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Conserved domains on  [gi|2736691195|ref|WP_347559334|]
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MULTISPECIES: GNAT family N-acetyltransferase [Anaerofustis]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10607277)

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

CATH:  3.40.630.30
EC:  2.3.1.-
Gene Ontology:  GO:0008080
PubMed:  27367672|26818562|15581578|10940244|9175471
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 45-113 1.38e-13

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


:

Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 61.32  E-value: 1.38e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2736691195  45 VYDEEKLIGCIRIL-TDGYFFGTITDLLVLPEYQKKGIGSKLLE----LAKEHTPTMLYFGSKPGTQNFYEKNG 113
Cdd:pfam13508   8 AEDDGKIVGFAALLpLDDEGALAELRLAVHPEYRGQGIGRALLEaaeaAAKEGGIKLLELETTNRAAAFYEKLG 81
 
Name Accession Description Interval E-value
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 45-113 1.38e-13

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 61.32  E-value: 1.38e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2736691195  45 VYDEEKLIGCIRIL-TDGYFFGTITDLLVLPEYQKKGIGSKLLE----LAKEHTPTMLYFGSKPGTQNFYEKNG 113
Cdd:pfam13508   8 AEDDGKIVGFAALLpLDDEGALAELRLAVHPEYRGQGIGRALLEaaeaAAKEGGIKLLELETTNRAAAFYEKLG 81
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 45-113 1.98e-12

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: 59.62  E-value: 1.98e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2736691195  45 VYDEEKLIGCIRILTDGYFFGTITDLLVLPEYQKKGIGSKLLE----LAKEHTPTMLYFGSKPGTQNFYEKNG 113
Cdd:COG1246    33 AEEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEallaEARELGLKRLFLLTTSAAIHFYEKLG 105
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 43-92 4.59e-10

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: 51.51  E-value: 4.59e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2736691195  43 ITVYDEEKLIGCIRILTDGYFFGT--ITDLLVLPEYQKKGIGSKLLELAKEH 92
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGGDTayIGDLAVLPEYRGKGIGSALLEAAEEE 53
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 46-113 5.30e-03

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: 34.61  E-value: 5.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2736691195  46 YDEEKLIGCIRILTDgYFFGTITDLLVLPEYQKKGIGSKLLE----LAKEHTPTMLYF---GSKPGTQNFYEKNG 113
Cdd:TIGR01575  37 RIGGKVVGYAGVQIV-LDEAHILNIAVKPEYQGQGIGRALLRelidEAKGRGVNEIFLevrVSNIAAQALYKKLG 110
 
Name Accession Description Interval E-value
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 45-113 1.38e-13

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 61.32  E-value: 1.38e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2736691195  45 VYDEEKLIGCIRIL-TDGYFFGTITDLLVLPEYQKKGIGSKLLE----LAKEHTPTMLYFGSKPGTQNFYEKNG 113
Cdd:pfam13508   8 AEDDGKIVGFAALLpLDDEGALAELRLAVHPEYRGQGIGRALLEaaeaAAKEGGIKLLELETTNRAAAFYEKLG 81
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 45-113 1.98e-12

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: 59.62  E-value: 1.98e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2736691195  45 VYDEEKLIGCIRILTDGYFFGTITDLLVLPEYQKKGIGSKLLE----LAKEHTPTMLYFGSKPGTQNFYEKNG 113
Cdd:COG1246    33 AEEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEallaEARELGLKRLFLLTTSAAIHFYEKLG 105
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
45-113 7.11e-11

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 55.58  E-value: 7.11e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2736691195  45 VYDEEKLIGCIRILTDGYFFGTITDLLVLPEYQKKGIGSKLL----ELAKEHTPTMLYFGSKPGTQNFYEKNG 113
Cdd:COG2153    39 AYDDGELVATARLLPPGDGEAKIGRVAVLPEYRGQGLGRALMeaaiEEARERGARRIVLSAQAHAVGFYEKLG 111
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 43-113 2.07e-10

