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Conserved domains on  [gi|489747904|ref|WP_003651913|]
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MULTISPECIES: GNAT family N-acetyltransferase [Lactobacillus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11688059)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

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 ...
 98-182 5.78e-15

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.60  E-value: 5.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  98 DNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVWEKNYQAQAFYKKDGFKRVSQHTFVVGDDpqtDFIL 177
Cdd:COG0456   11 GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDD---ALVM 87


                 ....*
gi 489747904 178 VKGLK 182
Cdd:COG0456   88 EKELA 92
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 22-160 6.11e-14

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member TIGR01575:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 131  Bit Score: 65.04  E-value: 6.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904   22 DIKDLQRISRETFSEtfgsqnssenmekfldkAYAEEKLKAEIENQNSNFYFLIVNNQVAGYLKVNEgdaqteqVTDNAl 101
Cdd:TIGR01575   1 DLKAVLEIEAAAFAF-----------------PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQI-------VLDEA- 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489747904  102 EVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVWEKNYQAQAFYKKDGFKRV 160
Cdd:TIGR01575  56 HILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 98-182 5.78e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.60  E-value: 5.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  98 DNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVWEKNYQAQAFYKKDGFKRVSQHTFVVGDDpqtDFIL 177
Cdd:COG0456   11 GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDD---ALVM 87


                 ....*
gi 489747904 178 VKGLK 182
Cdd:COG0456   88 EKELA 92
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 22-160 6.11e-14

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: 65.04  E-value: 6.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904   22 DIKDLQRISRETFSEtfgsqnssenmekfldkAYAEEKLKAEIENQNSNFYFLIVNNQVAGYLKVNEgdaqteqVTDNAl 101
Cdd:TIGR01575   1 DLKAVLEIEAAAFAF-----------------PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQI-------VLDEA- 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489747904  102 EVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVWEKNYQAQAFYKKDGFKRV 160
Cdd:TIGR01575  56 HILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 55-157 6.80e-12

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: 59.45  E-value: 6.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904   55 YAEEKLKAEIENQNSNFYFLIVNNQVAGYLKVNEGDaqteqVTDNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDK 134
Cdd:pfam00583  19 EPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIID-----DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGC 93

                          90       100
                  ....*....|....*....|...
gi 489747904  135 ANMWLGVWEKNYQAQAFYKKDGF 157
Cdd:pfam00583  94 ERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
12-160 7.93e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 60.39  E-value: 7.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  12 AYEIKEVTVADIKDLQRISRETFSETFGSqnssenmekFLDKAYAEEKLKAEIENQNSNFYFLIV---NNQVAGYLKVne 88
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTAT---------FETEPPSEEEREAWFAAILAPGRPVLVaeeDGEVVGFASL-- 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489747904  89 GDAQTEQVTDNALEvERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVWEKNYQAQAFYKKDGFKRV 160
Cdd:COG1247   70 GPFRPRPAYRGTAE-ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEV 140
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
14-130 5.36e-10

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 54.55  E-value: 5.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  14 EIKEVTVADIKDLQRISRETFSETFGSQNSSENMEKFLDKAYAEEKLKAEIENQNSNFYFL----IVNNQVAGYLKVneg 89
Cdd:NF041158   3 TIRKLSAEDVDALIEVARESWKWTYRDIYSNEFIESWISEKYSKEKLLNEIIRSQSNLDIIflgaFVNSALIGFIEL--- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489747904  90 daqteQVTDNALEVERIYLKQGFQHQGLGLVLIKLAEELAR 130
Cdd:NF041158  80 -----KIIADKAELLRLYLKPEYTHRGIGKLLLSEAEKIMK 115
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 51-161 6.34e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 43.76  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  51 LDKAYAEEK--------LKAEIENQNSNF--YFLIVNNQVAGYlkvnegdAQTEQVTDNAlEVERIYLKQGFQHQGLGLV 120
Cdd:PRK09491  12 LPAAYHIEQrahafpwsEKTFASNQGERYlnLKLTVNGQMAAF-------AITQVVLDEA-TLFNIAVDPDYQRQGLGRA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489747904 121 LIK-LAEELaRKKDKANMWLGVWEKNYQAQAFYKKDGFKRVS 161
Cdd:PRK09491  84 LLEhLIDEL-EKRGVATLWLEVRASNAAAIALYESLGFNEVT 124
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-139 1.09e-05

