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Conserved domains on  [gi|2214432179|ref|WP_242835995|]
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N-acetyltransferase [Clostridium sp. DL-VIII]

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 ...
 32-111 6.94e-07

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 44.26  E-value: 6.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214432179  32 ICVVTKEADRIYELKNIAIYKEFQGHGNGKKLVKHIFEYFKNDCA--MYVGTG-DSPLTVPFYKSCEFIESHRIKDFFID 108
Cdd:COG0456     3 ALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGArrLRLEVReDNEAAIALYEKLGFEEVGERPNYYGD 82


                  ...
gi 2214432179 109 NYY 111
Cdd:COG0456    83 DAL 85
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 32-111 6.94e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 44.26  E-value: 6.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214432179  32 ICVVTKEADRIYELKNIAIYKEFQGHGNGKKLVKHIFEYFKNDCA--MYVGTG-DSPLTVPFYKSCEFIESHRIKDFFID 108
Cdd:COG0456     3 ALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGArrLRLEVReDNEAAIALYEKLGFEEVGERPNYYGD 82


                  ...
gi 2214432179 109 NYY 111
Cdd:COG0456    83 DAL 85
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 32-98 6.06e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 38.97  E-value: 6.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214432179  32 ICVVTKEADRIYELKNIAIYKEFQGHGNGKKLVKHIFEYFKNDCAMYVGTGDSPLTVPFYKSCEFIE 98
Cdd:pfam13508  18 AALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 43-73 5.91e-03

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: 34.61  E-value: 5.91e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2214432179  43 YELKNIAIYKEFQGHGNGKKLVKHIFEYFKN 73
Cdd:TIGR01575  55 AHILNIAVKPEYQGQGIGRALLRELIDEAKG 85
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 32-73 6.77e-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: 33.02  E-value: 6.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2214432179  32 ICVVTKEADRIYELKNIAIYKEFQGHGNGKKLVKHIFEYFKN 73
Cdd:cd04301    15 SLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE 56
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 32-111 6.94e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 44.26  E-value: 6.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214432179  32 ICVVTKEADRIYELKNIAIYKEFQGHGNGKKLVKHIFEYFKNDCA--MYVGTG-DSPLTVPFYKSCEFIESHRIKDFFID 108
Cdd:COG0456     3 ALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGArrLRLEVReDNEAAIALYEKLGFEEVGERPNYYGD 82


                  ...
gi 2214432179 109 NYY 111
Cdd:COG0456    83 DAL 85
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 31-101 8.65e-06

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: 42.29  E-value: 8.65e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2214432179  31 GICVVTKEADRIYELKNIAIYKEFQGHGNGKKLVKHIFEYFKNDCA--MYVGTGDSplTVPFYKSCEFIESHR 101
Cdd:COG1246    41 GCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLkrLFLLTTSA--AIHFYEKLGFEEIDK 111
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 32-98 6.06e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 38.97  E-value: 6.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214432179  32 ICVVTKEADRIYELKNIAIYKEFQGHGNGKKLVKHIFEYFKNDCAMYVGTGDSPLTVPFYKSCEFIE 98
Cdd:pfam13508  18 AALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
40-101 2.08e-03

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 35.83  E-value: 2.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214432179  40 DRIYELKNIAIYKEFQGHGNGKKLVKHIFEYFKNDCAMYVGTGDSPLTVPFYKSCEFIESHR 101
Cdd:COG3153    65 GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGE 126
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 43-73 5.91e-03

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: 34.61  E-value: 5.91e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2214432179  43 YELKNIAIYKEFQGHGNGKKLVKHIFEYFKN 73
Cdd:TIGR01575  55 AHILNIAVKPEYQGQGIGRALLRELIDEAKG 85
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 32-73 6.77e-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: 33.02  E-value: 6.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2214432179  32 ICVVTKEADRIYELKNIAIYKEFQGHGNGKKLVKHIFEYFKN 73
Cdd:cd04301    15 SLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE 56
 
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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