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: 54.06  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2736691195  43 ITVYDEEKLIGCIRI--LTDGYFFGTITDLLVLPEYQKKGIGSKLL----ELAKEHTPTMLYFGSKP---GTQNFYEKNG 113
Cdd:pfam00583  36 FVAEEDGELVGFASLsiIDDEPPVGEIEGLAVAPEYRGKGIGTALLqallEWARERGCERIFLEVAAdnlAAIALYEKLG 115
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
47-113 2.39e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 54.32  E-value: 2.39e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2736691195  47 DEEKLIGCIRI----LTDGYFFGTITDLLVLPEYQKKGIGSKL----LELAKEHTPTMLYFGSKPGTQNFYEKNG 113
Cdd:COG3153    46 DDGEIVGHVALspvdIDGEGPALLLGPLAVDPEYRGQGIGRALmraaLEAARERGARAVVLLGDPSLLPFYERFG 120
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 43-92 4.59e-10

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: 51.51  E-value: 4.59e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2736691195  43 ITVYDEEKLIGCIRILTDGYFFGT--ITDLLVLPEYQKKGIGSKLLELAKEH 92
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGGDTayIGDLAVLPEYRGKGIGSALLEAAEEE 53
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 43-113 1.20e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 52.36  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2736691195  43 ITVYDEEKLIGC--IRILTDGYFFgtITDLLVLPEYQKKGIGSKLLE----LAKEHTPTMLY---FGSKPGTQNFYEKNG 113
Cdd:COG0454    37 IAVDDKGEPIGFagLRRLDDKVLE--LKRLYVLPEYRGKGIGKALLEalleWARERGCTALEldtLDGNPAAIRFYERLG 114
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 46-113 2.50e-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: 48.81  E-value: 2.50e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2736691195  46 YDEEKLIGCIRILTDGYffgtITDLLVLPEYQKKGIGSKLLELAKEHTPTMLYFGSK------PGTQNFYEKNG 113
Cdd:pfam13673  37 FEGGQIVGVIALRDRGH----ISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSEltvnasPYAVPFYEKLG 106
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 65-113 3.28e-07

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 45.03  E-value: 3.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2736691195  65 GTITDLLVLPEYQKKGIGSKLL----ELAKEHTPTMLYFG---SKPGTQNFYEKNG 113
Cdd:COG0456    14 AEIEDLAVDPEYRGRGIGRALLeaalERARERGARRLRLEvreDNEAAIALYEKLG 69
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
50-113 1.46e-04

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 37.97  E-value: 1.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2736691195  50 KLIGCIRILTDGYFFGTITDLLVLPEYQKKGIGSKLL-----ELAKEHTPTMLYF--GSKPGTQNFYEKNG 113
Cdd:COG3393     1 ELVAMAGVRAESPGVAEISGVYTHPEYRGRGLASALVaalarEALARGARTPFLYvdADNPAARRLYERLG 71
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 46-113 5.30e-03

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: 34.61  E-value: 5.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2736691195  46 YDEEKLIGCIRILTDgYFFGTITDLLVLPEYQKKGIGSKLLE----LAKEHTPTMLYF---GSKPGTQNFYEKNG 113
Cdd:TIGR01575  37 RIGGKVVGYAGVQIV-LDEAHILNIAVKPEYQGQGIGRALLRelidEAKGRGVNEIFLevrVSNIAAQALYKKLG 110
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 43-92 9.28e-03

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: 34.20  E-value: 9.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2736691195  43 ITVYDEEKLIGCIRILTDGYFFGTIT-DLLVLPEYQKKGIGSKLLELAKEH 92
Cdd:COG1670    65 IEDKEDGELIGVVGLYDIDRANRSAEiGYWLAPAYWGKGYATEALRALLDY 115
 
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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