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Conserved domains on  [gi|495777499|ref|WP_008502078|]
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MULTISPECIES: ribosomal protein S18-alanine N-acetyltransferase [Enterobacter]

Protein Classification

ribosomal-protein-alanine N-acetyltransferase( domain architecture ID 10013255)

ribosomal-protein-alanine N-acetyltransferase acetylates the N-terminal alanine of ribosomal protein S18; similar to Escherichia coli K-12 RimI

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 1-146 3.93e-110

ribosomal-protein-alanine N-acetyltransferase; Provisional


:

Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 308.78  E-value: 3.93e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499   1 MNTISSLTTPDLSTAFAIETRAHAFPWSEKTFASNQGERYLNYRLDVDGTMAAFAITQVVLDEATLFNIAVDPAFQRRGL 80
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495777499  81 GRELLEHLIRELETRDVFTLWLEVRASNVAAIALYESLGFNEATIRRNYYPTAEGREDAIIMALPI 146
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAIIMALPL 146
 
Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 1-146 3.93e-110

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 308.78  E-value: 3.93e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499   1 MNTISSLTTPDLSTAFAIETRAHAFPWSEKTFASNQGERYLNYRLDVDGTMAAFAITQVVLDEATLFNIAVDPAFQRRGL 80
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495777499  81 GRELLEHLIRELETRDVFTLWLEVRASNVAAIALYESLGFNEATIRRNYYPTAEGREDAIIMALPI 146
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAIIMALPL 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 11-142 7.13e-61

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: 183.68  E-value: 7.13e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499   11 DLSTAFAIETRAHAFPWSEKTFASNQGERYLNYRL-DVDGTMAAFAITQVVLDEATLFNIAVDPAFQRRGLGRELLEHLI 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLaRIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 495777499   90 RELETRDVFTLWLEVRASNVAAIALYESLGFNEATIRRNYYPTaeGREDAIIM 142
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPD--PGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 62-146 1.30e-25

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 93.18  E-value: 1.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499  62 DEATLFNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRASNVAAIALYESLGFNEATIRRNYYPtaegrEDAII 141
Cdd:COG0456   12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYG-----DDALV 86


                 ....*
gi 495777499 142 MALPI 146
Cdd:COG0456   87 MEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 11-120 4.93e-17

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: 71.78  E-value: 4.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499   11 DLSTAFAIETRAHAFPWSEKTFASNQGERYLNYRLDvdGT---MAAFAITQVVLDEATLFNIAVDPAFQRRGLGRELLEH 87
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEED--GElvgFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQA 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 495777499   88 LIRELETRDVFTLWLEVRASNVAAIALYESLGF 120
Cdd:pfam00583  84 LLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-103 5.67e-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: 5.67e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495777499  51 MAAFAITQVVLDEATLFNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLE 103
Cdd:cd04301   13 FASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 1-146 3.93e-110

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 308.78  E-value: 3.93e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499   1 MNTISSLTTPDLSTAFAIETRAHAFPWSEKTFASNQGERYLNYRLDVDGTMAAFAITQVVLDEATLFNIAVDPAFQRRGL 80
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495777499  81 GRELLEHLIRELETRDVFTLWLEVRASNVAAIALYESLGFNEATIRRNYYPTAEGREDAIIMALPI 146
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAIIMALPL 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 11-142 7.13e-61

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: 183.68  E-value: 7.13e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499   11 DLSTAFAIETRAHAFPWSEKTFASNQGERYLNYRL-DVDGTMAAFAITQVVLDEATLFNIAVDPAFQRRGLGRELLEHLI 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLaRIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 495777499   90 RELETRDVFTLWLEVRASNVAAIALYESLGFNEATIRRNYYPTaeGREDAIIM 142
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPD--PGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 62-146 1.30e-25

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 93.18  E-value: 1.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499  62 DEATLFNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRASNVAAIALYESLGFNEATIRRNYYPtaegrEDAII 141
Cdd:COG0456   12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYG-----DDALV 86


                 ....*
gi 495777499 142 MALPI 146
Cdd:COG0456   87 MEKEL 91
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
32-146 9.20e-18

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 75.03  E-value: 9.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499  32 FASNQGERYLNYRLDVDGTMAAFAI-----TQVVLDEATLFNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRA 106
Cdd:COG1247   44 FAAILAPGRPVLVAEEDGEVVGFASlgpfrPRPAYRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLA 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495777499 107 SNVAAIALYESLGFNEATIRRNYYPTAEGREDAIIMALPI 146
Cdd:COG1247  124 DNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 11-120 4.93e-17

