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Conserved domains on  [gi|1958762807|ref|XP_038961301|]
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N-terminal Xaa-Pro-Lys N-methyltransferase 1 isoform X5 [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 ...
 26-193 2.17e-101

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: 291.59  E-value: 2.17e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  26 GPNKTGTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPSSYDVIWIQ 105
Cdd:pfam05891  50 LPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807 106 WVIGHLTDQHLAEFLRRCRRGLRPNGIIVIKDNMAQEGV-ILDDVDSSVCRDLEVVRRIIRSAGLSLLAEERQENLPDEI 184
Cdd:pfam05891 130 WCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQEL 209


                  ....*....
gi 1958762807 185 YHVYSFALR 193
Cdd:pfam05891 210 YPVKMYALK 218
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 26-193 2.17e-101

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: 291.59  E-value: 2.17e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  26 GPNKTGTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPSSYDVIWIQ 105
Cdd:pfam05891  50 LPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807 106 WVIGHLTDQHLAEFLRRCRRGLRPNGIIVIKDNMAQEGV-ILDDVDSSVCRDLEVVRRIIRSAGLSLLAEERQENLPDEI 184
Cdd:pfam05891 130 WCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQEL 209


                  ....*....
gi 1958762807 185 YHVYSFALR 193
Cdd:pfam05891 210 YPVKMYALK 218
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 35-135 3.28e-15

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: 68.51  E-value: 3.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  35 ALDCGAGIGRITKRLLLPLFRVVdMVDVTEDFLAKAKTYLGEEGKRvrnYFCCGLQDFSPEPSSYDVIWIQWVIGHLTDq 114
Cdd:COG2227    28 VLDVGCGTGRLALALARRGADVT-GVDISPEALEIARERAAELNVD---FVQGDLEDLPLEDGSFDLVICSEVLEHLPD- 102

                          90       100
                  ....*....|....*....|.
gi 1958762807 115 hLAEFLRRCRRGLRPNGIIVI 135
Cdd:COG2227   103 -PAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 36-136 5.95e-12

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: 59.37  E-value: 5.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  36 LDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSP-EPSSYDVIWIQWVIGHLtDQ 114
Cdd:cd02440     3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL-VE 81

                          90       100
                  ....*....|....*....|..
gi 1958762807 115 HLAEFLRRCRRGLRPNGIIVIK 136
Cdd:cd02440    82 DLARFLEEARRLLKPGGVLVLT 103
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 33-142 1.48e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 38.41  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  33 SCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFsPEpSSYDVIWIQWVIGHLT 112
Cdd:PTZ00098   54 SKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKDF-PE-NTFDMIYSRDAILHLS 131

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958762807 113 DQHLAEFLRRCRRGLRPNGIIVIKDNMAQE 142
Cdd:PTZ00098  132 YADKKKLFEKCYKWLKPNGILLITDYCADK 161
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 26-193 2.17e-101

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: 291.59  E-value: 2.17e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  26 GPNKTGTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPSSYDVIWIQ 105
Cdd:pfam05891  50 LPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807 106 WVIGHLTDQHLAEFLRRCRRGLRPNGIIVIKDNMAQEGV-ILDDVDSSVCRDLEVVRRIIRSAGLSLLAEERQENLPDEI 184
Cdd:pfam05891 130 WCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQEL 209


                  ....*....
gi 1958762807 185 YHVYSFALR 193
Cdd:pfam05891 210 YPVKMYALK 218
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 36-131 1.85e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 78.76  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  36 LDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRnYFCCGLQDFSPEPSSYDVIWIQWVIGHLTDQH 115
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVE-FVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 1958762807 116 LAEFLRRCRRGLRPNG 131
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 35-135 3.28e-15

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: 68.51  E-value: 3.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  35 ALDCGAGIGRITKRLLLPLFRVVdMVDVTEDFLAKAKTYLGEEGKRvrnYFCCGLQDFSPEPSSYDVIWIQWVIGHLTDq 114
Cdd:COG2227    28 VLDVGCGTGRLALALARRGADVT-GVDISPEALEIARERAAELNVD---FVQGDLEDLPLEDGSFDLVICSEVLEHLPD- 102

                          90       100
                  ....*....|....*....|.
gi 1958762807 115 hLAEFLRRCRRGLRPNGIIVI 135
Cdd:COG2227   103 -PAALLRELARLLKPGGLLLL 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 36-170 1.53e-13

