NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2743014569|ref|WP_349496990|]
View 

GNAT family N-acetyltransferase [Bacillus cereus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10008168)

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

CATH:  3.40.630.30
EC:  2.3.1.-
Gene Ontology:  GO:0008080
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
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
1-170 3.43e-74

Predicted acetyltransferase [General function prediction only];


:

Pssm-ID: 443180  Cd Length: 170  Bit Score: 219.78  E-value: 3.43e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743014569   1 MKLLKLTYEYREQIMEYRQAFLNSGEqpHGSSSLQNFASLDEWFEKVSIQEVGENLPSNRVPSSQFLSF-EKGELIGFVN 79
Cdd:COG3981     2 MELVRPTLEDEESYLEYLAEFLKEHI--DGSGYLVSFEDFEAWLERLLDEEKGEELPEGWVPATTYWLVdEDGRIVGAIN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743014569  80 IRHRLNPELLLESGHIGYSVHPNKRRQEYATKQLQLSLAEAQKLGLKKVLITCDKSNIGSAKTIQKVGGVLENEVVSTHT 159
Cdd:COG3981    80 LRHELNEFLLRVGGHIGYGVRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASRKVIEANGGVLEDEVVDEED 159
                         170
                  ....*....|.
gi 2743014569 160 GEIVQRYWVEI 170
Cdd:COG3981   160 GRPVRRYWIDL 170
 
Name Accession Description Interval E-value
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
1-170 3.43e-74

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 219.78  E-value: 3.43e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743014569   1 MKLLKLTYEYREQIMEYRQAFLNSGEqpHGSSSLQNFASLDEWFEKVSIQEVGENLPSNRVPSSQFLSF-EKGELIGFVN 79
Cdd:COG3981     2 MELVRPTLEDEESYLEYLAEFLKEHI--DGSGYLVSFEDFEAWLERLLDEEKGEELPEGWVPATTYWLVdEDGRIVGAIN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743014569  80 IRHRLNPELLLESGHIGYSVHPNKRRQEYATKQLQLSLAEAQKLGLKKVLITCDKSNIGSAKTIQKVGGVLENEVVSTHT 159
Cdd:COG3981    80 LRHELNEFLLRVGGHIGYGVRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASRKVIEANGGVLEDEVVDEED 159
                         170
                  ....*....|.
gi 2743014569 160 GEIVQRYWVEI 170
Cdd:COG3981   160 GRPVRRYWIDL 170
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
41-147 2.06e-08

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 50.42  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743014569  41 DEWFEKVSIQEvgenlpsNRVPSSQFLSFEKGE-LIGFVNIRHRLNPELLLEsghIGYSVHPNKRRQEYATKQLQLSLAE 119
Cdd:pfam13302  39 REWLARIWAAD-------EAERGYGWAIELKDTgFIGSIGLYDIDGEPERAE---LGYWLGPDYWGKGYATEAVRALLEY 108
                          90       100
                  ....*....|....*....|....*....
gi 2743014569 120 A-QKLGLKKVLITCDKSNIGSAKTIQKVG 147
Cdd:pfam13302 109 AfEELGLPRLVARIDPENTASRRVLEKLG 137
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
66-131 1.25e-03

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: 35.71  E-value: 1.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2743014569  66 FLSFEKGELIGFVNIRHRLNPELLLESGHIGysVHPNKRRQEYATKQLQLSLAEAQKLGLKKVLIT 131
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGGDTAYIGDLA--VLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
1-170 3.43e-74

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 219.78  E-value: 3.43e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743014569   1 MKLLKLTYEYREQIMEYRQAFLNSGEqpHGSSSLQNFASLDEWFEKVSIQEVGENLPSNRVPSSQFLSF-EKGELIGFVN 79
Cdd:COG3981     2 MELVRPTLEDEESYLEYLAEFLKEHI--DGSGYLVSFEDFEAWLERLLDEEKGEELPEGWVPATTYWLVdEDGRIVGAIN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743014569  80 IRHRLNPELLLESGHIGYSVHPNKRRQEYATKQLQLSLAEAQKLGLKKVLITCDKSNIGSAKTIQKVGGVLENEVVSTHT 159
Cdd:COG3981    80 LRHELNEFLLRVGGHIGYGVRPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASRKVIEANGGVLEDEVVDEED 159
                         170
                  ....*....|.
gi 2743014569 160 GEIVQRYWVEI 170
Cdd:COG3981   160 GRPVRRYWIDL 170
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
70-151 4.24e-10

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: 55.39  E-value: 4.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743014569  70 EKGELIGFVNIRhrlNPELLLESGHIGYSVHPNKRRQEYATKQLQLSLAEA-QKLGLKKVLITCDKSNIGSAKTIQKVGG 148
Cdd:COG1670    69 EDGELIGVVGLY---DIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGF 145

                  ...
gi 2743014569 149 VLE 151
Cdd:COG1670   146 RLE 148
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
41-147 2.06e-08

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 50.42  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743014569  41 DEWFEKVSIQEvgenlpsNRVPSSQFLSFEKGE-LIGFVNIRHRLNPELLLEsghIGYSVHPNKRRQEYATKQLQLSLAE 119
Cdd:pfam13302  39 REWLARIWAAD-------EAERGYGWAIELKDTgFIGSIGLYDIDGEPERAE---LGYWLGPDYWGKGYATEAVRALLEY 108
                          90       100
                  ....*....|....*....|....*....
gi 2743014569 120 A-QKLGLKKVLITCDKSNIGSAKTIQKVG 147
Cdd:pfam13302 109 AfEELGLPRLVARIDPENTASRRVLEKLG 137
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
41-147 3.52e-07

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: 46.74  E-value: 3.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743014569  41 DEWFEKVSIQEVGENLPSNRVPSSQFLS-FEKGELIGFVNIRHRLNPELLlesGHI-GYSVHPNKRRQEYATKQLQLSLA 118
Cdd:pfam00583  10 EEFPEPWPDEPLDLLEDWDEDASEGFFVaEEDGELVGFASLSIIDDEPPV---GEIeGLAVAPEYRGKGIGTALLQALLE 86
                          90       100
                  ....*....|....*....|....*....
gi 2743014569 119 EAQKLGLKKVLITCDKSNIGSAKTIQKVG 147
Cdd:pfam00583  87 WARERGCERIFLEVAADNLAAIALYEKLG 115
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
40-138 5.30e-04

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 38.14  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743014569  40 LDEWFEKVSIQEVGENLPSNRVPSSQFLSFEKGELIGFVnirhRLNPELLLESGHIGY----SVHPNKRRQEYATKQLQL 115
Cdd:COG3153    16 LRAAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHV----ALSPVDIDGEGPALLlgplAVDPEYRGQGIGRALMRA 91
                          90       100
                  ....*....|....*....|...
gi 2743014569 116 SLAEAQKLGLKKVLITCDKSNIG 138
Cdd:COG3153    92 ALEAARERGARAVVLLGDPSLLP 114
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
66-131 1.25e-03

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: 35.71  E-value: 1.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2743014569  66 FLSFEKGELIGFVNIRHRLNPELLLESGHIGysVHPNKRRQEYATKQLQLSLAEAQKLGLKKVLIT 131
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGGDTAYIGDLA--VLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
76-147 8.65e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 33.86  E-value: 8.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2743014569  76 GFVNIRHRLNPEllleSGHIGY-SVHPNKRRQEYATKQLQLSLAEAQKLGLKKVLITCDKSNIGSAKTIQKVG 147
Cdd:COG0456     1 GFALLGLVDGGD----EAEIEDlAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLG 69
 
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