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Conserved domains on  [gi|2572083921|ref|WP_307845681|]
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MULTISPECIES: N-acetyltransferase [unclassified Bacillus (in: firmicutes)]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

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

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 40-131 4.55e-15

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: 67.72  E-value: 4.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572083921  40 DGDMPIGYAMYGWFEEKEKAVYLnQFMIDSNCQGKGYAKTLLRLLIDYLQKEYDRKVIYLSIHPENKLAQKLNESIGFHL 119
Cdd:COG1670    69 EDGELIGVVGLYDIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRL 147

                          90
                  ....*....|...
gi 2572083921 120 TGEIEG-EWINGK 131
Cdd:COG1670   148 EGTLRDaLVIDGR 160
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 40-131 4.55e-15

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: 67.72  E-value: 4.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572083921  40 DGDMPIGYAMYGWFEEKEKAVYLnQFMIDSNCQGKGYAKTLLRLLIDYLQKEYDRKVIYLSIHPENKLAQKLNESIGFHL 119
Cdd:COG1670    69 EDGELIGVVGLYDIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRL 147

                          90
                  ....*....|...
gi 2572083921 120 TGEIEG-EWINGK 131
Cdd:COG1670   148 EGTLRDaLVIDGR 160
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 36-117 4.08e-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: 56.37  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572083921  36 VGFYDGDmPIGYAMYGWFEEKEKAVYLNQFMIDSNCQGKGYAKTLLRLLIDYLqKEYDRKVIYLSIHPENKLAQKLNESI 115
Cdd:pfam00583  37 VAEEDGE-LVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWA-RERGCERIFLEVAADNLAAIALYEKL 114


                  ..
gi 2572083921 116 GF 117
Cdd:pfam00583 115 GF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 35-100 1.27e-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: 1.27e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2572083921  35 SVGFYDGDMPIGYAMYGWFEEKEKAVYLNQFMIDSNCQGKGYAKTLLRLLIDYLqKEYDRKVIYLS 100
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEA-RERGAKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 67-117 1.74e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 41.84  E-value: 1.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2572083921  67 IDSNCQGKGYAKTLLRLLIDYLQKeydRKV--IYLSIHPENKLAQKLNESIGF 117
Cdd:PRK09491   71 VDPDYQRQGLGRALLEHLIDELEK---RGVatLWLEVRASNAAAIALYESLGF 120
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 40-131 4.55e-15

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: 67.72  E-value: 4.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572083921  40 DGDMPIGYAMYGWFEEKEKAVYLnQFMIDSNCQGKGYAKTLLRLLIDYLQKEYDRKVIYLSIHPENKLAQKLNESIGFHL 119
Cdd:COG1670    69 EDGELIGVVGLYDIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRL 147

                          90
                  ....*....|...
gi 2572083921 120 TGEIEG-EWINGK 131
Cdd:COG1670   148 EGTLRDaLVIDGR 160
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 46-140 7.34e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 60.05  E-value: 7.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572083921  46 GYAMYgWFEEKEKAVYLNQFMIDSNCQGKGYAKTLLRLLIDYLqKEYDRKVIYLSIHPENKLAQKLNESIGFHLTGEIEG 125
Cdd:COG0456     1 GFALL-GLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERA-RERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78

                          90
                  ....*....|....*
gi 2572083921 126 EWINGKgFIMKRILN 140
Cdd:COG0456    79 YYGDDA-LVMEKELA 92
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
40-139 2.95e-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: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572083921  40 DGDMPIGYAMYGWFEEKE--KAVYLNQFMIDSNCQGKGYAKTLLRLLIDYLqKEYDRKVIYLSIHPENKLAQKLNESIGF 117
Cdd:COG1247    59 EDGEVVGFASLGPFRPRPayRGTAEESIYVDPDARGRGIGRALLEALIERA-RARGYRRLVAVVLADNEASIALYEKLGF 137

