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Conserved domains on  [gi|1071358978|ref|WP_069792980|]
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MULTISPECIES: GNAT family N-acetyltransferase [Staphylococcus]

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
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 105-185 5.45e-16

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 69.68  E-value: 5.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978 105 EANDDEWYIETVATFPEYRGRGVATQLVQHVIETYSE---EKWSLNCDVHNDGALYVYKKLGFQIASEFDLYGHMH-YHM 180
Cdd:COG0456     8 VDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARErgaRRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDaLVM 87


                  ....*
gi 1071358978 181 ILPIS 185
Cdd:COG0456    88 EKELA 92
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-184 2.95e-12

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 61.25  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978   2 IRKANPSDTSKIAELCYIIWSGLDiqmvadidESRLLKIMEQSmvdvpyrGHYSNTWVYEIEGEIAGCLIAYPGDKEIEL 81
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGR--------EAELVDRLRED-------PAAGLSLVAEDDGEIVGHVALSPVDIDGEG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  82 EQAWLNMdldddirsygtpmpmkeanddewyietVATFPEYRGRGVATQLVQHVIETYSEEKWSLnCDVH-NDGALYVYK 160
Cdd:COG3153    66 PALLLGP---------------------------LAVDPEYRGQGIGRALMRAALEAARERGARA-VVLLgDPSLLPFYE 117

                         170       180
                  ....*....|....*....|....*
gi 1071358978 161 KLGFQIASEFDL-YGHMHYHMILPI 184
Cdd:COG3153   118 RFGFRPAGELGLtLGPDEVFLAKEL 142
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 105-185 5.45e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 69.68  E-value: 5.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978 105 EANDDEWYIETVATFPEYRGRGVATQLVQHVIETYSE---EKWSLNCDVHNDGALYVYKKLGFQIASEFDLYGHMH-YHM 180
Cdd:COG0456     8 VDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARErgaRRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDaLVM 87


                  ....*
gi 1071358978 181 ILPIS 185
Cdd:COG0456    88 EKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 57-164 6.68e-13

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: 62.15  E-value: 6.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  57 TWVYEIEGEIAGCLIAYPGDKEieleqawlnmdldddirsygtpmpmkeanDDEWYIETVATFPEYRGRGVATQLVQHVI 136
Cdd:pfam00583  35 FFVAEEDGELVGFASLSIIDDE-----------------------------PPVGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1071358978 137 ETYSE---EKWSLNCDVHNDGALYVYKKLGF 164
Cdd:pfam00583  86 EWARErgcERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-184 2.95e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 61.25  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978   2 IRKANPSDTSKIAELCYIIWSGLDiqmvadidESRLLKIMEQSmvdvpyrGHYSNTWVYEIEGEIAGCLIAYPGDKEIEL 81
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGR--------EAELVDRLRED-------PAAGLSLVAEDDGEIVGHVALSPVDIDGEG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  82 EQAWLNMdldddirsygtpmpmkeanddewyietVATFPEYRGRGVATQLVQHVIETYSEEKWSLnCDVH-NDGALYVYK 160
Cdd:COG3153    66 PALLLGP---------------------------LAVDPEYRGQGIGRALMRAALEAARERGARA-VVLLgDPSLLPFYE 117

                         170       180
                  ....*....|....*....|....*
gi 1071358978 161 KLGFQIASEFDL-YGHMHYHMILPI 184
Cdd:COG3153   118 RFGFRPAGELGLtLGPDEVFLAKEL 142
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-137 2.77e-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: 48.43  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  58 WVYEIEGEIAGCLIAYPGDKEieleqawlnmdldddirsygtpmpmkeanDDEWYIETVATFPEYRGRGVATQLVQHVIE 137
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSG-----------------------------GDTAYIGDLAVLPEYRGKGIGSALLEAAEE 52
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-143 1.33e-07

