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Conserved domains on  [gi|446105817|ref|WP_000183672|]
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MULTISPECIES: N-acetyltransferase [Staphylococcus]

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
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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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 ...
 77-161 7.47e-11

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.43  E-value: 7.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817  77 DNQDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGYQYMGDSM-FIGRPVHI 155
Cdd:COG0456    9 DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE--RGARRLRLEVREDNEAAIALYEKLGFEEVGERPnYYGDDALV 86


                 ....*.
gi 446105817 156 MALTIK 161
Cdd:COG0456   87 MEKELA 92
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 77-161 7.47e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.43  E-value: 7.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817  77 DNQDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGYQYMGDSM-FIGRPVHI 155
Cdd:COG0456    9 DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE--RGARRLRLEVREDNEAAIALYEKLGFEEVGERPnYYGDDALV 86


                 ....*.
gi 446105817 156 MALTIK 161
Cdd:COG0456   87 MEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 17-140 3.54e-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: 3.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817   17 YSMLEAFQLSESDLKFVKTPEENITAAMSDNERYPIVVMDGRqCVAFFTLHrgkgvaPYSDNQDAVFFRSFSVDQRYRNR 96
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGE-LVGFASLS------IIDDEPPVGEIEGLAVAPEYRGK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 446105817   97 GIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGY 140
Cdd:pfam00583  75 GIGTALLQALLEWARE--RGCERIFLEVAADNLAAIALYEKLGF 116
PRK10140 PRK10140
N-acetyltransferase;
88-144 3.80e-04

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 38.81  E-value: 3.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446105817  88 SVDQRYRNRGIGKVVMEKLASFITSTFQdINEIVLTVNTDNPHAMALYRQQGYQYMG 144
Cdd:PRK10140  85 CVDSRWKNRGVASALMREMIEMCDNWLR-VDRIELTVFVDNAPAIKVYKKYGFEIEG 140
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-123 4.59e-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: 36.87  E-value: 4.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446105817  52 IVVMDGRQCVAFFTLHrgkgvaPYSDNQDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLT 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 ...
 77-161 7.47e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.43  E-value: 7.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817  77 DNQDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGYQYMGDSM-FIGRPVHI 155
Cdd:COG0456    9 DGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE--RGARRLRLEVREDNEAAIALYEKLGFEEVGERPnYYGDDALV 86


                 ....*.
gi 446105817 156 MALTIK 161
Cdd:COG0456   87 MEKELA 92
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
42-160 1.83e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 53.46  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817  42 AAMSDNERYPIVVMDGRQCVAFFTLHRGKGVAPYsdnqDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIV 121
Cdd:COG1247   45 AAILAPGRPVLVAEEDGEVVGFASLGPFRPRPAY----RGTAEESIYVDPDARGRGIGRALLEALIERARA--RGYRRLV 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446105817 122 LTVNTDNPHAMALYRQQGYQYMGDSMFIG------RPVHIMALTI 160
Cdd:COG1247  119 AVVLADNEASIALYEKLGFEEVGTLPEVGfkfgrwLDLVLMQKRL 163
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 30-159 2.12e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 52.75  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817  30 LKFVKTPEENI----TAAMSDNErypIVVMDGRQCVAFFTL--HRGKGVA-----PYSDnqDAVFFRSFSVDQRYRNRGI 98
Cdd:COG0454    1 MSIRKATPEDInfilLIEALDAE---LKAMEGSLAGAEFIAvdDKGEPIGfaglrRLDD--KVLELKRLYVLPEYRGKGI 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446105817  99 GKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGYQYMGDSMFIGRPVHIMALT 159
Cdd:COG0454   76 GKALLEALLEWARE--RGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEKELS 134
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 17-140 3.54e-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: 3.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817   17 YSMLEAFQLSESDLKFVKTPEENITAAMSDNERYPIVVMDGRqCVAFFTLHrgkgvaPYSDNQDAVFFRSFSVDQRYRNR 96
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGE-LVGFASLS------IIDDEPPVGEIEGLAVAPEYRGK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 446105817   97 GIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGY 140
Cdd:pfam00583  75 GIGTALLQALLEWARE--RGCERIFLEVAADNLAAIALYEKLGF 116
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 446105817  89 VDQRYRNRGIGKVVMEKLASFITStfQDINEIVLTVNTDNPHAMALYRQQGYQYMGDSMFI 149
Cdd:COG3393   23 THPEYRGRGLASALVAALAREALA--RGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 5-159 3.16e-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: 3.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817   5 DTIMLRHYVPQDYSMLEAFQLSESDLKFVKTPE----------ENITAAMSDNERYP--IVVMDGRQCVAFFTLHRgkgv 72
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARYLPGPPysleearawlERLLADWADGGALPfaIEDKEDGELIGVVGLYD---- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817  73 apYSDNQDAVFFrSFSVDQRYRNRGIGKVVMEKLASFITSTFqDINEIVLTVNTDNPHAMALYRQQGYQYMG---DSMFI 149
Cdd:COG1670   82 --IDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEEL-GLHRVEAEVDPDNTASIRVLEKLGFRLEGtlrDALVI 157

