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Conserved domains on  [gi|1718055438|ref|WP_144530565|]
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GNAT family N-acetyltransferase [Bacillus subtilis]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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

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List of domain hits

 Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-135 5.15e-23

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 88.51  E-value: 5.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438   1 MNIRQAKTSDTAAIAPLFNQYRE-----FYRQASDLQGAEAFLKARLENHESViLIAEENGEFIGFTQLYPtFSSVSMKR 75
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAIAegtatFETEPPSEEEREAWFAAILAPGRPV-LVAEEDGEVVGFASLGP-FRPRPAYR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438  76 IYILNDLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTLQTEHHNRKARSLYEQNGYEE 135
Cdd:COG1247    80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEE 139
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-135 5.15e-23

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 88.51  E-value: 5.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438   1 MNIRQAKTSDTAAIAPLFNQYRE-----FYRQASDLQGAEAFLKARLENHESViLIAEENGEFIGFTQLYPtFSSVSMKR 75
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAIAegtatFETEPPSEEEREAWFAAILAPGRPV-LVAEEDGEVVGFASLGP-FRPRPAYR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438  76 IYILNDLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTLQTEHHNRKARSLYEQNGYEE 135
Cdd:COG1247    80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEE 139
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-133 3.39e-14

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: 64.46  E-value: 3.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438  14 IAPLFNQYREFYRqASDLQGAEAFLKARLENHESVILIAEENGEFIGFTQLYPTFSSVsmKRIYILnDLFVVPHARTKGA 93
Cdd:pfam00583   1 LEALYELLSEEFP-EPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP--PVGEIE-GLAVAPEYRGKGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1718055438  94 GGLLLSAAKDYAGENGAKCLTLQTEHHNRKARSLYEQNGY 133
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 49-115 5.50e-09

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: 49.58  E-value: 5.50e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055438  49 ILIAEENGEFIGFTQLYPTFSSvsmKRIYILNDLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTL 115
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSG---GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
3-135 8.26e-07

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 45.68  E-value: 8.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438   3 IRQAKTSDTAAIAPLFNQYR--EFYRQAsdlqgAEAFLKARLENHESVILIAEENGEFIGFTQLYPTFSSVSMKRIYILN 80
Cdd:PRK10146    6 LRPATQYDTDAVYALICELKqaEFDHQA-----FRVGFNANLRDPNMRYHLALLDGEVVGMIGLHLQFHLHHVNWIGEIQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1718055438  81 DLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTLQTEHHNRKARSLYEQNGYEE 135
Cdd:PRK10146   81 ELVVMPQARGLNVGSKLLAWAEEEARQAGAEMTELSTNVKRHDAHRFYLREGYEQ 135
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-135 5.15e-23

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 88.51  E-value: 5.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438   1 MNIRQAKTSDTAAIAPLFNQYRE-----FYRQASDLQGAEAFLKARLENHESViLIAEENGEFIGFTQLYPtFSSVSMKR 75
Cdd:COG1247     2 MTIRPATPEDAPAIAAIYNEAIAegtatFETEPPSEEEREAWFAAILAPGRPV-LVAEEDGEVVGFASLGP-FRPRPAYR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438  76 IYILNDLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTLQTEHHNRKARSLYEQNGYEE 135
Cdd:COG1247    80 GTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEE 139
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-135 5.73e-17

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: 71.95  E-value: 5.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438   1 MNIRQAKTSDTAAIAPLFNQYRefyrqasdlqgaeaflkarLENHESVILIAEENGEFIGFTQLYPTFssvsmKRIYILN 80
Cdd:COG1246     1 MTIRPATPDDVPAILELIRPYA-------------------LEEEIGEFWVAEEDGEIVGCAALHPLD-----EDLAELR 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1718055438  81 DLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTLQTehhNRKARSLYEQNGYEE 135
Cdd:COG1246    57 SLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFEE 108
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-141 8.03e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 69.34  E-value: 8.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438   3 IRQAKTSDTAAIaplfnqyREFYRQASDlQGAEAFLKARLENHE--SVILIAEENGEFIGFTQLYPTFSSVSMKRIYiLN 80
Cdd:COG3153     1 IRPATPEDAEAI-------AALLRAAFG-PGREAELVDRLREDPaaGLSLVAEDDGEIVGHVALSPVDIDGEGPALL-LG 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718055438  81 DLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTLQTehhNRKARSLYEQNGYEEDTAFVH 141
Cdd:COG3153    72 PLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYERFGFRPAGELGL 129
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 1-135 2.84e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 65.07  E-value: 2.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438   1 MNIRQAKTSDTAAIAPLFNQYREFYRQASDLQGAEAflkarlenhesviLIAEENGEFIGFTqlypTFSSVSMKRIYILN 80
Cdd:COG0454     1 MSIRKATPEDINFILLIEALDAELKAMEGSLAGAEF-------------IAVDDKGEPIGFA----GLRRLDDKVLELKR 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1718055438  81 dLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTLQTEHHNRKARSLYEQNGYEE 135
Cdd:COG0454    64 -LYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-133 3.39e-14

