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Conserved domains on  [gi|18404927|ref|NP_565898|]
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Acyl-CoA N-acyltransferases (NAT) superfamily protein [Arabidopsis thaliana]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

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:  15581578|10940244|9175471|27367672|26818562
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 87-203 6.55e-18

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: 76.40  E-value: 6.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404927    87 FPTTHDASSPDFTPFLETHKVDLPIEDPDREK--FLPDKLNDVVVaGFVLFFPNYPSFlakQGFYIEDIFMREPYRRKGF 164
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASegFFVAEEDGELV-GFASLSIIDDEP---PVGEIEGLAVAPEYRGKGI 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 18404927   165 GKLLLTAVAKQAVKLGVGRVEWIVIDWNVNAINFYEQMG 203
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 87-203 6.55e-18

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: 76.40  E-value: 6.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404927    87 FPTTHDASSPDFTPFLETHKVDLPIEDPDREK--FLPDKLNDVVVaGFVLFFPNYPSFlakQGFYIEDIFMREPYRRKGF 164
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASegFFVAEEDGELV-GFASLSIIDDEP---PVGEIEGLAVAPEYRGKGI 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 18404927   165 GKLLLTAVAKQAVKLGVGRVEWIVIDWNVNAINFYEQMG 203
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
108-211 9.18e-18

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 77.34  E-value: 9.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404927 108 DLPIEDPDREKFLPDKLND---VVVA-------GFVLFFPnYPSFLAKQGFYIEDIFMREPYRRKGFGKLLLTAVAKQAV 177
Cdd:COG1247  32 TEPPSEEEREAWFAAILAPgrpVLVAeedgevvGFASLGP-FRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERAR 110

                        90       100       110
                ....*....|....*....|....*....|....
gi 18404927 178 KLGVGRVEWIVIDWNVNAINFYEQMGAQVFKEWR 211
Cdd:COG1247 111 ARGYRRLVAVVLADNEASIALYEKLGFEEVGTLP 144
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 124-185 3.21e-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: 46.11  E-value: 3.21e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18404927 124 LNDVVVAGFVLFFPNYPSflaKQGFYIEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVGRVE 185
Cdd:cd04301   5 EDDGEIVGFASLSPDGSG---GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
PRK09831 PRK09831
GNAT family N-acetyltransferase;
142-214 3.11e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 36.86  E-value: 3.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18404927  142 FLAKQGFYIEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVgrvewiviDWNVNAINFYEQMGAQVFKEWRL-CR 214
Cdd:PRK09831  67 FITCIEHYIDMLFVDPEYTRRGVASALLKPLIKSESELTV--------DASITAKPFFERYGFQTVKQQRVeCR 132
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 87-203 6.55e-18

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: 76.40  E-value: 6.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404927    87 FPTTHDASSPDFTPFLETHKVDLPIEDPDREK--FLPDKLNDVVVaGFVLFFPNYPSFlakQGFYIEDIFMREPYRRKGF 164
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASegFFVAEEDGELV-GFASLSIIDDEP---PVGEIEGLAVAPEYRGKGI 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 18404927   165 GKLLLTAVAKQAVKLGVGRVEWIVIDWNVNAINFYEQMG 203
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLG 115
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
108-211 9.18e-18

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 77.34  E-value: 9.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404927 108 DLPIEDPDREKFLPDKLND---VVVA-------GFVLFFPnYPSFLAKQGFYIEDIFMREPYRRKGFGKLLLTAVAKQAV 177
Cdd:COG1247  32 TEPPSEEEREAWFAAILAPgrpVLVAeedgevvGFASLGP-FRPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERAR 110

                        90       100       110
                ....*....|....*....|....*....|....
gi 18404927 178 KLGVGRVEWIVIDWNVNAINFYEQMGAQVFKEWR 211
Cdd:COG1247 111 ARGYRRLVAVVLADNEASIALYEKLGFEEVGTLP 144
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 131-209 1.59e-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: 1.59e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18404927 131 GFVLFFPNYPsflaKQGFYIEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVGRVEWIVIDWNVNAINFYEQMGAQVFKE 209
Cdd:COG0456   1 GFALLGLVDG----GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 129-211 1.92e-13