                        170
                 ....*....|...
gi 446105817 150 G---RPVHIMALT 159
Cdd:COG1670  158 DgryRDHVLYSLL 170
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
9-160 2.57e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 47.39  E-value: 2.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817   9 LRHYVPQDYSMLEAFQLSEsdlkFVKTPEENITAAM--SDNERYPIVVMDGRQCVAFFTLHRgkgvAPYSDNQDAVFFRS 86
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA----FGPGREAELVDRLreDPAAGLSLVAEDDGEIVGHVALSP----VDIDGEGPALLLGP 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446105817  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 4.28e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.83  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817   52 IVVMDGRQCVAFFTLHRgkgvapySDNQDAVFFRSFSVDQRYRNRGIGKVVMEKLAsfitsTFQDINEIVLTVNTDNPHA 131
Cdd:pfam13508   6 FVAEDDGKIVGFAALLP-------LDDEGALAELRLAVHPEYRGQGIGRALLEAAE-----AAAKEGGIKLLELETTNRA 73

                          90
                  ....*....|
gi 446105817  132 MALYRQQGYQ 141
Cdd:pfam13508  74 AAFYEKLGFE 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 43-144 1.00e-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: 39.98  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817  43 AMSDNERYPIVVMDGRQCVAFFTLHrgkgvaPYSDnqDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVL 122
Cdd:COG1246   22 ALEEEIGEFWVAEEDGEIVGCAALH------PLDE--DLAELRSLAVHPDYRGRGIGRRLLEALLAEARE--LGLKRLFL 91

                         90       100
                 ....*....|....*....|..
gi 446105817 123 TVNTDnphAMALYRQQGYQYMG 144
Cdd:COG1246   92 LTTSA---AIHFYEKLGFEEID 110
PRK10140 PRK10140
N-acetyltransferase;
88-144 3.80e-04

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 38.81  E-value: 3.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446105817  88 SVDQRYRNRGIGKVVMEKLASFITSTFQdINEIVLTVNTDNPHAMALYRQQGYQYMG 144
Cdd:PRK10140  85 CVDSRWKNRGVASALMREMIEMCDNWLR-VDRIELTVFVDNAPAIKVYKKYGFEIEG 140
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-123 4.59e-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: 36.87  E-value: 4.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446105817  52 IVVMDGRQCVAFFTLHrgkgvaPYSDNQDAVFFRSFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLT 123
Cdd:cd04301    2 LVAEDDGEIVGFASLS------PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE--RGAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
77-160 2.91e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 35.93  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446105817  77 DNQDAVFFRsFSVDQRYRNRGIGKVVMEKLASFITStfQDINEIVLTVNTdnpHAMALYRQQGYQYMGDsMFI--GRPvH 154
Cdd:COG2153   55 GDGEAKIGR-VAVLPEYRGQGLGRALMEAAIEEARE--RGARRIVLSAQA---HAVGFYEKLGFVPVGE-EFLeaGIP-H 126


                 ....*..
gi 446105817 155 I-MALTI 160
Cdd:COG2153  127 IdMRKPL 133
 
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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