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Conserved domains on  [gi|1237882497|gb|PAJ76309|]
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GNAT family N-acetyltransferase [Pseudoalteromonas sp. NBT06-2]

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 ...
 64-146 4.68e-12

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 58.51  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  64 AIIEVAIEAQHLNINSLTVDPHYFRKGIAGKLISFALNKVK---FSVAVVETAVKNLPAINLYKKYGFVECNRWTPSHGI 140
Cdd:COG0456     3 ALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARergARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD 82


                  ....*.
gi 1237882497 141 EKVAMS 146
Cdd:COG0456    83 DALVME 88
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 64-146 4.68e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 58.51  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  64 AIIEVAIEAQHLNINSLTVDPHYFRKGIAGKLISFALNKVK---FSVAVVETAVKNLPAINLYKKYGFVECNRWTPSHGI 140
Cdd:COG0456     3 ALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARergARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD 82


                  ....*.
gi 1237882497 141 EKVAMS 146
Cdd:COG0456    83 DALVME 88
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 49-130 1.00e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.07  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  49 SRTQFYGFIENERIAAIIEVAIEAQHLNI--NSLTVDPHYFRKGIAGKLISFALNKVKFSVAVVETAVKNLPAINLYKKY 126
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALaeLRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKL 80


                  ....
gi 1237882497 127 GFVE 130
Cdd:pfam13508  81 GFEE 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 20-130 5.53e-06

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: 43.09  E-value: 5.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  20 FQRSYKIEAQligSVNFP-PLLRNVKDITNSRTQFYGFIENERIAAIIEVAI---EAQHLNInslTVDPHYFRKGIAGKL 95
Cdd:TIGR01575   2 LKAVLEIEAA---AFAFPwTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIvldEAHILNI---AVKPEYQGQGIGRAL 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1237882497  96 ISFALNKVKFSVAVV---ETAVKNLPAINLYKKYGFVE 130
Cdd:TIGR01575  76 LRELIDEAKGRGVNEiflEVRVSNIAAQALYKKLGFNE 113
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-104 8.48e-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: 38.41  E-value: 8.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1237882497  53 FYGFIENERIAAIIEVAI---EAQHLNINSLTVDPHYFRKGIAGKLISFALNKVK 104
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEAR 55
PRK10562 PRK10562
putative acetyltransferase; Provisional
 38-132 3.26e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 35.81  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  38 PLLRNVKdITNSRTQFYGfiENERIAAIIEVaIEAQHlnINSLTVDPHYFRKGIAGKLISFAlnKVKFSVAVVETAVKNL 117
Cdd:PRK10562   38 PLVRDVY-LPAAQTWVWE--EDGKLLGFVSV-LEGRF--VGALFVAPKAVRRGIGKALMQHV--QQRYPHLSLEVYQKNQ 109

                          90
                  ....*....|....*..
gi 1237882497 118 PAINLYKKYGF--VECN 132
Cdd:PRK10562  110 RAVNFYHAQGFriVDSA 126
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 64-146 4.68e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 58.51  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  64 AIIEVAIEAQHLNINSLTVDPHYFRKGIAGKLISFALNKVK---FSVAVVETAVKNLPAINLYKKYGFVECNRWTPSHGI 140
Cdd:COG0456     3 ALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARergARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGD 82


                  ....*.
gi 1237882497 141 EKVAMS 146
Cdd:COG0456    83 DALVME 88
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 49-130 1.00e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.07  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  49 SRTQFYGFIENERIAAIIEVAIEAQHLNI--NSLTVDPHYFRKGIAGKLISFALNKVKFSVAVVETAVKNLPAINLYKKY 126
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALaeLRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEKL 80


                  ....
gi 1237882497 127 GFVE 130
Cdd:pfam13508  81 GFEE 84
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 53-128 3.77e-09

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: 51.36  E-value: 3.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  53 FYGFIENERIAAIIEVAI---EAQHLNINSLTVDPHYFRKGIAGKLISFALNKVK---FSVAVVETAVKNLPAINLYKKY 126
Cdd:pfam00583  35 FFVAEEDGELVGFASLSIiddEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARergCERIFLEVAADNLAAIALYEKL 114


                  ..
gi 1237882497 127 GF 128
Cdd:pfam00583 115 GF 116
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 46-148 2.77e-08

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: 49.19  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  46 ITNSRTQFYGFIENERIAAIIEVaIEAQHlnINSLTVDPHYFRKGIAGKLISFALNKV-KFSVAVVETAVK-NLPAINLY 123
Cdd:pfam13673  26 IDQGEYFFFVAFEGGQIVGVIAL-RDRGH--ISLLFVDPDYQGQGIGKALLEAVEDYAeKDGIKLSELTVNaSPYAVPFY 102

