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Conserved domains on  [gi|446549915|ref|WP_000627261|]
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MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

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, ...
3-176 5.03e-53

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: 166.33  E-value: 5.03e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915   3 TELHSQRLYLRKMKASDSLSMFKIWSDPDVTKFMNISNFTDEnQAKDMIQFLNELAQNNKAIRFTIIEKESNHIIGSCGY 82
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLE-EARAWLERLLADWADGGALPFAIEDKEDGELIGVVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915  83 NSLDFENSKTEIGYDISKTFWGKGYAPEAISSLLDYAFTHLKLNRVEAKVEPANVNSIKVLEKLNFTFEGTLRKSEKSAG 162
Cdd:COG1670   80 YDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159
                        170
                 ....*....|....
gi 446549915 163 KLIDLNIYSKLISD 176
Cdd:COG1670  160 RYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
3-176 5.03e-53

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: 166.33  E-value: 5.03e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915   3 TELHSQRLYLRKMKASDSLSMFKIWSDPDVTKFMNISNFTDEnQAKDMIQFLNELAQNNKAIRFTIIEKESNHIIGSCGY 82
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLE-EARAWLERLLADWADGGALPFAIEDKEDGELIGVVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915  83 NSLDFENSKTEIGYDISKTFWGKGYAPEAISSLLDYAFTHLKLNRVEAKVEPANVNSIKVLEKLNFTFEGTLRKSEKSAG 162
Cdd:COG1670   80 YDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159
                        170
                 ....*....|....
gi 446549915 163 KLIDLNIYSKLISD 176
Cdd:COG1670  160 RYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
9-149 8.07e-41

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 134.40  E-value: 8.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915    9 RLYLRKMKASDSLSMFKIWSDPDVTKFMNISNFTDEnQAKDMIQFLNELAQNNKAIRFTIIEKESNhIIGSCGYNSLDFE 88
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLE-EAREWLARIWAADEAERGYGWAIELKDTG-FIGSIGLYDIDGE 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549915   89 NSKTEIGYDISKTFWGKGYAPEAISSLLDYAFTHLKLNRVEAKVEPANVNSIKVLEKLNFT 149
Cdd:pfam13302  79 PERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
57-174 7.76e-07

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 46.68  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915  57 LAQNNKAIRFTIIEKESnhIIGSCGYNSLDFENSKTEIGYDISKTFWGKGYAPEAISSLLDYAFTHLKLNRVEAKVEPAN 136
Cdd:PRK10151  61 LHQRGYAKMFMIFKEDE--LIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDN 138
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446549915 137 VNSIKVLEKLNFTFEGTLRKSEKSAGKLIDLNIYSKLI 174
Cdd:PRK10151 139 PASNQVALRNGFTLEGCLKQAEYLNGAYDDVNLYARII 176
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
3-176 5.03e-53

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: 166.33  E-value: 5.03e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915   3 TELHSQRLYLRKMKASDSLSMFKIWSDPDVTKFMNISNFTDEnQAKDMIQFLNELAQNNKAIRFTIIEKESNHIIGSCGY 82
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLE-EARAWLERLLADWADGGALPFAIEDKEDGELIGVVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915  83 NSLDFENSKTEIGYDISKTFWGKGYAPEAISSLLDYAFTHLKLNRVEAKVEPANVNSIKVLEKLNFTFEGTLRKSEKSAG 162
Cdd:COG1670   80 YDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159
                        170
                 ....*....|....
gi 446549915 163 KLIDLNIYSKLISD 176
Cdd:COG1670  160 RYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
9-149 8.07e-41

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 134.40  E-value: 8.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915    9 RLYLRKMKASDSLSMFKIWSDPDVTKFMNISNFTDEnQAKDMIQFLNELAQNNKAIRFTIIEKESNhIIGSCGYNSLDFE 88
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLE-EAREWLARIWAADEAERGYGWAIELKDTG-FIGSIGLYDIDGE 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549915   89 NSKTEIGYDISKTFWGKGYAPEAISSLLDYAFTHLKLNRVEAKVEPANVNSIKVLEKLNFT 149
Cdd:pfam13302  79 PERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
41-148 6.94e-12

