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Conserved domains on  [gi|507061972|ref|WP_016132814|]
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GNAT family N-acetyltransferase [Bacillus cereus group sp. BfR-BA-01315]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 12-132 1.85e-14

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member pfam13527:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 124  Bit Score: 68.37  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507061972   12 VEESKKEPLFQLFEEVFRIPVQtlqnFEANGFWDTTYKPFSYL---QEGQVIANVSMFSLPMFVNGERIYAAGIQSVMTH 88
Cdd:pfam13527   4 LTEDEFDEVLRLLEYAFQDEDS----PELREYFRPLLEEGRVLgafDDGELVSTLALYPFELNVPGKTLPAAGITGVATY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 507061972   89 PEYRRKGLMKQLLCKVLQEI-DTKYECAILFTEKPELYEPFGFRV 132
Cdd:pfam13527  80 PEYRGRGVMSRLLRRSLEEMrERGVPLSFLYPSSYPIYRRFGYEI 124
 
Name Accession Description Interval E-value
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-132 1.85e-14

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 68.37  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507061972   12 VEESKKEPLFQLFEEVFRIPVQtlqnFEANGFWDTTYKPFSYL---QEGQVIANVSMFSLPMFVNGERIYAAGIQSVMTH 88
Cdd:pfam13527   4 LTEDEFDEVLRLLEYAFQDEDS----PELREYFRPLLEEGRVLgafDDGELVSTLALYPFELNVPGKTLPAAGITGVATY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 507061972   89 PEYRRKGLMKQLLCKVLQEI-DTKYECAILFTEKPELYEPFGFRV 132
Cdd:pfam13527  80 PEYRGRGVMSRLLRRSLEEMrERGVPLSFLYPSSYPIYRRFGYEI 124
Eis COG4552
Predicted acetyltransferase [General function prediction only];
11-130 6.00e-12

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 65.31  E-value: 6.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507061972  11 FVEESKKEPLFQLFEEVFRIPVqTLQNFEAngfWDTTYKPFSYL---QEGQVIANVSMFSLPMFVNGERIYAAGIQSVMT 87
Cdd:COG4552    5 PLTEDDLDAFARLLAYAFGPEP-DDEELEA---YRPLLEPGRVLgvfDDGELVGTLALYPFTLNVGGARVPMAGITGVAV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 507061972  88 HPEYRRKGLMKQLLCKVLQEI-DTKYECAILFTEKPELYEPFGF 130
Cdd:COG4552   81 APEHRRRGVARALLREALAELrERGQPLSALYPFEPGFYRRFGY 124
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-107 1.27e-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: 36.48  E-value: 1.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 507061972  51 FSYLQEGQVIANVSMFslpmfVNGERIYAAGIQSVMTHPEYRRKGLMKQLLCKVLQE 107
Cdd:cd04301    2 LVAEDDGEIVGFASLS-----PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
PTZ00330 PTZ00330
acetyltransferase; Provisional
 57-131 5.30e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 36.74  E-value: 5.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507061972  57 GQVIANVSMFSLPMFVNGERiyAAG-IQSVMTHPEYRRKGLMKQLLCKvLQEIDTKYEC--AIL-FTEKP-ELYEPFGFR 131
Cdd:PTZ00330  61 QRIVGTASLFVEPKFTRGGK--CVGhIEDVVVDPSYRGQGLGRALISD-LCEIARSSGCykVILdCTEDMvAFYKKLGFR 137
 
Name Accession Description Interval E-value
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-132 1.85e-14

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 68.37  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507061972   12 VEESKKEPLFQLFEEVFRIPVQtlqnFEANGFWDTTYKPFSYL---QEGQVIANVSMFSLPMFVNGERIYAAGIQSVMTH 88
Cdd:pfam13527   4 LTEDEFDEVLRLLEYAFQDEDS----PELREYFRPLLEEGRVLgafDDGELVSTLALYPFELNVPGKTLPAAGITGVATY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 507061972   89 PEYRRKGLMKQLLCKVLQEI-DTKYECAILFTEKPELYEPFGFRV 132
Cdd:pfam13527  80 PEYRGRGVMSRLLRRSLEEMrERGVPLSFLYPSSYPIYRRFGYEI 124
Eis COG4552
Predicted acetyltransferase [General function prediction only];
11-130 6.00e-12

