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Conserved domains on  [gi|1391268192|ref|WP_109408589|]
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MULTISPECIES: GNAT family N-acetyltransferase [Proteus]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 1-164 2.91e-52

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member PRK10140:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 162  Bit Score: 164.00  E-value: 2.91e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   1 MQEIKIRHGEPDDATAIQQLYTHPDLYICTCQFPYPSVTMWKKRLLEfaEQNIPNFVATIDGQVAGHLALIIDNHPRRRH 80
Cdd:PRK10140    1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLAD--RPGIKQLVACIDGDVVGHLTIDVQQRPRRSH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  81 IVSFGIGVGAEYSGKGVGKLLINTAIDYAFNWLAATRLELEVYSDNEKGLHLYKKLGFEVEGIRRKAAFRDGKYCDVVMM 160
Cdd:PRK10140   79 VADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYM 158


                  ....
gi 1391268192 161 SMLR 164
Cdd:PRK10140  159 ARVK 162
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-164 2.91e-52

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 164.00  E-value: 2.91e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   1 MQEIKIRHGEPDDATAIQQLYTHPDLYICTCQFPYPSVTMWKKRLLEfaEQNIPNFVATIDGQVAGHLALIIDNHPRRRH 80
Cdd:PRK10140    1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLAD--RPGIKQLVACIDGDVVGHLTIDVQQRPRRSH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  81 IVSFGIGVGAEYSGKGVGKLLINTAIDYAFNWLAATRLELEVYSDNEKGLHLYKKLGFEVEGIRRKAAFRDGKYCDVVMM 160
Cdd:PRK10140   79 VADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYM 158


                  ....
gi 1391268192 161 SMLR 164
Cdd:PRK10140  159 ARVK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-165 4.75e-32

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: 112.79  E-value: 4.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   1 MQEIKIRHGEPDDATAIQQLYTHPDL--YICTCQFPYPSVTMWKKRLLEFAEQNIPNFVATI---DGQVAGHLALIidNH 75
Cdd:COG1670     5 TERLRLRPLRPEDAEALAELLNDPEVarYLPGPPYSLEEARAWLERLLADWADGGALPFAIEdkeDGELIGVVGLY--DI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  76 PRRRHIVSFGIGVGAEYSGKGVGKLLINTAIDYAFNWLAATRLELEVYSDNEKGLHLYKKLGFEVEGIRRKAAFRDGKYC 155
Cdd:COG1670    83 DRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYR 162

                         170
                  ....*....|
gi 1391268192 156 DVVMMSMLRT 165
Cdd:COG1670   163 DHVLYSLLRE 172
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-138 1.38e-16

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: 71.39  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  25 DLYICTCQFPYPSVTMWKkRLLEFAEQNIPNFVATIDGQVAGHLALIIDNHPRRRHIVsFGIGVGAEYSGKGVGKLLINT 104
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDL-LEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEI-EGLAVAPEYRGKGIGTALLQA 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1391268192 105 AIDYAFNWlAATRLELEVYSDNEKGLHLYKKLGF 138
Cdd:pfam00583  84 LLEWARER-GCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 47-146 1.66e-14

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: 66.20  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  47 EFAEQNIPNFVATIDGQVAGHLALIIDNHprRRHIvsFGIGVGAEYSGKGVGKLLINTAIDYAFNwLAATRLELEVYSDN 126
Cdd:TIGR01575  25 ELANYHLCYLLARIGGKVVGYAGVQIVLD--EAHI--LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSN 99

                          90       100
                  ....*....|....*....|
gi 1391268192 127 EKGLHLYKKLGFEVEGIRRK 146
Cdd:TIGR01575 100 IAAQALYKKLGFNEIAIRRN 119
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-121 2.09e-07

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: 45.73  E-value: 2.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391268192  56 FVATIDGQVAGHLALIIDNHPRRRHIVSFgIGVGAEYSGKGVGKLLINTAIDYAFNWlAATRLELE 121
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGGDTAYIGD-LAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-164 2.91e-52

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 164.00  E-value: 2.91e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   1 MQEIKIRHGEPDDATAIQQLYTHPDLYICTCQFPYPSVTMWKKRLLEfaEQNIPNFVATIDGQVAGHLALIIDNHPRRRH 80
Cdd:PRK10140    1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLAD--RPGIKQLVACIDGDVVGHLTIDVQQRPRRSH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  81 IVSFGIGVGAEYSGKGVGKLLINTAIDYAFNWLAATRLELEVYSDNEKGLHLYKKLGFEVEGIRRKAAFRDGKYCDVVMM 160
Cdd:PRK10140   79 VADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYM 158


