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Conserved domains on  [gi|488056443|ref|WP_002127840|]
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MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10003213)

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
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 49-112 2.51e-11

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: 56.92  E-value: 2.51e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488056443  49 GCIGIALIHTNRARMCHIAVDEKYRNQGIALQMIKEII---REYELTYIEAETDTEAVGFYKKCNFK 112
Cdd:COG1246   41 GCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLaeaRELGLKRLFLLTTSAAIHFYEKLGFE 107
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 49-112 2.51e-11

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: 56.92  E-value: 2.51e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488056443  49 GCIGIALIHTNRARMCHIAVDEKYRNQGIALQMIKEII---REYELTYIEAETDTEAVGFYKKCNFK 112
Cdd:COG1246   41 GCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLaeaRELGLKRLFLLTTSAAIHFYEKLGFE 107
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 49-113 3.18e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.15  E-value: 3.18e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488056443   49 GCIGIALI-HTNRARMCHIAVDEKYRNQGIA---LQMIKEIIREYELTYIEAETDTEAVGFYKKCNFKI 113
Cdd:pfam13508  16 GFAALLPLdDEGALAELRLAVHPEYRGQGIGralLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 2-120 9.75e-06

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: 41.93  E-value: 9.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488056443    2 LQRVEHLEidpikkVLKHATGPSEASLFKAVSMYKNDQAVLYKYGNkgCIGIALIHTNR--ARMCHIAVDEKYRNQGIAL 79
Cdd:TIGR01575   2 LKAVLEIE------AAAFAFPWTEAQFAEELANYHLCYLLARIGGK--VVGYAGVQIVLdeAHILNIAVKPEYQGQGIGR 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 488056443   80 QMIKEIIREYE---LTYIEAE---TDTEAVGFYKKCNFKIESLGEKY 120
Cdd:TIGR01575  74 ALLRELIDEAKgrgVNEIFLEvrvSNIAAQALYKKLGFNEIAIRRNY 120
PRK10140 PRK10140
N-acetyltransferase;
58-120 2.62e-04

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 38.81  E-value: 2.62e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488056443  58 TNRARMCHIA-----VDEKYRNQGIALQMIKEII---------REYELTYIeaeTDTE-AVGFYKKCNFKIESLGEKY 120
Cdd:PRK10140  71 QQRPRRSHVAdfgicVDSRWKNRGVASALMREMIemcdnwlrvDRIELTVF---VDNApAIKVYKKYGFEIEGTGKKY 145
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 49-88 2.21e-03

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 34.56  E-value: 2.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 488056443  49 GCIGIALI--HTNRARMCHIAVDEKYRNQGIALQMIKEIIRE 88
Cdd:cd04301   12 GFASLSPDgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
 
Name Accession Description Interval E-value
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 49-112 2.51e-11

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: 56.92  E-value: 2.51e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488056443  49 GCIGIALIHTNRARMCHIAVDEKYRNQGIALQMIKEII---REYELTYIEAETDTEAVGFYKKCNFK 112
Cdd:COG1246   41 GCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLaeaRELGLKRLFLLTTSAAIHFYEKLGFE 107
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 49-113 3.18e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.15  E-value: 3.18e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488056443   49 GCIGIALI-HTNRARMCHIAVDEKYRNQGIA---LQMIKEIIREYELTYIEAETDTEAVGFYKKCNFKI 113
Cdd:pfam13508  16 GFAALLPLdDEGALAELRLAVHPEYRGQGIGralLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 49-127 3.82e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 47.73  E-value: 3.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488056443  49 GCIGIALIHT-NRARMCHIAVDEKYRNQGIALQMIKEII---REYELTYIEAETDTE---AVGFYKKCNFKIESLGEKYL 121
Cdd:COG0456    1 GFALLGLVDGgDEAEIEDLAVDPEYRGRGIGRALLEAALeraRERGARRLRLEVREDneaAIALYEKLGFEEVGERPNYY 80


                 ....*.
gi 488056443 122 GVERFY 127
Cdd:COG0456   81 GDDALV 86
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
35-121 1.79e-07

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 46.72  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488056443  35 YKNDQAVlykygnkGCIGIALIHTNRARMCHIAVDEKYRNQGIALQMIKEII---REYELTYIEAETDTEAVGFYKKCNF 111
Cdd:COG2153   40 YDDGELV-------ATARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIeeaRERGARRIVLSAQAHAVGFYEKLGF 112

