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Conserved domains on  [gi|446547216|ref|WP_000624562|]
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tRNA (adenine(22)-N(1))-methyltransferase TrmK [Staphylococcus aureus]

Protein Classification

tRNA (adenine(22)-N(1))-methyltransferase TrmK( domain architecture ID 10521698)

tRNA (adenine(22)-N(1))-methyltransferase TrmK is required for N1-adenosine methylation at position 22 of bacterial tRNA, preventing Watson-Crick-type base pairing, and is important for regulation of structure and stability of tRNA molecules

CATH:  3.40.50.150
EC:  2.1.1.217
PubMed:  18420655|24904644
SCOP:  4005114

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TrmK pfam04816
tRNA (adenine(22)-N(1))-methyltransferase; tRNA_MT is a family of bacterial tRNA (adenine(22) ...
20-222 3.38e-93

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: 271.50  E-value: 3.38e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446547216   20 IADIGSDHAYLPIYAIQNHLCDCGIAGEVIQGPFQAAVKNVAANQLVDKIDVRLGDGLSVIHPEDVIDNITICGMGGPLI 99
Cdd:pfam04816   1 LADIGSDHAYLPIYLVQNNLASFAIAGEVNAGPLQSAVNNVAKSGLTERIDVRLGDGLAVIELEDVIDVIVIAGMGGTLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446547216  100 AKILKDGQDKLSQHPRLILQSNIQTENLRQTLQQLNYEIIDEIIMEEKGHIYEIVVAEYSTQLIE-LSSDELKFGPKLLN 178
Cdd:pfam04816  81 REILEEGKDKLAGVKRLILQPNINPEDLREWLSANSYQIKAERILEEDGKIYEILVVEKGKKPDAkLSEADLRFGPFLLK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446547216  179 NKNEYFIKKWQRELEALYHIKSKLNTEQHHQRLAQINDEIAVIE 222
Cdd:pfam04816 161 EKSALFKKKWQKELEKLKKILAQLSSENAEAELAELSEKIEVIK 204
 
Name Accession Description Interval E-value
TrmK pfam04816
tRNA (adenine(22)-N(1))-methyltransferase; tRNA_MT is a family of bacterial tRNA (adenine(22) ...
20-222 3.38e-93

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: 271.50  E-value: 3.38e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446547216   20 IADIGSDHAYLPIYAIQNHLCDCGIAGEVIQGPFQAAVKNVAANQLVDKIDVRLGDGLSVIHPEDVIDNITICGMGGPLI 99
Cdd:pfam04816   1 LADIGSDHAYLPIYLVQNNLASFAIAGEVNAGPLQSAVNNVAKSGLTERIDVRLGDGLAVIELEDVIDVIVIAGMGGTLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446547216  100 AKILKDGQDKLSQHPRLILQSNIQTENLRQTLQQLNYEIIDEIIMEEKGHIYEIVVAEYSTQLIE-LSSDELKFGPKLLN 178
Cdd:pfam04816  81 REILEEGKDKLAGVKRLILQPNINPEDLREWLSANSYQIKAERILEEDGKIYEILVVEKGKKPDAkLSEADLRFGPFLLK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446547216  179 NKNEYFIKKWQRELEALYHIKSKLNTEQHHQRLAQINDEIAVIE 222
Cdd:pfam04816 161 EKSALFKKKWQKELEKLKKILAQLSSENAEAELAELSEKIEVIK 204
TrmK COG2384
tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase ...
4-225 1.22e-85

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: 253.17  E-value: 1.22e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446547216   4 LNNRLTTVSRFLKQG-TIADIGSDHAYLPIYAIQNHLCDCGIAGEVIQGPFQAAVKNVAANQLVDKIDVRLGDGLSVIHP 82
Cdd:COG2384    2 LSKRLQAIASLVPKGaRVADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDGLEVLEP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446547216  83 EDViDNITICGMGGPLIAKILKDGQDKLSQHPRLILQSNIQTENLRQTLQQLNYEIIDEIIMEEKGHIYEIVVAEYSTQL 162
Cdd:COG2384   82 GEV-DTIVIAGMGGELIADILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEELVEEDGKIYEIIVAEPGEEK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446547216 163 IELSSDELKFGPKLLNNKNEYFIKKWQRELEALYHIKSKL---NTEQHHQRLAQINDEIAVIERVL 225
Cdd:COG2384  161 LELSELELEFGPLLLEEKNPLLKEYLEREIEKYQRILEQLeksKTEEAAEKIEELEKKIKAIEEVL 226
 
