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Conserved domains on  [gi|2550304158|ref|WP_302117231|]
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tRNA (adenine(22)-N(1))-methyltransferase TrmK [Limosilactobacillus caviae]

Protein Classification

tRNA (adenine(22)-N(1))-methyltransferase( domain architecture ID 10006423)

tRNA (adenine(22)-N(1))-methyltransferase catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 22 (m1A22) in tRNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TrmK COG2384
tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase ...
5-232 4.40e-106

tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 441950  Cd Length: 228  Bit Score: 305.56  E-value: 4.40e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550304158   5 HLSARLACVASLVPAGARVADIGSDHAYLPAALVLDGKINFAIAGEVVKGPYENAVHEIKAHQLENKIVPRLADGLAAIR 84
Cdd:COG2384     1 KLSKRLQAIASLVPKGARVADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDGLEVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550304158  85 tADNIDTITIAGMGGSLIASILEKGKDKLKGVKRLVLQPNVGESQLRKWLMDNRYQIMTEKIIEEDNHIYEIIVAEPSIV 164
Cdd:COG2384    81 -PGEVDTIVIAGMGGELIADILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEELVEEDGKIYEIIVAEPGEE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2550304158 165 PFRYSQYELDFGPFLLENKGPVFKKKWQEYIQRETHVIKQMQQAQQPPV-QKINELNQVLLEVKEAIAD 232
Cdd:COG2384   160 KLELSELELEFGPLLLEEKNPLLKEYLEREIEKYQRILEQLEKSKTEEAaEKIEELEKKIKAIEEVLKC 228
 
Name Accession Description Interval E-value
TrmK COG2384
tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase ...
5-232 4.40e-106

tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441950  Cd Length: 228  Bit Score: 305.56  E-value: 4.40e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550304158   5 HLSARLACVASLVPAGARVADIGSDHAYLPAALVLDGKINFAIAGEVVKGPYENAVHEIKAHQLENKIVPRLADGLAAIR 84
Cdd:COG2384     1 KLSKRLQAIASLVPKGARVADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDGLEVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550304158  85 tADNIDTITIAGMGGSLIASILEKGKDKLKGVKRLVLQPNVGESQLRKWLMDNRYQIMTEKIIEEDNHIYEIIVAEPSIV 164
Cdd:COG2384    81 -PGEVDTIVIAGMGGELIADILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEELVEEDGKIYEIIVAEPGEE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2550304158 165 PFRYSQYELDFGPFLLENKGPVFKKKWQEYIQRETHVIKQMQQAQQPPV-QKINELNQVLLEVKEAIAD 232
Cdd:COG2384   160 KLELSELELEFGPLLLEEKNPLLKEYLEREIEKYQRILEQLEKSKTEEAaEKIEELEKKIKAIEEVLKC 228
Methyltransf_18 pfam12847
Methyltransferase domain; Protein in this family function as methyltransferases.
6-157 2.52e-76

Methyltransferase domain; Protein in this family function as methyltransferases.


Pssm-ID: 463730  Cd Length: 151  Bit Score: 227.31  E-value: 2.52e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550304158   6 LSARLACVASLVPAGARVADIGSDHAYLPAALVLDGKINFAIAGEVVKGPYENAVHEIKAHQLENKIVPRLADGLAAIRt 85
Cdd:pfam12847   1 LSKRLQAIASLVPPGSRVADIGTDHAYLPIYLVKNGIAPKAIASDINEGPLEKARENIEKYGLEDRIEVRLGDGLEVLE- 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550304158  86 ADNIDTITIAGMGGSLIASILEKGKDKLKGVKRLVLQPNVGESQLRKWLMDNRYQIMTEKIIEEDNHIYEII 157
Cdd:pfam12847  80 PGEVDTIVIAGMGGELIIDILEAGPEVLKSVKRLILQPQSDIEELRRWLYENGFEIIDEKLVEEDGKYYEII 151
 