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: 64.63  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  36 LDCGAGIGRITKRLLLPLFRVVdMVDVTEDFLAKAKTYLGEEGKRVRnyFCCG-LQDFSPEPSSYDVIWIQWVIGHLTDq 114
Cdd:COG2226    27 LDLGCGTGRLALALAERGARVT-GVDISPEMLELARERAAEAGLNVE--FVVGdAEDLPFPDGSFDLVISSFVLHHLPD- 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958762807 115 hLAEFLRRCRRGLRPNGIIVIKDNMAqegvilddvdssvcRDLEVVRRIIRSAGLS 170
Cdd:COG2226   103 -PERALAEIARVLKPGGRLVVVDFSP--------------PDLAELEELLAEAGFE 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 36-135 5.84e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 61.91  E-value: 5.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  36 LDCGAGIGRITKRLLLPLFRVVDmVDVTEDFLAKAKTYLGEEGKrvrNYFCCGLQDFSPEPSSYDVIWIQWVIGHLTDqh 115
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTG-VDISPEMLELAREKAPREGL---TFVVGDAEDLPFPDNSFDLVLSSEVLHHVED-- 74

                          90       100
                  ....*....|....*....|
gi 1958762807 116 LAEFLRRCRRGLRPNGIIVI 135
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
35-135 2.37e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 62.32  E-value: 2.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  35 ALDCGAGIGRITkRLLLPLFRVVDMVDVTEDFLAKAKTylgeegKRV-RNYFCCGLQDFSPEPSSYDVIWIQWVIGHLTD 113
Cdd:COG4976    50 VLDLGCGTGLLG-EALRPRGYRLTGVDLSEEMLAKARE------KGVyDRLLVADLADLAEPDGRFDLIVAADVLTYLGD 122

                          90       100
                  ....*....|....*....|..
gi 1958762807 114 qhLAEFLRRCRRGLRPNGIIVI 135
Cdd:COG4976   123 --LAAVFAGVARALKPGGLFIF 142
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 36-136 5.95e-12

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: 59.37  E-value: 5.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  36 LDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSP-EPSSYDVIWIQWVIGHLtDQ 114
Cdd:cd02440     3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL-VE 81

                          90       100
                  ....*....|....*....|..
gi 1958762807 115 HLAEFLRRCRRGLRPNGIIVIK 136
Cdd:cd02440    82 DLARFLEEARRLLKPGGVLVLT 103
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
35-135 8.85e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 58.68  E-value: 8.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  35 ALDCGAGIGRITKRLL--LPLFRVVdMVDVTEDFLAKAKTYLGeegkRVRnyFCCG-LQDFSPEPsSYDVIWIQWVIGHL 111
Cdd:COG4106     5 VLDLGCGTGRLTALLAerFPGARVT-GVDLSPEMLARARARLP----NVR--FVVAdLRDLDPPE-PFDLVVSNAALHWL 76

                          90       100
                  ....*....|....*....|....
gi 1958762807 112 TDQhlAEFLRRCRRGLRPNGIIVI 135
Cdd:COG4106    77 PDH--AALLARLAAALAPGGVLAV 98
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 36-133 1.75e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 55.45  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  36 LDCGAGIGRITKRLLLPLFRV-VDMVDVTEDFLAKAKTYLGEEGKRVR---NYFCcgLQDFSPEPSSYDVIWIQWVIGHL 111
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeYTGLDISPAALEAARERLAALGLLNAvrvELFQ--LDLGELDPGSFDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|..
gi 1958762807 112 TDqhLAEFLRRCRRGLRPNGII 133
Cdd:pfam08242  79 AD--PRAVLRNIRRLLKPGGVL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 31-144 1.13e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.91  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  31 GTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEG-KRVRnYFCCGLQDFSPEPS-SYDVIWIQWVI 108
Cdd:COG0500    26 KGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGlGNVE-FLVADLAELDPLPAeSFDLVVAFGVL 104

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958762807 109 GHLTDQHLAEFLRRCRRGLRPNGIIVIKDNMAQEGV 144
Cdd:COG0500   105 HHLPPEEREALLRELARALKPGGVLLLSASDAAAAL 140
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 36-135 1.60e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 46.08  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  36 LDCGAGIGRITKRLLlPLFRV-VDMVDVTEDFLAKAKTYLGEEG--KRVRnYFCCGLQDFsPEPSSYDVIWIQWVIGHLT 112
Cdd:COG2230    56 LDIGCGWGGLALYLA-RRYGVrVTGVTLSPEQLEYARERAAEAGlaDRVE-VRLADYRDL-PADGQFDAIVSIGMFEHVG 132

                          90       100
                  ....*....|....*....|...
gi 1958762807 113 DQHLAEFLRRCRRGLRPNGIIVI 135
Cdd:COG2230   133 PENYPAYFAKVARLLKPGGRLLL 155
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
39-135 2.41e-04

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 40.20  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  39 GAGIGRITKRLL-LPLFRVVDMVDVTEDFLAKAKTYLGE-----EGKRVRNYFCCGLQDFSPEPSSYDVIwiqwvIGHLT 112
Cdd:COG0421    45 GGGDGGLARELLkHPPVERVDVVEIDPEVVELAREYFPLlapafDDPRLRVVIGDGRAFLREAEESYDVI-----IVDLT 119

