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Conserved domains on  [gi|446464664|ref|WP_000542518|]
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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
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, ...
 29-138 2.92e-17

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: 74.27  E-value: 2.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664  29 YDIEADEEDLDEFLHG-ESRGDHTFSV--KQNGILIGFFTVCKMN--DGTVDIGLGMRPDITGNGFGLQFVNAGLAFSEE 103
Cdd:COG1670   39 YSLEEARAWLERLLADwADGGALPFAIedKEDGELIGVVGLYDIDraNRSAEIGYWLAPAYWGKGYATEALRALLDYAFE 118

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446464664 104 KYGCNYITLSVATFNERAIKVYKRAGFEAVGTFIQ 138
Cdd:COG1670  119 ELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRD 153
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 29-138 2.92e-17

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: 74.27  E-value: 2.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664  29 YDIEADEEDLDEFLHG-ESRGDHTFSV--KQNGILIGFFTVCKMN--DGTVDIGLGMRPDITGNGFGLQFVNAGLAFSEE 103
Cdd:COG1670   39 YSLEEARAWLERLLADwADGGALPFAIedKEDGELIGVVGLYDIDraNRSAEIGYWLAPAYWGKGYATEALRALLDYAFE 118

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446464664 104 KYGCNYITLSVATFNERAIKVYKRAGFEAVGTFIQ 138
Cdd:COG1670  119 ELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRD 153
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-130 4.18e-09

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: 51.36  E-value: 4.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664   18 YNWYYEGKYSFYDIEADEEDLDEFLHgesRGDHTFSVKQNGILIGFFTVCKMNDG---TVDIGLGMRPDITGNGFGLQFV 94
Cdd:pfam00583   5 YELLSEEFPEPWPDEPLDLLEDWDED---ASEGFFVAEEDGELVGFASLSIIDDEppvGEIEGLAVAPEYRGKGIGTALL 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446464664   95 NAGLAFSEEKyGCNYITLSVATFNERAIKVYKRAGF 130
Cdd:pfam00583  82 QALLEWARER-GCERIFLEVAADNLAAIALYEKLGF 116
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 52-138 1.33e-05

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: 42.73  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664   52 FSVKQNGILIGFFTVCKMNDGT--VDIGLGMRPDITGnGFGLQFVNAGLAFSEEKYGCNYITLSVATFNERAIKVYKRAG 129
Cdd:TIGR03585  54 WIVCQESRPIGVISFTDINLVHksAFWGIYANPFCKP-GVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFG 132


                  ....*....
gi 446464664  130 FEAVGTFIQ 138
Cdd:TIGR03585 133 FEREGVFRQ 141
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 29-138 2.92e-17

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: 74.27  E-value: 2.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664  29 YDIEADEEDLDEFLHG-ESRGDHTFSV--KQNGILIGFFTVCKMN--DGTVDIGLGMRPDITGNGFGLQFVNAGLAFSEE 103
Cdd:COG1670   39 YSLEEARAWLERLLADwADGGALPFAIedKEDGELIGVVGLYDIDraNRSAEIGYWLAPAYWGKGYATEALRALLDYAFE 118

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446464664 104 KYGCNYITLSVATFNERAIKVYKRAGFEAVGTFIQ 138
Cdd:COG1670  119 ELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRD 153
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
8-136 4.08e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 60.39  E-value: 4.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664   8 MKQEEAEEIA--YNWYY-EGKYSFYDIEADEEDLDEFLHGESRGDHTFSV-KQNGILIGF-----FTVCKMNDGTVDIGL 78
Cdd:COG1247    7 ATPEDAPAIAaiYNEAIaEGTATFETEPPSEEEREAWFAAILAPGRPVLVaEEDGEVVGFaslgpFRPRPAYRGTAEESI 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446464664  79 GMRPDITGNGFGLQFVNAGLAFSEEKyGCNYITLSVATFNERAIKVYKRAGFEAVGTF 136
Cdd:COG1247   87 YVDPDARGRGIGRALLEALIERARAR-GYRRLVAVVLADNEASIALYEKLGFEEVGTL 143
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 30-142 5.20e-12

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 59.68  E-value: 5.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664  30 DIEADEEDLDEFLhGESRGDHTFSVKQNGILIGFFTVCKMNDGTVDIG-LGMRPDITGNGFGLQFVNAGLAFSEEKyGCN 108
Cdd:COG0454   16 LIEALDAELKAME-GSLAGAEFIAVDDKGEPIGFAGLRRLDDKVLELKrLYVLPEYRGKGIGKALLEALLEWARER-GCT 93

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446464664 109 YITLSVATFNERAIKVYKRAGFEAVGTFIQKTNG 142
Cdd:COG0454   94 ALELDTLDGNPAAIRFYERLGFKEIERYVAYVGG 127
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-130 4.18e-09

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: 51.36  E-value: 4.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664   18 YNWYYEGKYSFYDIEADEEDLDEFLHgesRGDHTFSVKQNGILIGFFTVCKMNDG---TVDIGLGMRPDITGNGFGLQFV 94
Cdd:pfam00583   5 YELLSEEFPEPWPDEPLDLLEDWDED---ASEGFFVAEEDGELVGFASLSIIDDEppvGEIEGLAVAPEYRGKGIGTALL 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446464664   95 NAGLAFSEEKyGCNYITLSVATFNERAIKVYKRAGF 130
Cdd:pfam00583  82 QALLEWARER-GCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 78-136 9.24e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 47.34  E-value: 9.24e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446464664  78 LGMRPDITGNGFGLQFVNAGLAFSEEKyGCNYITLSVATFNERAIKVYKRAGFEAVGTF 136
Cdd:COG0456   19 LAVDPEYRGRGIGRALLEAALERARER-GARRLRLEVREDNEAAIALYEKLGFEEVGER 76
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 5-131 6.94e-07

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 45.80  E-value: 6.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664    5 YTVMKQEEAEEIAYNWYYegkysfyDIEADEEDLDEFLHGESRGD-HTFSV--KQNGIlIGFFTVCKMND--GTVDIGLG 79
Cdd:pfam13302  16 FELLSDPEVMRYGVPWPL-------TLEEAREWLARIWAADEAERgYGWAIelKDTGF-IGSIGLYDIDGepERAELGYW 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446464664   80 MRPDITGNGFGLQFVNAGLAFSEEKYGCNYITLSVATFNERAIKVYKRAGFE 131
Cdd:pfam13302  88 LGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
32-136 6.34e-06

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 43.54  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664  32 EADEEDLDEFLHGESRGDHTFSVKQNGILIGF--FTVCKMNDGTVDIGLGM---RPDITGNGFGLQFVNAGLAFSEEKyG 106
Cdd:COG3153   22 PGREAELVDRLREDPAAGLSLVAEDDGEIVGHvaLSPVDIDGEGPALLLGPlavDPEYRGQGIGRALMRAALEAARER-G 100

                         90       100       110
                 ....*....|....*....|....*....|
gi 446464664 107 CNYITLSVatfNERAIKVYKRAGFEAVGTF 136
Cdd:COG3153  101 ARAVVLLG---DPSLLPFYERFGFRPAGEL 127
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
76-136 7.70e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 41.82  E-value: 7.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446464664  76 IGLGMRPDITGNGFGLQFVNAGLAFSEEKyGCNYITLSVATFNERAIKVYKRAGFEAVGTF 136
Cdd:COG3393   19 SGVYTHPEYRGRGLASALVAALAREALAR-GARTPFLYVDADNPAARRLYERLGFRPVGEY 78
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 52-138 1.33e-05

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: 42.73  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664   52 FSVKQNGILIGFFTVCKMNDGT--VDIGLGMRPDITGnGFGLQFVNAGLAFSEEKYGCNYITLSVATFNERAIKVYKRAG 129
Cdd:TIGR03585  54 WIVCQESRPIGVISFTDINLVHksAFWGIYANPFCKP-GVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFG 132


                  ....*....
gi 446464664  130 FEAVGTFIQ 138
Cdd:TIGR03585 133 FEREGVFRQ 141
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 56-134 5.76e-05

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 40.39  E-value: 5.76e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446464664   56 QNGILIGFFTVCKMNDGTVDIGLGMRPDITGNGFGLQFVNAGLAFSEEKyGCNYITLSVATFNERAIKVYKRAGFEAVG 134
Cdd:TIGR01575  38 IGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKGR-GVNEIFLEVRVSNIAAQALYKKLGFNEIA 115
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 32-134 8.27e-04

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 37.28  E-value: 8.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664  32 EADEEDLDEFLH------GESRGDHTFSVKQNGILIGFFTVCKMNDGTVDIG-LGMRPDITGNGFGLQFVNAGLAFSEEK 104
Cdd:COG1246    5 PATPDDVPAILElirpyaLEEEIGEFWVAEEDGEIVGCAALHPLDEDLAELRsLAVHPDYRGRGIGRRLLEALLAEAREL 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 446464664 105 yGCNYITLSVatfNERAIKVYKRAGFEAVG 134
Cdd:COG1246   85 -GLKRLFLLT---TSAAIHFYEKLGFEEID 110
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 47-131 7.59e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 33.97  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464664   47 RGDHTFSVKQNGILIGFFTVCKMNDGTVDIGLGM--RPDITGNGFGLQFVNAgLAFSEEKYGCNYITLSVatfNERAIKV 124
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAELRLavHPEYRGQGIGRALLEA-AEAAAKEGGIKLLELET---TNRAAAF 76


                  ....*..
gi 446464664  125 YKRAGFE 131
Cdd:pfam13508  77 YEKLGFE 83
 
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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