NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|502820042|ref|WP_013055018|]
View 

MULTISPECIES: ribosomal protein S18-alanine N-acetyltransferase [Bacillaceae]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 14-145 1.93e-53

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: 164.81  E-value: 1.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   14 DIDQVVKIEEKSFTTPWSSEAFQNELTNnQFSTYIVMEEGENIIGYCGTWIVIDEAHVTNIALLPDYRGKGLGELLLRNV 93
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELAN-YHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLREL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 502820042   94 MDVLRKLGATSMTLEVRVSNHIAQSLYQKLGFKPGGIRKNYYSDNNEDALVM 145
Cdd:TIGR01575  80 IDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 14-145 1.93e-53

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: 164.81  E-value: 1.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   14 DIDQVVKIEEKSFTTPWSSEAFQNELTNnQFSTYIVMEEGENIIGYCGTWIVIDEAHVTNIALLPDYRGKGLGELLLRNV 93
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELAN-YHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLREL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 502820042   94 MDVLRKLGATSMTLEVRVSNHIAQSLYQKLGFKPGGIRKNYYSDNNEDALVM 145
Cdd:TIGR01575  80 IDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 14-145 3.81e-35

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 118.88  E-value: 3.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  14 DIDQVVKIEEKSFTTPWSSEAFQNeltnNQFSTYI--VMEEGENIIGYCGTWIVIDEAHVTNIALLPDYRGKGLGELLLR 91
Cdd:PRK09491  11 DLPAAYHIEQRAHAFPWSEKTFAS----NQGERYLnlKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLE 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502820042  92 NVMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGFKPGGIRKNYY--SDNNEDALVM 145
Cdd:PRK09491  87 HLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYptADGREDAIIM 142
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 58-149 1.03e-28

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 100.89  E-value: 1.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  58 GYCGTWIVI--DEAHVTNIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGFKPGGIRKNYY 135
Cdd:COG0456    1 GFALLGLVDggDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....
gi 502820042 136 SDnneDALVMWVNL 149
Cdd:COG0456   81 GD---DALVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 15-125 9.42e-24

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: 89.11  E-value: 9.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   15 IDQVVKIEEKSFTTPWSSEAF--QNELTNNQFSTYIVMEEGENIIGYCGTWIV---IDEAHVTNIALLPDYRGKGLGELL 89
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLdlLEDWDEDASEGFFVAEEDGELVGFASLSIIddePPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 502820042   90 LRNVMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGF 125
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-108 3.94e-13

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: 60.37  E-value: 3.94e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502820042  47 YIVMEEGENIIGYCGTWI---VIDEAHVTNIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLE 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 ...
 14-145 1.93e-53

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: 164.81  E-value: 1.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   14 DIDQVVKIEEKSFTTPWSSEAFQNELTNnQFSTYIVMEEGENIIGYCGTWIVIDEAHVTNIALLPDYRGKGLGELLLRNV 93
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELAN-YHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLREL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 502820042   94 MDVLRKLGATSMTLEVRVSNHIAQSLYQKLGFKPGGIRKNYYSDNNEDALVM 145
Cdd:TIGR01575  80 IDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 14-145 3.81e-35

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 118.88  E-value: 3.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  14 DIDQVVKIEEKSFTTPWSSEAFQNeltnNQFSTYI--VMEEGENIIGYCGTWIVIDEAHVTNIALLPDYRGKGLGELLLR 91
Cdd:PRK09491  11 DLPAAYHIEQRAHAFPWSEKTFAS----NQGERYLnlKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLE 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502820042  92 NVMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGFKPGGIRKNYY--SDNNEDALVM 145
Cdd:PRK09491  87 HLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYptADGREDAIIM 142
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 58-149 1.03e-28

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 100.89  E-value: 1.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  58 GYCGTWIVI--DEAHVTNIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGFKPGGIRKNYY 135
Cdd:COG0456    1 GFALLGLVDggDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....
gi 502820042 136 SDnneDALVMWVNL 149
Cdd:COG0456   81 GD---DALVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 15-125 9.42e-24

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: 89.11  E-value: 9.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   15 IDQVVKIEEKSFTTPWSSEAF--QNELTNNQFSTYIVMEEGENIIGYCGTWIV---IDEAHVTNIALLPDYRGKGLGELL 89
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLdlLEDWDEDASEGFFVAEEDGELVGFASLSIIddePPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 502820042   90 LRNVMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGF 125
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
7-127 6.09e-22