                  ....
gi 1391268192 161 SMLR 164
Cdd:PRK10140  159 ARVK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-165 4.75e-32

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: 112.79  E-value: 4.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   1 MQEIKIRHGEPDDATAIQQLYTHPDL--YICTCQFPYPSVTMWKKRLLEFAEQNIPNFVATI---DGQVAGHLALIidNH 75
Cdd:COG1670     5 TERLRLRPLRPEDAEALAELLNDPEVarYLPGPPYSLEEARAWLERLLADWADGGALPFAIEdkeDGELIGVVGLY--DI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  76 PRRRHIVSFGIGVGAEYSGKGVGKLLINTAIDYAFNWLAATRLELEVYSDNEKGLHLYKKLGFEVEGIRRKAAFRDGKYC 155
Cdd:COG1670    83 DRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYR 162

                         170
                  ....*....|
gi 1391268192 156 DVVMMSMLRT 165
Cdd:COG1670   163 DHVLYSLLRE 172
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-160 4.83e-30

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 107.39  E-value: 4.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   3 EIKIRHGEPDDATAIQQLYTHpdlYICTCQFPY----PSVTMWKKRLLEFAEQNIPNFVATIDGQVAGHLAL-IIDNHPR 77
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNE---AIAEGTATFetepPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLgPFRPRPA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  78 RRHIVSFGIGVGAEYSGKGVGKLLINTAIDYAfnwLAA--TRLELEVYSDNEKGLHLYKKLGFEVEGIRRKAAFRDGKYC 155
Cdd:COG1247    78 YRGTAEESIYVDPDARGRGIGRALLEALIERA---RARgyRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWL 154


                  ....*
gi 1391268192 156 DVVMM 160
Cdd:COG1247   155 DLVLM 159
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-138 1.38e-16

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: 71.39  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  25 DLYICTCQFPYPSVTMWKkRLLEFAEQNIPNFVATIDGQVAGHLALIIDNHPRRRHIVsFGIGVGAEYSGKGVGKLLINT 104
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDL-LEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEI-EGLAVAPEYRGKGIGTALLQA 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1391268192 105 AIDYAFNWlAATRLELEVYSDNEKGLHLYKKLGF 138
Cdd:pfam00583  84 LLEWARER-GCERIFLEVAADNLAAIALYEKLGF 116
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 3-164 1.07e-15

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 70.60  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   3 EIKIRHGEPDDATAIQQLYTHPDLYICTCQFPYPSVT----MWKKRLLEFAEQNipnFVATIDGQVAGHLALIIDNHPRR 78
Cdd:PRK15130    6 SVKLRPLEREDLRFVHQLDNNASVMRYWFEEPYEAFVelsdLYDKHIHDQSERR---FVVECDGEKAGLVELVEINHVHR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  79 RhiVSFGIGVGAEYSGKGVGKLLINTAIDYAFNWLAATRLELEVYSDNEKGLHLYKKLGFEVEGIRRKAAFRDGKYCDVV 158
Cdd:PRK15130   83 R--AEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTI 160


                  ....*.
gi 1391268192 159 MMSMLR 164
Cdd:PRK15130  161 RMCIFQ 166
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 47-146 1.66e-14

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: 66.20  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  47 EFAEQNIPNFVATIDGQVAGHLALIIDNHprRRHIvsFGIGVGAEYSGKGVGKLLINTAIDYAFNwLAATRLELEVYSDN 126
Cdd:TIGR01575  25 ELANYHLCYLLARIGGKVVGYAGVQIVLD--EAHI--LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSN 99

                          90       100
                  ....*....|....*....|
gi 1391268192 127 EKGLHLYKKLGFEVEGIRRK 146
Cdd:TIGR01575 100 IAAQALYKKLGFNEIAIRRN 119
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 66-145 5.66e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.91  E-value: 5.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  66 GHLALIIDNHPRRRHIvsFGIGVGAEYSGKGVGKLLINTAIDYAFNwLAATRLELEVYSDNEKGLHLYKKLGFEVEGIRR 145
Cdd:COG0456     1 GFALLGLVDGGDEAEI--EDLAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-142 3.66e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 60.48  E-value: 3.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   6 IRHGEPDDATAIQQLYTHpdlyictcQFPYPSVTMWKKRLLEFAEQNIPnFVATIDGQVAGHLALIIDNHPRRRHIVSFG 85
Cdd:COG3153     1 IRPATPEDAEAIAALLRA--------AFGPGREAELVDRLREDPAAGLS-LVAEDDGEIVGHVALSPVDIDGEGPALLLG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1391268192  86 -IGVGAEYSGKGVGKLLINTAIDYAfNWLAATRLELEVysdNEKGLHLYKKLGFEVEG 142
Cdd:COG3153    72 pLAVDPEYRGQGIGRALMRAALEAA-RERGARAVVLLG---DPSLLPFYERFGFRPAG 125
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 4-160 7.66e-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: 59.24  E-value: 7.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   4 IKIRHGEPDDATAIQQLYTHPDLYictcqfpypsvtmwkkrllefaeQNIPNF-VATIDGQVAGHLALIIDNhPRRRHIV 82
Cdd:COG1246     1 MTIRPATPDDVPAILELIRPYALE-----------------------EEIGEFwVAEEDGEIVGCAALHPLD-EDLAELR 56

