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Conserved domains on  [gi|504816836|ref|WP_015003938|]
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GNAT family N-acetyltransferase [Paraburkholderia phenoliruptrix]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

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
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 28-193 9.67e-10

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: 55.78  E-value: 9.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816836  28 LVRELTAVDRDRLLthflALDEDDRLLRFGQVVPDHV------IENYVRAIDFTRDTVFGVF---DDQLqltgVGHLAYL 98
Cdd:COG1670    9 RLRPLRPEDAEALA----ELLNDPEVARYLPGPPYSLeearawLERLLADWADGGALPFAIEdkeDGEL----IGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816836  99 PAEGDKRTAEFGVSVLESVRGQGIGSRLFeRAAIR--SRNTHVTTLYMHCLSRNSTMMHIAKKAGMKIEyayGEADAYLT 176
Cdd:COG1670   81 DIDRANRSAEIGYWLAPAYWGKGYATEAL-RALLDyaFEELGLHRVEAEVDPDNTASIRVLEKLGFRLE---GTLRDALV 156

                        170
                 ....*....|....*..
gi 504816836 177 LPPADQTSIITEMLQEQ 193
Cdd:COG1670  157 IDGRYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 28-193 9.67e-10

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: 55.78  E-value: 9.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816836  28 LVRELTAVDRDRLLthflALDEDDRLLRFGQVVPDHV------IENYVRAIDFTRDTVFGVF---DDQLqltgVGHLAYL 98
Cdd:COG1670    9 RLRPLRPEDAEALA----ELLNDPEVARYLPGPPYSLeearawLERLLADWADGGALPFAIEdkeDGEL----IGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816836  99 PAEGDKRTAEFGVSVLESVRGQGIGSRLFeRAAIR--SRNTHVTTLYMHCLSRNSTMMHIAKKAGMKIEyayGEADAYLT 176
Cdd:COG1670   81 DIDRANRSAEIGYWLAPAYWGKGYATEAL-RALLDyaFEELGLHRVEAEVDPDNTASIRVLEKLGFRLE---GTLRDALV 156

                        170
                 ....*....|....*..
gi 504816836 177 LPPADQTSIITEMLQEQ 193
Cdd:COG1670  157 IDGRYRDHVLYSLLREE 173
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 92-162 1.32e-05

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: 42.89  E-value: 1.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504816836   92 VGHLAYLPA-EGDKRTAEFGVSVLESVRGQGIGSRLFERAAIRSRNTHVTTLYMHCLSRNSTMMHIAKKAGM 162
Cdd:pfam00583  45 VGFASLSIIdDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 92-145 1.26e-04

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: 38.80  E-value: 1.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504816836  92 VGHLAYLPAEGDKRTAEFG-VSVLESVRGQGIGSRLFERAAIRSRNTHVTTLYMH 145
Cdd:cd04301   11 VGFASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 28-193 9.67e-10

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: 55.78  E-value: 9.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816836  28 LVRELTAVDRDRLLthflALDEDDRLLRFGQVVPDHV------IENYVRAIDFTRDTVFGVF---DDQLqltgVGHLAYL 98
Cdd:COG1670    9 RLRPLRPEDAEALA----ELLNDPEVARYLPGPPYSLeearawLERLLADWADGGALPFAIEdkeDGEL----IGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816836  99 PAEGDKRTAEFGVSVLESVRGQGIGSRLFeRAAIR--SRNTHVTTLYMHCLSRNSTMMHIAKKAGMKIEyayGEADAYLT 176
Cdd:COG1670   81 DIDRANRSAEIGYWLAPAYWGKGYATEAL-RALLDyaFEELGLHRVEAEVDPDNTASIRVLEKLGFRLE---GTLRDALV 156

                        170
                 ....*....|....*..
gi 504816836 177 LPPADQTSIITEMLQEQ 193
Cdd:COG1670  157 IDGRYRDHVLYSLLREE 173
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
29-165 3.43e-07