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 85.14  E-value: 6.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   7 FRLMEVKDIDQVVKIEEKSFTTPWSSEAFQNELTNNQFSTYIVMEEGENIIGYCGTWIV-----IDEAHVTNIALLPDYR 81
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVdidgeGPALLLGPLAVDPEYR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 502820042  82 GKGLGELLLRNVMDVLRKLGATSMTLevrVSNHIAQSLYQKLGFKP 127
Cdd:COG3153   81 GQGIGRALMRAALEAARERGARAVVL---LGDPSLLPFYERFGFRP 123
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
4-149 4.14e-20

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 81.19  E-value: 4.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   4 TIKFRLMEVKDIDQVVKI-----EEKSFT---TPWSSEAFQNELTNNQFSTY--IVMEEGENIIGYCG-----TWIVIDE 68
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIyneaiAEGTATfetEPPSEEEREAWFAAILAPGRpvLVAEEDGEVVGFASlgpfrPRPAYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  69 AHVTNIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGFKPGGIRKNYYSDNNE--DALVMW 146
Cdd:COG1247   81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRwlDLVLMQ 160


                 ...
gi 502820042 147 VNL 149
Cdd:COG1247  161 KRL 163
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 5-147 2.15e-19

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: 78.50  E-value: 2.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   5 IKFRLMEVKDIDQVVKIEEksfttpwsSEAFQNELtnnqfSTYIVMEEGENIIGyCGTWIVIDE--AHVTNIALLPDYRG 82
Cdd:COG1246    1 MTIRPATPDDVPAILELIR--------PYALEEEI-----GEFWVAEEDGEIVG-CAALHPLDEdlAELRSLAVHPDYRG 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502820042  83 KGLGELLLRNVMDVLRKLGATSMTLEvrvSNHIAQSLYQKLGFKPGGIRKNYYSDNNEDALVMWV 147
Cdd:COG1246   67 RGIGRRLLEALLAEARELGLKRLFLL---TTSAAIHFYEKLGFEEIDKEDLPYAKVWQRDSVVME 128
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 18-127 3.41e-18

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 75.48  E-value: 3.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  18 VVKIEEKSFTTPWSSEAFQNELTN----NQFSTYIVMEEGENIIGYCGTWIVIDE-AHVTNIALLPDYRGKGLGELLLRN 92
Cdd:COG0454    3 IRKATPEDINFILLIEALDAELKAmegsLAGAEFIAVDDKGEPIGFAGLRRLDDKvLELKRLYVLPEYRGKGIGKALLEA 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502820042  93 VMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGFKP 127
Cdd:COG0454   83 LLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 45-127 3.43e-18

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 74.03  E-value: 3.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   45 STYIVMEEGENIIGYCGTWIVIDEAHVTNIAL--LPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVRVSnhiAQSLYQK 122
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAALLPLDDEGALAELRLavHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAAFYEK 79


                  ....*
gi 502820042  123 LGFKP 127
Cdd:pfam13508  80 LGFEE 84
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 31-131 5.25e-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: 66.91  E-value: 5.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   31 SSEAFQNELTNNQFsTYIVMEEGENIIGYCGtwiVIDEAHVTNIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVR 110
Cdd:pfam13673  18 SPEALRERIDQGEY-FFFVAFEGGQIVGVIA---LRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVN 93

                          90       100
                  ....*....|....*....|....*...
gi 502820042  111 VSNHiAQSLYQKLGFKP-------GGIR 131
Cdd:pfam13673  94 ASPY-AVPFYEKLGFRAtgpeqefNGIR 120
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 5-145 7.14e-15

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: 67.72  E-value: 7.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   5 IKFRLMEVKDIDQVVK------IEEKSFTTPWSSEAFQNELTNNQFSTY--------IVMEEGENIIGYCGTWIVIDEAH 70
Cdd:COG1670    8 LRLRPLRPEDAEALAEllndpeVARYLPGPPYSLEEARAWLERLLADWAdggalpfaIEDKEDGELIGVVGLYDIDRANR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  71 VTNIA--LLPDYRGKGLGELLLRNVMD-VLRKLGATSMTLEVRVSNHIAQSLYQKLGFKPGGIRKNYYSDNNE--DALVM 145
Cdd:COG1670   88 SAEIGywLAPAYWGKGYATEALRALLDyAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRyrDHVLY 167
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
69-129 9.03e-15

