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Conserved domains on  [gi|2306699122|ref|WP_260856127|]
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tRNA (adenine(22)-N(1))-methyltransferase TrmK [Bacillus licheniformis]

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 ...
1-213 1.42e-89

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: 262.80  E-value: 1.42e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306699122   1 MADIGSDHAYLPCYCVLNRLASAAIAGEITDGPFLSAKQQVEKLQLSSLISVRKGDGLEVIEKGEADVITIAGMGGSLIA 80
Cdd:COG2384    19 VADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDGLEVLEPGEVDTIVIAGMGGELIA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306699122  81 HILKTGKDKLSGKERLVLQPNIHAQHIREWLYLEGYALINEEILEEDGKYYEVLVAEAGDRDAAYDGVSFaagmLVGPFL 160
Cdd:COG2384    99 DILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEELVEEDGKIYEIIVAEPGEEKLELSELEL----EFGPLL 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2306699122 161 VKEQNDVFIKKWSQELKHTENIYRQIEAApPSEENRQKLLELSERIEILKEVL 213
Cdd:COG2384   175 LEEKNPLLKEYLEREIEKYQRILEQLEKS-KTEEAAEKIEELEKKIKAIEEVL 226
 
Name Accession Description Interval E-value
TrmK COG2384
tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase ...
1-213 1.42e-89

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: 262.80  E-value: 1.42e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306699122   1 MADIGSDHAYLPCYCVLNRLASAAIAGEITDGPFLSAKQQVEKLQLSSLISVRKGDGLEVIEKGEADVITIAGMGGSLIA 80
Cdd:COG2384    19 VADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDGLEVLEPGEVDTIVIAGMGGELIA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306699122  81 HILKTGKDKLSGKERLVLQPNIHAQHIREWLYLEGYALINEEILEEDGKYYEVLVAEAGDRDAAYDGVSFaagmLVGPFL 160
Cdd:COG2384    99 DILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEELVEEDGKIYEIIVAEPGEEKLELSELEL----EFGPLL 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2306699122 161 VKEQNDVFIKKWSQELKHTENIYRQIEAApPSEENRQKLLELSERIEILKEVL 213
Cdd:COG2384   175 LEEKNPLLKEYLEREIEKYQRILEQLEKS-KTEEAAEKIEELEKKIKAIEEVL 226
TrmK pfam04816
tRNA (adenine(22)-N(1))-methyltransferase; tRNA_MT is a family of bacterial tRNA (adenine(22) ...
1-211 5.99e-87

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: 255.32  E-value: 5.99e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306699122   1 MADIGSDHAYLPCYCVLNRLASAAIAGEITDGPFLSAKQQVEKLQLSSLISVRKGDGLEVIEKGE-ADVITIAGMGGSLI 79
Cdd:pfam04816   1 LADIGSDHAYLPIYLVQNNLASFAIAGEVNAGPLQSAVNNVAKSGLTERIDVRLGDGLAVIELEDvIDVIVIAGMGGTLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306699122  80 AHILKTGKDKLSGKERLVLQPNIHAQHIREWLYLEGYALINEEILEEDGKYYEVLVAEAGDRDAAYdgvSFAAGMLVGPF 159
Cdd:pfam04816  81 REILEEGKDKLAGVKRLILQPNINPEDLREWLSANSYQIKAERILEEDGKIYEILVVEKGKKPDAK---LSEADLRFGPF 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2306699122 160 LVKEQNDVFIKKWSQELKHTENIYRQIeaapPSEENRQKLLELSERIEILKE 211
Cdd:pfam04816 158 LLKEKSALFKKKWQKELEKLKKILAQL----SSENAEAELAELSEKIEVIKE 205
 
Name Accession Description Interval E-value
TrmK COG2384
tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase ...
1-213 1.42e-89

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: 262.80  E-value: 1.42e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306699122   1 MADIGSDHAYLPCYCVLNRLASAAIAGEITDGPFLSAKQQVEKLQLSSLISVRKGDGLEVIEKGEADVITIAGMGGSLIA 80
Cdd:COG2384    19 VADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDGLEVLEPGEVDTIVIAGMGGELIA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306699122  81 HILKTGKDKLSGKERLVLQPNIHAQHIREWLYLEGYALINEEILEEDGKYYEVLVAEAGDRDAAYDGVSFaagmLVGPFL 160
Cdd:COG2384    99 DILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEELVEEDGKIYEIIVAEPGEEKLELSELEL----EFGPLL 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2306699122 161 VKEQNDVFIKKWSQELKHTENIYRQIEAApPSEENRQKLLELSERIEILKEVL 213
Cdd:COG2384   175 LEEKNPLLKEYLEREIEKYQRILEQLEKS-KTEEAAEKIEELEKKIKAIEEVL 226
TrmK pfam04816
tRNA (adenine(22)-N(1))-methyltransferase; tRNA_MT is a family of bacterial tRNA (adenine(22) ...
1-211 5.99e-87

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: 255.32  E-value: 5.99e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306699122   1 MADIGSDHAYLPCYCVLNRLASAAIAGEITDGPFLSAKQQVEKLQLSSLISVRKGDGLEVIEKGE-ADVITIAGMGGSLI 79
Cdd:pfam04816   1 LADIGSDHAYLPIYLVQNNLASFAIAGEVNAGPLQSAVNNVAKSGLTERIDVRLGDGLAVIELEDvIDVIVIAGMGGTLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306699122  80 AHILKTGKDKLSGKERLVLQPNIHAQHIREWLYLEGYALINEEILEEDGKYYEVLVAEAGDRDAAYdgvSFAAGMLVGPF 159
Cdd:pfam04816  81 REILEEGKDKLAGVKRLILQPNINPEDLREWLSANSYQIKAERILEEDGKIYEILVVEKGKKPDAK---LSEADLRFGPF 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2306699122 160 LVKEQNDVFIKKWSQELKHTENIYRQIeaapPSEENRQKLLELSERIEILKE 211
Cdd:pfam04816 158 LLKEKSALFKKKWQKELEKLKKILAQL----SSENAEAELAELSEKIEVIKE 205
Methyltransf_18 pfam12847
Methyltransferase domain; Protein in this family function as methyltransferases.
1-134 1.12e-63

Methyltransferase domain; Protein in this family function as methyltransferases.


Pssm-ID: 463730  Cd Length: 151  Bit Score: 194.19  E-value: 1.12e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306699122   1 MADIGSDHAYLPCYCVLNRLASAAIAGEITDGPFLSAKQQVEKLQLSSLISVRKGDGLEVIEKGEADVITIAGMGGSLIA 80
Cdd:pfam12847  18 VADIGTDHAYLPIYLVKNGIAPKAIASDINEGPLEKARENIEKYGLEDRIEVRLGDGLEVLEPGEVDTIVIAGMGGELII 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2306699122  81 HILKTGKDKLSGKERLVLQPNIHAQHIREWLYLEGYALINEEILEEDGKYYEVL 134
Cdd:pfam12847  98 DILEAGPEVLKSVKRLILQPQSDIEELRRWLYENGFEIIDEKLVEEDGKYYEII 151
 
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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