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Conserved domains on  [gi|1560390128|gb|RXA76173|]
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ribosomal-protein-alanine N-acetyltransferase [Enterococcus hirae]

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 ...
 17-145 2.98e-41

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 TIGR01575:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 131  Bit Score: 134.38  E-value: 2.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  17 LWALCEEAYEHgsPWTKDQFLMDIQQPHTQYYLLVENSLLQGFIGYSKVIDETEITNIAVAKKLQKKGYARQLLRFLLDR 96
Cdd:TIGR01575   5 VLEIEAAAFAF--PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1560390128  97 EKQAGTYNVYLEVRTSNLAARHLYQSEKFRELGKRKSYYHDPVEDAIIM 145
Cdd:TIGR01575  83 AKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 17-145 2.98e-41

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: 134.38  E-value: 2.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  17 LWALCEEAYEHgsPWTKDQFLMDIQQPHTQYYLLVENSLLQGFIGYSKVIDETEITNIAVAKKLQKKGYARQLLRFLLDR 96
Cdd:TIGR01575   5 VLEIEAAAFAF--PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1560390128  97 EKQAGTYNVYLEVRTSNLAARHLYQSEKFRELGKRKSYYHDPVEDAIIM 145
Cdd:TIGR01575  83 AKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 22-145 3.09e-22

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 86.14  E-value: 3.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  22 EEAYE-----HGSPWTKDQFLMDiQQPHTQYYLLVENSLLQGFIGYSKVIDETEITNIAVAKKLQKKGYARQLLRFLLDR 96
Cdd:PRK09491   13 PAAYHieqraHAFPWSEKTFASN-QGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDE 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1560390128  97 EKQAGTYNVYLEVRTSNLAARHLYQSEKFRELGKRKSYYHDPV--EDAIIM 145
Cdd:PRK09491   92 LEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADgrEDAIIM 142
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 58-150 9.94e-22

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 83.55  E-value: 9.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  58 GFIGYSKVI--DETEITNIAVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLEVRTSNLAARHLYQSEKFRELGKRKSYY 135
Cdd:COG0456     1 GFALLGLVDggDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                          90
                  ....*....|....*
gi 1560390128 136 HDpveDAIIMSTKLK 150
Cdd:COG0456    81 GD---DALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-121 4.03e-14

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: 64.46  E-value: 4.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  18 WALCEEAYEHGSPWTKDQFLMDIQQPHTQYYLLVENSLLqGFIGYSKV---IDETEITNIAVAKKLQKKGYARQLLRFLL 94
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELV-GFASLSIIddePPVGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100
                  ....*....|....*....|....*..
gi 1560390128  95 DREKQAGTYNVYLEVRTSNLAARHLYQ 121
Cdd:pfam00583  86 EWARERGCERIFLEVAADNLAAIALYE 112
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-108 3.86e-07

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: 44.96  E-value: 3.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390128  47 YYLLVENSLLQGFIGYSK---VIDETEITNIAVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLE 108
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 17-145 2.98e-41

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: 134.38  E-value: 2.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  17 LWALCEEAYEHgsPWTKDQFLMDIQQPHTQYYLLVENSLLQGFIGYSKVIDETEITNIAVAKKLQKKGYARQLLRFLLDR 96
Cdd:TIGR01575   5 VLEIEAAAFAF--PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELIDE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1560390128  97 EKQAGTYNVYLEVRTSNLAARHLYQSEKFRELGKRKSYYHDPVEDAIIM 145
Cdd:TIGR01575  83 AKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 22-145 3.09e-22

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 86.14  E-value: 3.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  22 EEAYE-----HGSPWTKDQFLMDiQQPHTQYYLLVENSLLQGFIGYSKVIDETEITNIAVAKKLQKKGYARQLLRFLLDR 96
Cdd:PRK09491   13 PAAYHieqraHAFPWSEKTFASN-QGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDE 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1560390128  97 EKQAGTYNVYLEVRTSNLAARHLYQSEKFRELGKRKSYYHDPV--EDAIIM 145
Cdd:PRK09491   92 LEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADgrEDAIIM 142
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 58-150 9.94e-22

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 83.55  E-value: 9.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  58 GFIGYSKVI--DETEITNIAVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLEVRTSNLAARHLYQSEKFRELGKRKSYY 135
Cdd:COG0456     1 GFALLGLVDggDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                          90
                  ....*....|....*
gi 1560390128 136 HDpveDAIIMSTKLK 150
Cdd:COG0456    81 GD---DALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-121 4.03e-14

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: 64.46  E-value: 4.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  18 WALCEEAYEHGSPWTKDQFLMDIQQPHTQYYLLVENSLLqGFIGYSKV---IDETEITNIAVAKKLQKKGYARQLLRFLL 94
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELV-GFASLSIIddePPVGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100
                  ....*....|....*....|....*..
gi 1560390128  95 DREKQAGTYNVYLEVRTSNLAARHLYQ 121
Cdd:pfam00583  86 EWARERGCERIFLEVAADNLAAIALYE 112
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 39-150 2.17e-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: 57.69  E-value: 2.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  39 DIQQPHTQYYLLVENSLLQGFIGYSKVIDET-EITNIAVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLEvrtSNLAAR 117
Cdd:COG1246    22 ALEEEIGEFWVAEEDGEIVGCAALHPLDEDLaELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL---TTSAAI 98

