NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1125814653|gb|APQ48517|]
View 

SAM-dependent methyltransferase [Bacillus amyloliquefaciens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
5-220 4.99e-98

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: 284.37  E-value: 4.99e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125814653   5 KLSKRLQSVAEYIPPGALVADIGSDHAYLPCYAVLNHLASRAIAGEITDGPFLSAKQQVEKLDLSTLISVRKGDGLSVLE 84
Cdd:COG2384     1 KLSKRLQAIASLVPKGARVADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDGLEVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125814653  85 KGEAGAITIAGMGGALIAHILESGKTKLTGRERLILQPNIHAVHIREWLYQEGYELLDEVILEEDGKCYEILVAETGDRD 164
Cdd:COG2384    81 PGEVDTIVIAGMGGELIADILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEELVEEDGKIYEIIVAEPGEEK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1125814653 165 APYRDLPmaagMLAGPFLLKERNEVFLRKWSQELKHTEQIYEQISRSAKHENHEKI 220
Cdd:COG2384   161 LELSELE----LEFGPLLLEEKNPLLKEYLEREIEKYQRILEQLEKSKTEEAAEKI 212
 
Name Accession Description Interval E-value
TrmK COG2384
tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase ...
5-220 4.99e-98

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: 284.37  E-value: 4.99e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125814653   5 KLSKRLQSVAEYIPPGALVADIGSDHAYLPCYAVLNHLASRAIAGEITDGPFLSAKQQVEKLDLSTLISVRKGDGLSVLE 84
Cdd:COG2384     1 KLSKRLQAIASLVPKGARVADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDGLEVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125814653  85 KGEAGAITIAGMGGALIAHILESGKTKLTGRERLILQPNIHAVHIREWLYQEGYELLDEVILEEDGKCYEILVAETGDRD 164
Cdd:COG2384    81 PGEVDTIVIAGMGGELIADILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEELVEEDGKIYEIIVAEPGEEK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1125814653 165 APYRDLPmaagMLAGPFLLKERNEVFLRKWSQELKHTEQIYEQISRSAKHENHEKI 220
Cdd:COG2384   161 LELSELE----LEFGPLLLEEKNPLLKEYLEREIEKYQRILEQLEKSKTEEAAEKI 212
TrmK pfam04816
tRNA (adenine(22)-N(1))-methyltransferase; tRNA_MT is a family of bacterial tRNA (adenine(22) ...
23-209 4.50e-82

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: 243.38  E-value: 4.50e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125814653  23 VADIGSDHAYLPCYAVLNHLASRAIAGEITDGPFLSAKQQVEKLDLSTLISVRKGDGLSVLEKGE-AGAITIAGMGGALI 101
Cdd:pfam04816   1 LADIGSDHAYLPIYLVQNNLASFAIAGEVNAGPLQSAVNNVAKSGLTERIDVRLGDGLAVIELEDvIDVIVIAGMGGTLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125814653 102 AHILESGKTKLTGRERLILQPNIHAVHIREWLYQEGYELLDEVILEEDGKCYEILVAETGDRDAPYrdlPMAAGMLAGPF 181
Cdd:pfam04816  81 REILEEGKDKLAGVKRLILQPNINPEDLREWLSANSYQIKAERILEEDGKIYEILVVEKGKKPDAK---LSEADLRFGPF 157
                         170       180
                  ....*....|....*....|....*...
gi 1125814653 182 LLKERNEVFLRKWSQELKHTEQIYEQIS 209
Cdd:pfam04816 158 LLKEKSALFKKKWQKELEKLKKILAQLS 185
 
Name Accession Description Interval E-value
TrmK COG2384
tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase ...
5-220 4.99e-98

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: 284.37  E-value: 4.99e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125814653   5 KLSKRLQSVAEYIPPGALVADIGSDHAYLPCYAVLNHLASRAIAGEITDGPFLSAKQQVEKLDLSTLISVRKGDGLSVLE 84
Cdd:COG2384     1 KLSKRLQAIASLVPKGARVADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDGLEVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125814653  85 KGEAGAITIAGMGGALIAHILESGKTKLTGRERLILQPNIHAVHIREWLYQEGYELLDEVILEEDGKCYEILVAETGDRD 164
Cdd:COG2384    81 PGEVDTIVIAGMGGELIADILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEELVEEDGKIYEIIVAEPGEEK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1125814653 165 APYRDLPmaagMLAGPFLLKERNEVFLRKWSQELKHTEQIYEQISRSAKHENHEKI 220
Cdd:COG2384   161 LELSELE----LEFGPLLLEEKNPLLKEYLEREIEKYQRILEQLEKSKTEEAAEKI 212
TrmK pfam04816
tRNA (adenine(22)-N(1))-methyltransferase; tRNA_MT is a family of bacterial tRNA (adenine(22) ...
23-209 4.50e-82

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: 243.38  E-value: 4.50e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125814653  23 VADIGSDHAYLPCYAVLNHLASRAIAGEITDGPFLSAKQQVEKLDLSTLISVRKGDGLSVLEKGE-AGAITIAGMGGALI 101
Cdd:pfam04816   1 LADIGSDHAYLPIYLVQNNLASFAIAGEVNAGPLQSAVNNVAKSGLTERIDVRLGDGLAVIELEDvIDVIVIAGMGGTLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125814653 102 AHILESGKTKLTGRERLILQPNIHAVHIREWLYQEGYELLDEVILEEDGKCYEILVAETGDRDAPYrdlPMAAGMLAGPF 181
Cdd:pfam04816  81 REILEEGKDKLAGVKRLILQPNINPEDLREWLSANSYQIKAERILEEDGKIYEILVVEKGKKPDAK---LSEADLRFGPF 157
                         170       180
                  ....*....|....*....|....*...
gi 1125814653 182 LLKERNEVFLRKWSQELKHTEQIYEQIS 209
Cdd:pfam04816 158 LLKEKSALFKKKWQKELEKLKKILAQLS 185
Methyltransf_18 pfam12847
Methyltransferase domain; Protein in this family function as methyltransferases.
6-156 1.86e-76

Methyltransferase domain; Protein in this family function as methyltransferases.


Pssm-ID: 463730  Cd Length: 151  Bit Score: 226.93  E-value: 1.86e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125814653   6 LSKRLQSVAEYIPPGALVADIGSDHAYLPCYAVLNHLASRAIAGEITDGPFLSAKQQVEKLDLSTLISVRKGDGLSVLEK 85
Cdd:pfam12847   1 LSKRLQAIASLVPPGSRVADIGTDHAYLPIYLVKNGIAPKAIASDINEGPLEKARENIEKYGLEDRIEVRLGDGLEVLEP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125814653  86 GEAGAITIAGMGGALIAHILESGKTKLTGRERLILQPNIHAVHIREWLYQEGYELLDEVILEEDGKCYEIL 156
Cdd:pfam12847  81 GEVDTIVIAGMGGELIIDILEAGPEVLKSVKRLILQPQSDIEELRRWLYENGFEIIDEKLVEEDGKYYEII 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH