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Conserved domains on  [gi|1526356919|gb|AZH83148|]
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GNAT family N-acetyltransferase [Plantibacter sp. PA-3-X8]

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
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 ...
51-133 7.46e-10

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: 53.29  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISANFDHEstqEEFRSALWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNVIYEPGDLGPEAFFLR 130
Cdd:pfam00583  37 VAEEDGELVGFASLSIIDD---EPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEK 113

                  ...
gi 1526356919 131 VGF 133
Cdd:pfam00583 114 LGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
51-133 7.46e-10

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: 53.29  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISANFDHEstqEEFRSALWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNVIYEPGDLGPEAFFLR 130
Cdd:pfam00583  37 VAEEDGELVGFASLSIIDD---EPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEK 113

                  ...
gi 1526356919 131 VGF 133
Cdd:pfam00583 114 LGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
51-138 1.73e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 53.07  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISanFDHESTQEEFR-SALWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNVIYEPGDLGPEAFFL 129
Cdd:COG1247    56 VAEEDGEVVGFAS--LGPFRPRPAYRgTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYE 133

                  ....*....
gi 1526356919 130 RVGFTPVGE 138
Cdd:COG1247   134 KLGFEEVGT 142
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
51-113 1.27e-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: 43.42  E-value: 1.27e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1526356919  51 VILDGDEVVGFISANFDHESTQEEFrsaLWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHV 113
Cdd:cd04301     3 VAEDDGEIVGFASLSPDGSGGDTAY---IGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
PRK07757 PRK07757
N-acetyltransferase;
51-136 2.38e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 36.33  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISANFdHESTQEEFRSalwrINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNVI-YEPGdlgpeaFFL 129
Cdd:PRK07757   45 VAEEEGEIVGCCALHI-LWEDLAEIRS----LAVSEDYRGQGIGRMLVEACLEEARELGVKRVFALtYQPE------FFE 113

                  ....*..
gi 1526356919 130 RVGFTPV 136
Cdd:PRK07757  114 KLGFREV 120
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
51-133 7.46e-10

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: 53.29  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISANFDHEstqEEFRSALWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNVIYEPGDLGPEAFFLR 130
Cdd:pfam00583  37 VAEEDGELVGFASLSIIDD---EPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEK 113

                  ...
gi 1526356919 131 VGF 133
Cdd:pfam00583 114 LGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
51-138 1.73e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 53.07  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISanFDHESTQEEFR-SALWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNVIYEPGDLGPEAFFL 129
Cdd:COG1247    56 VAEEDGEVVGFAS--LGPFRPRPAYRgTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYE 133

                  ....*....
gi 1526356919 130 RVGFTPVGE 138
Cdd:COG1247   134 KLGFEEVGT 142
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
51-141 6.24e-09

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 51.24  E-value: 6.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISANFDHESTQEEFRsALWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNVIyepGDLGPEAFFLR 130
Cdd:COG3153    43 VAEDDGEIVGHVALSPVDIDGEGPAL-LLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLL---GDPSLLPFYER 118
                          90
                  ....*....|.
gi 1526356919 131 VGFTPVGETQY 141
Cdd:COG3153   119 FGFRPAGELGL 129
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
60-139 5.85e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 47.73  E-value: 5.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  60 GFISANFDHESTQEEfrsaLWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNVIYEPGDLGPEAFFLRVGFTPVGET 139
Cdd:COG0456     1 GFALLGLVDGGDEAE----IEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
51-140 1.81e-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: 47.29  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISANFDHESTQEefrsaLWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNViyepgDLGPEA--FF 128
Cdd:COG1246    32 VAEEDGEIVGCAALHPLDEDLAE-----LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFL-----LTTSAAihFY 101
                          90
                  ....*....|..
gi 1526356919 129 LRVGFTPVGETQ 140
Cdd:COG1246   102 EKLGFEEIDKED 113
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
51-113 1.27e-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: 43.42  E-value: 1.27e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1526356919  51 VILDGDEVVGFISANFDHESTQEEFrsaLWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHV 113
Cdd:cd04301     3 VAEDDGEIVGFASLSPDGSGGDTAY---IGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRL 62
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
81-136 1.92e-05

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 43.28  E-value: 1.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1526356919  81 RINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNV--IYEPGDLgpeAFFLRVGFTPV 136
Cdd:COG1444   490 RIAVHPALQRRGLGSRLLAEIREEAKEEGLDWLGVsfGATPELL---RFWQRNGFVPV 544
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
51-138 6.36e-05

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 40.42  E-value: 6.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISAN-FDHESTQeefrsaLWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNViyEPGDLGPEA--F 127
Cdd:COG0454    38 AVDDKGEPIGFAGLRrLDDKVLE------LKRLYVLPEYRGKGIGKALLEALLEWARERGCTALEL--DTLDGNPAAirF 109
                          90
                  ....*....|.
gi 1526356919 128 FLRVGFTPVGE 138
Cdd:COG0454   110 YERLGFKEIER 120
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
57-138 1.03e-04

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 38.74  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  57 EVVGFISANFDHESTQEefrsaLWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNVIYEPGDLGPEAFFLRVGFTPV 136
Cdd:COG3393     1 ELVAMAGVRAESPGVAE-----ISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPV 75

                  ..
gi 1526356919 137 GE 138
Cdd:COG3393    76 GE 77
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
51-138 2.88e-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: 38.83  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISANFDHEstqeEFRSALWRINVDADDQGRGVGRFAVASLIEEA-KQRDFDHVNVIYEPGDLGPEAFFL 129
Cdd:COG1670    66 EDKEDGELIGVVGLYDIDR----ANRSAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLE 141

                  ....*....
gi 1526356919 130 RVGFTPVGE 138
Cdd:COG1670   142 KLGFRLEGT 150
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
51-135 3.98e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 37.05  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISANFDHEstqeEFRSALWRINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNVIYEPGDLgpeAFFLR 130
Cdd:pfam13508   7 VAEDDGKIVGFAALLPLDD----EGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAA---AFYEK 79

                  ....*
gi 1526356919 131 VGFTP 135
Cdd:pfam13508  80 LGFEE 84
PRK07757 PRK07757
N-acetyltransferase;
51-136 2.38e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 36.33  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526356919  51 VILDGDEVVGFISANFdHESTQEEFRSalwrINVDADDQGRGVGRFAVASLIEEAKQRDFDHVNVI-YEPGdlgpeaFFL 129
Cdd:PRK07757   45 VAEEEGEIVGCCALHI-LWEDLAEIRS----LAVSEDYRGQGIGRMLVEACLEEARELGVKRVFALtYQPE------FFE 113

                  ....*..
gi 1526356919 130 RVGFTPV 136
Cdd:PRK07757  114 KLGFREV 120
 
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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