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 64.93  E-value: 9.03e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502820042  69 AHVTNIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGFKPGG 129
Cdd:COG3393   16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 47-108 3.94e-13

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: 60.37  E-value: 3.94e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502820042  47 YIVMEEGENIIGYCGTWI---VIDEAHVTNIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLE 108
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
45-127 4.62e-13

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 62.12  E-value: 4.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  45 STYIVMEEGENIIGYCgTWIVID--EAHVTNIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVRVSnhiAQSLYQK 122
Cdd:COG2153   34 ARHLLAYDDGELVATA-RLLPPGdgEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEK 109


                 ....*
gi 502820042 123 LGFKP 127
Cdd:COG2153  110 LGFVP 114
PRK03624 PRK03624
putative acetyltransferase; Provisional
 14-125 7.51e-09

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 51.08  E-value: 7.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  14 DIDQVVKIEEKSF-TTPWS--SEAFQNELtNNQFSTYIVMEEGENIIGycgTWIVIDEAH---VTNIALLPDYRGKGLGE 87
Cdd:PRK03624  12 DFEAVIALWERCDlTRPWNdpEMDIERKL-NHDPSLFLVAEVGGEVVG---TVMGGYDGHrgwAYYLAVHPDFRGRGIGR 87

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 502820042  88 LLLRNVMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGF 125
Cdd:PRK03624  88 ALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGY 125
PRK07757 PRK07757
N-acetyltransferase;
47-134 9.28e-09

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 50.96  E-value: 9.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  47 YIVMEEGENIIGYCGTWIV-IDEAHVTNIALLPDYRGKGLGELLLRNVMDVLRKLGAT---SMTLEVRvsnhiaqsLYQK 122
Cdd:PRK07757  43 FYVAEEEGEIVGCCALHILwEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKrvfALTYQPE--------FFEK 114

                         90
                 ....*....|..
gi 502820042 123 LGFKPggIRKNY 134
Cdd:PRK07757 115 LGFRE--VDKEA 124
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 7-126 2.42e-07

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 46.96  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042    7 FRLMEVKDIDQVVKI----EEKSFTTPWSS------EAFQNELTNNQFST---YIVMEEGENIIGYCGTWIVIDEAHVTN 73
Cdd:pfam13302   4 LRPLTEEDAEALFELlsdpEVMRYGVPWPLtleearEWLARIWAADEAERgygWAIELKDTGFIGSIGLYDIDGEPERAE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 502820042   74 IA--LLPDYRGKGLGELLLRNVMD-VLRKLGATSMTLEVRVSNHIAQSLYQKLGFK 126
Cdd:pfam13302  84 LGywLGPDYWGKGYATEAVRALLEyAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Eis COG4552
Predicted acetyltransferase [General function prediction only];
5-134 1.31e-06

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 46.43  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   5 IKFRLMEVKDIDQVVKIEEKSFTTPWSSEAFQNELTNNQFSTYIVMEEGENIIGYCGTW--------IVIDEAHVTNIAL 76
Cdd:COG4552    1 MEIRPLTEDDLDAFARLLAYAFGPEPDDEELEAYRPLLEPGRVLGVFDDGELVGTLALYpftlnvggARVPMAGITGVAV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502820042  77 LPDYRGKGLGELLLRNVMDVLRKLGATSMTLevrvsnH-IAQSLYQKLGFKPGGIRKNY 134
Cdd:COG4552   81 APEHRRRGVARALLREALAELRERGQPLSAL------YpFEPGFYRRFGYELAGDRRRY 133
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 74-125 3.91e-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: 42.70  E-value: 3.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 502820042   74 IALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLeVRVSNHIAQSLYQKLGF 125
Cdd:pfam08445  27 LQTLPEHRRRGLGSRLVAALARGIAERGITPFAV-VVAGNTPSRRLYEKLGF 77
PRK10514 PRK10514
putative acetyltransferase; Provisional
 66-129 7.01e-06