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391268192  83 SfgIGVGAEYSGKGVGKLLINTAIDYAFNwLAATRLELEVYSDNEkglHLYKKLGFEVEGIRRKAAFRDGKYCDVVMM 160
Cdd:COG1246    57 S--LAVHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLLTTSAAI---HFYEKLGFEEIDKEDLPYAKVWQRDSVVME 128
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 95-160 9.29e-11

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 56.98  E-value: 9.29e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391268192  95 KGVGKLLINTAIDYAFNWLAATRLELEVYSDNEKGLHLYKKLGFEVEGIRRKAafrdGKYCDVVMM 160
Cdd:TIGR03585  90 PGVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQG----GEYYDVLLM 151
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 56-140 3.39e-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: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  56 FVATIDGQVAGHLALIIDNHPrrrHIVSFGIGVGAEYSGKGVGKLLINTAIDyafnWLAA---TRLELEVYSDNEKGLHL 132
Cdd:COG0454    37 IAVDDKGEPIGFAGLRRLDDK---VLELKRLYVLPEYRGKGIGKALLEALLE----WARErgcTALELDTLDGNPAAIRF 109


                  ....*...
gi 1391268192 133 YKKLGFEV 140
Cdd:COG0454   110 YERLGFKE 117
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 56-140 4.00e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.92  E-value: 4.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  56 FVATIDGQVAGHLALIIDNHPRRRHIVSfgIGVGAEYSGKGVGKLLIntaiDYAFNWLAATRLELEVYSDNEKGLHLYKK 135
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEGALAELR--LAVHPEYRGQGIGRALL----EAAEAAAKEGGIKLLELETTNRAAAFYEK 79


                  ....*
gi 1391268192 136 LGFEV 140
Cdd:pfam13508  80 LGFEE 84
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 47-142 4.10e-09

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: 51.89  E-value: 4.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  47 EFAEQNIPNFVATIDGQVAGHLALIidnhpRRRHIvsFGIGVGAEYSGKGVGKLLINTAIDYAFNWLAATRlELEVYSDN 126
Cdd:pfam13673  25 RIDQGEYFFFVAFEGGQIVGVIALR-----DRGHI--SLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLS-ELTVNASP 96

                          90
                  ....*....|....*.
gi 1391268192 127 EkGLHLYKKLGFEVEG 142
Cdd:pfam13673  97 Y-AVPFYEKLGFRATG 111
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
6-159 1.45e-08

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 50.83  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   6 IRHGEPDDATAIQQLYTHPDL-YICTCQFPYPSVTMWKKRLLE-FAEQNIPnFVATIDGQVAGHLALIiDNHPRRRH--I 81
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVnPAFTQEYAHSSIEEFETFLAAyLSPGEIV-FGVAESDRLIGYATLR-QFDYVKTHkaE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391268192  82 VSFGIGVGAEysgKGVGKLLINTAIDYAFNWLAATRLELEVYSDNEKGLHLYKKLGFEVEGIRRKAAFRDGKYCDVVM 159
Cdd:pfam13420  79 LSFYVVKNND---EGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDMMW 153
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 6-139 2.18e-08

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 50.04  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   6 IRHGEPDDATAIQQLYTHPDLYICTCQFPYPSVTMWKKRLLEFAEQNIPN-FVATIDGQVAGHLALI-IDNHPRRRHIVS 83
Cdd:pfam13302   4 LRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEAERgYGWAIELKDTGFIGSIgLYDIDGEPERAE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1391268192  84 FGIGVGAEYSGKGVGKLLINTAIDYAFNWLAATRLELEVYSDNEKGLHLYKKLGFE 139
Cdd:pfam13302  84 LGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 56-121 2.09e-07