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 48.45  E-value: 3.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816836  29 VRELTAVDRDRLLTHFLALDEDDRLLRFGQVVPDHVIENYVRAIDFTRDTVFgVFDDQLQLTGVGHL-AYLPAEGDKRTA 107
Cdd:COG1247    4 IRPATPEDAPAIAAIYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRPVL-VAEEDGEVVGFASLgPFRPRPAYRGTA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504816836 108 EFGVSVLESVRGQGIGSRLFERAAIRSRNTHVTTLYMHCLSRNSTMMHIAKKAGMKIE 165
Cdd:COG1247   83 EESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEV 140
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 92-162 1.32e-05

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: 42.89  E-value: 1.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504816836   92 VGHLAYLPA-EGDKRTAEFGVSVLESVRGQGIGSRLFERAAIRSRNTHVTTLYMHCLSRNSTMMHIAKKAGM 162
Cdd:pfam00583  45 VGFASLSIIdDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 92-149 4.35e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 40.90  E-value: 4.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 504816836   92 VGHLAYLPAEGDKRTAEFGVSVLESVRGQGIGSRLFERAAIRSRNTHVTTLYMHCLSR 149
Cdd:pfam13508  15 VGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR 72
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 59-169 8.93e-05

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 41.19  E-value: 8.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816836  59 VVPDHVIENYVRAID--FTRDTVFGVfDDQLQLTGVGHLAYLpaegDKRTAEFG-VSVLESVRGQGIGSRLFErAAIR-S 134
Cdd:COG0454   14 ILLIEALDAELKAMEgsLAGAEFIAV-DDKGEPIGFAGLRRL----DDKVLELKrLYVLPEYRGKGIGKALLE-ALLEwA 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504816836 135 RNTHVTTLYMHCLSRNSTMMHIAKKAGMKIEYAYG 169
Cdd:COG0454   88 RERGCTALELDTLDGNPAAIRFYERLGFKEIERYV 122
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 92-145 1.26e-04

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: 38.80  E-value: 1.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504816836  92 VGHLAYLPAEGDKRTAEFG-VSVLESVRGQGIGSRLFERAAIRSRNTHVTTLYMH 145
Cdd:cd04301   11 VGFASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 93-175 5.84e-04

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 37.71  E-value: 5.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816836  93 GHLAYLPAEGDKRTAEFGVSVLESVRGQGIGSRLFERAAIRSRNTHVTTLYMHCLSRNSTMMHIAKKAGMKIE---YAYG 169
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVgerPNYY 80


                 ....*.
gi 504816836 170 EADAYL 175
Cdd:COG0456   81 GDDALV 86
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 28-163 9.56e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 38.10  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504816836   28 LVRELTAVDRDRLLthflALDEDDRLLRFGQVVP------DHVIENYVRAIDFTRDTVFGVFDDQLQLTGVGHLAYLpaE 101
Cdd:pfam13302   3 LLRPLTEEDAEALF----ELLSDPEVMRYGVPWPltleeaREWLARIWAADEAERGYGWAIELKDTGFIGSIGLYDI--D 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504816836  102 GDKRTAEFGVSVLESVRGQGIGSrLFERAAIR--SRNTHVTTLYMHCLSRNSTMMHIAKKAGMK 163
Cdd:pfam13302  77 GEPERAELGYWLGPDYWGKGYAT-EAVRALLEyaFEELGLPRLVARIDPENTASRRVLEKLGFK 139
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
96-161 9.77e-04

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 37.20  E-value: 9.77e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504816836  96 AYLPAEGDKRTAEFGVSVLESVRGQGIGSRLFERAAIRSRNTHVTTLYMHCLSRNSTMMHIAKKAG 161
Cdd:COG3393    6 AGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLG 71
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
92-146 1.31e-03

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 37.76  E-value: 1.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504816836  92 VGHLAYLPA--EGDKRTAEFG-VSVLESVRGQGIGSRLFERAAIRSRNTHVTTLYMHC 146
Cdd:COG3153   51 VGHVALSPVdiDGEGPALLLGpLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG 108
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 80-149 8.77e-03

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: 35.35  E-value: 8.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504816836  80 FGVFDDQLQLTGVGHLAYLPAEgdkrTAEFG-VSVLESVRGQGIGSRLFERAAIRSRNTHVTTLYMHCLSR 149
Cdd:COG1246   30 FWVAEEDGEIVGCAALHPLDED----LAELRsLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSA 96
 
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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