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Conserved domains on  [gi|446389790|ref|WP_000467645|]
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MULTISPECIES: GNAT family N-acetyltransferase [Staphylococcus]

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

 Zoom to residue level

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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 5.43e-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: 146.30  E-value: 5.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790   8 EQIRLKILEAHDTEALFNLVNRSRnsLREWLPWVDATeqPSDTRAFIKSGLLQFADGNGFQCGIWY--EGTLVGVIGLHE 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPE--VARYLPGPPYS--LEEARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790  86 INHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGFTREGMLRDNELLNGIY 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 446389790 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 5.43e-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: 146.30  E-value: 5.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790   8 EQIRLKILEAHDTEALFNLVNRSRnsLREWLPWVDATeqPSDTRAFIKSGLLQFADGNGFQCGIWY--EGTLVGVIGLHE 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPE--VARYLPGPPYS--LEEARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790  86 INHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGFTREGMLRDNELLNGIY 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 446389790 166 SSSYIYSLLKSE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
11-150 2.82e-26

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 97.42  E-value: 2.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790   11 RLKI--LEAHDTEALFNLVNRSRnSLREWLPWVDATEQpsdTRAFIKSGLLQFADGNGFQCGIWYEGT-LVGVIGLHEIN 87
Cdd:pfam13302   1 RLLLrpLTEEDAEALFELLSDPE-VMRYGVPWPLTLEE---AREWLARIWAADEAERGYGWAIELKDTgFIGSIGLYDID 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446389790   88 HMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGFT 150
Cdd:pfam13302  77 GEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
4-171 1.59e-24

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 94.06  E-value: 1.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790   4 MKVNEQIRLKILEAHDTEALFNLVNRSRNSLREWLPWVDATEQPSDTRAFIKSGLLQFADGNGFQCGIWYEGTLVGVIGL 83
Cdd:PRK10151   5 IPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIGVLSF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790  84 HEINHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGFTREGMLRDNELLNG 163
Cdd:PRK10151  85 NRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYLNG 164

                 ....*...
gi 446389790 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 2.89e-07

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: 47.74  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790   73 YEGTLVGVIGLHEINHMHRKTSLGYY---LDKQFEGHGIMtqavEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGF 149
Cdd:TIGR03585  58 QESRPIGVISFTDINLVHKSAFWGIYanpFCKPGVGSVLE----EAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGF 133

                  ....*...
gi 446389790  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 5.43e-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: 146.30  E-value: 5.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790   8 EQIRLKILEAHDTEALFNLVNRSRnsLREWLPWVDATeqPSDTRAFIKSGLLQFADGNGFQCGIWY--EGTLVGVIGLHE 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPE--VARYLPGPPYS--LEEARAWLERLLADWADGGALPFAIEDkeDGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790  86 INHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGFTREGMLRDNELLNGIY 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 446389790 166 SSSYIYSLLKSE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
11-150 2.82e-26

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 97.42  E-value: 2.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790   11 RLKI--LEAHDTEALFNLVNRSRnSLREWLPWVDATEQpsdTRAFIKSGLLQFADGNGFQCGIWYEGT-LVGVIGLHEIN 87
Cdd:pfam13302   1 RLLLrpLTEEDAEALFELLSDPE-VMRYGVPWPLTLEE---AREWLARIWAADEAERGYGWAIELKDTgFIGSIGLYDID 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446389790   88 HMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGFT 150
Cdd:pfam13302  77 GEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
4-171 1.59e-24

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 94.06  E-value: 1.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790   4 MKVNEQIRLKILEAHDTEALFNLVNRSRNSLREWLPWVDATEQPSDTRAFIKSGLLQFADGNGFQCGIWYEGTLVGVIGL 83
Cdd:PRK10151   5 IPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEDTRKTVQGNVMLHQRGYAKMFMIFKEDELIGVLSF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790  84 HEINHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGFTREGMLRDNELLNG 163
Cdd:PRK10151  85 NRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYLNG 164

