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Conserved domains on  [gi|2324454598|gb|UYY93226|]
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GNAT family N-acetyltransferase [Bacillus cereus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10579273)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate; similar to Bacillus subtilis N-acetyltransferase YdfB

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 14-255 1.21e-69

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


:

Pssm-ID: 403833  Cd Length: 239  Bit Score: 214.44  E-value: 1.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598  14 PVLEGNTRTMtFAYAVCDQVvdGEVFVNGQ--LTAGLIITANgIYYLFGDTddqnyNEELFSYLKTaiEKTEKRFTLFTS 91
Cdd:pfam12746   2 PLFNGWDETL-IWSCLQGGM--GKVYVDNLenPTSALIVLGD-FVFFAGEP-----NEELVRFEPE--KSGLKRFILVPQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598  92 SEEWEMMLEERFSNTLRNIPR--MKFQRVTFEERK----RDFNKNTYEVKRIDRRDIER-SSEFKEEYYKEYWGSKETFL 164
Cdd:pfam12746  71 SEEWERLIEEVYGDKLRKITRyaFKKEPEVFDKEKleklVASLPQGYTLKKIDEELYEAcLEEEWSRDFVSQFSSYEDFL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598 165 NSGFGFCIEQDGIIVAECVSIFSGNGYAEIDIATHEAHQGKGLAQAVATRFIEHCMQNDIIPSWDCyvDNIPSRKLASKL 244
Cdd:pfam12746 151 KNGLGFVILKDGEIVSGASSYSVYEGGIEIEIDTHPDYRGKGLATICAAALILECLKRGLYPSWDA--HNEASVALAEKL 228

                         250
                  ....*....|.
gi 2324454598 245 SFYHPIEYSLF 255
Cdd:pfam12746 229 GYEFVKEYTAY 239
 
Name Accession Description Interval E-value
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 14-255 1.21e-69

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 214.44  E-value: 1.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598  14 PVLEGNTRTMtFAYAVCDQVvdGEVFVNGQ--LTAGLIITANgIYYLFGDTddqnyNEELFSYLKTaiEKTEKRFTLFTS 91
Cdd:pfam12746   2 PLFNGWDETL-IWSCLQGGM--GKVYVDNLenPTSALIVLGD-FVFFAGEP-----NEELVRFEPE--KSGLKRFILVPQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598  92 SEEWEMMLEERFSNTLRNIPR--MKFQRVTFEERK----RDFNKNTYEVKRIDRRDIER-SSEFKEEYYKEYWGSKETFL 164
Cdd:pfam12746  71 SEEWERLIEEVYGDKLRKITRyaFKKEPEVFDKEKleklVASLPQGYTLKKIDEELYEAcLEEEWSRDFVSQFSSYEDFL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598 165 NSGFGFCIEQDGIIVAECVSIFSGNGYAEIDIATHEAHQGKGLAQAVATRFIEHCMQNDIIPSWDCyvDNIPSRKLASKL 244
Cdd:pfam12746 151 KNGLGFVILKDGEIVSGASSYSVYEGGIEIEIDTHPDYRGKGLATICAAALILECLKRGLYPSWDA--HNEASVALAEKL 228

                         250
                  ....*....|.
gi 2324454598 245 SFYHPIEYSLF 255
Cdd:pfam12746 229 GYEFVKEYTAY 239
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
178-260 2.85e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.60  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598 178 IVAECVSIFSGNGYAEI-DIATHEAHQGKGLAQAVATRFIEHCMQNDI-IPSWDCYVDNIPSRKLASKLSFYHPIEYSLF 255
Cdd:COG3393     2 LVAMAGVRAESPGVAEIsGVYTHPEYRGRGLASALVAALAREALARGArTPFLYVDADNPAARRLYERLGFRPVGEYATV 81


                  ....*
gi 2324454598 256 VRKKT 260
Cdd:COG3393    82 LFRKP 86
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 170-224 6.30e-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: 6.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2324454598 170 FCIEQDGIIV--AECVSIFSGNGYAEI-DIATHEAHQGKGLAQAVATRFIEHCMQNDI 224
Cdd:cd04301     2 LVAEDDGEIVgfASLSPDGSGGDTAYIgDLAVLPEYRGKGIGSALLEAAEEEARERGA 59
 
Name Accession Description Interval E-value
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 14-255 1.21e-69

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 214.44  E-value: 1.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598  14 PVLEGNTRTMtFAYAVCDQVvdGEVFVNGQ--LTAGLIITANgIYYLFGDTddqnyNEELFSYLKTaiEKTEKRFTLFTS 91
Cdd:pfam12746   2 PLFNGWDETL-IWSCLQGGM--GKVYVDNLenPTSALIVLGD-FVFFAGEP-----NEELVRFEPE--KSGLKRFILVPQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598  92 SEEWEMMLEERFSNTLRNIPR--MKFQRVTFEERK----RDFNKNTYEVKRIDRRDIER-SSEFKEEYYKEYWGSKETFL 164
Cdd:pfam12746  71 SEEWERLIEEVYGDKLRKITRyaFKKEPEVFDKEKleklVASLPQGYTLKKIDEELYEAcLEEEWSRDFVSQFSSYEDFL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598 165 NSGFGFCIEQDGIIVAECVSIFSGNGYAEIDIATHEAHQGKGLAQAVATRFIEHCMQNDIIPSWDCyvDNIPSRKLASKL 244
Cdd:pfam12746 151 KNGLGFVILKDGEIVSGASSYSVYEGGIEIEIDTHPDYRGKGLATICAAALILECLKRGLYPSWDA--HNEASVALAEKL 228

