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Conserved domains on  [gi|2564843269|ref|WP_306046852|]
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GNAT family N-acetyltransferase [Nioella sp. MMSF_3534]

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, ...
9-180 6.62e-26

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: 97.38  E-value: 6.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564843269   9 PTLETERLVLRAPRMGDVQHWCDFTASSRAEFIGGPMIADPAKAWRAFAHVAGMWMLRGYGSFVFALRSDPEtPIGMTGp 88
Cdd:COG1670     1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGE-LIGVVG- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564843269  89 WHPIDWPEQ--ELGWTVwNADAEGKGFALEAAKEARRFAYQDLGWPTAVSYIDSRNTRSIALAERMGCEVDANAKAPEAE 166
Cdd:COG1670    79 LYDIDRANRsaEIGYWL-APAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI 157
                         170
                  ....*....|....*.
gi 2564843269 167 EGEVI--LVFRHPAPE 180
Cdd:COG1670   158 DGRYRdhVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
9-180 6.62e-26

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: 97.38  E-value: 6.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564843269   9 PTLETERLVLRAPRMGDVQHWCDFTASSRAEFIGGPMIADPAKAWRAFAHVAGMWMLRGYGSFVFALRSDPEtPIGMTGp 88
Cdd:COG1670     1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGE-LIGVVG- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564843269  89 WHPIDWPEQ--ELGWTVwNADAEGKGFALEAAKEARRFAYQDLGWPTAVSYIDSRNTRSIALAERMGCEVDANAKAPEAE 166
Cdd:COG1670    79 LYDIDRANRsaEIGYWL-APAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI 157
                         170
                  ....*....|....*.
gi 2564843269 167 EGEVI--LVFRHPAPE 180
Cdd:COG1670   158 DGRYRdhVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
15-155 1.43e-24

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 93.18  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564843269  15 RLVLRAPRMGDVQHWCDFTASSRAEFIGGPMIADPAKAWRAFAHvagMWMLRGYG-SFVFALRSDPETPIGMTGPWHPID 93
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLAR---IWAADEAErGYGWAIELKDTGFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2564843269  94 WPEQ-ELGWTVWnADAEGKGFALEAAKEARRFAYQDLGWPTAVSYIDSRNTRSIALAERMGCE 155
Cdd:pfam13302  78 EPERaELGYWLG-PDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
9-180 6.62e-26

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: 97.38  E-value: 6.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564843269   9 PTLETERLVLRAPRMGDVQHWCDFTASSRAEFIGGPMIADPAKAWRAFAHVAGMWMLRGYGSFVFALRSDPEtPIGMTGp 88
Cdd:COG1670     1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGE-LIGVVG- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564843269  89 WHPIDWPEQ--ELGWTVwNADAEGKGFALEAAKEARRFAYQDLGWPTAVSYIDSRNTRSIALAERMGCEVDANAKAPEAE 166
Cdd:COG1670    79 LYDIDRANRsaEIGYWL-APAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI 157
                         170
                  ....*....|....*.
gi 2564843269 167 EGEVI--LVFRHPAPE 180
Cdd:COG1670   158 DGRYRdhVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
15-155 1.43e-24

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 93.18  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2564843269  15 RLVLRAPRMGDVQHWCDFTASSRAEFIGGPMIADPAKAWRAFAHvagMWMLRGYG-SFVFALRSDPETPIGMTGPWHPID 93
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLAR---IWAADEAErGYGWAIELKDTGFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2564843269  94 WPEQ-ELGWTVWnADAEGKGFALEAAKEARRFAYQDLGWPTAVSYIDSRNTRSIALAERMGCE 155
Cdd:pfam13302  78 EPERaELGYWLG-PDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 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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