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Conserved domains on  [gi|497616304|ref|WP_009930488|]
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GNAT family N-acetyltransferase [Listeria monocytogenes]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
63-166 7.18e-12

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 60.01  E-value: 7.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497616304  63 VLDENEKPIGLVDIVSDYPRKGRWFIGL--LLLTPDARHNGLGKVLHQTIKEWANDGGADSLALGVLAENEKGRGFFEFL 140
Cdd:COG1247   56 VAEEDGEVVGFASLGPFRPRPAYRGTAEesIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKL 135

                         90       100
                 ....*....|....*....|....*...
gi 497616304 141 GYTKEET--KQASYGGKEQEVSIFTLAI 166
Cdd:COG1247  136 GFEEVGTlpEVGFKFGRWLDLVLMQKRL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
63-166 7.18e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 60.01  E-value: 7.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497616304  63 VLDENEKPIGLVDIVSDYPRKGRWFIGL--LLLTPDARHNGLGKVLHQTIKEWANDGGADSLALGVLAENEKGRGFFEFL 140
Cdd:COG1247   56 VAEEDGEVVGFASLGPFRPRPAYRGTAEesIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKL 135

                         90       100
                 ....*....|....*....|....*...
gi 497616304 141 GYTKEET--KQASYGGKEQEVSIFTLAI 166
Cdd:COG1247  136 GFEEVGTlpEVGFKFGRWLDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 63-142 4.52e-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: 56.76  E-value: 4.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497616304   63 VLDENEKPIGLVDIVSDYPRKGRWFIGLLLLTPDARHNGLGKVLHQTIKEWANDGGADSLALGVLAENEKGRGFFEFLGY 142
Cdd:pfam00583  37 VAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 61-124 2.89e-08

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: 48.04  E-value: 2.89e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497616304  61 LAVLDENEKPIGLVDIVSDYPRKGRWFIGLLLLTPDARHNGLGKVLHQTIKEWANDGGADSLAL 124
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PRK03624 PRK03624
putative acetyltransferase; Provisional
 95-147 2.51e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.45  E-value: 2.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497616304  95 PDARHNGLGKVLHQTIKEWANDGGADSLALGVLAENEKGRGFFEFLGYTKEET 147
Cdd:PRK03624  78 PDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDR 130
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
63-166 7.18e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 60.01  E-value: 7.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497616304  63 VLDENEKPIGLVDIVSDYPRKGRWFIGL--LLLTPDARHNGLGKVLHQTIKEWANDGGADSLALGVLAENEKGRGFFEFL 140
Cdd:COG1247   56 VAEEDGEVVGFASLGPFRPRPAYRGTAEesIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKL 135

                         90       100
                 ....*....|....*....|....*...
gi 497616304 141 GYTKEET--KQASYGGKEQEVSIFTLAI 166
Cdd:COG1247  136 GFEEVGTlpEVGFKFGRWLDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 63-142 4.52e-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: 56.76  E-value: 4.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497616304   63 VLDENEKPIGLVDIVSDYPRKGRWFIGLLLLTPDARHNGLGKVLHQTIKEWANDGGADSLALGVLAENEKGRGFFEFLGY 142
Cdd:pfam00583  37 VAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 76-156 2.27e-10

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 54.28  E-value: 2.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497616304  76 IVSDYPRKGRWFIGLLLLTPDARHNGLGKVLHQTIKEWANDGGADSLALGVLAENEKGRGFFEFLGYTKEETKQASYGGK 155
Cdd:COG0456    4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDD 83


                 .
gi 497616304 156 E 156
Cdd:COG0456   84 A 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 61-124 2.89e-08

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: 48.04  E-value: 2.89e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497616304  61 LAVLDENEKPIGLVDIVSDYPRKGRWFIGLLLLTPDARHNGLGKVLHQTIKEWANDGGADSLAL 124
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 63-162 5.75e-07

