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Conserved domains on  [gi|1029687323|emb|SBC13483|]
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acetyltransferase [Staphylococcus aureus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
SCOP:  3000403

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
75-161 4.89e-11

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.82  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323  75 FSDNQDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGYQYMGDSM-FIGRPV 153
Cdd:COG0456     7 LVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE--RGARRLRLEVREDNEAAIALYEKLGFEEVGERPnYYGDDA 84

                  ....*...
gi 1029687323 154 HIMALTIK 161
Cdd:COG0456    85 LVMEKELA 92
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
75-161 4.89e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.82  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323  75 FSDNQDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGYQYMGDSM-FIGRPV 153
Cdd:COG0456     7 LVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE--RGARRLRLEVREDNEAAIALYEKLGFEEVGERPnYYGDDA 84

                  ....*...
gi 1029687323 154 HIMALTIK 161
Cdd:COG0456    85 LVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
17-140 3.36e-09

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: 51.75  E-value: 3.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323  17 YSMLEAFQLSESDLKFVKTPEENITAAMSDNERYPIVVMDGRqCVAFFTLHrgkgvaPFSDNQDAVFFRSFSVDQRYRNR 96
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGE-LVGFASLS------IIDDEPPVGEIEGLAVAPEYRGK 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1029687323  97 GIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGY 140
Cdd:pfam00583  75 GIGTALLQALLEWARE--RGCERIFLEVAADNLAAIALYEKLGF 116
PRK10140 PRK10140
N-acetyltransferase;
88-144 3.48e-04

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 38.81  E-value: 3.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1029687323  88 SVDQRYRNRGIGKVVMEKLASFITSTFQdINEIVLTVNTDNPHAMALYRQQGYQYMG 144
Cdd:PRK10140   85 CVDSRWKNRGVASALMREMIEMCDNWLR-VDRIELTVFVDNAPAIKVYKKYGFEIEG 140
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
52-123 7.82e-04

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


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 36.10  E-value: 7.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1029687323  52 IVVMDGRQCVAFFTLHrgkgvaPFSDNQDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLT 123
Cdd:cd04301     2 LVAEDDGEIVGFASLS------PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE--RGAKRLRLE 65
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
75-161 4.89e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.82  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323  75 FSDNQDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGYQYMGDSM-FIGRPV 153
Cdd:COG0456     7 LVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE--RGARRLRLEVREDNEAAIALYEKLGFEEVGERPnYYGDDA 84

                  ....*...
gi 1029687323 154 HIMALTIK 161
Cdd:COG0456    85 LVMEKELA 92
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
30-159 7.89e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 53.90  E-value: 7.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323  30 LKFVKTPEENI----TAAMSDNErypIVVMDGRQCVAFFTL--HRGK--GVAPFSD-NQDAVFFRSFSVDQRYRNRGIGK 100
Cdd:COG0454     1 MSIRKATPEDInfilLIEALDAE---LKAMEGSLAGAEFIAvdDKGEpiGFAGLRRlDDKVLELKRLYVLPEYRGKGIGK 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1029687323 101 VVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGYQYMGDSMFIGRPVHIMALT 159
Cdd:COG0454    78 ALLEALLEWARE--RGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEKELS 134
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
17-140 3.36e-09

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: 51.75  E-value: 3.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323  17 YSMLEAFQLSESDLKFVKTPEENITAAMSDNERYPIVVMDGRqCVAFFTLHrgkgvaPFSDNQDAVFFRSFSVDQRYRNR 96
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGE-LVGFASLS------IIDDEPPVGEIEGLAVAPEYRGK 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1029687323  97 GIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGY 140
Cdd:pfam00583  75 GIGTALLQALLEWARE--RGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
42-160 1.21e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 51.15  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323  42 AAMSDNERYPIVVMDGRQCVAFFTLHRGKGVAPFsdnqDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIV 121
Cdd:COG1247    45 AAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAY----RGTAEESIYVDPDARGRGIGRALLEALIERARA--RGYRRLV 118
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1029687323 122 LTVNTDNPHAMALYRQQGYQYMGDSMFIG------RPVHIMALTI 160
Cdd:COG1247   119 AVVLADNEASIALYEKLGFEEVGTLPEVGfkfgrwLDLVLMQKRL 163
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
89-149 2.38e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 48.75  E-value: 2.38e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1029687323  89 VDQRYRNRGIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGYQYMGDSMFI 149
Cdd:COG3393    23 THPEYRGRGLASALVAALAREALA--RGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
5-159 2.98e-08

