Methyltransferase family protein [Arabidopsis thaliana]
class I SAM-dependent methyltransferase( domain architecture ID 18294757)
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; Drosophila melanogaster tRNA N(3)-methylcytidine methyltransferase Mettl2
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
107-230 | 2.76e-14 | |||
Methyltransferase domain; This family appears to be a methyltransferase domain. : Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 67.59 E-value: 2.76e-14
|
|||||||
COG4627 super family | cl44094 | Predicted SAM-depedendent methyltransferase [General function prediction only]; |
210-278 | 2.90e-03 | |||
Predicted SAM-depedendent methyltransferase [General function prediction only]; The actual alignment was detected with superfamily member COG4627: Pssm-ID: 443666 [Multi-domain] Cd Length: 161 Bit Score: 37.92 E-value: 2.90e-03
|
|||||||
Name | Accession | Description | Interval | E-value | ||||
Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
107-230 | 2.76e-14 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 67.59 E-value: 2.76e-14
|
||||||||
UbiE | COG2226 | Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
87-256 | 6.55e-14 | ||||
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: 67.71 E-value: 6.55e-14
|
||||||||
AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
105-234 | 1.75e-08 | ||||
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: 51.66 E-value: 1.75e-08
|
||||||||
COG4627 | COG4627 | Predicted SAM-depedendent methyltransferase [General function prediction only]; |
210-278 | 2.90e-03 | ||||
Predicted SAM-depedendent methyltransferase [General function prediction only]; Pssm-ID: 443666 [Multi-domain] Cd Length: 161 Bit Score: 37.92 E-value: 2.90e-03
|
||||||||
hemK_fam | TIGR00536 | HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
92-148 | 5.28e-03 | ||||
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair] Pssm-ID: 273125 [Multi-domain] Cd Length: 284 Bit Score: 38.10 E-value: 5.28e-03
|
||||||||
Name | Accession | Description | Interval | E-value | ||||
Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
107-230 | 2.76e-14 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 67.59 E-value: 2.76e-14
|
||||||||
UbiE | COG2226 | Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
87-256 | 6.55e-14 | ||||
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: 67.71 E-value: 6.55e-14
|
||||||||
SmtA | COG0500 | SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
70-274 | 2.95e-12 | ||||
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]; Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 64.55 E-value: 2.95e-12
|
||||||||
Methyltransf_12 | pfam08242 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
107-232 | 6.58e-11 | ||||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 58.15 E-value: 6.58e-11
|
||||||||
UbiG | COG2227 | 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
100-237 | 1.53e-09 | ||||
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: 55.02 E-value: 1.53e-09
|
||||||||
Methyltransf_11 | pfam08241 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
107-234 | 4.73e-09 | ||||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 52.67 E-value: 4.73e-09
|
||||||||
AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
105-234 | 1.75e-08 | ||||
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: 51.66 E-value: 1.75e-08
|
||||||||
Cfa | COG2230 | Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
71-236 | 1.70e-07 | ||||
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism]; Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 49.93 E-value: 1.70e-07
|
||||||||
Methyltransf_23 | pfam13489 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
83-283 | 1.73e-05 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 44.34 E-value: 1.73e-05
|
||||||||
Tam | COG4106 | Trans-aconitate methyltransferase [Energy production and conversion]; |
102-234 | 1.12e-04 | ||||
Trans-aconitate methyltransferase [Energy production and conversion]; Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 40.58 E-value: 1.12e-04
|
||||||||
RsmC | COG2813 | 16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
88-234 | 1.07e-03 | ||||
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification Pssm-ID: 442062 [Multi-domain] Cd Length: 191 Bit Score: 39.40 E-value: 1.07e-03
|
||||||||
COG4627 | COG4627 | Predicted SAM-depedendent methyltransferase [General function prediction only]; |
210-278 | 2.90e-03 | ||||
Predicted SAM-depedendent methyltransferase [General function prediction only]; Pssm-ID: 443666 [Multi-domain] Cd Length: 161 Bit Score: 37.92 E-value: 2.90e-03
|
||||||||
hemK_fam | TIGR00536 | HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
92-148 | 5.28e-03 | ||||
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair] Pssm-ID: 273125 [Multi-domain] Cd Length: 284 Bit Score: 38.10 E-value: 5.28e-03
|
||||||||
HemK | COG2890 | Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
96-148 | 6.79e-03 | ||||
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis]; Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 37.44 E-value: 6.79e-03
|
||||||||
Blast search parameters | ||||
|