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 65.31  E-value: 6.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507061972  11 FVEESKKEPLFQLFEEVFRIPVqTLQNFEAngfWDTTYKPFSYL---QEGQVIANVSMFSLPMFVNGERIYAAGIQSVMT 87
Cdd:COG4552    5 PLTEDDLDAFARLLAYAFGPEP-DDEELEA---YRPLLEPGRVLgvfDDGELVGTLALYPFTLNVGGARVPMAGITGVAV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 507061972  88 HPEYRRKGLMKQLLCKVLQEI-DTKYECAILFTEKPELYEPFGF 130
Cdd:COG4552   81 APEHRRRGVARALLREALAELrERGQPLSALYPFEPGFYRRFGY 124
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
80-140 3.65e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.60  E-value: 3.65e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507061972  80 AGIQSVMTHPEYRRKGLMKQLLCKVLQEI-DTKYECAILFTEK--PE---LYEPFGFRVVQEYLMTL 140
Cdd:COG3393   16 AEISGVYTHPEYRGRGLASALVAALAREAlARGARTPFLYVDAdnPAarrLYERLGFRPVGEYATVL 82
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
20-146 4.61e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 51.24  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507061972  20 LFQLFEEVFRIPV--QTLQNFEANGFWDTTykpFSYLQEGQVIANVSMFslPMFVNGERiYAAGIQSVMTHPEYRRKGLM 97
Cdd:COG3153   12 IAALLRAAFGPGReaELVDRLREDPAAGLS---LVAEDDGEIVGHVALS--PVDIDGEG-PALLLGPLAVDPEYRGQGIG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 507061972  98 KQLLCKVLQEIDTK-YECAILFTEKP--ELYEPFGFRVVQEYLMTLSYENIL 146
Cdd:COG3153   86 RALMRAALEAARERgARAVVLLGDPSllPFYERFGFRPAGELGLTLGPDEVF 137
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-130 2.32e-04

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: 40.19  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507061972   18 EPLFQLFEEVFRIPVQTLQNFE-ANGFWDTTYKPFSYLQEGQVIANVSMFslpmfVNGERIYAAGIQSVMTHPEYRRKGL 96
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLlEDWDEDASEGFFVAEEDGELVGFASLS-----IIDDEPPVGEIEGLAVAPEYRGKGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 507061972   97 MKQLLCKVLQE-IDTKYECAILFTEKP-----ELYEPFGF 130
Cdd:pfam00583  77 GTALLQALLEWaRERGCERIFLEVAADnlaaiALYEKLGF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 51-132 3.34e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 38.59  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507061972   51 FSYLQEGQVIANVsmfslpMFVNGERIYAAGIQSVMTHPEYRRKGLMKQLL---CKVLQEIDTKYECAILFTEKPELYEP 127
Cdd:pfam13508   6 FVAEDDGKIVGFA------ALLPLDDEGALAELRLAVHPEYRGQGIGRALLeaaEAAAKEGGIKLLELETTNRAAAFYEK 79


                  ....*
gi 507061972  128 FGFRV 132
Cdd:pfam13508  80 LGFEE 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 82-135 7.28e-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: 38.82  E-value: 7.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 507061972  82 IQSVMTHPEYRRKGLMKQLLCKVLQEIDTK-YECAILFT--EKPELYEPFGFRVVQE 135
Cdd:COG1246   55 LRSLAVHPDYRGRGIGRRLLEALLAEARELgLKRLFLLTtsAAIHFYEKLGFEEIDK 111
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 71-135 1.23e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 37.33  E-value: 1.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507061972  71 FVNGERIYAAG---IQSVMTHPEYRRKGLMKQLLCKVLQEI-DTKYECAILFTEKP-----ELYEPFGFRVVQE 135
Cdd:COG0456    2 FALLGLVDGGDeaeIEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEVREDneaaiALYEKLGFEEVGE 75
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-107 1.27e-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: 36.48  E-value: 1.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 507061972  51 FSYLQEGQVIANVSMFslpmfVNGERIYAAGIQSVMTHPEYRRKGLMKQLLCKVLQE 107
Cdd:cd04301    2 LVAEDDGEIVGFASLS-----PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
PTZ00330 PTZ00330
acetyltransferase; Provisional
 57-131 5.30e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 36.74  E-value: 5.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507061972  57 GQVIANVSMFSLPMFVNGERiyAAG-IQSVMTHPEYRRKGLMKQLLCKvLQEIDTKYEC--AIL-FTEKP-ELYEPFGFR 131
Cdd:PTZ00330  61 QRIVGTASLFVEPKFTRGGK--CVGhIEDVVVDPSYRGQGLGRALISD-LCEIARSSGCykVILdCTEDMvAFYKKLGFR 137
 
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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