Name Accession Description Interval E-value
TrmK COG2384
tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase ...
5-232 4.40e-106

tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441950  Cd Length: 228  Bit Score: 305.56  E-value: 4.40e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550304158   5 HLSARLACVASLVPAGARVADIGSDHAYLPAALVLDGKINFAIAGEVVKGPYENAVHEIKAHQLENKIVPRLADGLAAIR 84
Cdd:COG2384     1 KLSKRLQAIASLVPKGARVADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDGLEVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550304158  85 tADNIDTITIAGMGGSLIASILEKGKDKLKGVKRLVLQPNVGESQLRKWLMDNRYQIMTEKIIEEDNHIYEIIVAEPSIV 164
Cdd:COG2384    81 -PGEVDTIVIAGMGGELIADILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEELVEEDGKIYEIIVAEPGEE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2550304158 165 PFRYSQYELDFGPFLLENKGPVFKKKWQEYIQRETHVIKQMQQAQQPPV-QKINELNQVLLEVKEAIAD 232
Cdd:COG2384   160 KLELSELELEFGPLLLEEKNPLLKEYLEREIEKYQRILEQLEKSKTEEAaEKIEELEKKIKAIEEVLKC 228
Methyltransf_18 pfam12847
Methyltransferase domain; Protein in this family function as methyltransferases.
6-157 2.52e-76

Methyltransferase domain; Protein in this family function as methyltransferases.


Pssm-ID: 463730  Cd Length: 151  Bit Score: 227.31  E-value: 2.52e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550304158   6 LSARLACVASLVPAGARVADIGSDHAYLPAALVLDGKINFAIAGEVVKGPYENAVHEIKAHQLENKIVPRLADGLAAIRt 85
Cdd:pfam12847   1 LSKRLQAIASLVPPGSRVADIGTDHAYLPIYLVKNGIAPKAIASDINEGPLEKARENIEKYGLEDRIEVRLGDGLEVLE- 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550304158  86 ADNIDTITIAGMGGSLIASILEKGKDKLKGVKRLVLQPNVGESQLRKWLMDNRYQIMTEKIIEEDNHIYEII 157
Cdd:pfam12847  80 PGEVDTIVIAGMGGELIIDILEAGPEVLKSVKRLILQPQSDIEELRRWLYENGFEIIDEKLVEEDGKYYEII 151
TrmK pfam04816
tRNA (adenine(22)-N(1))-methyltransferase; tRNA_MT is a family of bacterial tRNA (adenine(22) ...
23-228 1.98e-75

tRNA (adenine(22)-N(1))-methyltransferase; tRNA_MT is a family of bacterial tRNA (adenine(22)-N(1))-methyltransferase enzymes with a Rossmann-like fold. This enzyme carries out the function of N1-adenosine methylation at position 22 of bacterial tRNA.


Pssm-ID: 428139  Cd Length: 205  Bit Score: 226.81  E-value: 1.98e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550304158  23 VADIGSDHAYLPAALVLDGKINFAIAGEVVKGPYENAVHEIKAHQLENKIVPRLADGLAAIRTADNIDTITIAGMGGSLI 102
Cdd:pfam04816   1 LADIGSDHAYLPIYLVQNNLASFAIAGEVNAGPLQSAVNNVAKSGLTERIDVRLGDGLAVIELEDVIDVIVIAGMGGTLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550304158 103 ASILEKGKDKLKGVKRLVLQPNVGESQLRKWLMDNRYQIMTEKIIEEDNHIYEIIVAEPSIVPFRY-SQYELDFGPFLLE 181
Cdd:pfam04816  81 REILEEGKDKLAGVKRLILQPNINPEDLREWLSANSYQIKAERILEEDGKIYEILVVEKGKKPDAKlSEADLRFGPFLLK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2550304158 182 NKGPVFKKKWQEYIQRETHVIKQMQQAQQppVQKINELNQVLLEVKE 228
Cdd:pfam04816 161 EKSALFKKKWQKELEKLKKILAQLSSENA--EAELAELSEKIEVIKE 205
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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