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Conserved domains on  [gi|489082356|ref|WP_002992278|]
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ribosomal protein S18-alanine N-acetyltransferase [Streptococcus pyogenes]

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 ...
 8-133 8.29e-31

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 TIGR01575:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 131  Bit Score: 107.03  E-value: 8.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356    8 AKNIYQLLEMVYgTSPWTLEQVLIDIRRDQTDYFLLYDHDKLLGFLAIQDLAGEVEMTQIAILPSHQGLGLASQLMTHL- 86
Cdd:TIGR01575   2 LKAVLEIEAAAF-AFPWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELi 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489082356   87 -DSIESD---IFLEVRESNHRAQGLYQKFGFKFIGKRPDYYRNPIETALLM 133
Cdd:TIGR01575  81 dEAKGRGvneIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 8-133 8.29e-31

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: 107.03  E-value: 8.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356    8 AKNIYQLLEMVYgTSPWTLEQVLIDIRRDQTDYFLLYDHDKLLGFLAIQDLAGEVEMTQIAILPSHQGLGLASQLMTHL- 86
Cdd:TIGR01575   2 LKAVLEIEAAAF-AFPWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELi 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489082356   87 -DSIESD---IFLEVRESNHRAQGLYQKFGFKFIGKRPDYYRNPIETALLM 133
Cdd:TIGR01575  81 dEAKGRGvneIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 51-136 8.96e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 75.46  E-value: 8.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356  51 GFLAIQ--DLAGEVEMTQIAILPSHQGLGLASQLMTHLDSIESD-----IFLEVRESNHRAQGLYQKFGFKFIGKRPDYY 123
Cdd:COG0456    1 GFALLGlvDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARErgarrLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|...
gi 489082356 124 RNPietALLMKRE 136
Cdd:COG0456   81 GDD---ALVMEKE 90
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 23-133 1.33e-15

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 68.80  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356  23 PWTlEQVLIDirrDQTDYFL---LYDHDKLLGFLAIQDLAGEVEMTQIAILPSHQGLGLASQLMTHL--DSIESDIF--- 94
Cdd:PRK09491  26 PWS-EKTFAS---NQGERYLnlkLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLidELEKRGVAtlw 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489082356  95 LEVRESNHRAQGLYQKFGFKFIGKRPDYYRNPI--ETALLM 133
Cdd:PRK09491 102 LEVRASNAAAIALYESLGFNEVTIRRNYYPTADgrEDAIIM 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 15-113 1.30e-13

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: 62.92  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356   15 LEMVYGTSPWTLEQVLIDIRRDQTD---YFLLYDHDKLLGFLAI---QDLAGEVEMTQIAILPSHQGLGLASQLMTHLDS 88
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDAsegFFVAEEDGELVGFASLsiiDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLE 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 489082356   89 I-----ESDIFLEVRESNHRAQGLYQKFGF 113
Cdd:pfam00583  87 WarergCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 40-86 5.50e-06

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: 41.49  E-value: 5.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489082356  40 YFLLYDHDKLLGFLAI---QDLAGEVEMTQIAILPSHQGLGLASQLMTHL 86
Cdd:cd04301    1 FLVAEDDGEIVGFASLspdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAA 50
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 8-133 8.29e-31

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: 107.03  E-value: 8.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356    8 AKNIYQLLEMVYgTSPWTLEQVLIDIRRDQTDYFLLYDHDKLLGFLAIQDLAGEVEMTQIAILPSHQGLGLASQLMTHL- 86
Cdd:TIGR01575   2 LKAVLEIEAAAF-AFPWTEAQFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELi 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489082356   87 -DSIESD---IFLEVRESNHRAQGLYQKFGFKFIGKRPDYYRNPIETALLM 133
Cdd:TIGR01575  81 dEAKGRGvneIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 51-136 8.96e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 75.46  E-value: 8.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356  51 GFLAIQ--DLAGEVEMTQIAILPSHQGLGLASQLMTHLDSIESD-----IFLEVRESNHRAQGLYQKFGFKFIGKRPDYY 123
Cdd:COG0456    1 GFALLGlvDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARErgarrLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|...
gi 489082356 124 RNPietALLMKRE 136
Cdd:COG0456   81 GDD---ALVMEKE 90
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 23-133 1.33e-15