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 65.07  E-value: 1.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404927 129 VAGFVLFFPnypsfLAKQGFYIEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVGRVEWIVIDWNVNAINFYEQMGAQVFK 208
Cdd:COG0454  45 PIGFAGLRR-----LDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIE 119


                ...
gi 18404927 209 EWR 211
Cdd:COG0454 120 RYV 122
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
149-216 7.94e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 53.76  E-value: 7.94e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18404927 149 YIEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVGRVEWIVIDWNVNAINFYEQMGAQVFKEWRLCRLT 216
Cdd:COG3393  17 EISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLFR 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
129-224 4.03e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 50.47  E-value: 4.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404927 129 VAGFVLFFPnYPSFLAKQGFYIEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVGRVewiVIDWNVNAINFYEQMGAQVFK 208
Cdd:COG3153  50 IVGHVALSP-VDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAV---VLLGDPSLLPFYERFGFRPAG 125

                        90
                ....*....|....*.
gi 18404927 209 EWRLCRLTGDALQAID 224
Cdd:COG3153 126 ELGLTLGPDEVFLAKE 141
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 26-203 4.46e-08

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: 50.38  E-value: 4.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404927  26 RIRLATPTDVPFIHKLIHQMAVFERLTHLFVATESGlastlfnsrpfqavtvflleispspfptthdasspdftpfleth 105
Cdd:COG1246   2 TIRPATPDDVPAILELIRPYALEEEIGEFWVAEEDG-------------------------------------------- 37

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404927 106 kvdlpiedpdrekflpdklndvVVAGFVLFFPNYPSFLakqgfYIEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVGRVE 185
Cdd:COG1246  38 ----------------------EIVGCAALHPLDEDLA-----ELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLF 90

                       170
                ....*....|....*...
gi 18404927 186 WIVidwNVNAINFYEQMG 203
Cdd:COG1246  91 LLT---TSAAIHFYEKLG 105
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 124-185 3.21e-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: 46.11  E-value: 3.21e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18404927 124 LNDVVVAGFVLFFPNYPSflaKQGFYIEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVGRVE 185
Cdd:cd04301   5 EDDGEIVGFASLSPDGSG---GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 125-209 4.15e-07

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 46.29  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404927   125 NDVVVAGFVLFFPNYPSFlakqGFYIEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVGRVEWIVidwNVNAINFYEQMGa 204
Cdd:pfam13508  10 DDGKIVGFAALLPLDDEG----ALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEKLG- 81


                  ....*
gi 18404927   205 qvFKE 209
Cdd:pfam13508  82 --FEE 84
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 153-205 1.15e-04

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: 41.52  E-value: 1.15e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 18404927 153 IFMREPYRRKGFGKLLLTAVAKQAVK-LGVGRVEWIVIDWNVNAINFYEQMGAQ 205
Cdd:COG1670  93 YWLAPAYWGKGYATEALRALLDYAFEeLGLHRVEAEVDPDNTASIRVLEKLGFR 146
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 143-206 1.65e-04

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: 39.24  E-value: 1.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18404927   143 LAKQGFYIEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVGRVEWIVIDwNVNAINFYEQMGAQV 206
Cdd:pfam08445  17 LRLPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVVAG-NTPSRRLYEKLGFRK 79
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
150-203 1.30e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 37.86  E-value: 1.30e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 18404927 150 IEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVGRvewIVIDWNVNAINFYEQMG 203
Cdd:COG2153  61 IGRVAVLPEYRGQGLGRALMEAAIEEARERGARR---IVLSAQAHAVGFYEKLG 111
PRK09831 PRK09831
GNAT family N-acetyltransferase;
142-214 3.11e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 36.86  E-value: 3.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18404927  142 FLAKQGFYIEDIFMREPYRRKGFGKLLLTAVAKQAVKLGVgrvewiviDWNVNAINFYEQMGAQVFKEWRL-CR 214
Cdd:PRK09831  67 FITCIEHYIDMLFVDPEYTRRGVASALLKPLIKSESELTV--------DASITAKPFFERYGFQTVKQQRVeCR 132
 
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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