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Conserved domains on  [gi|489513191|ref|WP_003418034|]
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MULTISPECIES: ribosomal protein S18-alanine N-acetyltransferase [Mycobacterium]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11492820)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 17-150 2.11e-57

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: 175.21  E-value: 2.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   17 DAQRCAELEAQLFVGddPWPPAAFNRELASPHNHYVGARSGGTLVGYAGisrlGRTPPFEYEVHTIGVDPAYQGRGIGRR 96
Cdd:TIGR01575   1 DLKAVLEIEAAAFAF--PWTEAQFAEELANYHLCYLLARIGGKVVGYAG----VQIVLDEAHILNIAVKPEYQGQGIGRA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489513191   97 LLRELLDFARG---GVVYLEVRTDNDAALALYRSVGFQRVGLRRRYYRVSGADAYTM 150
Cdd:TIGR01575  75 LLRELIDEAKGrgvNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 17-150 2.11e-57

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: 175.21  E-value: 2.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   17 DAQRCAELEAQLFVGddPWPPAAFNRELASPHNHYVGARSGGTLVGYAGisrlGRTPPFEYEVHTIGVDPAYQGRGIGRR 96
Cdd:TIGR01575   1 DLKAVLEIEAAAFAF--PWTEAQFAEELANYHLCYLLARIGGKVVGYAG----VQIVLDEAHILNIAVKPEYQGQGIGRA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489513191   97 LLRELLDFARG---GVVYLEVRTDNDAALALYRSVGFQRVGLRRRYYRVSGADAYTM 150
Cdd:TIGR01575  75 LLRELIDEAKGrgvNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 62-153 5.72e-23

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 86.63  E-value: 5.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191  62 GYAGISRLGRTPpfEYEVHTIGVDPAYQGRGIGRRLLRELLDFAR---GGVVYLEVRTDNDAALALYRSVGFQRVGLRRR 138
Cdd:COG0456    1 GFALLGLVDGGD--EAEIEDLAVDPEYRGRGIGRALLEAALERARergARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78

                         90
                 ....*....|....*
gi 489513191 139 YYrvsGADAYTMRRD 153
Cdd:COG0456   79 YY---GDDALVMEKE 90
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 23-130 9.65e-21

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: 81.80  E-value: 9.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   23 ELEAQLFVGDDPWPPAAFNRELASPHNHYVGARSGGTLVGYAGISRLGRTPPfEYEVHTIGVDPAYQGRGIGRRLLRELL 102
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP-VGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 489513191  103 DFARG---GVVYLEVRTDNDAALALYRSVGF 130
Cdd:pfam00583  86 EWARErgcERIFLEVAADNLAAIALYEKLGF 116
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 82-140 1.90e-18

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 76.51  E-value: 1.90e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489513191  82 IGVDPAYQGRGIGRRLLRELLDFARG-GVV--YLEVRTDNDAALALYRSVGFQRVGLRRRYY 140
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKrGVAtlWLEVRASNAAAIALYESLGFNEVTIRRNYY 130
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-106 9.68e-12

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: 56.90  E-value: 9.68e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489513191  51 YVGARSGGTLVGYAGISRLGRTPPfEYEVHTIGVDPAYQGRGIGRRLLRELLDFAR 106
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGD-TAYIGDLAVLPEYRGKGIGSALLEAAEEEAR 55
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 17-150 2.11e-57

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: 175.21  E-value: 2.11e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   17 DAQRCAELEAQLFVGddPWPPAAFNRELASPHNHYVGARSGGTLVGYAGisrlGRTPPFEYEVHTIGVDPAYQGRGIGRR 96
Cdd:TIGR01575   1 DLKAVLEIEAAAFAF--PWTEAQFAEELANYHLCYLLARIGGKVVGYAG----VQIVLDEAHILNIAVKPEYQGQGIGRA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489513191   97 LLRELLDFARG---GVVYLEVRTDNDAALALYRSVGFQRVGLRRRYYRVSGADAYTM 150
Cdd:TIGR01575  75 LLRELIDEAKGrgvNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 62-153 5.72e-23