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 46.20  E-value: 5.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497616304  63 VLDENEKPIGLVdIVSDYPRKGrWFIGLLLLTPDARHNGLGKVLHQTIKEWANDGGADSLALGVLAENEKGRGFFEFLGY 142
Cdd:COG0454   38 AVDDKGEPIGFA-GLRRLDDKV-LELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGF 115

                         90       100
                 ....*....|....*....|.
gi 497616304 143 TK-EETKQASYGGKEQEVSIF 162
Cdd:COG0454  116 KEiERYVAYVGGEFEKELSLS 136
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 36-145 6.71e-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: 46.92  E-value: 6.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497616304  36 PASKSDALKIITEIPDGKTRFDKFVLAVLD-ENEKPIGLVDIVSDYPRKGRWFIGLLLLtPDARHNGLGKVLHQTIKEWA 114
Cdd:COG1670   38 PYSLEEARAWLERLLADWADGGALPFAIEDkEDGELIGVVGLYDIDRANRSAEIGYWLA-PAYWGKGYATEALRALLDYA 116

                         90       100       110
                 ....*....|....*....|....*....|..
gi 497616304 115 -NDGGADSLALGVLAENEKGRGFFEFLGYTKE 145
Cdd:COG1670  117 fEELGLHRVEAEVDPDNTASIRVLEKLGFRLE 148
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 36-162 8.53e-05

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: 40.36  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497616304  36 PASKSDALKIITEIPDGKTRFDKFVLAVLDENEKPIGLVDIVSDYPRKGrwFIGLLLLTPDARHNGLGKVLHQTIKEWAN 115
Cdd:COG1246    5 PATPDDVPAILELIRPYALEEEIGEFWVAEEDGEIVGCAALHPLDEDLA--ELRSLAVHPDYRGRGIGRRLLEALLAEAR 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 497616304 116 DGGADSLALGVlaeNEKGRGFFEFLGYTKEETKQASYGGKEQEVSIF 162
Cdd:COG1246   83 ELGLKRLFLLT---TSAAIHFYEKLGFEEIDKEDLPYAKVWQRDSVV 126
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
63-156 1.76e-04

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 39.68  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497616304  63 VLDENEKPIG--LVDIVSDYPRKGRWFIGLLLLTPDARHNGLGKVLHQTIKEWANDGGADSLALGVlaeNEKGRGFFEFL 140
Cdd:COG3153   43 VAEDDGEIVGhvALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERF 119

                         90
                 ....*....|....*.
gi 497616304 141 GYTKEETKQASYGGKE 156
Cdd:COG3153  120 GFRPAGELGLTLGPDE 135
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 63-144 7.46e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 36.66  E-value: 7.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497616304   63 VLDENEKPIGLVDIVSDYPRKGRWFIGLLLLtPDARHNGLGKVLHQTIKEWANDGGADSLalgVLAENEKGRGFFEFLGY 142
Cdd:pfam13508   7 VAEDDGKIVGFAALLPLDDEGALAELRLAVH-PEYRGQGIGRALLEAAEAAAKEGGIKLL---ELETTNRAAAFYEKLGF 82


                  ..
gi 497616304  143 TK 144
Cdd:pfam13508  83 EE 84
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
69-143 2.46e-03

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 35.27  E-value: 2.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497616304  69 KPIGLVDIVSDYPrkGRWFIGLLLLTPDARHNGLGKVLHQTIKEWANDGGADSLALGVLAENEKGRGFFEFLGYT 143
Cdd:COG3393    1 ELVAMAGVRAESP--GVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFR 73
PRK03624 PRK03624
putative acetyltransferase; Provisional
 95-147 2.51e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 36.45  E-value: 2.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497616304  95 PDARHNGLGKVLHQTIKEWANDGGADSLALGVLAENEKGRGFFEFLGYTKEET 147
Cdd:PRK03624  78 PDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDR 130
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 87-144 6.69e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 34.23  E-value: 6.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 497616304   87 FIGLLLLTPDARHNGLGKVLHQTIKEWANDGGADSLALgVLAENEKGRGFFEFLGYTK 144
Cdd:pfam08445  23 ELGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAV-VVAGNTPSRRLYEKLGFRK 79
 
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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