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: 41.49  E-value: 1.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489747904  71 FYFLIVNNQVAGYLKVNEGDAqteqvTDNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWL 139
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGS-----GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 98-182 5.78e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.60  E-value: 5.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  98 DNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVWEKNYQAQAFYKKDGFKRVSQHTFVVGDDpqtDFIL 177
Cdd:COG0456   11 GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDD---ALVM 87


                 ....*
gi 489747904 178 VKGLK 182
Cdd:COG0456   88 EKELA 92
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 44-169 2.43e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 66.23  E-value: 2.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  44 SENMEKFLDKAYAEEKLKAEIENQNSNFYFLI-VNNQVAGYlkvnegdAQTEQVTDNALEVERIYLKQGFQHQGLGLVLI 122
Cdd:COG0454    8 PEDINFILLIEALDAELKAMEGSLAGAEFIAVdDKGEPIGF-------AGLRRLDDKVLELKRLYVLPEYRGKGIGKALL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489747904 123 KLAEELARKKDKANMWLGVWEKNYQAQAFYKKDGFKRVSQHTFVVGD 169
Cdd:COG0454   81 EALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGG 127
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 22-160 6.11e-14

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: 65.04  E-value: 6.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904   22 DIKDLQRISRETFSEtfgsqnssenmekfldkAYAEEKLKAEIENQNSNFYFLIVNNQVAGYLKVNEgdaqteqVTDNAl 101
Cdd:TIGR01575   1 DLKAVLEIEAAAFAF-----------------PWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQI-------VLDEA- 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489747904  102 EVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVWEKNYQAQAFYKKDGFKRV 160
Cdd:TIGR01575  56 HILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 55-157 6.80e-12

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: 59.45  E-value: 6.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904   55 YAEEKLKAEIENQNSNFYFLIVNNQVAGYLKVNEGDaqteqVTDNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDK 134
Cdd:pfam00583  19 EPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIID-----DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGC 93

                          90       100
                  ....*....|....*....|...
gi 489747904  135 ANMWLGVWEKNYQAQAFYKKDGF 157
Cdd:pfam00583  94 ERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
12-160 7.93e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 60.39  E-value: 7.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  12 AYEIKEVTVADIKDLQRISRETFSETFGSqnssenmekFLDKAYAEEKLKAEIENQNSNFYFLIV---NNQVAGYLKVne 88
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYNEAIAEGTAT---------FETEPPSEEEREAWFAAILAPGRPVLVaeeDGEVVGFASL-- 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489747904  89 GDAQTEQVTDNALEvERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVWEKNYQAQAFYKKDGFKRV 160
Cdd:COG1247   70 GPFRPRPAYRGTAE-ESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEV 140
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
14-130 5.36e-10

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 54.55  E-value: 5.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  14 EIKEVTVADIKDLQRISRETFSETFGSQNSSENMEKFLDKAYAEEKLKAEIENQNSNFYFL----IVNNQVAGYLKVneg 89
Cdd:NF041158   3 TIRKLSAEDVDALIEVARESWKWTYRDIYSNEFIESWISEKYSKEKLLNEIIRSQSNLDIIflgaFVNSALIGFIEL--- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489747904  90 daqteQVTDNALEVERIYLKQGFQHQGLGLVLIKLAEELAR 130
Cdd:NF041158  80 -----KIIADKAELLRLYLKPEYTHRGIGKLLLSEAEKIMK 115
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
15-181 2.28e-09

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.17  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  15 IKEVTVADIKDLQRISRETFSETfgsqnssenmekfldkayAEEKLKAEIENQNSNFYFLI--VNNQVAGYLKVNEGDAQ 92
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPG------------------REAELVDRLREDPAAGLSLVaeDDGEIVGHVALSPVDID 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  93 TEqvtDNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVWEknyQAQAFYKKDGFKRVSQHTFVVGDDpq 172
Cdd:COG3153   63 GE---GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDP---SLLPFYERFGFRPAGELGLTLGPD-- 134


