7SK snRNA methylphosphate capping enzyme isoform B [Homo sapiens]
Bin3 domain-containing protein( domain architecture ID 10536334)
Bin3 domain-containing protein is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Danio rerio pre-miRNA 5'-monophosphate methyltransferase\tthat specifically monomethylates 5'-monophosphate of cytoplasmic histidyl tRNA (tRNA(His))
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Bin3 | pfam06859 | Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ... |
106-214 | 1.89e-69 | |||
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif. : Pssm-ID: 462022 Cd Length: 109 Bit Score: 207.78 E-value: 1.89e-69
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Bin3 | pfam06859 | Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ... |
106-214 | 1.89e-69 | |||
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif. Pssm-ID: 462022 Cd Length: 109 Bit Score: 207.78 E-value: 1.89e-69
|
|||||||
AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
80-147 | 1.95e-05 | |||
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: 42.42 E-value: 1.95e-05
|
|||||||
Cfa | COG2230 | Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
82-146 | 1.51e-04 | |||
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism]; Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 40.68 E-value: 1.51e-04
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Bin3 | pfam06859 | Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ... |
106-214 | 1.89e-69 | |||
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif. Pssm-ID: 462022 Cd Length: 109 Bit Score: 207.78 E-value: 1.89e-69
|
|||||||
AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
80-147 | 1.95e-05 | |||
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: 42.42 E-value: 1.95e-05
|
|||||||
Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
106-142 | 1.32e-04 | |||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 39.85 E-value: 1.32e-04
|
|||||||
Cfa | COG2230 | Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
82-146 | 1.51e-04 | |||
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism]; Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 40.68 E-value: 1.51e-04
|
|||||||
Tam | COG4106 | Trans-aconitate methyltransferase [Energy production and conversion]; |
83-147 | 2.13e-04 | |||
Trans-aconitate methyltransferase [Energy production and conversion]; Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 39.04 E-value: 2.13e-04
|
|||||||
COG4976 | COG4976 | Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
93-146 | 1.12e-03 | |||
Predicted methyltransferase, contains TPR repeat [General function prediction only]; Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 38.44 E-value: 1.12e-03
|
|||||||
SmtA | COG0500 | SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
82-148 | 1.22e-03 | |||
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]; Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 38.74 E-value: 1.22e-03
|
|||||||
Methyltransf_12 | pfam08242 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
81-144 | 3.11e-03 | |||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 35.81 E-value: 3.11e-03
|
|||||||
UbiG | COG2227 | 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
97-147 | 3.62e-03 | |||
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: 36.15 E-value: 3.62e-03
|
|||||||
UbiE | COG2226 | Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
106-146 | 6.98e-03 | |||
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: 35.74 E-value: 6.98e-03
|
|||||||
Methyltransf_2 | pfam00891 | O-methyltransferase domain; This family includes a range of O-methyltransferases. These ... |
66-147 | 7.50e-03 | |||
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: 36.23 E-value: 7.50e-03
|
|||||||
Blast search parameters | ||||
|