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 48.34  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  55 SNTWVYEIEGEIAGCLIAYPgdkeieleqawlnmdldDDIRSYGTPMPMKeanddewYIETVATFPEYRGRGVATQLVQH 134
Cdd:pfam13527  39 GRVLGAFDDGELVSTLALYP-----------------FELNVPGKTLPAA-------GITGVATYPEYRGRGVMSRLLRR 94


                  ....*....
gi 1071358978 135 VIETYSEEK 143
Cdd:pfam13527  95 SLEEMRERG 103
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 109-167 2.42e-05

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 42.32  E-value: 2.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1071358978 109 DEWYIETVATFPEYRGRGVATQLVQHVIETYSEE---KWSLNCDVHNDGALYVYKKLGFQIA 167
Cdd:TIGR01575  53 DEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRgvnEIFLEVRVSNIAAQALYKKLGFNEI 114
PRK10514 PRK10514
putative acetyltransferase; Provisional
 120-171 3.42e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 39.22  E-value: 3.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1071358978 120 PEYRGRGVATQLVQHVIETYSEekwsLNCDVH--NDGALYVYKKLGFQIA--SEFD 171
Cdd:PRK10514   79 PDVRGCGVGRMLVEHALSLHPE----LTTDVNeqNEQAVGFYKKMGFKVTgrSEVD 130
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 105-185 5.45e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 69.68  E-value: 5.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978 105 EANDDEWYIETVATFPEYRGRGVATQLVQHVIETYSE---EKWSLNCDVHNDGALYVYKKLGFQIASEFDLYGHMH-YHM 180
Cdd:COG0456     8 VDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARErgaRRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDaLVM 87


                  ....*
gi 1071358978 181 ILPIS 185
Cdd:COG0456    88 EKELA 92
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
107-173 1.78e-13

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 63.00  E-value: 1.78e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978 107 NDDEWYIETVATFPEYRGRGVATQLVQHVIETYSEE---KWSLNCDVHNDGALYVYKKLGFQIASEFDLY 173
Cdd:COG3393    12 SPGVAEISGVYTHPEYRGRGLASALVAALAREALARgarTPFLYVDADNPAARRLYERLGFRPVGEYATV 81
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 57-164 6.68e-13

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: 62.15  E-value: 6.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  57 TWVYEIEGEIAGCLIAYPGDKEieleqawlnmdldddirsygtpmpmkeanDDEWYIETVATFPEYRGRGVATQLVQHVI 136
Cdd:pfam00583  35 FFVAEEDGELVGFASLSIIDDE-----------------------------PPVGEIEGLAVAPEYRGKGIGTALLQALL 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1071358978 137 ETYSE---EKWSLNCDVHNDGALYVYKKLGF 164
Cdd:pfam00583  86 EWARErgcERIFLEVAADNLAAIALYEKLGF 116
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
105-185 1.02e-12

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 62.12  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978 105 EANDDEWYIETVATFPEYRGRGVATQLVQHVIETYSEEKWS---LNCDVHndgALYVYKKLGFQIASE-FDLYGHMHYHM 180
Cdd:COG2153    53 PPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARrivLSAQAH---AVGFYEKLGFVPVGEeFLEAGIPHIDM 129


                  ....*
gi 1071358978 181 ILPIS 185
Cdd:COG2153   130 RKPLS 134
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-184 2.95e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 61.25  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978   2 IRKANPSDTSKIAELCYIIWSGLDiqmvadidESRLLKIMEQSmvdvpyrGHYSNTWVYEIEGEIAGCLIAYPGDKEIEL 81
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGR--------EAELVDRLRED-------PAAGLSLVAEDDGEIVGHVALSPVDIDGEG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  82 EQAWLNMdldddirsygtpmpmkeanddewyietVATFPEYRGRGVATQLVQHVIETYSEEKWSLnCDVH-NDGALYVYK 160
Cdd:COG3153    66 PALLLGP---------------------------LAVDPEYRGQGIGRALMRAALEAARERGARA-VVLLgDPSLLPFYE 117