                 ....*....
gi 489747904 173 tDFILVKGL 181
Cdd:COG3153  135 -EVFLAKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 64-164 4.58e-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: 46.91  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  64 IENQNSNFYFLIVNNQVAGYlkvnegdAQTEQVTDNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVwe 143
Cdd:COG1246   23 LEEEIGEFWVAEEDGEIVGC-------AALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT-- 93

                         90       100
                 ....*....|....*....|.
gi 489747904 144 kNYQAQAFYKKDGFKRVSQHT 164
Cdd:COG1246   94 -TSAAIHFYEKLGFEEIDKED 113
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 43-161 2.06e-06

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: 44.95  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904   43 SSENMEKFLDKAYAEEkLKAEIENQNSNFYFLIVNNQVAGYLKVNEGDaqteqvtdnalEVERIYLKQGFQHQGLGLVLI 122
Cdd:pfam13673   6 SEEGIETFYEFISPEA-LRERIDQGEYFFFVAFEGGQIVGVIALRDRG-----------HISLLFVDPDYQGQGIGKALL 73

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 489747904  123 KLAEELARKKDKANMWLGVWEKNYqAQAFYKKDGFKRVS 161
Cdd:pfam13673  74 EAVEDYAEKDGIKLSELTVNASPY-AVPFYEKLGFRATG 111
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 67-159 2.17e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 43.98  E-value: 2.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904   67 QNSNFYFLIVNNQVAGYLKVNEGDAqteqvtDNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVwekNY 146
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDD------EGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TN 71

                          90
                  ....*....|...
gi 489747904  147 QAQAFYKKDGFKR 159
Cdd:pfam13508  72 RAAAFYEKLGFEE 84
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
72-161 2.67e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 44.79  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  72 YFLIVNNQVAGYLKVNEGDaqteqvtDNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVwekNYQAQAF 151
Cdd:COG2153   37 LLAYDDGELVATARLLPPG-------DGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA---QAHAVGF 106

                         90
                 ....*....|
gi 489747904 152 YKKDGFKRVS 161
Cdd:COG2153  107 YEKLGFVPVG 116
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
91-167 5.57e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.97  E-value: 5.57e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489747904  91 AQTEQVTDNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWLGVWEKNYQAQAFYKKDGFKRVSQHTFVV 167
Cdd:COG3393    6 AGVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVL 82
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 51-161 6.34e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 43.76  E-value: 6.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  51 LDKAYAEEK--------LKAEIENQNSNF--YFLIVNNQVAGYlkvnegdAQTEQVTDNAlEVERIYLKQGFQHQGLGLV 120
Cdd:PRK09491  12 LPAAYHIEQrahafpwsEKTFASNQGERYlnLKLTVNGQMAAF-------AITQVVLDEA-TLFNIAVDPDYQRQGLGRA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489747904 121 LIK-LAEELaRKKDKANMWLGVWEKNYQAQAFYKKDGFKRVS 161
Cdd:PRK09491  84 LLEhLIDEL-EKRGVATLWLEVRASNAAAIALYESLGFNEVT 124
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 71-139 1.09e-05

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: 41.49  E-value: 1.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489747904  71 FYFLIVNNQVAGYLKVNEGDAqteqvTDNALEVERIYLKQGFQHQGLGLVLIKLAEELARKKDKANMWL 139
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPDGS-----GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 15-160 3.39e-05

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: 42.29  E-value: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489747904  15 IKEVTVADIKDLQRI--SRETFSETFGSQNSSENMEKFLDKAYAEEKlkaeienQNSNFYFLIV---NNQVAGYLKVNEG 89
Cdd:COG1670   10 LRPLRPEDAEALAELlnDPEVARYLPGPPYSLEEARAWLERLLADWA-------DGGALPFAIEdkeDGELIGVVGLYDI 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489747904  90 DAqteqvTDNALEVeRIYLKQGFQHQGLGLVLIKLAEELARKKDKAN-MWLGVWEKNYQAQAFYKKDGFKRV 160
Cdd:COG1670   83 DR-----ANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGLHrVEAEVDPDNTASIRVLEKLGFRLE 148
 
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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