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Conserved domains on  [gi|1728079423|ref|WP_147808096|]
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N-acetyltransferase [Bacillus sp. SH7-1]

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 ...
 206-285 4.05e-15

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 69.30  E-value: 4.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 206 GYVYVEVNPGFQEANIEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELCLNTNNDGAMKLYKKVGFEEKACLQHY 285
Cdd:COG0456     1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 206-285 4.05e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 69.30  E-value: 4.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 206 GYVYVEVNPGFQEANIEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELCLNTNNDGAMKLYKKVGFEEKACLQHY 285
Cdd:COG0456     1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 164-276 1.72e-11

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: 60.22  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 164 FEQFVALHNHVFPNTYYKGDEIIERLSDTNK---LFVSMKNDKLEGYV-YVEVNPGFQEANIEFIATAENSRRNGIGERL 239
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDAsegFFVAEEDGELVGFAsLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1728079423 240 LQAAIQYIFSfKGMREIELCLNTNNDGAMKLYKKVGF 276
Cdd:pfam00583  81 LQALLEWARE-RGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 190-285 7.32e-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: 58.88  E-value: 7.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 190 SDTNKLFVSMKNDKLEGYVYVEVNPGfqEANIEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELCLNTNNDGAMK 269
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGYAGVQIVLD--EAHILNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQA 104

                          90
                  ....*....|....*.
gi 1728079423 270 LYKKVGFEEKACLQHY 285
Cdd:TIGR01575 105 LYKKLGFNEIAIRRNY 120
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 195-259 8.95e-06

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: 42.65  E-value: 8.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728079423 195 LFVSMKNDKLEGYVYVEVNPGFQ-EANIEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELC 259
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGdTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRLE 65
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
217-276 3.13e-04

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 40.68  E-value: 3.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 217 QEANIEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELCLNTNNDGAMKLYKKVGF 276
Cdd:PRK10975  125 TDARIGLLAVFPGAQGRGIGARLMQAALNWCQA-RGLTRLRVATQMGNLAALRLYIRSGA 183
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 206-285 4.05e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 69.30  E-value: 4.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 206 GYVYVEVNPGFQEANIEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELCLNTNNDGAMKLYKKVGFEEKACLQHY 285
Cdd:COG0456     1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERPNY 79
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 164-276 1.72e-11

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: 60.22  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 164 FEQFVALHNHVFPNTYYKGDEIIERLSDTNK---LFVSMKNDKLEGYV-YVEVNPGFQEANIEFIATAENSRRNGIGERL 239
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDAsegFFVAEEDGELVGFAsLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1728079423 240 LQAAIQYIFSfKGMREIELCLNTNNDGAMKLYKKVGF 276
Cdd:pfam00583  81 LQALLEWARE-RGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 190-285 7.32e-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: 58.88  E-value: 7.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 190 SDTNKLFVSMKNDKLEGYVYVEVNPGfqEANIEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELCLNTNNDGAMK 269
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGYAGVQIVLD--EAHILNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQA 104

                          90
                  ....*....|....*.
gi 1728079423 270 LYKKVGFEEKACLQHY 285
Cdd:TIGR01575 105 LYKKLGFNEIAIRRNY 120
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 191-278 8.89e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 51.69  E-value: 8.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 191 DTNKLFVSMKNDKLEGYVYVEVNPGFQEANIEFIATAENSRRNGIGERLLQAAIQYifsfKGMREIELCLNTNNDGAMKL 270
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAA----AKEGGIKLLELETTNRAAAF 76