                         170       180
                  ....*....|....*....|....*
gi 1071358978 161 KLGFQIASEFDL-YGHMHYHMILPI 184
Cdd:COG3153   118 RFGFRPAGELGLtLGPDEVFLAKEL 142
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-177 4.22e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 58.47  E-value: 4.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978   1 MIRKANPSDTSKIAElcyIIWSGLDIQMVADIDESRLLKIMEQSMVDVPYRGHYsnTWVYEIEGEIAGCLIAYPgdkeie 80
Cdd:COG1247     3 TIRPATPEDAPAIAA---IYNEAIAEGTATFETEPPSEEEREAWFAAILAPGRP--VLVAEEDGEVVGFASLGP------ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  81 leqawlnmdldddIRSYgtpmpmkeANDDEWYIETVATFPEYRGRGVATQLVQHVIEtYSEEK--WSLNCDV--HNDGAL 156
Cdd:COG1247    72 -------------FRPR--------PAYRGTAEESIYVDPDARGRGIGRALLEALIE-RARARgyRRLVAVVlaDNEASI 129

                         170       180
                  ....*....|....*....|.
gi 1071358978 157 YVYKKLGFQIASEFDLYGHMH 177
Cdd:COG1247   130 ALYEKLGFEEVGTLPEVGFKF 150
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-166 1.98e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.07  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  55 SNTWVYEIEGEIAGCLIAYPGDkeieleqawlnmdldddirsygtpmpmkeaNDDEWYIETVATFPEYRGRGVATQLVQH 134
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAALLPLD------------------------------DEGALAELRLAVHPEYRGQGIGRALLEA 52

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1071358978 135 VIETYSEEKWSLNCDVHNDGALYVYKKLGFQI 166
Cdd:pfam13508  53 AEAAAKEGGIKLLELETTNRAAAFYEKLGFEE 84
Eis COG4552
Predicted acetyltransferase [General function prediction only];
55-173 3.63e-09

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 54.90  E-value: 3.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  55 SNTWVYEIEGEIAGCLIAYPgdkeieLEQAWlnmdldddirsYGTPMPMkeanddeWYIETVATFPEYRGRGVATQLVQH 134
Cdd:COG4552    41 GRVLGVFDDGELVGTLALYP------FTLNV-----------GGARVPM-------AGITGVAVAPEHRRRGVARALLRE 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1071358978 135 VIETYSEEKWSLncdvhndGALY-----VYKKLGFQIASEFDLY 173
Cdd:COG4552    97 ALAELRERGQPL-------SALYpfepgFYRRFGYELAGDRRRY 133
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-172 6.47e-09

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: 51.92  E-value: 6.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978   1 MIRKANPSDTSKIAELcyiiwsgldIQMVADIDESRllkimeqsmvdvpyrghysNTWVYEIEGEIAGCLIAYPGDkeie 80
Cdd:COG1246     2 TIRPATPDDVPAILEL---------IRPYALEEEIG-------------------EFWVAEEDGEIVGCAALHPLD---- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  81 leqawlnmdldddirsygtpmpmkeanDDEWYIETVATFPEYRGRGVATQLVQHVIETYSE---EKWSLNCdvhNDGALY 157
Cdd:COG1246    50 ---------------------------EDLAELRSLAVHPDYRGRGIGRRLLEALLAEARElglKRLFLLT---TSAAIH 99

                         170
                  ....*....|....*
gi 1071358978 158 VYKKLGFQIASEFDL 172
Cdd:COG1246   100 FYEKLGFEEIDKEDL 114
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 103-185 7.18e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 51.98  E-value: 7.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978 103 MKEANDDEWYIETVATFPEYRGRGVATQLVQHVIE-------TYSEekwsLNCDVHNDGALYVYKKLGFQIASEFDLYGH 175
Cdd:COG0454    51 LRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEwarergcTALE----LDTLDGNPAAIRFYERLGFKEIERYVAYVG 126