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 68.80  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356  23 PWTlEQVLIDirrDQTDYFL---LYDHDKLLGFLAIQDLAGEVEMTQIAILPSHQGLGLASQLMTHL--DSIESDIF--- 94
Cdd:PRK09491  26 PWS-EKTFAS---NQGERYLnlkLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLidELEKRGVAtlw 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489082356  95 LEVRESNHRAQGLYQKFGFKFIGKRPDYYRNPI--ETALLM 133
Cdd:PRK09491 102 LEVRASNAAAIALYESLGFNEVTIRRNYYPTADgrEDAIIM 142
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 15-113 1.30e-13

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: 62.92  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356   15 LEMVYGTSPWTLEQVLIDIRRDQTD---YFLLYDHDKLLGFLAI---QDLAGEVEMTQIAILPSHQGLGLASQLMTHLDS 88
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDAsegFFVAEEDGELVGFASLsiiDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLE 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 489082356   89 I-----ESDIFLEVRESNHRAQGLYQKFGF 113
Cdd:pfam00583  87 WarergCERIFLEVAADNLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 40-131 3.25e-13

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 62.38  E-value: 3.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356  40 YFLLYDHDKLLGFLAIQDLAGEV-EMTQIAILPSHQGLGLASQLMTHLDSIE-----SDIFLEVRESNHRAQGLYQKFGF 113
Cdd:COG0454   36 FIAVDDKGEPIGFAGLRRLDDKVlELKRLYVLPEYRGKGIGKALLEALLEWArergcTALELDTLDGNPAAIRFYERLGF 115

                         90
                 ....*....|....*...
gi 489082356 114 KFIGKRPDYYRNPIETAL 131
Cdd:COG0454  116 KEIERYVAYVGGEFEKEL 133
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 36-114 1.24e-12

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 59.39  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356   36 DQTDYFLLYDHDKLLGFLAIQDLAGEVEMT--QIAILPSHQGLGLASQLMTHLDSI--ESDIFLEVRESNHRAQGLYQKF 111
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIGRALLEAAEAAakEGGIKLLELETTNRAAAFYEKL 80


                  ...
gi 489082356  112 GFK 114
Cdd:pfam13508  81 GFE 83
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 32-118 8.12e-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: 58.46  E-value: 8.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356  32 DIRRDQTDYFLLYDHDKLLGFLAIQDLAGEV-EMTQIAILPSHQGLGLASQLMTHLdsIE-------SDIFLevrESNHR 103
Cdd:COG1246   22 ALEEEIGEFWVAEEDGEIVGCAALHPLDEDLaELRSLAVHPDYRGRGIGRRLLEAL--LAearelglKRLFL---LTTSA 96

                         90
                 ....*....|....*
gi 489082356 104 AQGLYQKFGFKFIGK 118
Cdd:COG1246   97 AIHFYEKLGFEEIDK 111
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
18-124 1.92e-10

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 55.39  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356  18 VYGTSPWTLEQV---LIDIRRDQTDYFLLYDHDKLLGFLAIQD------LAGEVEmTQIAILPSHQGLGLASQLMTHLds 88
Cdd:COG1247   29 TFETEPPSEEEReawFAAILAPGRPVLVAEEDGEVVGFASLGPfrprpaYRGTAE-ESIYVDPDARGRGIGRALLEAL-- 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489082356  89 IE-------SDIFLEVRESNHRAQGLYQKFGFKFIGKRPDYYR 124
Cdd:COG1247  106 IErarargyRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGF 148
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
57-117 7.49e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.22  E-value: 7.49e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489082356  57 DLAGEVEMTQIAILPSHQGLGLASQLMTHL-----DSIESDIFLEVRESNHRAQGLYQKFGFKFIG 117
Cdd:COG3393   11 ESPGVAEISGVYTHPEYRGRGLASALVAALarealARGARTPFLYVDADNPAARRLYERLGFRPVG 76
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 19-124 1.52e-09

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: 53.08  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356  19 YGTSPWTLEQVLIDIRRDQTDY---------FLLYDHDKLLGFLAIQDL---AGEVEMtQIAILPSHQGLGLASQLMTHL 86
Cdd:COG1670   34 LPGPPYSLEEARAWLERLLADWadggalpfaIEDKEDGELIGVVGLYDIdraNRSAEI-GYWLAPAYWGKGYATEALRAL 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489082356  87 dsIE--------SDIFLEVRESNHRAQGLYQKFGFKFIGKRPDYYR 124
Cdd:COG1670  113 --LDyafeelglHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
31-117 3.81e-09