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958762807 113 D-----QHL--AEFLRRCRRGLRPNGIIVI 135
Cdd:COG0421   120 DpvgpaEGLftREFYEDCRRALKPGGVLVV 149
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 36-163 3.41e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.32  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  36 LDCGAGIGRITKRLLLPLFRVVDMV--DVTEDFLAKAKTYLGEEG-KRVRnyFCcgLQDFSPEPS-----SYDVIWIQWV 107
Cdd:pfam13847   8 LDLGCGTGHLSFELAEELGPNAEVVgiDISEEAIEKARENAQKLGfDNVE--FE--QGDIEELPElleddKFDVVISNCV 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958762807 108 IGHLTDQhlAEFLRRCRRGLRPNGIIVIkdnmaQEGVILDDVDSSVCRDLEVVRRI 163
Cdd:pfam13847  84 LNHIPDP--DKVLQEILRVLKPGGRLII-----SDPDSLAELPAHVKEDSTYYAGC 132
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 37-143 5.19e-04

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: 39.31  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  37 DCGAGIGRITKRL--LLPLFR--VVDMVDVtedfLAKAKTYLgEEGKRVRNYFCCGlqDFSPEP-SSYDVIWIQWVIGHL 111
Cdd:pfam00891  66 DVGGGTGALAQAIvsLYPGCKgiVFDLPHV----VEAAPTHF-SAGEEPRVTFHGG--DFFKDSlPEADAYILKRVLHDW 138

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958762807 112 TDQHLAEFLRRCRRGLRPNGIIVIKDNMAQEG 143
Cdd:pfam00891 139 SDEKCVKLLKRCYKACPAGGKVILVESLLGAD 170
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
23-135 7.86e-04

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 38.96  E-value: 7.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  23 CSGGpnKTGTScALDCGAGIGRITKRLLL---PLFRVVdMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPSSY 99
Cdd:pfam01209  37 CMGV--KRGNK-FLDVAGGTGDWTFGLSDsagSSGKVV-GLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSF 112

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958762807 100 DVIWIQWVIGHLTDQHLAefLRRCRRGLRPNGIIVI 135
Cdd:pfam01209 113 DIVTISFGLRNFPDYLKV--LKEAFRVLKPGGRVVC 146
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 33-142 1.48e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 38.41  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  33 SCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFsPEpSSYDVIWIQWVIGHLT 112
Cdd:PTZ00098   54 SKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKDF-PE-NTFDMIYSRDAILHLS 131

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958762807 113 DQHLAEFLRRCRRGLRPNGIIVIKDNMAQE 142
Cdd:PTZ00098  132 YADKKKLFEKCYKWLKPNGILLITDYCADK 161
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
95-135 2.13e-03

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 37.15  E-value: 2.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958762807  95 EPSSYDVIWIQWVIGHLTDQHLAEFLRRCRRGLRPNGIIVI 135
Cdd:COG4627    43 PDNSVDAIYSSHVLEHLDYEEAPLALKECYRVLKPGGILRI 83
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 36-137 2.70e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 37.81  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  36 LDCGAGIGRITKRLLLPLFRVVDMvDVTEDFLAKAKTYLGEEgKRVRnyFCCG---LQDFSPEPSSYDVIWIQWVIGHLT 112
Cdd:PLN02336   42 LELGAGIGRFTGELAKKAGQVIAL-DFIESVIKKNESINGHY-KNVK--FMCAdvtSPDLNISDGSVDLIFSNWLLMYLS 117

                          90       100
                  ....*....|....*....|....*
gi 1958762807 113 DQHLAEFLRRCRRGLRPNGIIVIKD 137
Cdd:PLN02336  118 DKEVENLAERMVKWLKVGGYIFFRE 142
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 60-147 3.90e-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: 36.32  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  60 VDVTEDFLAKAKTYLGEEG--KRVRnyFCCG-----LQDFSPEPssYDVIWIqwvighltD---QHLAEFLRRCRRGLRP 129
Cdd:COG4122    47 IEIDPERAAIARENFARAGlaDRIR--LILGdalevLPRLADGP--FDLVFI--------DadkSNYPDYLELALPLLRP 114

                          90
                  ....*....|....*...
gi 1958762807 130 NGIIVIkDNMAQEGVILD 147
Cdd:COG4122   115 GGLIVA-DNVLWHGRVAD 131
PRK00811 PRK00811
polyamine aminopropyltransferase;
57-134 3.93e-03

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 37.06  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958762807  57 VDMVDVTEDFLAKAKTYLGE------EGKRVRNYFCCGLQDFSPEPSSYDVIwiqwvIGHLTD-----QHL--AEFLRRC 123
Cdd:PRK00811  103 ITLVEIDERVVEVCRKYLPEiaggayDDPRVELVIGDGIKFVAETENSFDVI-----IVDSTDpvgpaEGLftKEFYENC 177

                          90
                  ....*....|.
gi 1958762807 124 RRGLRPNGIIV 134
Cdd:PRK00811  178 KRALKEDGIFV 188
 
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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