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 86.63  E-value: 5.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191  62 GYAGISRLGRTPpfEYEVHTIGVDPAYQGRGIGRRLLRELLDFAR---GGVVYLEVRTDNDAALALYRSVGFQRVGLRRR 138
Cdd:COG0456    1 GFALLGLVDGGD--EAEIEDLAVDPEYRGRGIGRALLEAALERARergARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78

                         90
                 ....*....|....*
gi 489513191 139 YYrvsGADAYTMRRD 153
Cdd:COG0456   79 YY---GDDALVMEKE 90
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
8-153 5.64e-21

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 83.51  E-value: 5.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   8 VTIGALTRADAQRCAELEAQLFVG------DDPWPPA---AFNRELASPHNHYVGARSGGTLVGYAGISRLGRTPPFEYE 78
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEgtatfeTEPPSEEereAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191  79 V-HTIGVDPAYQGRGIGRRLLRELLDFARG---GVVYLEVRTDNDAALALYRSVGFQRVGLRRRYYRVSGA--DAYTMRR 152
Cdd:COG1247   82 AeESIYVDPDARGRGIGRALLEALIERARArgyRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRwlDLVLMQK 161


                 .
gi 489513191 153 D 153
Cdd:COG1247  162 R 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 23-130 9.65e-21

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: 81.80  E-value: 9.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   23 ELEAQLFVGDDPWPPAAFNRELASPHNHYVGARSGGTLVGYAGISRLGRTPPfEYEVHTIGVDPAYQGRGIGRRLLRELL 102
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP-VGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 489513191  103 DFARG---GVVYLEVRTDNDAALALYRSVGF 130
Cdd:pfam00583  86 EWARErgcERIFLEVAADNLAAIALYEKLGF 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-152 8.02e-20

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: 80.81  E-value: 8.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   1 MTADTEPVTIGALTRADAQRCAEL----EAQLFVGDDPWPPAAFNRELASPHNHY---------VGARSGGTLVGYAGIS 67
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELlndpEVARYLPGPPYSLEEARAWLERLLADWadggalpfaIEDKEDGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191  68 RLGRTPPfEYEVHtIGVDPAYQGRGIGRRLLRELLDFARGGV----VYLEVRTDNDAALALYRSVGFQRVGLRRRYYRVS 143
Cdd:COG1670   81 DIDRANR-SAEIG-YWLAPAYWGKGYATEALRALLDYAFEELglhrVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVID 158

                        170
                 ....*....|.
gi 489513191 144 GA--DAYTMRR 152
Cdd:COG1670  159 GRyrDHVLYSL 169
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 82-140 1.90e-18

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 76.51  E-value: 1.90e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489513191  82 IGVDPAYQGRGIGRRLLRELLDFARG-GVV--YLEVRTDNDAALALYRSVGFQRVGLRRRYY 140
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKrGVAtlWLEVRASNAAAIALYESLGFNEVTIRRNYY 130
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
12-153 1.57e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 71.65  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191  12 ALTRADAQRCAELEAQLFVGDDPWPPAAFNRELASPHNHYVgARSGGTLVGYAGISRLGRTPPFE-YEVHTIGVDPAYQG 90
Cdd:COG3153    3 PATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSLV-AEDDGEIVGHVALSPVDIDGEGPaLLLGPLAVDPEYRG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489513191  91 RGIGRRLLRELLDFARG-GVVYLEVRTDNDaALALYRSVGFQRVGlrrRYYRVSGADAYTMRRD 153
Cdd:COG3153   82 QGIGRALMRAALEAARErGARAVVLLGDPS-LLPFYERFGFRPAG---ELGLTLGPDEVFLAKE 141
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 47-132 1.72e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 67.09  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   47 PHNHYVGARSGGTLVGYAGISRLGRTPPFEYevHTIGVDPAYQGRGIGRRLLRELLDFARGGVVYLEVRTDNDAALALYR 126
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAE--LRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYE 78


                  ....*.
gi 489513191  127 SVGFQR 132
Cdd:pfam13508  79 KLGFEE 84
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 50-134 2.05e-15