                          90       100
                  ....*....|....*....|....*
gi 1237882497 124 KKYGFVECNRWTPSHGIEKVAMSVE 148
Cdd:pfam13673 103 EKLGFRATGPEQEFNGIRFVPMEKE 127
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
43-148 1.95e-06

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 44.69  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  43 VKDITNSRTQFYGFI--ENERIAAII-----EVAIEAQHLNINSLTVDPHYFRKGIAGKLISFALNKVK---FSVAVVET 112
Cdd:COG3153    29 VDRLREDPAAGLSLVaeDDGEIVGHValspvDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARergARAVVLLG 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1237882497 113 AVKNLPainLYKKYGFVECNRWTPSHGIEKVAMSVE 148
Cdd:COG3153   109 DPSLLP---FYERFGFRPAGELGLTLGPDEVFLAKE 141
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 40-133 4.48e-06

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: 43.44  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  40 LRNVKDITNSRTQFYGFIENERIAAIIEVAI-EAQHLNINSLTVDPHYFRKGIAGKLISFALNKVK---FSVAVVETavk 115
Cdd:COG1246    17 LIRPYALEEEIGEFWVAEEDGEIVGCAALHPlDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARelgLKRLFLLT--- 93

                          90
                  ....*....|....*...
gi 1237882497 116 NLPAINLYKKYGFVECNR 133
Cdd:COG1246    94 TSAAIHFYEKLGFEEIDK 111
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 20-130 5.53e-06

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: 43.09  E-value: 5.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  20 FQRSYKIEAQligSVNFP-PLLRNVKDITNSRTQFYGFIENERIAAIIEVAI---EAQHLNInslTVDPHYFRKGIAGKL 95
Cdd:TIGR01575   2 LKAVLEIEAA---AFAFPwTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIvldEAHILNI---AVKPEYQGQGIGRAL 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1237882497  96 ISFALNKVKFSVAVV---ETAVKNLPAINLYKKYGFVE 130
Cdd:TIGR01575  76 LRELIDEAKGRGVNEiflEVRVSNIAAQALYKKLGFNE 113
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
78-134 9.30e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 43.06  E-value: 9.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  78 NSLTVDPHYFRKGIAGKLISFALNKVK---FSVAVVETAVKNLPAINLYKKYGFVECNRW 134
Cdd:COG1247    84 ESIYVDPDARGRGIGRALLEALIERARargYRRLVAVVLADNEASIALYEKLGFEEVGTL 143
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
77-135 4.93e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 39.51  E-value: 4.93e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237882497  77 INSLTVDPHYFRKGIAGKLISFALNKVK---FSVAVVETAVKNLPAINLYKKYGFVECNRWT 135
Cdd:COG3393    18 ISGVYTHPEYRGRGLASALVAALAREALargARTPFLYVDADNPAARRLYERLGFRPVGEYA 79
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-104 8.48e-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: 38.41  E-value: 8.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1237882497  53 FYGFIENERIAAIIEVAI---EAQHLNINSLTVDPHYFRKGIAGKLISFALNKVK 104
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEAR 55
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 82-130 2.55e-04

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 39.21  E-value: 2.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237882497  82 VDPHYFRKGIA----GKLISFALNKVKFSVAVVETAVKNLPAINLYKKYGFVE 130
Cdd:COG1670    95 LAPAYWGKGYAtealRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRL 147
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 82-141 4.20e-04

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 38.11  E-value: 4.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237882497  82 VDPHYFRKGIAGKLISFALNKVK---FSVAVVETAVKNLPAINLYKKYGFVECNRWTPSHGIE 141
Cdd:COG0454    66 VLPEYRGKGIGKALLEALLEWARergCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGE 128
PRK10562 PRK10562
putative acetyltransferase; Provisional
 38-132 3.26e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 35.81  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237882497  38 PLLRNVKdITNSRTQFYGfiENERIAAIIEVaIEAQHlnINSLTVDPHYFRKGIAGKLISFAlnKVKFSVAVVETAVKNL 117
Cdd:PRK10562   38 PLVRDVY-LPAAQTWVWE--EDGKLLGFVSV-LEGRF--VGALFVAPKAVRRGIGKALMQHV--QQRYPHLSLEVYQKNQ 109

                          90
                  ....*....|....*..
gi 1237882497 118 PAINLYKKYGF--VECN 132
Cdd:PRK10562  110 RAVNFYHAQGFriVDSA 126
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
80-129 7.68e-03

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 35.29  E-value: 7.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237882497  80 LTVDPHYFRKGIAGKLISFALNKVK---FSVAVVETAVKNLPAINLYKKYGFV 129
Cdd:PRK10975  132 LAVFPGAQGRGIGARLMQAALNWCQargLTRLRVATQMGNLAALRLYIRSGAN 184
 
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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