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: 50.38  E-value: 2.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323   5 DTIMLRHYVPQDYSMLEAFQLSESDLKFVKTPE----------ENITAAMSDNERYP--IVVMDGRQCVAFFTLHRgkgv 72
Cdd:COG1670     6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPysleearawlERLLADWADGGALPfaIEDKEDGELIGVVGLYD---- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323  73 apFSDNQDAVFFrSFSVDQRYRNRGIGKVVMEKLASFITSTFqDINEIVLTVNTDNPHAMALYRQQGYQYMG---DSMFI 149
Cdd:COG1670    82 --IDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEEL-GLHRVEAEVDPDNTASIRVLEKLGFRLEGtlrDALVI 157
                         170
                  ....*....|...
gi 1029687323 150 G---RPVHIMALT 159
Cdd:COG1670   158 DgryRDHVLYSLL 170
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
9-160 1.26e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.16  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323   9 LRHYVPQDYSMLEAFQLSEsdlkFVKTPEENITAAM--SDNERYPIVVMDGRQCVAFFTLHRgkgvAPFSDNQDAVFFRS 86
Cdd:COG3153     1 IRPATPEDAEAIAALLRAA----FGPGREAELVDRLreDPAAGLSLVAEDDGEIVGHVALSP----VDIDGEGPALLLGP 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1029687323  87 FSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLTVntdNPHAMALYRQQGYQYMGD-SMFIGRPVHIMALTI 160
Cdd:COG3153    73 LAVDPEYRGQGIGRALMRAALEAARE--RGARAVVLLG---DPSLLPFYERFGFRPAGElGLTLGPDEVFLAKEL 142
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
52-141 3.90e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.83  E-value: 3.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323  52 IVVMDGRQCVAFFTLHRgkgvapfSDNQDAVFFRSFSVDQRYRNRGIGKVVMEKLAsfitsTFQDINEIVLTVNTDNPHA 131
Cdd:pfam13508   6 FVAEDDGKIVGFAALLP-------LDDEGALAELRLAVHPEYRGQGIGRALLEAAE-----AAAKEGGIKLLELETTNRA 73
                          90
                  ....*....|
gi 1029687323 132 MALYRQQGYQ 141
Cdd:pfam13508  74 AAFYEKLGFE 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
43-144 1.25e-04

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 39.59  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1029687323  43 AMSDNERYPIVVMDGRQCVAFFTLHRgkgvapfsDNQDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVL 122
Cdd:COG1246    22 ALEEEIGEFWVAEEDGEIVGCAALHP--------LDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARE--LGLKRLFL 91
                          90       100
                  ....*....|....*....|..
gi 1029687323 123 TVNTDnphAMALYRQQGYQYMG 144
Cdd:COG1246    92 LTTSA---AIHFYEKLGFEEID 110
PRK10140 PRK10140
N-acetyltransferase;
88-144 3.48e-04

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 38.81  E-value: 3.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1029687323  88 SVDQRYRNRGIGKVVMEKLASFITSTFQdINEIVLTVNTDNPHAMALYRQQGYQYMG 144
Cdd:PRK10140   85 CVDSRWKNRGVASALMREMIEMCDNWLR-VDRIELTVFVDNAPAIKVYKKYGFEIEG 140
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
52-123 7.82e-04

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


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 36.10  E-value: 7.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1029687323  52 IVVMDGRQCVAFFTLHrgkgvaPFSDNQDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLT 123
Cdd:cd04301     2 LVAEDDGEIVGFASLS------PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE--RGAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
75-145 2.77e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 35.93  E-value: 2.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1029687323  75 FSDNQDAVFFRsFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLTVNTdnpHAMALYRQQGYQYMGD 145
Cdd:COG2153    53 PPGDGEAKIGR-VAVLPEYRGQGLGRALMEAAIEEARE--RGARRIVLSAQA---HAVGFYEKLGFVPVGE 117
 
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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