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: 64.46  E-value: 3.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438  14 IAPLFNQYREFYRqASDLQGAEAFLKARLENHESVILIAEENGEFIGFTQLYPTFSSVsmKRIYILnDLFVVPHARTKGA 93
Cdd:pfam00583   1 LEALYELLSEEFP-EPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEP--PVGEIE-GLAVAPEYRGKGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1718055438  94 GGLLLSAAKDYAGENGAKCLTLQTEHHNRKARSLYEQNGY 133
Cdd:pfam00583  77 GTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 60-142 2.50e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 61.60  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438  60 GFTQLYPTFSSvsmKRIYILnDLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTLQTEHHNRKARSLYEQNGYEEDTAF 139
Cdd:COG0456     1 GFALLGLVDGG---DEAEIE-DLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76


                  ...
gi 1718055438 140 VHY 142
Cdd:COG0456    77 PNY 79
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 46-135 1.21e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 57.08  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438  46 ESVILIAEENGEFIGFTQLYPTFSSVSMKRIyilnDLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTLQTehhNRKAR 125
Cdd:pfam13508   2 GGRFFVAEDDGKIVGFAALLPLDDEGALAEL----RLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAA 74

                          90
                  ....*....|
gi 1718055438 126 SLYEQNGYEE 135
Cdd:pfam13508  75 AFYEKLGFEE 84
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 49-115 5.50e-09

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: 49.58  E-value: 5.50e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055438  49 ILIAEENGEFIGFTQLYPTFSSvsmKRIYILNDLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTL 115
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDGSG---GDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
79-144 8.95e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.52  E-value: 8.95e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055438  79 LNDLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTLQTEHHNRKARSLYEQNGYEEDTAFVHYSL 144
Cdd:COG3393    18 ISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLF 83
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-142 2.89e-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: 50.00  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438   3 IRQAKTSDTAAIAPLFNQ---YREFYRQASDLQGAEAFLKARLENHES-----VILIAEENGEFIGFTQLYPTfsSVSMK 74
Cdd:COG1670    10 LRPLRPEDAEALAELLNDpevARYLPGPPYSLEEARAWLERLLADWADggalpFAIEDKEDGELIGVVGLYDI--DRANR 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055438  75 RIYIlnDLFVVPHARTKGAGGLLLSAAKDYA-GENGAKCLTLQTEHHNRKARSLYEQNGYEEDTAFVHY 142
Cdd:COG1670    88 SAEI--GYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDA 154
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 32-135 5.78e-07

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: 45.72  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438  32 QGAEAF--------LKARLENHESVILIAEENGEFIGFtqlyptfssVSMKRIYILNDLFVVPHARTKGAGGLLLSAAKD 103
Cdd:pfam13673   8 EGIETFyefispeaLRERIDQGEYFFFVAFEGGQIVGV---------IALRDRGHISLLFVDPDYQGQGIGKALLEAVED 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1718055438 104 YAGENGAKCLTLqTEHHNRKARSLYEQNGYEE 135
Cdd:pfam13673  79 YAEKDGIKLSEL-TVNASPYAVPFYEKLGFRA 109
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
3-135 8.26e-07

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 45.68  E-value: 8.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055438   3 IRQAKTSDTAAIAPLFNQYR--EFYRQAsdlqgAEAFLKARLENHESVILIAEENGEFIGFTQLYPTFSSVSMKRIYILN 80
Cdd:PRK10146    6 LRPATQYDTDAVYALICELKqaEFDHQA-----FRVGFNANLRDPNMRYHLALLDGEVVGMIGLHLQFHLHHVNWIGEIQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1718055438  81 DLFVVPHARTKGAGGLLLSAAKDYAGENGAKCLTLQTEHHNRKARSLYEQNGYEE 135
Cdd:PRK10146   81 ELVVMPQARGLNVGSKLLAWAEEEARQAGAEMTELSTNVKRHDAHRFYLREGYEQ 135
 
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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