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: 45.73  E-value: 2.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391268192  56 FVATIDGQVAGHLALIIDNHPRRRHIVSFgIGVGAEYSGKGVGKLLINTAIDYAFNWlAATRLELE 121
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGGDTAYIGD-LAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
PRK03624 PRK03624
putative acetyltransferase; Provisional
 56-141 1.17e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.69  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  56 FVATIDGQVAGHLALIIDNHprRRHIVSFGigVGAEYSGKGVGKLLINTAIDyafnWLAA---TRLELEVYSDNEKGLHL 132
Cdd:PRK03624   48 LVAEVGGEVVGTVMGGYDGH--RGWAYYLA--VHPDFRGRGIGRALVARLEK----KLIArgcPKINLQVREDNDAVLGF 119


                  ....*....
gi 1391268192 133 YKKLGFEVE 141
Cdd:PRK03624  120 YEALGYEEQ 128
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
50-142 4.59e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 43.63  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  50 EQNIP-------------NFVATIDGQVAGHLALIIDNHPrrrhIVSFG-IGVGAEYSGKGVGKLLINTAIDYAFNwLAA 115
Cdd:COG2153    18 EQGVPpyleldgkdedarHLLAYDDGELVATARLLPPGDG----EAKIGrVAVLPEYRGQGLGRALMEAAIEEARE-RGA 92

                          90       100
                  ....*....|....*....|....*..
gi 1391268192 116 TRLELEVYSDNEKglhLYKKLGFEVEG 142
Cdd:COG2153    93 RRIVLSAQAHAVG---FYEKLGFVPVG 116
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
85-142 7.18e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 39.51  E-value: 7.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1391268192  85 GIGVGAEYSGKGVGKLLINTAIDYAFNwLAATRLELEVYSDNEKGLHLYKKLGFEVEG 142
Cdd:COG3393    20 GVYTHPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFRPVG 76
PRK10562 PRK10562
putative acetyltransferase; Provisional
 88-142 1.39e-04

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 40.05  E-value: 1.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1391268192  88 VGAEYSGKGVGKLLInTAIDYAFNWLAatrleLEVYSDNEKGLHLYKKLGFEVEG 142
Cdd:PRK10562   76 VAPKAVRRGIGKALM-QHVQQRYPHLS-----LEVYQKNQRAVNFYHAQGFRIVD 124
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
56-109 7.96e-04

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 36.67  E-value: 7.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1391268192  56 FVATIDGQVAGHLALIIDNHprrrHIVSFGIGVGAEYSGKGVGKLLINTAIDYA 109
Cdd:COG2388    12 FELEVDGELAGELTYRLEGG----VIIITHTEVPPALRGQGIASALVEAALDDA 61
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 84-145 1.05e-03

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 37.60  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192  84 FGIGVGAEYSGKGVGKLLINTAIDyafnwlaatRLE--------LEVYSDNEKGLHLYKKLGFEVEGIRR 145
Cdd:PRK09491   67 FNIAVDPDYQRQGLGRALLEHLID---------ELEkrgvatlwLEVRASNAAAIALYESLGFNEVTIRR 127
PRK10514 PRK10514
putative acetyltransferase; Provisional
 88-142 1.19e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 37.29  E-value: 1.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1391268192  88 VGAEYSGKGVGKLLINTAidyafnwLA-ATRLELEVYSDNEKGLHLYKKLGFEVEG 142
Cdd:PRK10514   77 VDPDVRGCGVGRMLVEHA-------LSlHPELTTDVNEQNEQAVGFYKKMGFKVTG 125
PRK07757 PRK07757
N-acetyltransferase;
3-109 2.48e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 36.33  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268192   3 EIKIRHGEPDDATAIQQLythpdlyictcqfpypsVTMWKKR-------LLEFAEqNIPNF-VATIDGQVAGHLALiidn 74
Cdd:PRK07757    1 MMEIRKARLSDVKAIHAL-----------------INVYAKKglmlprsLDELYE-NIRDFyVAEEEGEIVGCCAL---- 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1391268192  75 hprrrHIVSFGIG------VGAEYSGKGVGKLLINTAIDYA 109
Cdd:PRK07757   59 -----HILWEDLAeirslaVSEDYRGQGIGRMLVEACLEEA 94
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 90-142 3.62e-03

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 35.96  E-value: 3.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1391268192  90 AEYSGKGVGKLLINTAIDYAFNWLAATRLELEVYSDNEKGLHLYKKLGFEVEG 142
Cdd:pfam13523  89 PAFRGRGFTTALLRALVHYLFADPRTRRVVVEPDVRNERAIRLLERAGFRKVK 141
 
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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