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 68.54  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191  50 HYVGARSGGTLVGYAGISRLGRTPPfeyEVHTIGVDPAYQGRGIGRRLLRELLDFARG---GVVYLEVRTDNDAALALYR 126
Cdd:COG0454   35 EFIAVDDKGEPIGFAGLRRLDDKVL---ELKRLYVLPEYRGKGIGKALLEALLEWARErgcTALELDTLDGNPAAIRFYE 111


                 ....*...
gi 489513191 127 SVGFQRVG 134
Cdd:COG0454  112 RLGFKEIE 119
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 44-153 2.44e-15

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: 68.09  E-value: 2.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191  44 LASPHNHYVGARSGGTLVGYAGISRLGRTppfEYEVHTIGVDPAYQGRGIGRRLLRELLDFARG-GVVYLEVRTdNDAAL 122
Cdd:COG1246   23 LEEEIGEFWVAEEDGEIVGCAALHPLDED---LAELRSLAVHPDYRGRGIGRRLLEALLAEARElGLKRLFLLT-TSAAI 98

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489513191 123 ALYRSVGFQRVGLRRR-YYRVSGADAYTMRRD 153
Cdd:COG1246   99 HFYEKLGFEEIDKEDLpYAKVWQRDSVVMEKD 130
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 36-134 9.15e-15

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: 66.53  E-value: 9.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   36 PPAAFNRELASPHNHYVGARSGGTLVGYAGISRLGRtppfeyeVHTIGVDPAYQGRGIGRRLLRELLDFAR---GGVVYL 112
Cdd:pfam13673  18 SPEALRERIDQGEYFFFVAFEGGQIVGVIALRDRGH-------ISLLFVDPDYQGQGIGKALLEAVEDYAEkdgIKLSEL 90

                          90       100
                  ....*....|....*....|..
gi 489513191  113 EVRTDNdAALALYRSVGFQRVG 134
Cdd:pfam13673  91 TVNASP-YAVPFYEKLGFRATG 111
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
60-134 1.39e-12

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 59.54  E-value: 1.39e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489513191  60 LVGYAGIsrlGRTPPFEYEVHTIGVDPAYQGRGIGRRLLRELLDFAR---GGVVYLEVRTDNDAALALYRSVGFQRVG 134
Cdd:COG3393    2 LVAMAGV---RAESPGVAEISGVYTHPEYRGRGLASALVAALAREALargARTPFLYVDADNPAARRLYERLGFRPVG 76
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-106 9.68e-12

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: 56.90  E-value: 9.68e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489513191  51 YVGARSGGTLVGYAGISRLGRTPPfEYEVHTIGVDPAYQGRGIGRRLLRELLDFAR 106
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGD-TAYIGDLAVLPEYRGKGIGSALLEAAEEEAR 55
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
47-134 6.00e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 54.03  E-value: 6.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191  47 PHNHYVGARSGGTLVGYAgisrlgRTPPFEYEVHTIG---VDPAYQGRGIGRRLLRELLDFAR---GGVVYLEVRTDnda 120
Cdd:COG2153   32 EDARHLLAYDDGELVATA------RLLPPGDGEAKIGrvaVLPEYRGQGLGRALMEAAIEEARergARRIVLSAQAH--- 102

                         90
                 ....*....|....
gi 489513191 121 ALALYRSVGFQRVG 134
Cdd:COG2153  103 AVGFYEKLGFVPVG 116
PRK03624 PRK03624
putative acetyltransferase; Provisional
 34-133 1.41e-09

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 53.01  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191  34 PW--PPAAFNRELASPHNHYVGARSGGTLVG--YAGisrlgrtppfeYEVH-----TIGVDPAYQGRGIGRRLLRELLDF 104
Cdd:PRK03624  28 PWndPEMDIERKLNHDPSLFLVAEVGGEVVGtvMGG-----------YDGHrgwayYLAVHPDFRGRGIGRALVARLEKK 96

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489513191 105 --ARGGV-VYLEVRTDNDAALALYRSVGFQRV 133
Cdd:PRK03624  97 liARGCPkINLQVREDNDAVLGFYEALGYEEQ 128
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
71-134 2.79e-08

Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 50.32  E-value: 2.79e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489513191  71 RTPPFEYeVHTIGVDPAYQGRGIGRRLLRELLDFARGG---VVYLEVRTD--NDAALALYRSVGFQRVG 134
Cdd:COG3818   80 RYDNFLY-IDRIVVAPSARGRGLGRALYADVFSYARARgvpRVTCEVNLEppNPGSLAFHARLGFREVG 147
PRK10140 PRK10140
N-acetyltransferase;
58-152 1.03e-06

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 45.74  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191  58 GTLVGYAGISRLGRtpPFEYEVHTIG--VDPAYQGRGIGRRLLRELLDFA----RGGVVYLEVRTDNDAALALYRSVGFQ 131
Cdd:PRK10140  60 GDVVGHLTIDVQQR--PRRSHVADFGicVDSRWKNRGVASALMREMIEMCdnwlRVDRIELTVFVDNAPAIKVYKKYGFE 137

                         90       100
                 ....*....|....*....|...
gi 489513191 132 RVGLRRRYYRVSG--ADAYTMRR 152
Cdd:PRK10140 138 IEGTGKKYALRNGeyVDAYYMAR 160
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
54-106 2.48e-06

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 43.22  E-value: 2.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489513191  54 ARSGGTLVGYAGISRLGRTPPFeyeVHTiGVDPAYQGRGIGRRLLRELLDFAR 106
Cdd:COG2388   14 LEVDGELAGELTYRLEGGVIII---THT-EVPPALRGQGIASALVEAALDDAR 62
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 51-142 6.20e-06

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: 42.32  E-value: 6.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   51 YVGARSGGTLVGYAGISRLGRTppfeyEVHTIGVDPAYQGRGIGRRLLRELLD--FARGGVVYLEVRTDNDAALALYRSV 128
Cdd:pfam08445   1 VLGIYRGDTGELAAWCLRLPGG-----ELGALQTLPEHRRRGLGSRLVAALARgiAERGITPFAVVVAGNTPSRRLYEKL 75

                          90
                  ....*....|....
gi 489513191  129 GFQrvgLRRRYYRV 142
Cdd:pfam08445  76 GFR---KIDETYWV 86
PRK07922 PRK07922
amino-acid N-acetyltransferase;
78-106 1.33e-05

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 42.99  E-value: 1.33e-05
                         10        20
                 ....*....|....*....|....*....
gi 489513191  78 EVHTIGVDPAYQGRGIGRRLLRELLDFAR 106
Cdd:PRK07922  72 EIRTVAVDPAARGRGVGHAIVERLLDVAR 100
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 57-106 1.33e-05

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: 40.97  E-value: 1.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 489513191   57 GGTLVGYAGISRLGRTPPFeyeVHTiGVDPAYQGRGIGRRLLRELLDFAR 106
Cdd:pfam14542   8 GGAEVAFLTYRRGDGVLII---THT-EVPPALRGQGIASKLVKAALDDAR 53
Eis COG4552
Predicted acetyltransferase [General function prediction only];
9-139 3.10e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 42.58  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   9 TIGALTRADAQRCAELEAQLFVGDDPWPPAAFNRELASPHNHYvGARSGGTLVGYAGIsrlgrtppFEYEVHT------- 81
Cdd:COG4552    2 EIRPLTEDDLDAFARLLAYAFGPEPDDEELEAYRPLLEPGRVL-GVFDDGELVGTLAL--------YPFTLNVggarvpm 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489513191  82 -----IGVDPAYQGRGIGRRLLRELLDFARggvvylevrtDNDAALA--------LYRSVGFQRVGLRRRY 139
Cdd:COG4552   73 agitgVAVAPEHRRRGVARALLREALAELR----------ERGQPLSalypfepgFYRRFGYELAGDRRRY 133
PRK10514 PRK10514
putative acetyltransferase; Provisional
 84-134 8.64e-05