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 43.07  E-value: 7.01e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502820042  66 IDEAHVTNIALLPDYRGKGLGELLLRNVMDVlrklgATSMTLEVRVSNHIAQSLYQKLGFKPGG 129
Cdd:PRK10514  67 LSGGHMEALFVDPDVRGCGVGRMLVEHALSL-----HPELTTDVNEQNEQAVGFYKKMGFKVTG 125
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 78-129 1.21e-05

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 42.51  E-value: 1.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 502820042   78 PDYRGKGLGELLLRNVMD-VLRKLGATSMTLEVRVSNHIAQSLYQKLGFKPGG 129
Cdd:pfam13523  89 PAFRGRGFTTALLRALVHyLFADPRTRRVVVEPDVRNERAIRLLERAGFRKVK 141
mycothiol_MshD TIGR03448
mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the ...
 66-125 2.31e-05

mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 132489 [Multi-domain]  Cd Length: 292  Bit Score: 42.77  E-value: 2.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042   66 IDEAHVtnIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGF 125
Cdd:TIGR03448 226 LGEVYV--VGVDPAAQGRGLGDALTLIGLHHLAARGLPAVMLYVEADNEAAVRTYEKLGF 283
PTZ00330 PTZ00330
acetyltransferase; Provisional
 70-126 2.01e-04

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 39.06  E-value: 2.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502820042  70 HVTNIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEvrvSNHIAQSLYQKLGFK 126
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILD---CTEDMVAFYKKLGFR 137
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 70-135 3.99e-04

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 38.53  E-value: 3.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502820042  70 HVTNIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVRVSNhiaQSLYQKLGFKPGGIRKNYY 135
Cdd:PLN02706  87 HIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEEN---KAFYEKCGYVRKEIQMVKY 149
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
74-129 1.14e-03

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


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 37.22  E-value: 1.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502820042  74 IALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVRV--SNHIAQSLYQKLGFKPGG 129
Cdd:COG3818   90 IVVAPSARGRGLGRALYADVFSYARARGVPRVTCEVNLepPNPGSLAFHARLGFREVG 147
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 7-127 1.25e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 36.40  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042    7 FRLMEVKDIDQVVKIEEKSF---TTPWSSEAFQNELTNNQfstYIVMEEGENIIG-YCGTW-------IVIDEAHVTNIA 75
Cdd:pfam13527   1 IRPLTEDEFDEVLRLLEYAFqdeDSPELREYFRPLLEEGR---VLGAFDDGELVStLALYPfelnvpgKTLPAAGITGVA 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 502820042   76 LLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVrvsnhIAQSLYQKLGFKP 127
Cdd:pfam13527  78 TYPEYRGRGVMSRLLRRSLEEMRERGVPLSFLYP-----SSYPIYRRFGYEI 124
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 38-104 1.72e-03

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 37.44  E-value: 1.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  38 ELTNNQFSTYIVMEEGENIIGyCGTWIVIDEAHVTNIALL---PDYRGKGLGELLLRNVMDVLRKLGATS 104
Cdd:PRK05279 327 EQLEREIDKFTVIERDGLIIG-CAALYPFPEEKMGEMACLavhPDYRGSGRGERLLKRIEQRARQLGLKR 395
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
68-126 6.19e-03

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 35.29  E-value: 6.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502820042  68 EAHVTNIALLPDYRGKGLGELLLRNVMDVLRKLGATSMTLEVRVSNHIAQSLYQKLGFK 126
Cdd:PRK10975 126 DARIGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGAN 184
PRK10562 PRK10562
putative acetyltransferase; Provisional
 49-146 6.81e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 34.66  E-value: 6.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820042  49 VMEEGENIIGYCGtwiVIDEAHVTNIALLPDYRGKGLGELLLRNVMDVLRKLgatsmTLEVRVSNHIAQSLYQKLGFKPg 128
Cdd:PRK10562  52 VWEEDGKLLGFVS---VLEGRFVGALFVAPKAVRRGIGKALMQHVQQRYPHL-----SLEVYQKNQRAVNFYHAQGFRI- 122

                         90
                 ....*....|....*....
gi 502820042 129 gIRKNYYSDNNEDALVM-W 146
Cdd:PRK10562 123 -VDSAWQEETQHPTWIMsW 140
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH