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tRNA (guanine(10)-N2)-methyltransferase homolog isoform c [Homo sapiens]
TRM11 family SAM-dependent methyltransferase( domain architecture ID 11437146)
TRM11 family 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; similar to tRNA (guanine(10)-N2)-methyltransferase
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
Trm11 | COG1041 | tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
134-323 | 1.11e-25 | ||||
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification : Pssm-ID: 440663 [Multi-domain] Cd Length: 172 Bit Score: 101.95 E-value: 1.11e-25
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Name | Accession | Description | Interval | E-value | ||||
Trm11 | COG1041 | tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
134-323 | 1.11e-25 | ||||
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 440663 [Multi-domain] Cd Length: 172 Bit Score: 101.95 E-value: 1.11e-25
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TIGR01177 | TIGR01177 | putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ... |
76-269 | 2.85e-23 | ||||
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved] Pssm-ID: 273486 [Multi-domain] Cd Length: 329 Bit Score: 99.43 E-value: 2.85e-23
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UPF0020 | pfam01170 | Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
127-258 | 4.74e-12 | ||||
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains. Pssm-ID: 395932 [Multi-domain] Cd Length: 184 Bit Score: 64.30 E-value: 4.74e-12
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PRK14968 | PRK14968 | putative methyltransferase; Provisional |
141-248 | 1.67e-06 | ||||
putative methyltransferase; Provisional Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 47.97 E-value: 1.67e-06
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
156-314 | 1.10e-04 | ||||
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: 41.26 E-value: 1.10e-04
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Name | Accession | Description | Interval | E-value | ||||
Trm11 | COG1041 | tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
134-323 | 1.11e-25 | ||||
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 440663 [Multi-domain] Cd Length: 172 Bit Score: 101.95 E-value: 1.11e-25
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TIGR01177 | TIGR01177 | putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ... |
76-269 | 2.85e-23 | ||||
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved] Pssm-ID: 273486 [Multi-domain] Cd Length: 329 Bit Score: 99.43 E-value: 2.85e-23
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UPF0020 | pfam01170 | Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ... |
127-258 | 4.74e-12 | ||||
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains. Pssm-ID: 395932 [Multi-domain] Cd Length: 184 Bit Score: 64.30 E-value: 4.74e-12
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HsdM | COG0286 | Type I restriction-modification system, DNA methylase subunit [Defense mechanisms]; |
151-253 | 1.88e-07 | ||||
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms]; Pssm-ID: 440055 [Multi-domain] Cd Length: 243 Bit Score: 51.73 E-value: 1.88e-07
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PRK14968 | PRK14968 | putative methyltransferase; Provisional |
141-248 | 1.67e-06 | ||||
putative methyltransferase; Provisional Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 47.97 E-value: 1.67e-06
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hemK_rel_arch | TIGR00537 | HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ... |
141-259 | 1.20e-05 | ||||
HemK-related putative methylase; 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. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 129628 [Multi-domain] Cd Length: 179 Bit Score: 45.62 E-value: 1.20e-05
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COG2263 | COG2263 | Predicted RNA methylase [General function prediction only]; |
152-252 | 1.86e-05 | ||||
Predicted RNA methylase [General function prediction only]; Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 45.28 E-value: 1.86e-05
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PrmA | pfam06325 | Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ... |
136-225 | 2.88e-05 | ||||
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences. Pssm-ID: 428888 [Multi-domain] Cd Length: 294 Bit Score: 45.33 E-value: 2.88e-05
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
156-314 | 1.10e-04 | ||||
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: 41.26 E-value: 1.10e-04
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prmA | PRK00517 | 50S ribosomal protein L11 methyltransferase; |
150-197 | 1.37e-04 | ||||
50S ribosomal protein L11 methyltransferase; Pssm-ID: 234786 [Multi-domain] Cd Length: 250 Bit Score: 43.22 E-value: 1.37e-04
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N6_Mtase | pfam02384 | N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against ... |
128-257 | 1.00e-03 | ||||
N-6 DNA Methylase; Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes. Pssm-ID: 426749 [Multi-domain] Cd Length: 310 Bit Score: 40.77 E-value: 1.00e-03
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TrmA | COG2265 | tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
151-269 | 1.59e-03 | ||||
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 441866 [Multi-domain] Cd Length: 377 Bit Score: 40.16 E-value: 1.59e-03
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YhdJ | COG0863 | DNA modification methylase [Replication, recombination and repair]; |
151-183 | 2.90e-03 | ||||
DNA modification methylase [Replication, recombination and repair]; Pssm-ID: 440623 Cd Length: 236 Bit Score: 39.14 E-value: 2.90e-03
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N6_N4_Mtase | pfam01555 | DNA methylase; Members of this family are DNA methylases. The family contains both N-4 ... |
151-183 | 3.34e-03 | ||||
DNA methylase; Members of this family are DNA methylases. The family contains both N-4 cytosine-specific DNA methylases and N-6 Adenine-specific DNA methylases. Pssm-ID: 396230 [Multi-domain] Cd Length: 221 Bit Score: 38.53 E-value: 3.34e-03
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Trm5 | COG2520 | tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ... |
150-252 | 5.90e-03 | ||||
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 442010 [Multi-domain] Cd Length: 333 Bit Score: 38.30 E-value: 5.90e-03
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hydroxyacyl_CoA_DH | cd08254 | 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ... |
148-243 | 6.39e-03 | ||||
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. Pssm-ID: 176216 [Multi-domain] Cd Length: 338 Bit Score: 38.38 E-value: 6.39e-03
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Blast search parameters | ||||
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