                 ....*...
gi 446389790 164 IYSSSYIY 171
Cdd:PRK10151 165 AYDDVNLY 172
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
71-165 1.26e-10

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 57.50  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790  71 IWYEGTLVGVIGLHEINHMHRKTSLGYYLDKQFEGHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGFT 150
Cdd:PRK15130  62 VECDGEKAGLVELVEINHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFE 141
                         90
                 ....*....|....*
gi 446389790 151 REGMLRDNELLNGIY 165
Cdd:PRK15130 142 VEGELIHEFFINGEY 156
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
95-181 1.76e-08

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 51.66  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790  95 LGYYLDKQFEGHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGFTREGMLRDNELLNGIYSSSYIYSLL 174
Cdd:PRK10809 107 LGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVLTALT 186

                 ....*..
gi 446389790 175 KSEYNEG 181
Cdd:PRK10809 187 TPEWTPG 193
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
73-157 2.89e-07

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: 47.74  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790   73 YEGTLVGVIGLHEINHMHRKTSLGYY---LDKQFEGHGIMtqavEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGF 149
Cdd:TIGR03585  58 QESRPIGVISFTDINLVHKSAFWGIYanpFCKPGVGSVLE----EAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGF 133

                  ....*...
gi 446389790  150 TREGMLRD 157
Cdd:TIGR03585 134 EREGVFRQ 141
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
72-153 1.39e-06

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: 45.34  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790   72 WYEGTLVGVIGLHEINHMHRktslgYYLDKQFEGHGIMTQAVEALIKYCF-DEIELNRIEISAAVNneksqAIP--ERLG 148
Cdd:pfam13673  37 FEGGQIVGVIALRDRGHISL-----LFVDPDYQGQGIGKALLEAVEDYAEkDGIKLSELTVNASPY-----AVPfyEKLG 106

                  ....*
gi 446389790  149 FTREG 153
Cdd:pfam13673 107 FRATG 111
PRK10140 PRK10140
N-acetyltransferase;
74-175 1.62e-06

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 45.74  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790  74 EGTLVGVIGLHEINHMHRK--TSLGYYLDKQFEGHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGFTR 151
Cdd:PRK10140  59 DGDVVGHLTIDVQQRPRRShvADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEI 138
                         90       100
                 ....*....|....*....|....
gi 446389790 152 EGMLRDNELLNGIYSSSYIYSLLK 175
Cdd:PRK10140 139 EGTGKKYALRNGEYVDAYYMARVK 162
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
70-157 1.24e-03

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 37.73  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790   70 GIWYEGTLVGVIGLHEINHMHRKTS-LGYYLDKQFEgHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLG 148
Cdd:pfam13420  53 GVAESDRLIGYATLRQFDYVKTHKAeLSFYVVKNND-EGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIG 131

                  ....*....
gi 446389790  149 FTREGMLRD 157
Cdd:pfam13420 132 FEWLGIERN 140
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
74-174 1.97e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 37.28  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446389790  74 EGTLVGVIGLHEINHMHRKTSLGY---YLDKQFEGHGIMTQAVEALIKYCfDEIELNRIEISAAVNNEKSQAIPERLGFT 150
Cdd:COG1247   60 DGEVVGFASLGPFRPRPAYRGTAEesiYVDPDARGRGIGRALLEALIERA-RARGYRRLVAVVLADNEASIALYEKLGFE 138
                         90       100
                 ....*....|....*....|....
gi 446389790 151 REGMLRDNELLNGIYSSSYIYSLL 174
Cdd:COG1247  139 EVGTLPEVGFKFGRWLDLVLMQKR 162
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
105-153 2.14e-03

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 36.73  E-value: 2.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 446389790  105 GHGIMTQAVEALIKYCFDEIELNRIEISAAVNNEKSQAIPERLGFTREG 153
Cdd:pfam13523  93 GRGFTTALLRALVHYLFADPRTRRVVVEPDVRNERAIRLLERAGFRKVK 141
 
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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