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 40.37  E-value: 8.64e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489513191  84 VDPAYQGRGIGRRLLRELLdfARGGVVYLEVRTDNDAALALYRSVGFQRVG 134
Cdd:PRK10514  77 VDPDVRGCGVGRMLVEHAL--SLHPELTTDVNEQNEQAVGFYKKMGFKVTG 125
PTZ00330 PTZ00330
acetyltransferase; Provisional
 79-132 1.17e-04

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 39.83  E-value: 1.17e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489513191  79 VHTIGVDPAYQGRGIGRRLLRELLDFARGGVVYLEVRTDNDAALALYRSVGFQR 132
Cdd:PTZ00330  85 IEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILDCTEDMVAFYKKLGFRA 138
COG3375 COG3375
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
5-106 1.98e-04

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


Pssm-ID: 442602 [Multi-domain]  Cd Length: 271  Bit Score: 40.31  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191   5 TEPVTIGAL-TRADAQRCAELEAQLFvGDDPWPPAAFNRELASPHN-HYV-GARSGGTLVGYAgISRLGRTPPFEY-EVH 80
Cdd:COG3375    2 AAGVEIRELtTPAELEAVQRLQRSVW-GSPPNEPVPVHLLRALAHAgGYVlGAFDGGELVGFS-FGFPGFRPGGLYlHSH 79

                         90       100
                 ....*....|....*....|....*.
gi 489513191  81 TIGVDPAYQGRGIGRRLLRELLDFAR 106
Cdd:COG3375   80 MAGVLPEYRGRGVGYALKLHQREWAL 105
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 82-131 5.23e-04

Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.


Pssm-ID: 173920 [Multi-domain]  Cd Length: 297  Bit Score: 38.78  E-value: 5.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489513191  82 IGVDPAYQGRGIGRRLLRELLDFARG-GVVYLEVRTDNDAAlALYRSVGFQ 131
Cdd:cd02169   31 VAVCPKYQGEGLALKIVSELINKAYEeGIFHLFLFTKPKNA-KFFRGLGFK 80
PRK07757 PRK07757
N-acetyltransferase;
49-106 7.34e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 37.87  E-value: 7.34e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489513191  49 NHYVgARSGGTLVGYAGIS----RLGrtppfeyEVHTIGVDPAYQGRGIGRRLLRELLDFAR 106
Cdd:PRK07757  42 DFYV-AEEEGEIVGCCALHilweDLA-------EIRSLAVSEDYRGQGIGRMLVEACLEEAR 95
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 84-132 1.72e-03

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 36.61  E-value: 1.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489513191  84 VDPAYQGRGIGRRLLRELLDFARGGVVY---LEVRTDNdaaLALYRSVGFQR 132
Cdd:PLN02706  93 VDSAARGKGLGKKIIEALTEHARSAGCYkviLDCSEEN---KAFYEKCGYVR 141
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 53-131 6.00e-03

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 35.54  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489513191  53 GARSGgtLVGYAGISRLGRTPPFEyevhtIGVDPAYQGRGIGRRLLRELLDFARGGV----VYLEVRTDNDAALALYRSV 128
Cdd:PRK15130  66 GEKAG--LVELVEINHVHRRAEFQ-----IIISPEYQGKGLATRAAKLAMDYGFTVLnlykLYLIVDKENEKAIHIYRKL 138


                 ...
gi 489513191 129 GFQ 131
Cdd:PRK15130 139 GFE 141
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 92-150 6.93e-03

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: 35.03  E-value: 6.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489513191   92 GIGRRLLRELLDFARGGV----VYLEVRTDNDAALALYRSVGFQRVGLRRRYYRvsGADAYTM 150
Cdd:TIGR03585  91 GVGSVLEEAALEYAFEHLglhkLSLEVLESNNKALKLYEKFGFEREGVFRQGGE--YYDVLLM 151
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
82-131 7.63e-03

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 35.29  E-value: 7.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489513191  82 IGVDPAYQGRGIGRRLLRELLDFARG-GVVYLEVRTD--NDAALALYRSVGFQ 131
Cdd:PRK10975 132 LAVFPGAQGRGIGARLMQAALNWCQArGLTRLRVATQmgNLAALRLYIRSGAN 184
 
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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