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Conserved domains on  [gi|1860944948|ref|WP_175801798|]
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GNAT family N-acetyltransferase [Burkholderia anthina]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
6-178 1.19e-32

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 115.10  E-value: 1.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860944948   6 EIETARLRLRRWRPDDAAPFAAIHADPDVTAWLARGPMSVDEARAGIERFEAHFDEHGFGQWAVERKTDRALIALCGLSR 85
Cdd:COG1670     2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLYD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860944948  86 EVRETHpmapCVEIAWRQARAAWGHGYIAEAAAAVLADGFERIGLADIFAWTAQRNLRSQRVMQRIGMERqpERDFDHPV 165
Cdd:COG1670    82 IDRANR----SAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRL--EGTLRDAL 155
                         170
                  ....*....|...
gi 1860944948 166 LPEGHvLRPHVVY 178
Cdd:COG1670   156 VIDGR-YRDHVLY 167
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
6-178 1.19e-32

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 115.10  E-value: 1.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860944948   6 EIETARLRLRRWRPDDAAPFAAIHADPDVTAWLARGPMSVDEARAGIERFEAHFDEHGFGQWAVERKTDRALIALCGLSR 85
Cdd:COG1670     2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLYD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860944948  86 EVRETHpmapCVEIAWRQARAAWGHGYIAEAAAAVLADGFERIGLADIFAWTAQRNLRSQRVMQRIGMERqpERDFDHPV 165
Cdd:COG1670    82 IDRANR----SAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRL--EGTLRDAL 155
                         170
                  ....*....|...
gi 1860944948 166 LPEGHvLRPHVVY 178
Cdd:COG1670   156 VIDGR-YRDHVLY 167
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
11-154 5.43e-25

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 94.33  E-value: 5.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860944948  11 RLRLRRWRPDDAAPFAAIHADPDVTAWLARGPMSVDEARAGIERFEAHFDEHGFGQWAVERKTDRAlIALCGLSREVRET 90
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEAERGYGWAIELKDTGF-IGSIGLYDIDGEP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860944948  91 HPmapcVEIAWRQARAAWGHGYIAEAAAAVLADGFERIGLADIFAWTAQRNLRSQRVMQRIGME 154
Cdd:pfam13302  80 ER----AELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
6-178 1.19e-32

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 115.10  E-value: 1.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860944948   6 EIETARLRLRRWRPDDAAPFAAIHADPDVTAWLARGPMSVDEARAGIERFEAHFDEHGFGQWAVERKTDRALIALCGLSR 85
Cdd:COG1670     2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLYD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860944948  86 EVRETHpmapCVEIAWRQARAAWGHGYIAEAAAAVLADGFERIGLADIFAWTAQRNLRSQRVMQRIGMERqpERDFDHPV 165
Cdd:COG1670    82 IDRANR----SAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRL--EGTLRDAL 155
                         170
                  ....*....|...
gi 1860944948 166 LPEGHvLRPHVVY 178
Cdd:COG1670   156 VIDGR-YRDHVLY 167
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
11-154 5.43e-25

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 94.33  E-value: 5.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860944948  11 RLRLRRWRPDDAAPFAAIHADPDVTAWLARGPMSVDEARAGIERFEAHFDEHGFGQWAVERKTDRAlIALCGLSREVRET 90
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEAERGYGWAIELKDTGF-IGSIGLYDIDGEP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860944948  91 HPmapcVEIAWRQARAAWGHGYIAEAAAAVLADGFERIGLADIFAWTAQRNLRSQRVMQRIGME 154
Cdd:pfam13302  80 ER----AELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
 
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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