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Conserved domains on  [gi|612670687|gb|EZS86793|]
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hypothetical protein W470_02007 [Staphylococcus aureus VET0159R]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10629420)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate; similar to vertebrate protein NATD1

CATH:  3.40.630.30
EC:  2.3.1.-
Gene Ontology:  GO:0008080
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
12-91 9.10e-33

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


:

Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 108.38  E-value: 9.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612670687  12 KFYIGDDENHALAEITYRfVDNNEINIDHTGVSDELGGQGVGKKLVKAVVEHARENHLKIIASCSFAKHMLEKEDSYQDV 91
Cdd:pfam14542  1 RFEIRVDGGAEVAFLTYR-RGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
 
Name Accession Description Interval E-value
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
12-91 9.10e-33

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 108.38  E-value: 9.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612670687  12 KFYIGDDENHALAEITYRfVDNNEINIDHTGVSDELGGQGVGKKLVKAVVEHARENHLKIIASCSFAKHMLEKEDSYQDV 91
Cdd:pfam14542  1 RFEIRVDGGAEVAFLTYR-RGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
4-91 7.04e-30

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 101.38  E-value: 7.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612670687  4 LEIKQGENK--FYIGDDENHAlAEITYRfVDNNEINIDHTGVSDELGGQGVGKKLVKAVVEHARENHLKIIASCSFAKHM 81
Cdd:COG2388   1 MEITHNEEKgrFELEVDGELA-GELTYR-LEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAAY 78
                        90
                ....*....|
gi 612670687 82 LEKEDSYQDV 91
Cdd:COG2388  79 FERHPEYADL 88
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
13-72 2.84e-05

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: 38.41  E-value: 2.84e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612670687 13 FYIGDDENH--ALAEITYRFVDNNEINIDHTGVSDELGGQGVGKKLVKAVVEHARENHLKII 72
Cdd:cd04301   1 FLVAEDDGEivGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
PRK07757 PRK07757
N-acetyltransferase;
43-70 1.03e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 35.56  E-value: 1.03e-03
                         10        20
                 ....*....|....*....|....*...
gi 612670687  43 VSDELGGQGVGKKLVKAVVEHARENHLK 70
Cdd:PRK07757  73 VSEDYRGQGIGRMLVEACLEEARELGVK 100
 
Name Accession Description Interval E-value
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
12-91 9.10e-33

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 108.38  E-value: 9.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612670687  12 KFYIGDDENHALAEITYRfVDNNEINIDHTGVSDELGGQGVGKKLVKAVVEHARENHLKIIASCSFAKHMLEKEDSYQDV 91
Cdd:pfam14542  1 RFEIRVDGGAEVAFLTYR-RGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
4-91 7.04e-30

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 101.38  E-value: 7.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612670687  4 LEIKQGENK--FYIGDDENHAlAEITYRfVDNNEINIDHTGVSDELGGQGVGKKLVKAVVEHARENHLKIIASCSFAKHM 81
Cdd:COG2388   1 MEITHNEEKgrFELEVDGELA-GELTYR-LEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAAY 78
                        90
                ....*....|
gi 612670687 82 LEKEDSYQDV 91
Cdd:COG2388  79 FERHPEYADL 88
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
13-75 1.02e-05

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 40.81  E-value: 1.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612670687  13 FYIGDDENHALAEITYRFVDNNEINIDHTGVSDELGGQGVGKKLVKAVVEHARENHLKIIASC 75
Cdd:COG0454   36 FIAVDDKGEPIGFAGLRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELD 98
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
13-72 2.84e-05

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: 38.41  E-value: 2.84e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612670687 13 FYIGDDENH--ALAEITYRFVDNNEINIDHTGVSDELGGQGVGKKLVKAVVEHARENHLKII 72
Cdd:cd04301   1 FLVAEDDGEivGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
4-70 1.08e-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: 38.05  E-value: 1.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612670687   4 LEIKQGENKFYIGDDENHALAEITYRFVDNNEINIDHTGVSDELGGQGVGKKLVKAVVEHARENHLK 70
Cdd:COG1246   21 YALEEEIGEFWVAEEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLK 87
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
5-73 2.33e-04

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 37.25  E-value: 2.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612670687    5 EIKQGENKFYIGDDENHALAEITYRfvdnNEINIDHTGVSDELGGQGVGKKLVKAVVEHARENHLKIIA 73
Cdd:pfam13673  25 RIDQGEYFFFVAFEGGQIVGVIALR----DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSE 89
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
13-72 3.28e-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: 36.73  E-value: 3.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612670687   13 FYIGDDENHALAEITYRFVDNNEIN--IDHTGVSDELGGQGVGKKLVKAVVEHARENHLKII 72
Cdd:pfam00583  35 FFVAEEDGELVGFASLSIIDDEPPVgeIEGLAVAPEYRGKGIGTALLQALLEWARERGCERI 96
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
26-72 1.01e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 35.02  E-value: 1.01e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 612670687 26 ITYRFVDNNEINIDHTGVSDELGGQGVGKKLVKAVVEHARENHLKII 72
Cdd:COG0456   4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRL 50
PRK07757 PRK07757
N-acetyltransferase;
43-70 1.03e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 35.56  E-value: 1.03e-03
                         10        20
                 ....*....|....*....|....*...
gi 612670687  43 VSDELGGQGVGKKLVKAVVEHARENHLK 70
Cdd:PRK07757  73 VSEDYRGQGIGRMLVEACLEEARELGVK 100
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
43-72 4.21e-03

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 33.91  E-value: 4.21e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 612670687  43 VSDELGGQGVGKKLVKAVVEHARENHLKII 72
Cdd:COG3153   75 VDPEYRGQGIGRALMRAALEAARERGARAV 104
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
43-78 4.30e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 34.20  E-value: 4.30e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 612670687  43 VSDELGGQGVGKKLVKAVVEHARENHLKIIASCSFA 78
Cdd:COG1247   88 VDPDARGRGIGRALLEALIERARARGYRRLVAVVLA 123
 
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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