NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|562750718|ref|WP_023657597|]
View 

MULTISPECIES: N-acetyltransferase [Pseudomonas]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 76-156 8.44e-15

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.45  E-value: 8.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562750718  76 GYLWYEEDLSLHLAFINDFHILPVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNERAKHVYEGSGFCVTG------ 149
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGerpnyy 80

                         90
                 ....*....|.
gi 562750718 150 ----INMSKPL 156
Cdd:COG0456   81 gddaLVMEKEL 91
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 76-156 8.44e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.45  E-value: 8.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562750718  76 GYLWYEEDLSLHLAFINDFHILPVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNERAKHVYEGSGFCVTG------ 149
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGerpnyy 80

                         90
                 ....*....|.
gi 562750718 150 ----INMSKPL 156
Cdd:COG0456   81 gddaLVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 72-145 1.54e-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: 57.91  E-value: 1.54e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 562750718   72 EEVIGYLW-YEEDLSLHLAFINDFHILPVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNERAKHVYEGSGF 145
Cdd:pfam00583  42 GELVGFASlSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 68-127 5.56e-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: 47.27  E-value: 5.56e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 562750718  68 ADGPEEVIGYLWYE-EDLSLHLAFINDFHILPVHQGKGLAKQALESLERELKLRGFQQIKL 127
Cdd:cd04301    4 AEDDGEIVGFASLSpDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 96-145 1.25e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 42.61  E-value: 1.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 562750718  96 ILPVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNERAKHVYEGSGF 145
Cdd:PRK09491  71 VDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 76-156 8.44e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 65.45  E-value: 8.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562750718  76 GYLWYEEDLSLHLAFINDFHILPVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNERAKHVYEGSGFCVTG------ 149
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGerpnyy 80

                         90
                 ....*....|.
gi 562750718 150 ----INMSKPL 156
Cdd:COG0456   81 gddaLVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 72-145 1.54e-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: 57.91  E-value: 1.54e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 562750718   72 EEVIGYLW-YEEDLSLHLAFINDFHILPVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNERAKHVYEGSGF 145
Cdd:pfam00583  42 GELVGFASlSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
68-145 3.29e-11

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 58.08  E-value: 3.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562750718  68 ADGPEEVIGYLWYE---EDLSLHLAFINDFHILPVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNERAKHVYEGSG 144
Cdd:COG1247   57 AEEDGEVVGFASLGpfrPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLG 136


                 .
gi 562750718 145 F 145
Cdd:COG1247  137 F 137
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-150 7.99e-11

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: 57.32  E-value: 7.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562750718   1 MISLRPMRESEFSGYLDYfvpaYASEISSSHRLSYSESLVQAKLEIADDLPDgINTAGQSLLCLYDPADGpeEVIGYLWY 80
Cdd:COG1670    7 RLRLRPLRPEDAEALAEL----LNDPEVARYLPGPPYSLEEARAWLERLLAD-WADGGALPFAIEDKEDG--ELIGVVGL 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 562750718  81 -EEDLSLHLAFInDFHILPVHQGKGLAKQALESLEREL-KLRGFQQIKLRVAGDNERAKHVYEGSGFCVTGI 150
Cdd:COG1670   80 yDIDRANRSAEI-GYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGT 150
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
87-145 2.13e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 54.14  E-value: 2.13e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 562750718  87 HLAFINDFHILPVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNERAKHVYEGSGF 145
Cdd:COG3393   14 GVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGF 72
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 68-145 9.56e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 53.52  E-value: 9.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562750718  68 ADGPEEVIGY--LWYEEDLSLHLAFINdfhILPVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNERAKHVYEGSGF 145
Cdd:COG0454   39 VDDKGEPIGFagLRRLDDKVLELKRLY---VLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGF 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 68-127 5.56e-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: 47.27  E-value: 5.56e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 562750718  68 ADGPEEVIGYLWYE-EDLSLHLAFINDFHILPVHQGKGLAKQALESLERELKLRGFQQIKL 127
Cdd:cd04301    4 AEDDGEIVGFASLSpDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 68-145 5.09e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.44  E-value: 5.09e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 562750718   68 ADGPEEVIGYLWYEEDLSLHLAFINDFHILPVHQGKGLAKQALESLERELKLRGFQQIKLRVagdNERAKHVYEGSGF 145
Cdd:pfam13508   8 AEDDGKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEKLGF 82
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 96-145 1.25e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 42.61  E-value: 1.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 562750718  96 ILPVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNERAKHVYEGSGF 145
Cdd:PRK09491  71 VDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
21-145 2.54e-04

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 38.91  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562750718  21 PAYASEISSSHRLSYSESlvqAKLEIADDLPDGINtAGQSLLCLYDpadgpEEVIGYLWYEE---DLSLHLAFINDFHIL 97
Cdd:COG3153    6 PEDAEAIAALLRAAFGPG---REAELVDRLREDPA-AGLSLVAEDD-----GEIVGHVALSPvdiDGEGPALLLGPLAVD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 562750718  98 PVHQGKGLAKQALESLERELKLRGFQQIklRVAGDnERAKHVYEGSGF 145
Cdd:COG3153   77 PEYRGQGIGRALMRAALEAARERGARAV--VLLGD-PSLLPFYERFGF 121
PRK03624 PRK03624
putative acetyltransferase; Provisional
 98-156 5.24e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 37.99  E-value: 5.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 562750718  98 PVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNERAKHVYEGSGFCV-TGINMSKPL 156
Cdd:PRK03624  78 PDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEqDRISLGKRL 137
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 87-149 8.34e-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: 37.25  E-value: 8.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 562750718   87 HLAFINDFHI-----LPVHQGKGLAKQALESLERELKLRGFQQIKLRVAGDNErAKHVYEGSGFCVTG 149
Cdd:pfam13673  45 VIALRDRGHIsllfvDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPY-AVPFYEKLGFRATG 111
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 61-145 1.39e-03

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: 36.89  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 562750718  61 LLCLYDPADGPEEVIGYLWYEED------LSLH-----LAFINDFHILPVHQGKGLAKQALESLERELKLRGFQQIKLRV 129
Cdd:COG1246   14 ILELIRPYALEEEIGEFWVAEEDgeivgcAALHpldedLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT 93

                         90
                 ....*....|....*.
gi 562750718 130 agdNERAKHVYEGSGF 145
Cdd:COG1246   94 ---TSAAIHFYEKLGF 106
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 96-145 2.10e-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: 35.38  E-value: 2.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 562750718   96 ILPVHQGKGLAKQALESLERELKLRGfQQIKLRVAGDNERAKHVYEGSGF 145
Cdd:pfam08445  29 TLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGF 77
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 96-149 3.07e-03

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 36.31  E-value: 3.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 562750718  96 ILPVHQGKGLAKQALE-SLERELKLRGFQQIKLRVAGDNERAKHVYEGSGFCVTG 149
Cdd:PRK15130  90 ISPEYQGKGLATRAAKlAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEG 144
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH