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Conserved domains on  [gi|510798120|ref|WP_016172918|]
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MULTISPECIES: aminoglycoside 6'-N-acetyltransferase [Enterococcus]

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 ...
 58-175 1.49e-14

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.83  E-value: 1.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  58 GFVGAIPQYGQTGWEMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIYLGTDDENDettlsqvnlyneplQAIAnik 137
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNE--------------AAIA--- 63

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 510798120 138 nlkahpysFYEKLGYQITGVIPDAngWFKPDIIMSKRI 175
Cdd:COG0456   64 --------LYEKLGFEEVGERPNY--YGDDALVMEKEL 91
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 58-175 1.49e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.83  E-value: 1.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  58 GFVGAIPQYGQTGWEMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIYLGTDDENDettlsqvnlyneplQAIAnik 137
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNE--------------AAIA--- 63

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 510798120 138 nlkahpysFYEKLGYQITGVIPDAngWFKPDIIMSKRI 175
Cdd:COG0456   64 --------LYEKLGFEEVGERPNY--YGDDALVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 15-152 2.04e-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: 58.30  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120   15 DQLADLLAKTWPNDYGQTAKNEVEK-LLAPERIAVAALVDDDLVGFVGAIPQYGQTG-WEMHPLVVVADFRRQKIGARLV 92
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDwDEDASEGFFVAEEDGELVGFASLSIIDDEPPvGEIEGLAVAPEYRGKGIGTALL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120   93 SFLESEIASRGGITIYLGTDDENdettlsqvnlynepLQAIAniknlkahpysFYEKLGY 152
Cdd:pfam00583  82 QALLEWARERGCERIFLEVAADN--------------LAAIA-----------LYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-109 3.42e-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: 3.42e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510798120  48 VAALVDDDLVGFVGAIPQYGQTG-WEMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIYL 109
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PRK03624 PRK03624
putative acetyltransferase; Provisional
 39-176 1.07e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 40.30  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  39 KLLAPERIAVAALVDDDLVGFVGAipQY-GQTGWeMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIYLGTDDENDE 117
Cdd:PRK03624  39 KLNHDPSLFLVAEVGGEVVGTVMG--GYdGHRGW-AYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDA 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 510798120 118 TTlsqvnlyneplqaianiknlkahpySFYEKLGYQItgvipdangwfKPDIIMSKRIG 176
Cdd:PRK03624 116 VL-------------------------GFYEALGYEE-----------QDRISLGKRLI 138
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 58-175 1.49e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.83  E-value: 1.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  58 GFVGAIPQYGQTGWEMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIYLGTDDENDettlsqvnlyneplQAIAnik 137
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNE--------------AAIA--- 63

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 510798120 138 nlkahpysFYEKLGYQITGVIPDAngWFKPDIIMSKRI 175
Cdd:COG0456   64 --------LYEKLGFEEVGERPNY--YGDDALVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 15-152 2.04e-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: 58.30  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120   15 DQLADLLAKTWPNDYGQTAKNEVEK-LLAPERIAVAALVDDDLVGFVGAIPQYGQTG-WEMHPLVVVADFRRQKIGARLV 92
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDwDEDASEGFFVAEEDGELVGFASLSIIDDEPPvGEIEGLAVAPEYRGKGIGTALL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120   93 SFLESEIASRGGITIYLGTDDENdettlsqvnlynepLQAIAniknlkahpysFYEKLGY 152
Cdd:pfam00583  82 QALLEWARERGCERIFLEVAADN--------------LAAIA-----------LYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 50-175 2.78e-11

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: 58.08  E-value: 2.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  50 ALVDDDLVGFVGAIPQYGQTGwEMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIYLGTDDEndettlsqvnlynep 129
Cdd:COG1246   33 AEEDGEIVGCAALHPLDEDLA-ELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSA--------------- 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 510798120 130 lqaianiknlkAHPysFYEKLGYQITGV--IPDANGWFKPDIIMSKRI 175
Cdd:COG1246   97 -----------AIH--FYEKLGFEEIDKedLPYAKVWQRDSVVMEKDL 131
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
15-175 3.13e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.17  E-value: 3.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  15 DQLADLLAKTWPNDYGQTAKNEVEKLLAPERIAVAaLVDDDLVGFVGAIPQ--YGQTGW-EMHPLVVVADFRRQKIGARL 91
Cdd:COG3153   10 EAIAALLRAAFGPGREAELVDRLREDPAAGLSLVA-EDDGEIVGHVALSPVdiDGEGPAlLLGPLAVDPEYRGQGIGRAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  92 VSFLESEIASRGGITIYLGTDDENDEttlsqvnlyneplqaianiknlkahpysFYEKLGYQitgVIPDANGWFKPD-II 170
Cdd:COG3153   89 MRAALEAARERGARAVVLLGDPSLLP----------------------------FYERFGFR---PAGELGLTLGPDeVF 137