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 51.34  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356  31 IDIRRDQTDYFLLYDHDKLLGFLAI-QDLAGEVEMTQIAILPSHQGLGLASQLMTHLDSI-----ESDIFLEVRESnhrA 104
Cdd:COG2153   27 LDGKDEDARHLLAYDDGELVATARLlPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEarergARRIVLSAQAH---A 103

                         90
                 ....*....|...
gi 489082356 105 QGLYQKFGFKFIG 117
Cdd:COG2153  104 VGFYEKLGFVPVG 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-119 7.38e-08

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.16  E-value: 7.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356   5 EEQAKNIYQLLEMVYGTSPWtlEQVLIDIRRDQTDYFLL--YDHDKLLGFLAIQ--DLAGEVEMTQI---AILPSHQGLG 77
Cdd:COG3153    6 PEDAEAIAALLRAAFGPGRE--AELVDRLREDPAAGLSLvaEDDGEIVGHVALSpvDIDGEGPALLLgplAVDPEYRGQG 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489082356  78 LASQLMTH-LDSIESDIFLEVR-ESNHRAQGLYQKFGFKFIGKR 119
Cdd:COG3153   84 IGRALMRAaLEAARERGARAVVlLGDPSLLPFYERFGFRPAGEL 127
PRK10514 PRK10514
putative acetyltransferase; Provisional
 45-120 2.92e-07

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 46.53  E-value: 2.92e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489082356  45 DHDKLLGFLAIQDlageVEMTQIAILPSHQGLGLASQLMTHLDSIESDIFLEVRESNHRAQGLYQKFGFKFIGKRP 120
Cdd:PRK10514  57 ERDQPVGFMLLSG----GHMEALFVDPDVRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGRSE 128
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 36-128 4.63e-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: 4.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356   36 DQTDYFLL--YDHDKLLGFLAIQDlAGEVEMtqIAILPSHQGLGLASQLMTHL-DSIESD----IFLEVRESNHrAQGLY 108
Cdd:pfam13673  27 DQGEYFFFvaFEGGQIVGVIALRD-RGHISL--LFVDPDYQGQGIGKALLEAVeDYAEKDgiklSELTVNASPY-AVPFY 102

                          90       100
                  ....*....|....*....|
gi 489082356  109 QKFGFKFIGkrPDYYRNPIE 128
Cdd:pfam13673 103 EKLGFRATG--PEQEFNGIR 120
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 40-86 5.50e-06

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: 41.49  E-value: 5.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489082356  40 YFLLYDHDKLLGFLAI---QDLAGEVEMTQIAILPSHQGLGLASQLMTHL 86
Cdd:cd04301    1 FLVAEDDGEIVGFASLspdGSGGDTAYIGDLAVLPEYRGKGIGSALLEAA 50
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 63-119 2.29e-05

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: 40.39  E-value: 2.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489082356   63 EMTQIAILPSHQGLGLASQLMT----HLDSIESDIFLEVRESNHRAQGLYQKFGFKFIGKR 119
Cdd:pfam08445  23 ELGALQTLPEHRRRGLGSRLVAalarGIAERGITPFAVVVAGNTPSRRLYEKLGFRKIDET 83
Eis COG4552
Predicted acetyltransferase [General function prediction only];
5-113 5.64e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 41.42  E-value: 5.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489082356   5 EEQAKNIYQLLEMVYGtSPWTLEQVLIDIRR-DQTDYFLLYDHDKLLGFLAIQDL-----AGEVEM---TQIAILPSHQG 75
Cdd:COG4552    8 EDDLDAFARLLAYAFG-PEPDDEELEAYRPLlEPGRVLGVFDDGELVGTLALYPFtlnvgGARVPMagiTGVAVAPEHRR 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489082356  76 LGLASQLMTHLdsiesdiFLEVRESNHR-------AQGLYQKFGF 113
Cdd:COG4552   87 RGVARALLREA-------LAELRERGQPlsalypfEPGFYRRFGY 124
PRK03624 PRK03624
putative acetyltransferase; Provisional
 68-113 9.20e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 37.22  E-value: 9.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489082356  68 AILPSHQGLGLASQLMTHLDS--IE---SDIFLEVRESNHRAQGLYQKFGF 113
Cdd:PRK03624  75 AVHPDFRGRGIGRALVARLEKklIArgcPKINLQVREDNDAVLGFYEALGY 125
 
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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