N-terminal Xaa-Pro-Lys N-methyltransferase 1 isoform a [Homo sapiens]
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
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 ... |
8-223 | 4.70e-135 | ||||
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 characteristic GxGxG motif. : Pssm-ID: 283530 Cd Length: 217 Bit Score: 377.87 E-value: 4.70e-135
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Name | Accession | Description | Interval | E-value | ||||
Methyltransf_PK | pfam05891 | AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ... |
8-223 | 4.70e-135 | ||||
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 characteristic GxGxG motif. Pssm-ID: 283530 Cd Length: 217 Bit Score: 377.87 E-value: 4.70e-135
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
66-166 | 3.55e-11 | ||||
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: 58.21 E-value: 3.55e-11
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UbiG | COG2227 | 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
41-165 | 2.45e-08 | ||||
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; Pssm-ID: 225137 [Multi-domain] Cd Length: 243 Bit Score: 52.72 E-value: 2.45e-08
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PTZ00098 | PTZ00098 | phosphoethanolamine N-methyltransferase; Provisional |
33-172 | 6.05e-04 | ||||
phosphoethanolamine N-methyltransferase; Provisional Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 39.95 E-value: 6.05e-04
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Name | Accession | Description | Interval | E-value | ||||
Methyltransf_PK | pfam05891 | AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ... |
8-223 | 4.70e-135 | ||||
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 characteristic GxGxG motif. Pssm-ID: 283530 Cd Length: 217 Bit Score: 377.87 E-value: 4.70e-135
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Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
66-161 | 6.64e-18 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 433377 [Multi-domain] Cd Length: 97 Bit Score: 75.69 E-value: 6.64e-18
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Methyltransf_11 | pfam08241 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
66-165 | 5.26e-12 | ||||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 429883 [Multi-domain] Cd Length: 94 Bit Score: 59.99 E-value: 5.26e-12
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
66-166 | 3.55e-11 | ||||
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: 58.21 E-value: 3.55e-11
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Methyltransf_12 | pfam08242 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
66-163 | 2.28e-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: 2.28e-10
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UbiG | COG2227 | 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
41-165 | 2.45e-08 | ||||
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; Pssm-ID: 225137 [Multi-domain] Cd Length: 243 Bit Score: 52.72 E-value: 2.45e-08
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Methyltransf_31 | pfam13847 | Methyltransferase domain; This family appears to have methyltransferase activity. |
66-200 | 2.95e-04 | ||||
Methyltransferase domain; This family appears to have methyltransferase activity. Pssm-ID: 433524 [Multi-domain] Cd Length: 150 Bit Score: 39.70 E-value: 2.95e-04
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PTZ00098 | PTZ00098 | phosphoethanolamine N-methyltransferase; Provisional |
33-172 | 6.05e-04 | ||||
phosphoethanolamine N-methyltransferase; Provisional Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 39.95 E-value: 6.05e-04
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UbiE | COG2226 | Ubiquinone/menaquinone biosynthesis C-methylase UbiE [Coenzyme transport and metabolism]; |
46-165 | 6.14e-04 | ||||
Ubiquinone/menaquinone biosynthesis C-methylase UbiE [Coenzyme transport and metabolism]; Pssm-ID: 225136 [Multi-domain] Cd Length: 238 Bit Score: 39.55 E-value: 6.14e-04
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SmtA | COG0500 | SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
61-216 | 6.19e-04 | ||||
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]; Pssm-ID: 223574 [Multi-domain] Cd Length: 257 Bit Score: 39.88 E-value: 6.19e-04
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COG4798 | COG4798 | Predicted methyltransferase [General function prediction only]; |
146-220 | 7.81e-04 | ||||
Predicted methyltransferase [General function prediction only]; Pssm-ID: 227135 Cd Length: 238 Bit Score: 39.44 E-value: 7.81e-04
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SpeE | COG0421 | Spermidine synthase [Amino acid transport and metabolism]; |
69-165 | 8.85e-04 | ||||
Spermidine synthase [Amino acid transport and metabolism]; Pssm-ID: 223498 [Multi-domain] Cd Length: 282 Bit Score: 39.28 E-value: 8.85e-04
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PRK00811 | PRK00811 | polyamine aminopropyltransferase; |
86-164 | 3.45e-03 | ||||
polyamine aminopropyltransferase; Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 37.44 E-value: 3.45e-03
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Ubie_methyltran | pfam01209 | ubiE/COQ5 methyltransferase family; |
59-165 | 7.10e-03 | ||||
ubiE/COQ5 methyltransferase family; Pssm-ID: 395966 [Multi-domain] Cd Length: 228 Bit Score: 36.26 E-value: 7.10e-03
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YrrM | COG4122 | Predicted O-methyltransferase YrrM [General function prediction only]; |
65-178 | 8.92e-03 | ||||
Predicted O-methyltransferase YrrM [General function prediction only]; Pssm-ID: 226607 [Multi-domain] Cd Length: 219 Bit Score: 36.15 E-value: 8.92e-03
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Blast search parameters | ||||
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