Name Accession Description Interval E-value
TrmK pfam04816
tRNA (adenine(22)-N(1))-methyltransferase; tRNA_MT is a family of bacterial tRNA (adenine(22) ...
20-222 3.38e-93

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: 271.50  E-value: 3.38e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446547216   20 IADIGSDHAYLPIYAIQNHLCDCGIAGEVIQGPFQAAVKNVAANQLVDKIDVRLGDGLSVIHPEDVIDNITICGMGGPLI 99
Cdd:pfam04816   1 LADIGSDHAYLPIYLVQNNLASFAIAGEVNAGPLQSAVNNVAKSGLTERIDVRLGDGLAVIELEDVIDVIVIAGMGGTLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446547216  100 AKILKDGQDKLSQHPRLILQSNIQTENLRQTLQQLNYEIIDEIIMEEKGHIYEIVVAEYSTQLIE-LSSDELKFGPKLLN 178
Cdd:pfam04816  81 REILEEGKDKLAGVKRLILQPNINPEDLREWLSANSYQIKAERILEEDGKIYEILVVEKGKKPDAkLSEADLRFGPFLLK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446547216  179 NKNEYFIKKWQRELEALYHIKSKLNTEQHHQRLAQINDEIAVIE 222
Cdd:pfam04816 161 EKSALFKKKWQKELEKLKKILAQLSSENAEAELAELSEKIEVIK 204
TrmK COG2384
tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase ...
4-225 1.22e-85

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: 253.17  E-value: 1.22e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446547216   4 LNNRLTTVSRFLKQG-TIADIGSDHAYLPIYAIQNHLCDCGIAGEVIQGPFQAAVKNVAANQLVDKIDVRLGDGLSVIHP 82
Cdd:COG2384    2 LSKRLQAIASLVPKGaRVADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDGLEVLEP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446547216  83 EDViDNITICGMGGPLIAKILKDGQDKLSQHPRLILQSNIQTENLRQTLQQLNYEIIDEIIMEEKGHIYEIVVAEYSTQL 162
Cdd:COG2384   82 GEV-DTIVIAGMGGELIADILEAGKDKLKSVKRLILQPNTGAEELRRWLYENGFRIIDEELVEEDGKIYEIIVAEPGEEK 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446547216 163 IELSSDELKFGPKLLNNKNEYFIKKWQRELEALYHIKSKL---NTEQHHQRLAQINDEIAVIERVL 225
Cdd:COG2384  161 LELSELELEFGPLLLEEKNPLLKEYLEREIEKYQRILEQLeksKTEEAAEKIEELEKKIKAIEEVL 226
Methyltransf_18 pfam12847
Methyltransferase domain; Protein in this family function as methyltransferases.
4-153 3.05e-55

Methyltransferase domain; Protein in this family function as methyltransferases.


Pssm-ID: 463730  Cd Length: 151  Bit Score: 173.39  E-value: 3.05e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446547216    4 LNNRLTTVSRFLKQG-TIADIGSDHAYLPIYAIQNHLCDCGIAGEVIQGPFQAAVKNVAANQLVDKIDVRLGDGLSVIHP 82
Cdd:pfam12847   1 LSKRLQAIASLVPPGsRVADIGTDHAYLPIYLVKNGIAPKAIASDINEGPLEKARENIEKYGLEDRIEVRLGDGLEVLEP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446547216   83 EDViDNITICGMGGPLIAKILKDGQDKLSQHPRLILQSNIQTENLRQTLQQLNYEIIDEIIMEEKGHIYEI 153
Cdd:pfam12847  81 GEV-DTIVIAGMGGELIIDILEAGPEVLKSVKRLILQPQSDIEELRRWLYENGFEIIDEKLVEEDGKYYEI 150
 
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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