                         90
                 ....*....|
gi 488056443 112 KIEslGEKYL 121
Cdd:COG2153  113 VPV--GEEFL 120
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 9-124 4.97e-07

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 45.81  E-value: 4.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488056443   9 EIDPIKKVLKHATgpSEASLFKAVSMYKNDQAVLYKYGNK--GCIGIALIHTNRARMCHIAVDEKYRNQGIALQMIKEII 86
Cdd:COG0454    7 TPEDINFILLIEA--LDAELKAMEGSLAGAEFIAVDDKGEpiGFAGLRRLDDKVLELKRLYVLPEYRGKGIGKALLEALL 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488056443  87 ---REYELTYIEAET---DTEAVGFYKKCNFKIESLGEKYLGVE 124
Cdd:COG0454   85 ewaRERGCTALELDTldgNPAAIRFYERLGFKEIERYVAYVGGE 128
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 37-111 8.31e-07

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: 44.82  E-value: 8.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488056443   37 NDQAVLYKYGNK--GCIGIALI--HTNRARMCHIAVDEKYRNQGIALQMIKEII---REYELTYIEAETDTE---AVGFY 106
Cdd:pfam00583  32 SEGFFVAEEDGElvGFASLSIIddEPPVGEIEGLAVAPEYRGKGIGTALLQALLewaRERGCERIFLEVAADnlaAIALY 111


                  ....*
gi 488056443  107 KKCNF 111
Cdd:pfam00583 112 EKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
49-127 3.63e-06

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 43.54  E-value: 3.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488056443  49 GCIGIALIH----TNRARMCHIAVDEKYRNQGIALQMIKEII---REYELTYIEAETDTEAVGFYKKCNFKIESLGEKYL 121
Cdd:COG3153   52 GHVALSPVDidgeGPALLLGPLAVDPEYRGQGIGRALMRAALeaaRERGARAVVLLGDPSLLPFYERFGFRPAGELGLTL 131


                 ....*.
gi 488056443 122 GVERFY 127
Cdd:COG3153  132 GPDEVF 137
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 2-120 9.75e-06

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: 41.93  E-value: 9.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488056443    2 LQRVEHLEidpikkVLKHATGPSEASLFKAVSMYKNDQAVLYKYGNkgCIGIALIHTNR--ARMCHIAVDEKYRNQGIAL 79
Cdd:TIGR01575   2 LKAVLEIE------AAAFAFPWTEAQFAEELANYHLCYLLARIGGK--VVGYAGVQIVLdeAHILNIAVKPEYQGQGIGR 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 488056443   80 QMIKEIIREYE---LTYIEAE---TDTEAVGFYKKCNFKIESLGEKY 120
Cdd:TIGR01575  74 ALLRELIDEAKgrgVNEIFLEvrvSNIAAQALYKKLGFNEIAIRRNY 120
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 51-112 1.00e-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: 41.87  E-value: 1.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488056443   51 IGIALIhTNRARMCHIAVDEKYRNQGIALQMIKEIIREYE-----LTYIEAETDTEAVGFYKKCNFK 112
Cdd:pfam13673  43 VGVIAL-RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEkdgikLSELTVNASPYAVPFYEKLGFR 108
PRK10140 PRK10140
N-acetyltransferase;
58-120 2.62e-04

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 38.81  E-value: 2.62e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488056443  58 TNRARMCHIA-----VDEKYRNQGIALQMIKEII---------REYELTYIeaeTDTE-AVGFYKKCNFKIESLGEKY 120
Cdd:PRK10140  71 QQRPRRSHVAdfgicVDSRWKNRGVASALMREMIemcdnwlrvDRIELTVF---VDNApAIKVYKKYGFEIEGTGKKY 145
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 49-88 2.21e-03

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 34.56  E-value: 2.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 488056443  49 GCIGIALI--HTNRARMCHIAVDEKYRNQGIALQMIKEIIRE 88
Cdd:cd04301   12 GFASLSPDgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
49-112 3.79e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 34.11  E-value: 3.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488056443  49 GCIGIALIHTNRARMCHIAVDEKYRNQGIALQMIKEIIREY------ELTYIEAETDTEAVGFYKKCNFK 112
Cdd:COG3393    4 AMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREAlargarTPFLYVDADNPAARRLYERLGFR 73
 
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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