NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|445951684|ref|WP_000029539|]
View 

GNAT family N-acetyltransferase [Staphylococcus aureus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 179-273 2.85e-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: 43.83  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445951684 179 QDIIDSLDDHHHLFLFV---SEGLLKGYL-YLEIDSQQSIAEIKYFSSHvDYRLKGIAFELLAYALQYAFDNFDIRKVYF 254
Cdd:COG1670   49 ERLLADWADGGALPFAIedkEDGELIGVVgLYDIDRANRSAEIGYWLAP-AYWGKGYATEALRALLDYAFEELGLHRVEA 127

                         90       100
                 ....*....|....*....|..
gi 445951684 255 KIRNKNN---KLIERfngLGFH 273
Cdd:COG1670  128 EVDPDNTasiRVLEK---LGFR 146
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 179-273 2.85e-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: 43.83  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445951684 179 QDIIDSLDDHHHLFLFV---SEGLLKGYL-YLEIDSQQSIAEIKYFSSHvDYRLKGIAFELLAYALQYAFDNFDIRKVYF 254
Cdd:COG1670   49 ERLLADWADGGALPFAIedkEDGELIGVVgLYDIDRANRSAEIGYWLAP-AYWGKGYATEALRALLDYAFEELGLHRVEA 127

                         90       100
                 ....*....|....*....|..
gi 445951684 255 KIRNKNN---KLIERfngLGFH 273
Cdd:COG1670  128 EVDPDNTasiRVLEK---LGFR 146
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 185-272 7.07e-05

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: 41.35  E-value: 7.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445951684  185 LDDHHHLFLFVSEGLLKGYL-YLEIDSQQSIAEIKYFSSHVDYRLKGIAFELLAYALQYAFDnFDIRKVYFKIRNKNNKL 263
Cdd:pfam00583  29 EDASEGFFVAEEDGELVGFAsLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARE-RGCERIFLEVAADNLAA 107


                  ....*....
gi 445951684  264 IERFNGLGF 272
Cdd:pfam00583 108 IALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 191-253 6.78e-04

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: 37.26  E-value: 6.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445951684 191 LFLFVSEGLLKGYLYLEI-DSQQSIAEIKYFSSHVDYRLKGIAFELLAYALQYAFDNfDIRKVY 253
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARER-GAKRLR 63
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 179-273 2.85e-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: 43.83  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445951684 179 QDIIDSLDDHHHLFLFV---SEGLLKGYL-YLEIDSQQSIAEIKYFSSHvDYRLKGIAFELLAYALQYAFDNFDIRKVYF 254
Cdd:COG1670   49 ERLLADWADGGALPFAIedkEDGELIGVVgLYDIDRANRSAEIGYWLAP-AYWGKGYATEALRALLDYAFEELGLHRVEA 127

                         90       100
                 ....*....|....*....|..
gi 445951684 255 KIRNKNN---KLIERfngLGFH 273
Cdd:COG1670  128 EVDPDNTasiRVLEK---LGFR 146
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 185-272 7.07e-05

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: 41.35  E-value: 7.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445951684  185 LDDHHHLFLFVSEGLLKGYL-YLEIDSQQSIAEIKYFSSHVDYRLKGIAFELLAYALQYAFDnFDIRKVYFKIRNKNNKL 263
Cdd:pfam00583  29 EDASEGFFVAEEDGELVGFAsLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARE-RGCERIFLEVAADNLAA 107


                  ....*....
gi 445951684  264 IERFNGLGF 272
Cdd:pfam00583 108 IALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 191-253 6.78e-04

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: 37.26  E-value: 6.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445951684 191 LFLFVSEGLLKGYLYLEI-DSQQSIAEIKYFSSHVDYRLKGIAFELLAYALQYAFDNfDIRKVY 253
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARER-GAKRLR 63
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 202-274 3.83e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 35.79  E-value: 3.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445951684 202 GYLYLEIDSQQSIAEIKYFSSHVDYRLKGIAFELLAYALQYAFDNfDIRKVYFKIRNKNNKLIERFNGLGFHI 274
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARER-GARRLRLEVREDNEAAIALYEKLGFEE 72
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 223-273 8.02e-03

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 36.17  E-value: 8.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 445951684  223 HVDYRL------KGIAFELLAYALQYAFDNFDIRKVYFKIRNKNN---KLIERfngLGFH 273
Cdd:pfam13302  83 ELGYWLgpdywgKGYATEAVRALLEYAFEELGLPRLVARIDPENTasrRVLEK---LGFK 139
 
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