                 ....*
gi 510798120 171 MSKRI 175
Cdd:COG3153  138 LAKEL 142
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
38-175 5.40e-10

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 55.39  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  38 EKLLAPERIAVAALVDDDLVGFVGAIPQ-----YGQTGWEMhpLVVVADFRRQKIGARLVSFLESEIASRGGITIYLGTD 112
Cdd:COG1247   45 AAILAPGRPVLVAEEDGEVVGFASLGPFrprpaYRGTAEES--IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVL 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510798120 113 DENDEttlsqvnlyneplqAIAniknlkahpysFYEKLGYQITGVIPDA---NGWFKPDIIMSKRI 175
Cdd:COG1247  123 ADNEA--------------SIA-----------LYEKLGFEEVGTLPEVgfkFGRWLDLVLMQKRL 163
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 43-154 6.54e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.53  E-value: 6.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120   43 PERIAVAALVDDDLVGFVGAIPQYGQTGWEMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIYLGTDDEndettlsq 122
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR-------- 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 510798120  123 vnlyneplqAIAniknlkahpysFYEKLGYQI 154
Cdd:pfam13508  73 ---------AAA-----------FYEKLGFEE 84
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
59-156 1.04e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 50.29  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  59 FVGAIPQYGQTGWEMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIYLGTDDENDEttlsqvnlyneplqAIAnikn 138
Cdd:COG3393    4 AMAGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPA--------------ARR---- 65

                         90
                 ....*....|....*...
gi 510798120 139 lkahpysFYEKLGYQITG 156
Cdd:COG3393   66 -------LYERLGFRPVG 76
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 48-109 3.42e-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: 3.42e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510798120  48 VAALVDDDLVGFVGAIPQYGQTG-WEMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIYL 109
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
48-156 5.58e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 46.72  E-value: 5.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  48 VAALVDDDLVGfVGAIPQYGQTGWEMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIYLGtddendettlSQVnlyn 127
Cdd:COG2153   37 LLAYDDGELVA-TARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLS----------AQA---- 101

                         90       100
                 ....*....|....*....|....*....
gi 510798120 128 eplQAIAniknlkahpysFYEKLGYQITG 156
Cdd:COG2153  102 ---HAVG-----------FYEKLGFVPVG 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 31-163 7.55e-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: 7.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  31 QTAKNEVEKLLAPERIAVAALVDDD--LVGFVGaIPQYGQTGWEMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIY 108
Cdd:COG0454   18 EALDAELKAMEGSLAGAEFIAVDDKgePIGFAG-LRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALE 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 510798120 109 LGTDDENDettlsqvnlyneplqaianiknlKAHPysFYEKLGYQITGVIPDANG 163
Cdd:COG0454   97 LDTLDGNP-----------------------AAIR--FYERLGFKEIERYVAYVG 126
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 32-175 1.65e-05

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: 42.64  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120   32 TAKNEVEKLLAPERIAVAALVDDDLVGFVGAipqygQTGWEMHPLVVVADFRRQKIGARLVSFLESEIasrggitiylgt 111
Cdd:pfam13673  18 SPEALRERIDQGEYFFFVAFEGGQIVGVIAL-----RDRGHISLLFVDPDYQGQGIGKALLEAVEDYA------------ 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510798120  112 ddENDETTLSQVnlyneplqaianikNLKAHPYS--FYEKLGYQITGVIPDANG-WFKPdiiMSKRI 175
Cdd:pfam13673  81 --EKDGIKLSEL--------------TVNASPYAvpFYEKLGFRATGPEQEFNGiRFVP---MEKEL 128
PRK03624 PRK03624
putative acetyltransferase; Provisional
 39-176 1.07e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 40.30  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510798120  39 KLLAPERIAVAALVDDDLVGFVGAipQY-GQTGWeMHPLVVVADFRRQKIGARLVSFLESEIASRGGITIYLGTDDENDE 117
Cdd:PRK03624  39 KLNHDPSLFLVAEVGGEVVGTVMG--GYdGHRGW-AYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDA 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 510798120 118 TTlsqvnlyneplqaianiknlkahpySFYEKLGYQItgvipdangwfKPDIIMSKRIG 176
Cdd:PRK03624 116 VL-------------------------GFYEALGYEE-----------QDRISLGKRLI 138
 
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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