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Conserved domains on  [gi|446389784|ref|WP_000467639|]
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GNAT family N-acetyltransferase [Staphylococcus aureus]

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
PubMed:  27367672|26818562|15581578|10940244
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, ...
 8-177 1.16e-45

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: 147.84  E-value: 1.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784   8 EQIRLKILEAHDTEALFNLVNRSRdsLREWLPWVDATeqPSDTHAFIKRGLLQFADSNGFQCGIWY--EGTLVGVIGLHE 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPE--VARYLPGPPYS--LEEARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784  86 INHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGFTREGMLRDNELLNGIY 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161

                        170
                 ....*....|..
gi 446389784 166 SSSYIYSLLKSE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 8-177 1.16e-45

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: 147.84  E-value: 1.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784   8 EQIRLKILEAHDTEALFNLVNRSRdsLREWLPWVDATeqPSDTHAFIKRGLLQFADSNGFQCGIWY--EGTLVGVIGLHE 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPE--VARYLPGPPYS--LEEARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784  86 INHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGFTREGMLRDNELLNGIY 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161

                        170
                 ....*....|..
gi 446389784 166 SSSYIYSLLKSE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 11-150 4.23e-28

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 102.04  E-value: 4.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784   11 RLKI--LEAHDTEALFNLVNrSRDSLREWLPWVDATEQpsdTHAFIKRGLLQFADSNGFQCGIWYEGT-LVGVIGLHEIN 87
Cdd:pfam13302   1 RLLLrpLTEEDAEALFELLS-DPEVMRYGVPWPLTLEE---AREWLARIWAADEAERGYGWAIELKDTgFIGSIGLYDID 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446389784   88 HMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGFT 150
Cdd:pfam13302  77 GEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
4-171 4.30e-22

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 87.51  E-value: 4.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784   4 MKVNEQIRLKILEAHDTEALFNLVNRSRDSLREWLPWVDATEQPSDTHAFIKRGLLQFADSNGFQCGIWYEGTLVGVIGL 83
Cdd:PRK10151   5 IPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIGVLSF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784  84 HEINHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGFTREGMLRDNELLNG 163
Cdd:PRK10151  85 NRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYLNG 164


                 ....*...
gi 446389784 164 IYSSSYIY 171
Cdd:PRK10151 165 AYDDVNLY 172
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 73-157 2.13e-08

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 50.82  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784   73 YEGTLVGVIGLHEINHMHRKTSLGYY---LDKQFEGHGIMtqavEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGF 149
Cdd:TIGR03585  58 QESRPIGVISFTDINLVHKSAFWGIYanpFCKPGVGSVLE----EAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGF 133


                  ....*...
gi 446389784  150 TREGMLRD 157
Cdd:TIGR03585 134 EREGVFRQ 141
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 8-177 1.16e-45

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: 147.84  E-value: 1.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784   8 EQIRLKILEAHDTEALFNLVNRSRdsLREWLPWVDATeqPSDTHAFIKRGLLQFADSNGFQCGIWY--EGTLVGVIGLHE 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPE--VARYLPGPPYS--LEEARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLYD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784  86 INHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGFTREGMLRDNELLNGIY 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161

                        170
                 ....*....|..
gi 446389784 166 SSSYIYSLLKSE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 11-150 4.23e-28

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 102.04  E-value: 4.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784   11 RLKI--LEAHDTEALFNLVNrSRDSLREWLPWVDATEQpsdTHAFIKRGLLQFADSNGFQCGIWYEGT-LVGVIGLHEIN 87
Cdd:pfam13302   1 RLLLrpLTEEDAEALFELLS-DPEVMRYGVPWPLTLEE---AREWLARIWAADEAERGYGWAIELKDTgFIGSIGLYDID 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446389784   88 HMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGFT 150
Cdd:pfam13302  77 GEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
4-171 4.30e-22

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 87.51  E-value: 4.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784   4 MKVNEQIRLKILEAHDTEALFNLVNRSRDSLREWLPWVDATEQPSDTHAFIKRGLLQFADSNGFQCGIWYEGTLVGVIGL 83
Cdd:PRK10151   5 IPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIGVLSF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784  84 HEINHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGFTREGMLRDNELLNG 163
Cdd:PRK10151  85 NRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYLNG 164


                 ....*...
gi 446389784 164 IYSSSYIY 171
Cdd:PRK10151 165 AYDDVNLY 172
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 71-165 3.20e-11

