cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 [Homo sapiens]
Protein Classification
cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1( domain architecture ID 10482031)
cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 is a class I SAM-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| FtsJ | pfam01728 | FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
232-448 | 1.12e-35 | ||||
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping. : Pssm-ID: 426399 Cd Length: 179 Bit Score: 133.10 E-value: 1.12e-35
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| G-patch | pfam01585 | G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in ... |
87-129 | 4.11e-13 | ||||
G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines. : Pssm-ID: 396249 [Multi-domain] Cd Length: 45 Bit Score: 64.07 E-value: 4.11e-13
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| Adenylation_DNA_ligase_like super family | cl12015 | Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent ... |
625-716 | 6.80e-04 | ||||
Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent polynucleotide ligases catalyze the phosphodiester bond formation of nicked nucleic acid substrates using ATP as a cofactor in a three step reaction mechanism. This family includes ATP-dependent DNA and RNA ligases. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent DNA ligases have a highly modular architecture, consisting of a unique arrangement of two or more discrete domains, including a DNA-binding domain, an adenylation or nucleotidyltransferase (NTase) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation domain binds ATP and contains many active site residues. Together with the C-terminal OB-fold domain, it comprises a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases including eukaryotic GRP-dependent mRNA-capping enzymes. The catalytic core contains both the active site as well as many DNA-binding residues. The RNA circularization protein from archaea and bacteria contains the minimal catalytic unit, the adenylation domain, but does not contain an OB-fold domain. This family also includes the m3G-cap binding domain of snurportin, a nuclear import adaptor that binds m3G-capped spliceosomal U small nucleoproteins (snRNPs), but doesn't have enzymatic activity. The actual alignment was detected with superfamily member cd07895: Pssm-ID: 448381 [Multi-domain] Cd Length: 215 Bit Score: 41.85 E-value: 6.80e-04
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| Name | Accession | Description | Interval | E-value | ||||
| FtsJ | pfam01728 | FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
232-448 | 1.12e-35 | ||||
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping. Pssm-ID: 426399 Cd Length: 179 Bit Score: 133.10 E-value: 1.12e-35
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| G-patch | pfam01585 | G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in ... |
87-129 | 4.11e-13 | ||||
G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines. Pssm-ID: 396249 [Multi-domain] Cd Length: 45 Bit Score: 64.07 E-value: 4.11e-13
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| G_patch | smart00443 | glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in ... |
87-129 | 1.20e-11 | ||||
glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins. Pssm-ID: 197727 [Multi-domain] Cd Length: 47 Bit Score: 59.87 E-value: 1.20e-11
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| RlmE | COG0293 | 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ... |
390-450 | 3.87e-06 | ||||
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification Pssm-ID: 440062 [Multi-domain] Cd Length: 208 Bit Score: 48.53 E-value: 3.87e-06
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| Adenylation_mRNA_capping | cd07895 | Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ... |
625-716 | 6.80e-04 | ||||
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP from GTP to the 5'-diphosphate end of nascent mRNAs to form a G(5')ppp(5')RNA cap structure. The RNA cap is found only in eukarya. RNA capping is chemically analogous to the first two steps of polynucleotide ligation. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation of nicked nucleic acid substrates using the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. Structural studies reveal a shared structure for DNA ligases and capping enzymes, with a common catalytic core composed of an adenylation or nucleotidyltransferase domain and a C-terminal OB-fold domain containing conserved sequence motifs. The adenylation domain binds ATP and contains many active site residues. Pssm-ID: 185706 [Multi-domain] Cd Length: 215 Bit Score: 41.85 E-value: 6.80e-04
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| Name | Accession | Description | Interval | E-value | ||||
| FtsJ | pfam01728 | FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
232-448 | 1.12e-35 | ||||
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping. Pssm-ID: 426399 Cd Length: 179 Bit Score: 133.10 E-value: 1.12e-35
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| G-patch | pfam01585 | G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in ... |
87-129 | 4.11e-13 | ||||
G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines. Pssm-ID: 396249 [Multi-domain] Cd Length: 45 Bit Score: 64.07 E-value: 4.11e-13
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| G_patch | smart00443 | glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in ... |
87-129 | 1.20e-11 | ||||
glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins. Pssm-ID: 197727 [Multi-domain] Cd Length: 47 Bit Score: 59.87 E-value: 1.20e-11
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| RlmE | COG0293 | 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ... |
390-450 | 3.87e-06 | ||||
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification Pssm-ID: 440062 [Multi-domain] Cd Length: 208 Bit Score: 48.53 E-value: 3.87e-06
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| Adenylation_mRNA_capping | cd07895 | Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ... |
625-716 | 6.80e-04 | ||||
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP from GTP to the 5'-diphosphate end of nascent mRNAs to form a G(5')ppp(5')RNA cap structure. The RNA cap is found only in eukarya. RNA capping is chemically analogous to the first two steps of polynucleotide ligation. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation of nicked nucleic acid substrates using the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. Structural studies reveal a shared structure for DNA ligases and capping enzymes, with a common catalytic core composed of an adenylation or nucleotidyltransferase domain and a C-terminal OB-fold domain containing conserved sequence motifs. The adenylation domain binds ATP and contains many active site residues. Pssm-ID: 185706 [Multi-domain] Cd Length: 215 Bit Score: 41.85 E-value: 6.80e-04
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| G-patch_2 | pfam12656 | G-patch domain; Yeast Spp2, a G-patch protein and spliceosome component, interacts with the ... |
94-129 | 3.31e-03 | ||||
G-patch domain; Yeast Spp2, a G-patch protein and spliceosome component, interacts with the ATP-dependent DExH-box splicing factor Prp2. As this interaction involves the G-patch sequence in Spp2 and is required for the recruitment of Prp2 to the spliceosome before the first catalytic step of splicing, it is proposed that Spp2 might be an accessory factor that confers spliceosome specificity on Prp2. Pssm-ID: 432700 [Multi-domain] Cd Length: 61 Bit Score: 36.49 E-value: 3.31e-03
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| Blast search parameters | ||||
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