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Conserved domains on  [gi|1721234764|ref|WP_146164452|]
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N-acetyltransferase [Agitococcus lubricus]

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 ...
 131-210 3.92e-07

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 46.57  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721234764 131 HPHVPHWYLMAVGVAPEAQGRGYCSKLLRPILDIC-DRTQTPAYLE--NSKEQNIEIYQHFGFKVTEEVVVDKDVKLWLM 207
Cdd:COG0456     8 VDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEvrEDNEAAIALYEKLGFEEVGERPNYYGDDALVM 87


                  ...
gi 1721234764 208 WRE 210
Cdd:COG0456    88 EKE 90
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 131-210 3.92e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 46.57  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721234764 131 HPHVPHWYLMAVGVAPEAQGRGYCSKLLRPILDIC-DRTQTPAYLE--NSKEQNIEIYQHFGFKVTEEVVVDKDVKLWLM 207
Cdd:COG0456     8 VDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEvrEDNEAAIALYEKLGFEEVGERPNYYGDDALVM 87


                  ...
gi 1721234764 208 WRE 210
Cdd:COG0456    88 EKE 90
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 131-192 3.07e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 41.29  E-value: 3.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721234764 131 HPHVPHWYLMAVGVAPEAQGRGYCSKLLRPILDICDRTQTPAYLENSKEQNIEIYQHFGFKV 192
Cdd:pfam13508  23 LDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 132-165 2.42e-03

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: 35.33  E-value: 2.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1721234764 132 PHVPHWYLMAVGVAPEAQGRGYCSKLLRPILDIC 165
Cdd:cd04301    21 SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEA 54
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 131-210 3.92e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 46.57  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721234764 131 HPHVPHWYLMAVGVAPEAQGRGYCSKLLRPILDIC-DRTQTPAYLE--NSKEQNIEIYQHFGFKVTEEVVVDKDVKLWLM 207
Cdd:COG0456     8 VDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEvrEDNEAAIALYEKLGFEEVGERPNYYGDDALVM 87


                  ...
gi 1721234764 208 WRE 210
Cdd:COG0456    88 EKE 90
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
133-210 1.48e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 43.15  E-value: 1.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721234764 133 HVPHWYLMAVGVAPEAQGRGYCSKLLRPILDICDRTQTPAYLENSKEQNIEIYQHFGFKVTEEVVVDKDVKLWLMWRE 210
Cdd:COG3153    64 EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDEVFLAKE 141
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 131-192 3.07e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 41.29  E-value: 3.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721234764 131 HPHVPHWYLMAVGVAPEAQGRGYCSKLLRPILDICDRTQTPAYLENSKEQNIEIYQHFGFKV 192
Cdd:pfam13508  23 LDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
142-212 1.55e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 40.17  E-value: 1.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721234764 142 VGVAPEAQGRGYCSKLLRPILDIC-DRTQTPAYLeNSKEQNIEIYQHFGFKVTEEVVVDKDVKLWLMWREAR 212
Cdd:COG2153    64 VAVLPEYRGQGLGRALMEAAIEEArERGARRIVL-SAQAHAVGFYEKLGFVPVGEEFLEAGIPHIDMRKPLS 134
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 138-192 4.36e-04

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 38.71  E-value: 4.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1721234764 138 YLMAVGVAPEAQGRGYCSKLLRPILDIC-DRTQTPAYLENSkeqNIEIYQHFGFKV 192
Cdd:pfam13527  72 GITGVATYPEYRGRGVMSRLLRRSLEEMrERGVPLSFLYPS---SYPIYRRFGYEI 124
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 131-190 5.13e-04

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: 38.27  E-value: 5.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721234764 131 HPHVPHWYLMAVGVAPEAQGRGYCSKLLRPILDIC-DRTQTPAYLENSK--EQNIEIYQHFGF 190
Cdd:pfam00583  54 DDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWArERGCERIFLEVAAdnLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 135-199 1.90e-03

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 37.34  E-value: 1.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721234764 135 PHWYLMAVGVAPEAQGRGYCSKLLRPILDICdRTQTPAYLE----NSKEQNIEIYQHFGFKVTEEVVVD 199
Cdd:COG0454    57 KVLELKRLYVLPEYRGKGIGKALLEALLEWA-RERGCTALEldtlDGNPAAIRFYERLGFKEIERYVAY 124
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 132-165 2.42e-03

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: 35.33  E-value: 2.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1721234764 132 PHVPHWYLMAVGVAPEAQGRGYCSKLLRPILDIC 165
Cdd:cd04301    21 SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEA 54
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 136-195 8.74e-03

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: 35.35  E-value: 8.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721234764 136 HWYLMAVGVAPEAQGRGYCSKLLRPILDICdRTQ--TPAYLEnSKEQNIEIYQHFGFKVTEE 195
Cdd:COG1246    52 LAELRSLAVHPDYRGRGIGRRLLEALLAEA-RELglKRLFLL-TTSAAIHFYEKLGFEEIDK 111
 
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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