                          90       100
                  ....*....|....*....|....*.
gi 2572083921 118 HLTGEIEGE-WINGKGF---IMKRIL 139
Cdd:COG1247   138 EEVGTLPEVgFKFGRWLdlvLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 36-117 4.08e-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: 56.37  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572083921  36 VGFYDGDmPIGYAMYGWFEEKEKAVYLNQFMIDSNCQGKGYAKTLLRLLIDYLqKEYDRKVIYLSIHPENKLAQKLNESI 115
Cdd:pfam00583  37 VAEEDGE-LVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWA-RERGCERIFLEVAADNLAAIALYEKL 114


                  ..
gi 2572083921 116 GF 117
Cdd:pfam00583 115 GF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 35-100 1.27e-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: 1.27e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2572083921  35 SVGFYDGDMPIGYAMYGWFEEKEKAVYLNQFMIDSNCQGKGYAKTLLRLLIDYLqKEYDRKVIYLS 100
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEA-RERGAKRLRLE 65
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 22-118 4.09e-07

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 46.18  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572083921  22 LVDADTkykGEAASVGFYDGDMPIGYAMYGWfeekekavylnqfMIDSNCQGKGYAKTLLRLLIDYLQKEYDRKVIYLSI 101
Cdd:pfam13302  59 IELKDT---GFIGSIGLYDIDGEPERAELGY-------------WLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARI 122

                          90
                  ....*....|....*..
gi 2572083921 102 HPENKLAQKLNESIGFH 118
Cdd:pfam13302 123 DPENTASRRVLEKLGFK 139
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 67-117 1.74e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 41.84  E-value: 1.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2572083921  67 IDSNCQGKGYAKTLLRLLIDYLQKeydRKV--IYLSIHPENKLAQKLNESIGF 117
Cdd:PRK09491   71 VDPDYQRQGLGRALLEHLIDELEK---RGVatLWLEVRASNAAAIALYESLGF 120
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
72-123 2.70e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 40.28  E-value: 2.70e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2572083921  72 QGKGYAKTLLRLLIDYLQKEyDRKVIYLSIHPENKLAQKLNESIGFHLTGEI 123
Cdd:COG3393    28 RGRGLASALVAALAREALAR-GARTPFLYVDADNPAARRLYERLGFRPVGEY 78
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
40-138 6.82e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 40.07  E-value: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572083921  40 DGDMPIGYAMY--GWFEEKEKAVYLNQFMIDSNCQGKGYAKTLLRLLIDYLqKEYDRKVIYLSIHPENklaQKLNESIGF 117
Cdd:COG3153    46 DDGEIVGHVALspVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAA-RERGARAVVLLGDPSL---LPFYERFGF 121

                          90       100
                  ....*....|....*....|.
gi 2572083921 118 HLTGEIEGEWINGKGFIMKRI 138
Cdd:COG3153   122 RPAGELGLTLGPDEVFLAKEL 142
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 64-131 3.24e-04

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 38.62  E-value: 3.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2572083921  64 QFMIDSNCQGKGYAKTLLRLLIDYLQKEYDRKVIYLSIHPENKLAQKLNESIGFHLTGEIEGE-WINGK 131
Cdd:PRK15130   87 QIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEfFINGE 155
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
38-128 4.82e-04

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 38.12  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572083921  38 FYDGDMpIGYAMYGWFE-EKEKAVYLNQFMIDSNcqGKGYAKTLLRLLIDYLQKEYDRKVIYLSIHPENKLAQKLNESIG 116
Cdd:pfam13420  55 AESDRL-IGYATLRQFDyVKTHKAELSFYVVKNN--DEGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIG 131

                          90
                  ....*....|....*...
gi 2572083921 117 FHLTG------EIEGEWI 128
Cdd:pfam13420 132 FEWLGiernaiKKNGRWI 149
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 39-118 1.14e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 35.89  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2572083921  39 YDGDMPIGYAMYGWFEEKEKAVYLNqFMIDSNCQGKGYAktllRLLIDYLQKEYDRKVIYLSIHPENKLAQKLNESIGFH 118
Cdd:pfam13508   9 EDDGKIVGFAALLPLDDEGALAELR-LAVHPEYRGQGIG----RALLEAAEAAAKEGGIKLLELETTNRAAAFYEKLGFE 83
 
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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