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Conserved domains on  [gi|1567725638|ref|WP_129153315|]
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GNAT family N-acetyltransferase [Achromobacter aloeverae]

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, ...
28-203 3.59e-35

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: 123.57  E-value: 3.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638  28 VTLQGRHCRLEPLDAErHAADLHAAYQaapDGRDWTYLsVERPATLEDFKRYAANAAR---SRDPRHYAVIDLRTDKAVG 104
Cdd:COG1670     1 PTLETERLRLRPLRPE-DAEALAELLN---DPEVARYL-PGPPYSLEEARAWLERLLAdwaDGGALPFAIEDKEDGELIG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638 105 TLALMRITPAAGVIEVGHVtFSPLLKRTPISTEAQYLLMAYVFDQLGYRRYEWKCDSLNAPSRAAADRLGFTFEGIFRQL 184
Cdd:COG1670    76 VVGLYDIDRANRSAEIGYW-LAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDA 154
                         170
                  ....*....|....*....
gi 1567725638 185 VVYMGRSRDTAWFSIIDAE 203
Cdd:COG1670   155 LVIDGRYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
28-203 3.59e-35

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: 123.57  E-value: 3.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638  28 VTLQGRHCRLEPLDAErHAADLHAAYQaapDGRDWTYLsVERPATLEDFKRYAANAAR---SRDPRHYAVIDLRTDKAVG 104
Cdd:COG1670     1 PTLETERLRLRPLRPE-DAEALAELLN---DPEVARYL-PGPPYSLEEARAWLERLLAdwaDGGALPFAIEDKEDGELIG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638 105 TLALMRITPAAGVIEVGHVtFSPLLKRTPISTEAQYLLMAYVFDQLGYRRYEWKCDSLNAPSRAAADRLGFTFEGIFRQL 184
Cdd:COG1670    76 VVGLYDIDRANRSAEIGYW-LAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDA 154
                         170
                  ....*....|....*....
gi 1567725638 185 VVYMGRSRDTAWFSIIDAE 203
Cdd:COG1670   155 LVIDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
36-176 1.25e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 57.74  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638  36 RLEPLDAErHAADLHAAYQaapdGRDWTYLSVERPATLEDFKRYAANAARSRDPRHYA--VIDLRTDKAVGTLALMRITP 113
Cdd:pfam13302   3 LLRPLTEE-DAEALFELLS----DPEVMRYGVPWPLTLEEAREWLARIWAADEAERGYgwAIELKDTGFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1567725638 114 AAGVIEVGHvTFSPLLKRTPISTEAQYLLMAYVFDQLGYRRYEWKCDSLNAPSRAAADRLGFT 176
Cdd:pfam13302  78 EPERAELGY-WLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
43-203 3.46e-04

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 40.13  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638  43 ERHAADLHAAYQAapdGRDWTYLSVERPA---TLEDFKRYA-ANAARSRdpRHYAVIDL--RTDKAVGTLALMRITPAAG 116
Cdd:PRK10151   18 ESHVTPLHQLVCK---NKTWLQQSLNWPQfvqSEEDTRKTVqGNVMLHQ--RGYAKMFMifKEDELIGVLSFNRIEPLNK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638 117 VIEVGHVTFSPLLKRTPISTEAQYLLMAYVfdQLG-YRRYEWKCDSLNAPSRAAADRLGFTFEGIFRQLVVYMGRSRDTA 195
Cdd:PRK10151   93 TAYIGYWLDESHQGQGIISQALQALIHHYA--QSGeLRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYLNGAYDDVN 170

                  ....*....
gi 1567725638 196 WFS-IIDAE 203
Cdd:PRK10151  171 LYArIIDSD 179
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
28-203 3.59e-35

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: 123.57  E-value: 3.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638  28 VTLQGRHCRLEPLDAErHAADLHAAYQaapDGRDWTYLsVERPATLEDFKRYAANAAR---SRDPRHYAVIDLRTDKAVG 104
Cdd:COG1670     1 PTLETERLRLRPLRPE-DAEALAELLN---DPEVARYL-PGPPYSLEEARAWLERLLAdwaDGGALPFAIEDKEDGELIG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638 105 TLALMRITPAAGVIEVGHVtFSPLLKRTPISTEAQYLLMAYVFDQLGYRRYEWKCDSLNAPSRAAADRLGFTFEGIFRQL 184
Cdd:COG1670    76 VVGLYDIDRANRSAEIGYW-LAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDA 154
                         170
                  ....*....|....*....
gi 1567725638 185 VVYMGRSRDTAWFSIIDAE 203
Cdd:COG1670   155 LVIDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
36-176 1.25e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 57.74  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638  36 RLEPLDAErHAADLHAAYQaapdGRDWTYLSVERPATLEDFKRYAANAARSRDPRHYA--VIDLRTDKAVGTLALMRITP 113
Cdd:pfam13302   3 LLRPLTEE-DAEALFELLS----DPEVMRYGVPWPLTLEEAREWLARIWAADEAERGYgwAIELKDTGFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1567725638 114 AAGVIEVGHvTFSPLLKRTPISTEAQYLLMAYVFDQLGYRRYEWKCDSLNAPSRAAADRLGFT 176
Cdd:pfam13302  78 EPERAELGY-WLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
43-197 1.01e-05

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 44.60  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638  43 ERHAADLHAAYQAAPDGRDWTYLsvERPATLEDFKRYAANAARSRDPRHYAVIDlrtDKAVGTLALMRITPAAGVIEVGH 122
Cdd:COG1247     9 PEDAPAIAAIYNEAIAEGTATFE--TEPPSEEEREAWFAAILAPGRPVLVAEED---GEVVGFASLGPFRPRPAYRGTAE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638 123 VTFSpllkrtpISTEAQ-----YLLMAYVFD---QLGYRRYEWKCDSLNAPSRAAADRLGFTFEGIFRQLVVYMGRSRDT 194
Cdd:COG1247    84 ESIY-------VDPDARgrgigRALLEALIErarARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDL 156

                  ...
gi 1567725638 195 AWF 197
Cdd:COG1247   157 VLM 159
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
43-203 3.46e-04

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 40.13  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638  43 ERHAADLHAAYQAapdGRDWTYLSVERPA---TLEDFKRYA-ANAARSRdpRHYAVIDL--RTDKAVGTLALMRITPAAG 116
Cdd:PRK10151   18 ESHVTPLHQLVCK---NKTWLQQSLNWPQfvqSEEDTRKTVqGNVMLHQ--RGYAKMFMifKEDELIGVLSFNRIEPLNK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1567725638 117 VIEVGHVTFSPLLKRTPISTEAQYLLMAYVfdQLG-YRRYEWKCDSLNAPSRAAADRLGFTFEGIFRQLVVYMGRSRDTA 195
Cdd:PRK10151   93 TAYIGYWLDESHQGQGIISQALQALIHHYA--QSGeLRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYLNGAYDDVN 170

                  ....*....
gi 1567725638 196 WFS-IIDAE 203
Cdd:PRK10151  171 LYArIIDSD 179
 
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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