                          90
                  ....*....|
gi 1071358978 176 MHYHMILPIS 185
Cdd:COG0454   127 GEFEKELSLS 136
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-137 2.77e-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: 48.43  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  58 WVYEIEGEIAGCLIAYPGDKEieleqawlnmdldddirsygtpmpmkeanDDEWYIETVATFPEYRGRGVATQLVQHVIE 137
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSG-----------------------------GDTAYIGDLAVLPEYRGKGIGSALLEAAEE 52
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 55-143 1.33e-07

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 48.34  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978  55 SNTWVYEIEGEIAGCLIAYPgdkeieleqawlnmdldDDIRSYGTPMPMKeanddewYIETVATFPEYRGRGVATQLVQH 134
Cdd:pfam13527  39 GRVLGAFDDGELVSTLALYP-----------------FELNVPGKTLPAA-------GITGVATYPEYRGRGVMSRLLRR 94


                  ....*....
gi 1071358978 135 VIETYSEEK 143
Cdd:pfam13527  95 SLEEMRERG 103
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 120-186 3.36e-06

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: 45.38  E-value: 3.36e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1071358978 120 PEYRGRGVATQLVQHVIEtYSEEKWSLN-----CDVHNDGALYVYKKLGFQIASEFDLYGHM------HYHMILPISD 186
Cdd:COG1670    97 PAYWGKGYATEALRALLD-YAFEELGLHrveaeVDPDNTASIRVLEKLGFRLEGTLRDALVIdgryrdHVLYSLLREE 173
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 109-167 2.42e-05

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 42.32  E-value: 2.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1071358978 109 DEWYIETVATFPEYRGRGVATQLVQHVIETYSEE---KWSLNCDVHNDGALYVYKKLGFQIA 167
Cdd:TIGR01575  53 DEAHILNIAVKPEYQGQGIGRALLRELIDEAKGRgvnEIFLEVRVSNIAAQALYKKLGFNEI 114
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 109-165 1.90e-04

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: 39.56  E-value: 1.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071358978 109 DEWYIETVATFPEYRGRGVATQLVQHVIETYSE---EKWSLNCDVHNdGALYVYKKLGFQ 165
Cdd:pfam13673  50 DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKdgiKLSELTVNASP-YAVPFYEKLGFR 108
PRK10514 PRK10514
putative acetyltransferase; Provisional
 120-171 3.42e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 39.22  E-value: 3.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1071358978 120 PEYRGRGVATQLVQHVIETYSEekwsLNCDVH--NDGALYVYKKLGFQIA--SEFD 171
Cdd:PRK10514   79 PDVRGCGVGRMLVEHALSLHPE----LTTDVNeqNEQAVGFYKKMGFKVTgrSEVD 130
PRK03624 PRK03624
putative acetyltransferase; Provisional
 116-165 6.39e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 38.37  E-value: 6.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1071358978 116 VATFPEYRGRGVATQLVQHVietyseEKW-------SLNCDVH--NDGALYVYKKLGFQ 165
Cdd:PRK03624   74 LAVHPDFRGRGIGRALVARL------EKKliargcpKINLQVRedNDAVLGFYEALGYE 126
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
107-137 1.28e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 36.29  E-value: 1.28e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1071358978 107 NDDEWYIETVATFPEYRGRGVATQLVQHVIE 137
Cdd:COG2388    29 EGGVIIITHTEVPPALRGQGIASALVEAALD 59
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 112-165 2.54e-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: 35.77  E-value: 2.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1071358978 112 YIETVATFPEYRGRGVATQLVQHVIETYSEEKWSLNCDV--HNDGALYVYKKLGFQ 165
Cdd:pfam08445  23 ELGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVvaGNTPSRRLYEKLGFR 78
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 113-173 4.88e-03

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 36.48  E-value: 4.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1071358978 113 IEtVATFPEYRGRGVATQLVQHVIETYSEEKWSLNCDVHNDGALYVYKKLGFQIASEFDLY 173
Cdd:pfam12746 180 IE-IDTHPDYRGKGLATICAAALILECLKRGLYPSWDAHNEASVALAEKLGYEFVKEYTAY 239
 
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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