                         250
                  ....*....|.
gi 2324454598 245 SFYHPIEYSLF 255
Cdd:pfam12746 229 GYEFVKEYTAY 239
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
178-260 2.85e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.60  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598 178 IVAECVSIFSGNGYAEI-DIATHEAHQGKGLAQAVATRFIEHCMQNDI-IPSWDCYVDNIPSRKLASKLSFYHPIEYSLF 255
Cdd:COG3393     2 LVAMAGVRAESPGVAEIsGVYTHPEYRGRGLASALVAALAREALARGArTPFLYVDADNPAARRLYERLGFRPVGEYATV 81


                  ....*
gi 2324454598 256 VRKKT 260
Cdd:COG3393    82 LFRKP 86
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 168-246 2.02e-08

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: 52.69  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598 168 FGFCIEQDGIIVAEC--VSIFSGNGYAEIDIATHEAHQGKGLAQAVATRFIEHCMQNDIIP--SWDCYVDNIPSRKLASK 243
Cdd:COG1670    63 FAIEDKEDGELIGVVglYDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHrvEAEVDPDNTASIRVLEK 142


                  ...
gi 2324454598 244 LSF 246
Cdd:COG1670   143 LGF 145
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 132-246 3.33e-08

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: 50.59  E-value: 3.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598 132 YEVKRIDRRDIERSSEFKEEYYKEYWgskeTFLNSGFGFCIEQDGIIV--AECVSIFSGNGYAEI-DIATHEAHQGKGLA 208
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDW----DEDASEGFFVAEEDGELVgfASLSIIDDEPPVGEIeGLAVAPEYRGKGIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2324454598 209 QAVATRFIEHCMQNDII-PSWDCYVDNIPSRKLASKLSF 246
Cdd:pfam00583  78 TALLQALLEWARERGCErIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 150-246 4.26e-08

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 50.81  E-value: 4.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598 150 EEYYKEYWGSKETFLNSGFGFCIEQDGII-VAECVSIFSGNGYAEIDIATHEAHQGKGLAQAVATRFIEHCMQNDIIP-- 226
Cdd:pfam13302  39 REWLARIWAADEAERGYGWAIELKDTGFIgSIGLYDIDGEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPrl 118

                          90       100
                  ....*....|....*....|
gi 2324454598 227 SWDCYVDNIPSRKLASKLSF 246
Cdd:pfam13302 119 VARIDPENTASRRVLEKLGF 138
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
150-246 3.23e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 43.06  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598 150 EEYYKEYWGskETFLNSGFGFCIEQDGIIV--AECVSIFSGNGY---AEIDIATHEAHQGKGLAQAVATRFIEHCMQNDI 224
Cdd:COG1247    37 EEEREAWFA--AILAPGRPVLVAEEDGEVVgfASLGPFRPRPAYrgtAEESIYVDPDARGRGIGRALLEALIERARARGY 114

                          90       100
                  ....*....|....*....|....
gi 2324454598 225 --IpSWDCYVDNIPSRKLASKLSF 246
Cdd:COG1247   115 rrL-VAVVLADNEASIALYEKLGF 137
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 165-219 1.68e-04

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: 40.36  E-value: 1.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2324454598 165 NSGFGFCIEQDGIIVAeCVSI-FSGNGYAEI-DIATHEAHQGKGLAQAVATRFIEHC 219
Cdd:COG1246    26 EIGEFWVAEEDGEIVG-CAALhPLDEDLAELrSLAVHPDYRGRGIGRRLLEALLAEA 81
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 182-246 2.46e-04

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 39.25  E-value: 2.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2324454598 182 CVSIFSGNGYAEI-DIATHEAHQGKGLAQAVATRFIEHCMQNDIIP-SWDCYVDNIPSRKLASKLSF 246
Cdd:COG0456     4 LLGLVDGGDEAEIeDLAVDPEYRGRGIGRALLEAALERARERGARRlRLEVREDNEAAIALYEKLGF 70
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 170-224 6.30e-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: 6.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2324454598 170 FCIEQDGIIV--AECVSIFSGNGYAEI-DIATHEAHQGKGLAQAVATRFIEHCMQNDI 224
Cdd:cd04301     2 LVAEDDGEIVgfASLSPDGSGGDTAYIgDLAVLPEYRGKGIGSALLEAAEEEARERGA 59
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 167-246 1.10e-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: 37.31  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324454598 167 GFGFCIEQDGIIVAECVSIFSGNGYAeidIATHEAHQGKGLAQAVATRFIEHCMQNDIIPSWDCYVDNIPSRKLASKLSF 246
Cdd:pfam08445   1 VLGIYRGDTGELAAWCLRLPGGELGA---LQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVVAGNTPSRRLYEKLGF 77
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 170-234 1.19e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 37.05  E-value: 1.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2324454598 170 FCIEQDGIIVAECVSIFSGNGY--AEIDIATHEAHQGKGLAQAVaTRFIEHCMQNDIIPSWDCYVDN 234
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGalAELRLAVHPEYRGQGIGRAL-LEAAEAAAKEGGIKLLELETTN 71
 
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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