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Conserved domains on  [gi|497653207|ref|WP_009967391|]
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MULTISPECIES: N-acetyltransferase [Bacillus]

Protein Classification

N-acetyltransferase( domain architecture ID 18096338)

N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate; contains a YoaP-like domain with a single completely conserved residue A that may be functionally important; similar to Bacillus subtilis uncharacterized N-acetyltransferase YoaP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YoaP pfam14268
YoaP-like; The YoaP-like domain is found at the C-terminus of the B. subtilis YoaP protein. It ...
 202-245 9.86e-17

YoaP-like; The YoaP-like domain is found at the C-terminus of the B. subtilis YoaP protein. It is found in bacteria and archaea, and is approximately 40 amino acids in length. The family is found in association with pfam00583. There is a single completely conserved residue A that may be functionally important.


:

Pssm-ID: 433824  Cd Length: 44  Bit Score: 71.44  E-value: 9.86e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 497653207  202 QFQSIQLSSKEEAQKSPAIWTTFSVFFDGRFVTHEIMSINKFEK 245
Cdd:pfam14268   1 PLKIIKIESLEQAQNAPCPFTTFSLFYNGKFITNEILSEKKFEK 44
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 65-151 1.80e-05

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 42.34  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653207  65 AWVPINAPNFMYINCLWVSGRYKNNGHAKRLLDKCIADAKACGMDGIIhiagkkkLPYLSD----KHFFEHMGFTLQDEA 140
Cdd:COG0456    4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLR-------LEVREDneaaIALYEKLGFEEVGER 76

                         90
                 ....*....|.
gi 497653207 141 APYFQLMALTW 151
Cdd:COG0456   77 PNYYGDDALVM 87
 
Name Accession Description Interval E-value
YoaP pfam14268
YoaP-like; The YoaP-like domain is found at the C-terminus of the B. subtilis YoaP protein. It ...
 202-245 9.86e-17

YoaP-like; The YoaP-like domain is found at the C-terminus of the B. subtilis YoaP protein. It is found in bacteria and archaea, and is approximately 40 amino acids in length. The family is found in association with pfam00583. There is a single completely conserved residue A that may be functionally important.


Pssm-ID: 433824  Cd Length: 44  Bit Score: 71.44  E-value: 9.86e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 497653207  202 QFQSIQLSSKEEAQKSPAIWTTFSVFFDGRFVTHEIMSINKFEK 245
Cdd:pfam14268   1 PLKIIKIESLEQAQNAPCPFTTFSLFYNGKFITNEILSEKKFEK 44
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 65-151 1.80e-05

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 42.34  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653207  65 AWVPINAPNFMYINCLWVSGRYKNNGHAKRLLDKCIADAKACGMDGIIhiagkkkLPYLSD----KHFFEHMGFTLQDEA 140
Cdd:COG0456    4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLR-------LEVREDneaaIALYEKLGFEEVGER 76

                         90
                 ....*....|.
gi 497653207 141 APYFQLMALTW 151
Cdd:COG0456   77 PNYYGDDALVM 87
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 72-134 1.87e-03

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: 37.11  E-value: 1.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497653207   72 PNFMYINCLWVSGRYKNNGHAKRLLDKCIADAKACgmdGIIHIAGKKKLPYLSDKHFFEHMGF 134
Cdd:pfam00583  57 PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARER---GCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 72-112 4.19e-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: 34.94  E-value: 4.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 497653207  72 PNFMYINCLWVSGRYKNNGHAKRLLDKCIADAKACGMDGII 112
Cdd:cd04301   23 GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
 
Name Accession Description Interval E-value
YoaP pfam14268
YoaP-like; The YoaP-like domain is found at the C-terminus of the B. subtilis YoaP protein. It ...
 202-245 9.86e-17

YoaP-like; The YoaP-like domain is found at the C-terminus of the B. subtilis YoaP protein. It is found in bacteria and archaea, and is approximately 40 amino acids in length. The family is found in association with pfam00583. There is a single completely conserved residue A that may be functionally important.


Pssm-ID: 433824  Cd Length: 44  Bit Score: 71.44  E-value: 9.86e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 497653207  202 QFQSIQLSSKEEAQKSPAIWTTFSVFFDGRFVTHEIMSINKFEK 245
Cdd:pfam14268   1 PLKIIKIESLEQAQNAPCPFTTFSLFYNGKFITNEILSEKKFEK 44
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 65-151 1.80e-05

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 42.34  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653207  65 AWVPINAPNFMYINCLWVSGRYKNNGHAKRLLDKCIADAKACGMDGIIhiagkkkLPYLSD----KHFFEHMGFTLQDEA 140
Cdd:COG0456    4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLR-------LEVREDneaaIALYEKLGFEEVGER 76

                         90
                 ....*....|.
gi 497653207 141 APYFQLMALTW 151
Cdd:COG0456   77 PNYYGDDALVM 87
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 69-141 3.51e-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: 3.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497653207  69 INAPNFMYINCLWVSGRYKNNGHAKRLLDKCIADAKAcgmdgiihiAGKKKLpYL----SDKHFFEHMGFTLQDEAA 141
Cdd:COG1246   47 PLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARE---------LGLKRL-FLlttsAAIHFYEKLGFEEIDKED 113
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 72-134 1.87e-03

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: 37.11  E-value: 1.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497653207   72 PNFMYINCLWVSGRYKNNGHAKRLLDKCIADAKACgmdGIIHIAGKKKLPYLSDKHFFEHMGF 134
Cdd:pfam00583  57 PPVGEIEGLAVAPEYRGKGIGTALLQALLEWARER---GCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
73-149 3.16e-03

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 36.99  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497653207  73 NFMYINCLWVSGRYKNNGHAKRLLDKCIADAKACGMDGIIHIAGKKKLPylsdkhFFEHMGF----TLQDEAAPYFQLMA 148
Cdd:COG3153   66 PALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLP------FYERFGFrpagELGLTLGPDEVFLA 139


                 .
gi 497653207 149 L 149
Cdd:COG3153  140 K 140
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 72-112 4.19e-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: 34.94  E-value: 4.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 497653207  72 PNFMYINCLWVSGRYKNNGHAKRLLDKCIADAKACGMDGII 112
Cdd:cd04301   23 GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
 
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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