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Conserved domains on  [gi|446470066|ref|WP_000547920|]
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MULTISPECIES: N-acetyltransferase [Bacillus]

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 ...
 207-286 9.49e-16

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 70.84  E-value: 9.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066 207 GYVYVEVNPEFHEANIEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLCLNTNNDRAMKLYKKVGFEEKACLQHY 286
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 207-286 9.49e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 70.84  E-value: 9.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066 207 GYVYVEVNPEFHEANIEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLCLNTNNDRAMKLYKKVGFEEKACLQHY 286
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 165-277 3.64e-12

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: 62.15  E-value: 3.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066  165 FEQFIVLHNNIFPNTYYEGNEIIERLSDTNK---LFVSIKNGKLEGYV-YVEVNPEFHEANIEFIATAENSRRKGVGEQL 240
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDAsegFFVAEEDGELVGFAsLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446470066  241 LQVAIQYIFSfQGMREIVLCLNTNNDRAMKLYKKVGF 277
Cdd:pfam00583  81 LQALLEWARE-RGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 191-286 1.50e-11

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: 60.81  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066  191 SDTNKLFVSIKNGKLEGYVYVEVnpEFHEANIEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLCLNTNNDRAMK 270
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGYAGVQI--VLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQA 104

                          90
                  ....*....|....*.
gi 446470066  271 LYKKVGFEEKACLQHY 286
Cdd:TIGR01575 105 LYKKLGFNEIAIRRNY 120
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 196-260 7.81e-07

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: 45.73  E-value: 7.81e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446470066 196 LFVSIKNGKLEGYVYVEVNP-EFHEANIEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLC 260
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRLE 65
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
201-277 1.64e-05

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 44.54  E-value: 1.64e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446470066 201 KNGKLEGYVYVEVNPEfHEANIEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLCLNTNNDRAMKLYKKVGF 277
Cdd:PRK10975 109 ASGQIQGFVTLRELND-TDARIGLLAVFPGAQGRGIGARLMQAALNWCQA-RGLTRLRVATQMGNLAALRLYIRSGA 183
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 207-286 9.49e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 70.84  E-value: 9.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066 207 GYVYVEVNPEFHEANIEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLCLNTNNDRAMKLYKKVGFEEKACLQHY 286
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 165-277 3.64e-12

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: 62.15  E-value: 3.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066  165 FEQFIVLHNNIFPNTYYEGNEIIERLSDTNK---LFVSIKNGKLEGYV-YVEVNPEFHEANIEFIATAENSRRKGVGEQL 240
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDAsegFFVAEEDGELVGFAsLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446470066  241 LQVAIQYIFSfQGMREIVLCLNTNNDRAMKLYKKVGF 277
Cdd:pfam00583  81 LQALLEWARE-RGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 191-286 1.50e-11

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: 60.81  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066  191 SDTNKLFVSIKNGKLEGYVYVEVnpEFHEANIEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLCLNTNNDRAMK 270
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGYAGVQI--VLDEAHILNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQA 104

                          90
                  ....*....|....*.
gi 446470066  271 LYKKVGFEEKACLQHY 286
Cdd:TIGR01575 105 LYKKLGFNEIAIRRNY 120
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 192-279 4.33e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.46  E-value: 4.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066  192 DTNKLFVSIKNGKLEGYVYVEVNPEFHEANIEFIATAENSRRKGVGEQLLQVAIQYIfsfqGMREIVLCLNTNNDRAMKL 271
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAA----KEGGIKLLELETTNRAAAF 76


                  ....*...
gi 446470066  272 YKKVGFEE 279
Cdd:pfam13508  77 YEKLGFEE 84
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 202-288 8.70e-09

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: 53.85  E-value: 8.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066 202 NGKLEGYV-YVEVNPEFHEANIeFIATAENSRRKGVGEQLLQVAIQYIFSFQGMREIVLCLNTNNDRAMKLYKKVGFEEK 280
Cdd:COG1670   70 DGELIGVVgLYDIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLE 148


                 ....*...
gi 446470066 281 ACLQHYII 288
Cdd:COG1670  149 GTLRDALV 156
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
196-279 6.51e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 51.15  E-value: 6.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066 196 LFVSIKNGKLEGYVYVEVNPEFHEANI---EFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLCLNTNNDRAMKLY 272
Cdd:COG1247   54 VLVAEEDGEVVGFASLGPFRPRPAYRGtaeESIYVDPDARGRGIGRALLEALIERARA-RGYRRLVAVVLADNEASIALY 132


                 ....*..
gi 446470066 273 KKVGFEE 279
Cdd:COG1247  133 EKLGFEE 139
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
222-279 1.04e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 48.75  E-value: 1.04e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446470066 222 IEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLCLNTNNDRAMKLYKKVGFEE 279
Cdd:COG3393   18 ISGVYTHPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFRP 74
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 195-279 2.86e-07

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: 48.45  E-value: 2.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066 195 KLFVSIKNGKLEGYVYVEVNPEfHEANIEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLClnTnNDRAMKLYKK 274
Cdd:COG1246   29 EFWVAEEDGEIVGCAALHPLDE-DLAELRSLAVHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLL--T-TSAAIHFYEK 103


                 ....*
gi 446470066 275 VGFEE 279
Cdd:COG1246  104 LGFEE 108
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 202-279 6.18e-07

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 47.74  E-value: 6.18e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446470066 202 NGKLEGYV-YVEVNPEFHEanIEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLCLNTNNDRAMKLYKKVGFEE 279
Cdd:COG0454   42 KGEPIGFAgLRRLDDKVLE--LKRLYVLPEYRGKGIGKALLEALLEWARE-RGCTALELDTLDGNPAAIRFYERLGFKE 117
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 196-260 7.81e-07

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: 45.73  E-value: 7.81e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446470066 196 LFVSIKNGKLEGYVYVEVNP-EFHEANIEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLC 260
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRLE 65
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
165-279 2.29e-06

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 46.23  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066 165 FEQFIVLHNNIFPNTYYEgnEIIERLSDTNKL---FVSIKNGKLEGYV---YVEVNPEFHEANIEFIATAENSRRKGVGE 238
Cdd:COG3153    9 AEAIAALLRAAFGPGREA--ELVDRLREDPAAglsLVAEDDGEIVGHValsPVDIDGEGPALLLGPLAVDPEYRGQGIGR 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446470066 239 QLLQVAIQYIFSfQGMREIVLclnTNNDRAMKLYKKVGFEE 279
Cdd:COG3153   87 ALMRAALEAARE-RGARAVVL---LGDPSLLPFYERFGFRP 123
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
201-277 1.64e-05

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 44.54  E-value: 1.64e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446470066 201 KNGKLEGYVYVEVNPEfHEANIEFIATAENSRRKGVGEQLLQVAIQYIFSfQGMREIVLCLNTNNDRAMKLYKKVGF 277
Cdd:PRK10975 109 ASGQIQGFVTLRELND-TDARIGLLAVFPGAQGRGIGARLMQAALNWCQA-RGLTRLRVATQMGNLAALRLYIRSGA 183
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 198-278 4.12e-03

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 36.94  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446470066  198 VSIKNGKLEGYV-YVEVNPEFHEANIEFIAtAENSRRKGVGEQLLQVAIQYIFSFQGMREIVLCLNTNNDRAMKLYKKVG 276
Cdd:pfam13302  59 IELKDTGFIGSIgLYDIDGEPERAELGYWL-GPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLG 137


                  ..
gi 446470066  277 FE 278
Cdd:pfam13302 138 FK 139
 
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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