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 59.04  E-value: 3.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784  71 IWYEGTLVGVIGLHEINHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGFT 150
Cdd:PRK15130  62 VECDGEKAGLVELVEINHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFE 141

                         90
                 ....*....|....*
gi 446389784 151 REGMLRDNELLNGIY 165
Cdd:PRK15130 142 VEGELIHEFFINGEY 156
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 73-157 2.13e-08

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 50.82  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784   73 YEGTLVGVIGLHEINHMHRKTSLGYY---LDKQFEGHGIMtqavEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGF 149
Cdd:TIGR03585  58 QESRPIGVISFTDINLVHKSAFWGIYanpFCKPGVGSVLE----EAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGF 133


                  ....*...
gi 446389784  150 TREGMLRD 157
Cdd:TIGR03585 134 EREGVFRQ 141
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
95-178 2.60e-08

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 51.28  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784  95 LGYYLDKQFEGHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGFTREGMLRDNELLNGIYSSSYIYSLL 174
Cdd:PRK10809 107 LGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVLTALT 186


                 ....
gi 446389784 175 KSEY 178
Cdd:PRK10809 187 TPEW 190
PRK10140 PRK10140
N-acetyltransferase;
74-175 1.77e-06

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 45.74  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784  74 EGTLVGVIGLHEINHMHRK--TSLGYYLDKQFEGHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGFTR 151
Cdd:PRK10140  59 DGDVVGHLTIDVQQRPRRShvADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEI 138

                         90       100
                 ....*....|....*....|....
gi 446389784 152 EGMLRDNELLNGIYSSSYIYSLLK 175
Cdd:PRK10140 139 EGTGKKYALRNGEYVDAYYMARVK 162
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 72-153 1.07e-05

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 43.03  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784   72 WYEGTLVGVIGLHEINHMHRktslgYYLDKQFEGHGIMTQAVEALIKYCFE-ELDLNRIEISAAVNneksrAIP--ERLG 148
Cdd:pfam13673  37 FEGGQIVGVIALRDRGHISL-----LFVDPDYQGQGIGKALLEAVEDYAEKdGIKLSELTVNASPY-----AVPfyEKLG 106


                  ....*
gi 446389784  149 FTREG 153
Cdd:pfam13673 107 FRATG 111
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
74-174 3.85e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 41.90  E-value: 3.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784  74 EGTLVGVIGLHEINHMHRKTSLGY---YLDKQFEGHGIMTQAVEALIKYCfEELDLNRIEISAAVNNEKSRAIPERLGFT 150
Cdd:COG1247   60 DGEVVGFASLGPFRPRPAYRGTAEesiYVDPDARGRGIGRALLEALIERA-RARGYRRLVAVVLADNEASIALYEKLGFE 138

                         90       100
                 ....*....|....*....|....
gi 446389784 151 REGMLRDNELLNGIYSSSYIYSLL 174
Cdd:COG1247  139 EVGTLPEVGFKFGRWLDLVLMQKR 162
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
70-157 1.93e-04

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 40.04  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784   70 GIWYEGTLVGVIGLHEINHMHRKTS-LGYYLDKQFEgHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLG 148
Cdd:pfam13420  53 GVAESDRLIGYATLRQFDYVKTHKAeLSFYVVKNND-EGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIG 131


                  ....*....
gi 446389784  149 FTREGMLRD 157
Cdd:pfam13420 132 FEWLGIERN 140
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 105-153 2.77e-04

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 39.43  E-value: 2.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 446389784  105 GHGIMTQAVEALIKYCFEELDLNRIEISAAVNNEKSRAIPERLGFTREG 153
Cdd:pfam13523  93 GRGFTTALLRALVHYLFADPRTRRVVVEPDVRNERAIRLLERAGFRKVK 141
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 98-157 2.94e-03

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 35.40  E-value: 2.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389784  98 YLDKQFEGHGIMTQAVEALIKYCfEELDLNRIEISAAVNNEKSRAIPERLGFTREGMLRD 157
Cdd:COG0456   20 AVDPEYRGRGIGRALLEAALERA-RERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
98-153 5.09e-03

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 34.50  E-value: 5.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446389784  98 YLDKQFEGHGIMTQAVEALIKYCFEElDLNRIEISAAVNNEKSRAIPERLGFTREG 153
Cdd:COG3393   22 YTHPEYRGRGLASALVAALAREALAR-GARTPFLYVDADNPAARRLYERLGFRPVG 76
 
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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