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Conserved domains on  [gi|499271020|ref|WP_010968413|]
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GNAT family N-acetyltransferase [Sinorhizobium meliloti]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006981)

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
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
13-155 1.46e-17

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


:

Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 73.97  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020  13 YEELLSLIRASFaymdgridpPSSAHALTAASLNRKARDEIAFAAVAGRELLGCIFCKP-----EADCLYIGKLAVAPGR 87
Cdd:COG3153    9 AEAIAALLRAAF---------GPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPvdidgEGPALLLGPLAVDPEY 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499271020  88 QGKGVGRMLIAAAEETARDLGLPALRLQTRIELAGNqatFAAWGFVETARTAHPGFtrPTSVEMRKVL 155
Cdd:COG3153   80 RGQGIGRALMRAALEAARERGARAVVLLGDPSLLPF---YERFGFRPAGELGLTLG--PDEVFLAKEL 142
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
13-155 1.46e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 73.97  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020  13 YEELLSLIRASFaymdgridpPSSAHALTAASLNRKARDEIAFAAVAGRELLGCIFCKP-----EADCLYIGKLAVAPGR 87
Cdd:COG3153    9 AEAIAALLRAAF---------GPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPvdidgEGPALLLGPLAVDPEY 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499271020  88 QGKGVGRMLIAAAEETARDLGLPALRLQTRIELAGNqatFAAWGFVETARTAHPGFtrPTSVEMRKVL 155
Cdd:COG3153   80 RGQGIGRALMRAALEAARERGARAVVLLGDPSLLPF---YERFGFRPAGELGLTLG--PDEVFLAKEL 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 51-132 1.19e-11

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: 57.91  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020   51 DEIAFAAVAGRELLGCIFCKP---EADCLYIGKLAVAPGRQGKGVGRMLIAAAEETARDLGLPALRLQTRIELAGNQATF 127
Cdd:pfam00583  32 SEGFFVAEEDGELVGFASLSIiddEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALY 111


                  ....*
gi 499271020  128 AAWGF 132
Cdd:pfam00583 112 EKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 55-114 3.32e-11

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: 55.36  E-value: 3.32e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499271020  55 FAAVAGRELLGCIFCKP---EADCLYIGKLAVAPGRQGKGVGRMLIAAAEETARDLGLPALRL 114
Cdd:cd04301    2 LVAEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
PRK07757 PRK07757
N-acetyltransferase;
81-141 3.44e-08

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 49.81  E-value: 3.44e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271020  81 LAVAPGRQGKGVGRMLIAAAEETARDLGLP---ALRLQTRIelagnqatFAAWGFVETARTAHP 141
Cdd:PRK07757  71 LAVSEDYRGQGIGRMLVEACLEEARELGVKrvfALTYQPEF--------FEKLGFREVDKEALP 126
 
Name Accession Description Interval E-value
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
13-155 1.46e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 73.97  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020  13 YEELLSLIRASFaymdgridpPSSAHALTAASLNRKARDEIAFAAVAGRELLGCIFCKP-----EADCLYIGKLAVAPGR 87
Cdd:COG3153    9 AEAIAALLRAAF---------GPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPvdidgEGPALLLGPLAVDPEY 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499271020  88 QGKGVGRMLIAAAEETARDLGLPALRLQTRIELAGNqatFAAWGFVETARTAHPGFtrPTSVEMRKVL 155
Cdd:COG3153   80 RGQGIGRALMRAALEAARERGARAVVLLGDPSLLPF---YERFGFRPAGELGLTLG--PDEVFLAKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 38-156 3.54e-15

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: 67.71  E-value: 3.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020  38 HALTAASLNRKARDEIaFAAVAGRELLGCIFCKP-EADCLYIGKLAVAPGRQGKGVGRMLIAAAEETARDLGLPALRLQT 116
Cdd:COG1246   15 LELIRPYALEEEIGEF-WVAEEDGEIVGCAALHPlDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499271020 117 RIElagNQATFAAWGFVETARTAHP--GFTRPTSVEMRKVLS 156
Cdd:COG1246   94 TSA---AIHFYEKLGFEEIDKEDLPyaKVWQRDSVVMEKDLE 132
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 66-156 1.84e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 64.68  E-value: 1.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020  66 CIFCKPEADCLYIGKLAVAPGRQGKGVGRMLIAAAEETARDLGLPALRLQTRIELAGNQATFAAWGFVETARtaHPGFTR 145
Cdd:COG0456    4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGE--RPNYYG 81

                         90
                 ....*....|.
gi 499271020 146 PTSVEMRKVLS 156
Cdd:COG0456   82 DDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 51-132 1.19e-11

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: 57.91  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020   51 DEIAFAAVAGRELLGCIFCKP---EADCLYIGKLAVAPGRQGKGVGRMLIAAAEETARDLGLPALRLQTRIELAGNQATF 127
Cdd:pfam00583  32 SEGFFVAEEDGELVGFASLSIiddEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALY 111


                  ....*
gi 499271020  128 AAWGF 132
Cdd:pfam00583 112 EKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 50-156 1.26e-11

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 58.53  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020  50 RDEIAFAAVAGRELLGCI-FCKPEADCLYIGKLAVAPGRQGKGVGRMLIAAAEETARDLGLPALRLQTRIELAGNQATFA 128
Cdd:COG0454   32 AGAEFIAVDDKGEPIGFAgLRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYE 111

                         90       100
                 ....*....|....*....|....*...
gi 499271020 129 AWGFVETARtahpgFTRPTSVEMRKVLS 156
Cdd:COG0454  112 RLGFKEIER-----YVAYVGGEFEKELS 134
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 55-114 3.32e-11

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: 55.36  E-value: 3.32e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499271020  55 FAAVAGRELLGCIFCKP---EADCLYIGKLAVAPGRQGKGVGRMLIAAAEETARDLGLPALRL 114
Cdd:cd04301    2 LVAEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
49-135 3.81e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 54.42  E-value: 3.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020  49 ARDEIA--FAAVAGRELLGCI-FCKPEADCLYIGKLAVAPGRQGKGVGRMLIAAAEETARDLGLPALRLQTRIELAGnqa 125
Cdd:COG2153   29 GKDEDArhLLAYDDGELVATArLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAHAVG--- 105

                         90
                 ....*....|.
gi 499271020 126 tF-AAWGFVET 135
Cdd:COG2153  106 -FyEKLGFVPV 115
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 50-122 1.62e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.99  E-value: 1.62e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499271020   50 RDEIAFAAVAGRELLGCIFCKPEADCLYIG--KLAVAPGRQGKGVGRMLIAAAEETARDLGLPALRLQTRIELAG 122
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAA 75
PRK07757 PRK07757
N-acetyltransferase;
81-141 3.44e-08

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 49.81  E-value: 3.44e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271020  81 LAVAPGRQGKGVGRMLIAAAEETARDLGLP---ALRLQTRIelagnqatFAAWGFVETARTAHP 141
Cdd:PRK07757  71 LAVSEDYRGQGIGRMLVEACLEEARELGVKrvfALTYQPEF--------FEKLGFREVDKEALP 126
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
13-137 3.22e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 44.60  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020  13 YEELLSLIRASFAYmdgridPPSSAHALTAASLNRKARDEIAFAAVAGRELLGCIFC-----KPEADCLYIGKLAVAPGR 87
Cdd:COG1247   19 YNEAIAEGTATFET------EPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLgpfrpRPAYRGTAEESIYVDPDA 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499271020  88 QGKGVGRMLIAAAEETARDLGLPALRLQTrieLAGNQAT---FAAWGFVETAR 137
Cdd:COG1247   93 RGRGIGRALLEALIERARARGYRRLVAVV---LADNEASialYEKLGFEEVGT 142
COG3818 COG3818
Predicted N-acetyltransferase, GNAT superfamily [General function prediction only];
74-156 3.31e-06

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


Pssm-ID: 443030 [Multi-domain]  Cd Length: 168  Bit Score: 44.54  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020  74 DCLYIGKLAVAPGRQGKGVGRMLIAAAEETARDLGLPALRLQTRIELA--GNQATFAAWGFVETARTAHPGFTRPTSVEM 151
Cdd:COG3818   83 NFLYIDRIVVAPSARGRGLGRALYADVFSYARARGVPRVTCEVNLEPPnpGSLAFHARLGFREVGQQRVAGGKKRVSLLA 162


                 ....*
gi 499271020 152 RKVLS 156
Cdd:COG3818  163 KELCS 167
PRK03624 PRK03624
putative acetyltransferase; Provisional
 81-138 2.87e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 41.45  E-value: 2.87e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499271020  81 LAVAPGRQGKGVGRMLIAAAEETARDLGLPALRLQTRIELAGNQATFAAWGFVETART 138
Cdd:PRK03624  74 LAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDRI 131
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
78-125 5.33e-05

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 41.45  E-value: 5.33e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 499271020  78 IGKLAVAPGRQGKGVGRMLIAAAEETARDLGLPALRLQTRIelaGNQA 125
Cdd:PRK10975 129 IGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQM---GNLA 173
PRK07922 PRK07922
amino-acid N-acetyltransferase;
81-109 3.50e-03

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 36.05  E-value: 3.50e-03
                         10        20
                 ....*....|....*....|....*....
gi 499271020  81 LAVAPGRQGKGVGRMLIAAAEETARDLGL 109
Cdd:PRK07922  76 VAVDPAARGRGVGHAIVERLLDVARELGL 104
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 71-151 6.72e-03

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 35.90  E-value: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271020  71 PEADCLYIGKLAVAPGRQGKGVGRMLIAAAEETARDLGLPALrlqtrielagnqatfaawgFVETARTAH----PGFTrP 146
Cdd:PRK05279 355 PEEKMGEMACLAVHPDYRGSGRGERLLKRIEQRARQLGLKRL-------------------FVLTTRTAHwfleRGFV-P 414


                 ....*
gi 499271020 147 TSVEM 151
Cdd:PRK05279 415 VDVDD 419
 
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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