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


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 59.07  E-value: 6.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915   41 FTDENQAKDMIQFLNELAQNNkaiRFTIIEKESNHIIGSCGYNSLDFENSKTEI-GYDISKTFWGKGYAPEAISSLLDYA 119
Cdd:pfam00583  12 FPEPWPDEPLDLLEDWDEDAS---EGFFVAEEDGELVGFASLSIIDDEPPVGEIeGLAVAPEYRGKGIGTALLQALLEWA 88
                          90       100
                  ....*....|....*....|....*....
gi 446549915  120 FtHLKLNRVEAKVEPANVNSIKVLEKLNF 148
Cdd:pfam00583  89 R-ERGCERIFLEVAADNLAAIALYEKLGF 116
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
94-158 2.01e-07

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 48.37  E-value: 2.01e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549915  94 IGYDISKTFWGKGYAPEAISSLLDYAFThLKLNRVEAKVEPANVNSIKVLEKLNFTFEGTLRKSE 158
Cdd:COG3981   95 IGYGVRPSERGKGYATEMLRLALEEARE-LGLDRVLITCDKDNIASRKVIEANGGVLEDEVVDEE 158
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
57-174 7.76e-07

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 46.68  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915  57 LAQNNKAIRFTIIEKESnhIIGSCGYNSLDFENSKTEIGYDISKTFWGKGYAPEAISSLLDYAFTHLKLNRVEAKVEPAN 136
Cdd:PRK10151  61 LHQRGYAKMFMIFKEDE--LIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDN 138
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446549915 137 VNSIKVLEKLNFTFEGTLRKSEKSAGKLIDLNIYSKLI 174
Cdd:PRK10151 139 PASNQVALRNGFTLEGCLKQAEYLNGAYDDVNLYARII 176
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
98-174 3.25e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 44.99  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915  98 ISKTFWGKGYApeaiSSLLDYAFTHLK---LNRVEAKVEPANVNSIKVLEKLNFTFEGTLRKSEKSAGKLIDLNIYSKLI 174
Cdd:COG1247   88 VDPDARGRGIG----RALLEALIERARargYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKRL 163
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
102-153 1.10e-05

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 43.28  E-value: 1.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446549915  102 FWGKGYAPEAISSLLDYAFTHLKLNRVeaKVEP--ANVNSIKVLEKLNFTFEGT 153
Cdd:pfam13523  91 FRGRGFTTALLRALVHYLFADPRTRRV--VVEPdvRNERAIRLLERAGFRKVKE 142
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
72-169 1.63e-05

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 42.74  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915   72 ESNHIIGSCGYNSLDF-ENSKTEIGYDISKTFwGKGYAPEAISSLLDYAFTHLKLNRVEAKVEPANVNSIKVLEKLNFTF 150
Cdd:pfam13420  56 ESDRLIGYATLRQFDYvKTHKAELSFYVVKNN-DEGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEW 134
                          90
                  ....*....|....*....
gi 446549915  151 EGTLRKSEKSAGKLIDLNI 169
Cdd:pfam13420 135 LGIERNAIKKNGRWIDMMW 153
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
53-152 3.95e-05

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 42.03  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549915  53 FLNELAQNNKAIRFTIIEKESNHIIGSCGY-NSLDFENSKTEIGYDISKTFWGKGYAPEAISSLLDYAFTHLKLNRVEAK 131
Cdd:PRK10809  65 MINEFHKQGSAFYFALLDPDEKEIIGVANFsNVVRGSFHACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMAN 144
                         90       100
                 ....*....|....*....|.
gi 446549915 132 VEPANVNSIKVLEKLNFTFEG 152
Cdd:PRK10809 145 YMPHNKRSGDLLARLGFEKEG 165
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
98-154 5.02e-05

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 41.71  E-value: 5.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446549915  98 ISKTFWGKGYAPEAISSLLDYAFTHLKLNRVEAKVEPANVNSIKVLEKLNFTFEGTL 154
Cdd:PRK15130  90 ISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGEL 146
 
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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