                  ....*...
gi 1728079423 271 YKKVGFEE 278
Cdd:pfam13508  77 YEKLGFEE 84
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
155-278 2.68e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 52.30  E-value: 2.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 155 NIEEALPQMFEQFVALHNHVFPN---TYYKG----DEIIERLSDTNK----LFVSMKNDKLEGYVYVEVN---PGFQEAN 220
Cdd:COG1247     3 TIRPATPEDAPAIAAIYNEAIAEgtaTFETEppseEEREAWFAAILApgrpVLVAEEDGEVVGFASLGPFrprPAYRGTA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1728079423 221 IEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELCLNTNNDGAMKLYKKVGFEE 278
Cdd:COG1247    83 EESIYVDPDARGRGIGRALLEALIERARA-RGYRRLVAVVLADNEASIALYEKLGFEE 139
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
156-278 4.15e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 51.24  E-value: 4.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 156 IEEALPQMFEQFVALHNHVFPNTYYkgDEIIERLSDTNKL---FVSMKNDKLEGYV---YVEVNPGFQEANIEFIATAEN 229
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGRE--AELVDRLREDPAAglsLVAEDDGEIVGHValsPVDIDGEGPALLLGPLAVDPE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1728079423 230 SRRNGIGERLLQAAIQYifsFKGMREIELCLNTnNDGAMKLYKKVGFEE 278
Cdd:COG3153    79 YRGQGIGRALMRAALEA---ARERGARAVVLLG-DPSLLPFYERFGFRP 123
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 201-287 1.62e-07

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: 50.00  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 201 NDKLEGYV-YVEVNPGFQEANIeFIATAENSRRNGIGERLLQAAIQYIFSFKGMREIELCLNTNNDGAMKLYKKVGFEEK 279
Cdd:COG1670    70 DGELIGVVgLYDIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLE 148


                  ....*...
gi 1728079423 280 ACLQHYII 287
Cdd:COG1670   149 GTLRDALV 156
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
221-278 1.70e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 47.98  E-value: 1.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1728079423 221 IEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELCLNTNNDGAMKLYKKVGFEE 278
Cdd:COG3393    18 ISGVYTHPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFRP 74
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 221-278 9.69e-07

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 47.36  E-value: 9.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1728079423 221 IEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELCLNTNNDGAMKLYKKVGFEE 278
Cdd:COG0454    61 LKRLYVLPEYRGKGIGKALLEALLEWARE-RGCTALELDTLDGNPAAIRFYERLGFKE 117
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 194-278 3.13e-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: 45.75  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 194 KLFVSMKNDKLEGYVYVEVNPGfQEANIEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELClnTnNDGAMKLYKK 273
Cdd:COG1246    29 EFWVAEEDGEIVGCAALHPLDE-DLAELRSLAVHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLL--T-TSAAIHFYEK 103


                  ....*
gi 1728079423 274 VGFEE 278
Cdd:COG1246   104 LGFEE 108
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 195-259 8.95e-06

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: 42.65  E-value: 8.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728079423 195 LFVSMKNDKLEGYVYVEVNPGFQ-EANIEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELC 259
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGdTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
214-278 2.91e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 42.86  E-value: 2.91e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728079423 214 PGFQEANIEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELclntnN--DGAMKLYKKVGFEE 278
Cdd:COG2153    54 PGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARE-RGARRIVL-----SaqAHAVGFYEKLGFVP 114
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
217-276 3.13e-04

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 40.68  E-value: 3.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 217 QEANIEFIATAENSRRNGIGERLLQAAIQYIFSfKGMREIELCLNTNNDGAMKLYKKVGF 276
Cdd:PRK10975  125 TDARIGLLAVFPGAQGRGIGARLMQAALNWCQA-RGLTRLRVATQMGNLAALRLYIRSGA 183
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 178-278 2.26e-03

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: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728079423 178 TYYKGDEIIERLSD-TNKLFVSMKNDKLEGYVYVEVNPGfqeanIEFIATAENSRRNGIGERLLQAAIQYIfSFKGMREI 256
Cdd:pfam13673  15 EFISPEALRERIDQgEYFFFVAFEGGQIVGVIALRDRGH-----ISLLFVDPDYQGQGIGKALLEAVEDYA-EKDGIKLS 88

                          90       100
                  ....*....|....*....|..
gi 1728079423 257 ELCLNTNNdGAMKLYKKVGFEE 278
Cdd:pfam13673  89 ELTVNASP-YAVPFYEKLGFRA 109
 
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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