALLRELARLLKPGGLLLL 122
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-208 8.35e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.64  E-value: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738     48 NFLRKLKSRMLPQENNVKYAVDIGAGIGRVSKTMlHKHAAKIDLVEPVkpfieqmhVELAELKDKGQIGQIYEVgmQDWT 127
Cdd:pfam13489   7 RLLADLLLRLLPKLPSPGRVLDFGCGTGIFLRLL-RAQGFSVTGVDPS--------PIAIERALLNVRFDQFDE--QEAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738    128 PDAGKYWLIWCQWCVGHLPD-AELVAFLKRCivgLQPNGTIVVKENNTPTDTDDFDET----------DSSVTRSDakFR 196
Cdd:pfam13489  76 VPAGKFDVIVAREVLEHVPDpPALLRQIAAL---LKPGGLLLLSTPLASDEADRLLLEwpylrprnghISLFSARS--LK 150

                         170
                  ....*....|..
gi 6319738    197 QIFEEAGLKLIA 208
Cdd:pfam13489 151 RLLEEAGFEVVS 162
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
67-169 5.65e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 38.27  E-value: 5.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738   67 AVDIGAGIGRVSKTMLHKH-AAKIDLVEPVKPFIEQMHVELAELKdkgqigqiYEVG-MQDWTPDaGKYWLIWCQWCVGH 144
Cdd:COG4106   5 VLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLPNVR--------FVVAdLRDLDPP-EPFDLVVSNAALHW 75

                        90       100
                ....*....|....*....|....*
gi 6319738  145 LPDaeLVAFLKRCIVGLQPNGTIVV 169
Cdd:COG4106  76 LPD--HAALLARLAAALAPGGVLAV 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 68-170 4.07e-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: 35.87  E-value: 4.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319738   68 VDIGAGIGRVSKTMLHKHAAKIDLVEPVKPFIEQMHVELAELKDKGqiGQIYEVGMQDWTPDAGKYW-LIWCQWCVGHLP 146
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN--VEVLKGDAEELPPEADESFdVIISDPPLHHLV 80

                        90       100
                ....*....|....*....|....
gi 6319738  147 DaELVAFLKRCIVGLQPNGTIVVK 170
Cdd:cd02440  81 E-DLARFLEEARRLLKPGGVLVLT 103
 
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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