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1560390128 118 HLYQSEKFRELGKRKSYYHDPVE-DAIIMSTKLK 150
Cdd:COG1246    99 HFYEKLGFEEIDKEDLPYAKVWQrDSVVMEKDLE 132
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
4-149 5.05e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 57.31  E-value: 5.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128   4 TKSDFEDeqlascLWALCEEAYEHGS------PWTKDQ---FLMDIQQPHTQYYLLVENSLLQGFI---------GYSKV 65
Cdd:COG1247     8 TPEDAPA------IAAIYNEAIAEGTatfetePPSEEEreaWFAAILAPGRPVLVAEEDGEVVGFAslgpfrprpAYRGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  66 IDETeitnIAVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLEVRTSNLAARHLYQSEKFRELGKRKS--YYHDPVEDAI 143
Cdd:COG1247    82 AEES----IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEvgFKFGRWLDLV 157


                  ....*.
gi 1560390128 144 IMSTKL 149
Cdd:COG1247   158 LMQKRL 163
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
69-129 3.04e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 53.37  E-value: 3.04e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390128  69 TEITNIAVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLEVRTSNLAARHLYQSEKFRELG 129
Cdd:COG3393    16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 43-127 1.12e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.07  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  43 PHTQYYLLVENSLLQGFIGYSKVIDETEIT--NIAVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLEVRTsnlAARHLY 120
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN---RAAAFY 77


                  ....*..
gi 1560390128 121 QSEKFRE 127
Cdd:pfam13508  78 EKLGFEE 84
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 38-129 1.29e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 53.13  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  38 MDIQQPHTQYYLLVENSLLQGFIGYSKVIDET-EITNIAVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLEVRTSNLAA 116
Cdd:COG0454    27 MEGSLAGAEFIAVDDKGEPIGFAGLRRLDDKVlELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAA 106

                          90
                  ....*....|...
gi 1560390128 117 RHLYQSEKFRELG 129
Cdd:COG0454   107 IRFYERLGFKEIE 119
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-146 3.39e-09

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: 52.69  E-value: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128   4 TKSDFEDeqlascLWALCEEA----YEHGSPWTKDQFLMDIQ------QPHTQYYLLVENSL---LQGFIGYSKVIDETE 70
Cdd:COG1670    14 RPEDAEA------LAELLNDPevarYLPGPPYSLEEARAWLErlladwADGGALPFAIEDKEdgeLIGVVGLYDIDRANR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  71 ITNIA--VAKKLQKKGYARQLLRFLLDR-EKQAGTYNVYLEVRTSNLAARHLYqsEK--FRELGKRKSYYH--DPVEDAI 143
Cdd:COG1670    88 SAEIGywLAPAYWGKGYATEALRALLDYaFEELGLHRVEAEVDPDNTASIRVL--EKlgFRLEGTLRDALVidGRYRDHV 165


                  ...
gi 1560390128 144 IMS 146
Cdd:COG1670   166 LYS 168
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-149 6.51e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.54  E-value: 6.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128   3 YTKSDFEDeqlascLWALCEEAYEHGspwTKDQFLMDIQQPHTQYYLLV--ENSLLQGFIGYSKVIDETE-----ITNIA 75
Cdd:COG3153     4 ATPEDAEA------IAALLRAAFGPG---REAELVDRLREDPAAGLSLVaeDDGEIVGHVALSPVDIDGEgpallLGPLA 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560390128  76 VAKKLQKKGYARQLLRFLLDREKQAGTYNVYLevrTSNLAARHLYQSEKFRELGKrksYYHDPVEDAIIMSTKL 149
Cdd:COG3153    75 VDPEYRGQGIGRALMRAALEAARERGARAVVL---LGDPSLLPFYERFGFRPAGE---LGLTLGPDEVFLAKEL 142
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-108 3.86e-07

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: 44.96  E-value: 3.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390128  47 YYLLVENSLLQGFIGYSK---VIDETEITNIAVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLE 108
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 40-129 1.55e-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: 44.57  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  40 IQQPHTQYYLLVENSLLQGFIGyskVIDETEITNIAVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLEVRTSNlAARHL 119
Cdd:pfam13673  26 IDQGEYFFFVAFEGGQIVGVIA---LRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASP-YAVPF 101

                          90
                  ....*....|
gi 1560390128 120 YQSEKFRELG 129
Cdd:pfam13673 102 YEKLGFRATG 111
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
74-129 1.27e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.40  E-value: 1.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1560390128  74 IAVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLEVRTSnlaARHLYQSEKFRELG 129
Cdd:COG2153    64 VAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFVPVG 116
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
58-117 1.73e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 36.81  E-value: 1.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560390128  58 GFIGYSkvideteitniaVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLEVRTSNLAAR 117
Cdd:COG3981    93 GHIGYG------------VRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASR 140
PRK03624 PRK03624
putative acetyltransferase; Provisional
 75-131 3.28e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 35.67  E-value: 3.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560390128  75 AVAKKLQKKGYARQLLRFLLDREKQAGTYNVYLEVRTSNLAARHLYQSEKFRE-----LGKR 131
Cdd:PRK03624   75 AVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEqdrisLGKR 136
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 46-101 3.51e-03

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 34.42  E-value: 3.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560390128  46 QYYLLVENSLLQGFIGYSK-----VIDETEitniaVAKKLQKKGYARQLLRFLLDREKQAG 101
Cdd:pfam14542   1 RFEIRVDGGAEVAFLTYRRgdgvlIITHTE-----VPPALRGQGIASKLVKAALDDAREEG 56
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 67-131 5.48e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 34.23  E-value: 5.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560390128  67 DETEITNIAVAKKLQKKGYARQLLRFLLDREKQAGtYNVYLEVRTSNLAARHLYQSEKFRELGKR 131
Cdd:pfam08445  20 PGGELGALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGFRKIDET 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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