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: 71.78  E-value: 4.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499   11 DLSTAFAIETRAHAFPWSEKTFASNQGERYLNYRLDvdGT---MAAFAITQVVLDEATLFNIAVDPAFQRRGLGRELLEH 87
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEED--GElvgFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQA 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 495777499   88 LIRELETRDVFTLWLEVRASNVAAIALYESLGF 120
Cdd:pfam00583  84 LLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 45-122 2.95e-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: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499  45 LDVDGTMAAFAITQVvLDEATLF--NIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRASNVAAIALYESLGFNE 122
Cdd:COG0454   39 VDDKGEPIGFAGLRR-LDDKVLElkRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
64-120 2.29e-13

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 61.46  E-value: 2.29e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495777499  64 ATLFNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRASNVAAIALYESLGF 120
Cdd:COG3393   16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGF 72
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-122 5.58e-13

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 60.55  E-value: 5.58e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495777499   48 DGTMAAFAITQVVLDEATLF--NIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRasnVAAIALYESLGFNE 122
Cdd:pfam13508  11 DGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETT---NRAAAFYEKLGFEE 84
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 69-144 6.17e-13

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: 62.32  E-value: 6.17e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495777499  69 IAVDPAFQRRGLGRELLEHLIREL-ETRDVFTLWLEVRASNVAAIALYESLGFNEATIRRNYYPTAEGREDAIIMAL 144
Cdd:COG1670   93 YWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVLYSL 169
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 46-146 9.24e-13

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: 61.16  E-value: 9.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499  46 DVDGTMAAF-AITQVVLDEATLFNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEvraSNVAAIALYESLGFNEAT 124
Cdd:COG1246   34 EEDGEIVGCaALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL---TTSAAIHFYEKLGFEEID 110

                         90       100
                 ....*....|....*....|..
gi 495777499 125 IRRNYYPTAEGReDAIIMALPI 146
Cdd:COG1246  111 KEDLPYAKVWQR-DSVVMEKDL 131
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
48-120 1.94e-11

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 57.50  E-value: 1.94e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777499  48 DGTMAAFA-ITQVVLDEATLFNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRASnvaAIALYESLGF 120
Cdd:COG2153   42 DGELVATArLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGF 112
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-146 8.68e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 56.25  E-value: 8.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499   4 ISSLTTPDLSTAFAIETRAHAFPWSEKTFAS--NQGERYLNYRLDVDGTMAAFAITQVV-----LDEATLFNIAVDPAFQ 76
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELVDRlrEDPAAGLSLVAEDDGEIVGHVALSPVdidgeGPALLLGPLAVDPEYR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499  77 RRGLGRELLEHLIRELETRDVFTLWLEvraSNVAAIALYESLGFNEATIRRNYYPtaegrEDAIIMALPI 146
Cdd:COG3153   81 GQGIGRALMRAALEAARERGARAVVLL---GDPSLLPFYERFGFRPAGELGLTLG-----PDEVFLAKEL 142
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 69-120 1.63e-10

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: 54.97  E-value: 1.63e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 495777499   69 IAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRASNvAAIALYESLGF 120
Cdd:pfam13673  57 LFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASP-YAVPFYEKLGF 107
PRK03624 PRK03624
putative acetyltransferase; Provisional
 66-122 7.52e-10

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 53.78  E-value: 7.52e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495777499  66 LFNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRASNVAAIALYESLGFNE 122
Cdd:PRK03624  71 AYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEE 127
mycothiol_MshD TIGR03448
mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the ...
 46-120 2.43e-09

mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 132489 [Multi-domain]  Cd Length: 292  Bit Score: 53.94  E-value: 2.43e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495777499   46 DVDGTMAAFAITQVVLDEATL---FNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRASNVAAIALYESLGF 120
Cdd:TIGR03448 206 DAPGELLGFHWTKVHPDEPALgevYVVGVDPAAQGRGLGDALTLIGLHHLAARGLPAVMLYVEADNEAAVRTYEKLGF 283
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-103 5.67e-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: 5.67e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495777499  51 MAAFAITQVVLDEATLFNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLE 103
Cdd:cd04301   13 FASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 49-127 1.61e-08

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: 48.87  E-value: 1.61e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495777499   49 GTMAAFAITqvvLDEATLFNIAVDPAFQRRGLGRELLEHLIRELETRDVfTLWLEVRASNVAAIALYESLGFNEATIRR 127
Cdd:pfam08445  10 GELAAWCLR---LPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGI-TPFAVVVAGNTPSRRLYEKLGFRKIDETY 84
PRK07757 PRK07757
N-acetyltransferase;
70-131 2.55e-07

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 47.11  E-value: 2.55e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495777499  70 AVDPAFQRRGLGRELLEHLI---RELETRDVFTLWLEVRasnvaaiaLYESLGFNEatIRRNYYP 131
Cdd:PRK07757  72 AVSEDYRGQGIGRMLVEACLeeaRELGVKRVFALTYQPE--------FFEKLGFRE--VDKEALP 126
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
45-124 4.11e-05

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 41.45  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499  45 LDVDGTMAAFaITQVVLD--EATLFNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRASNVAAIALYESLGFN- 121
Cdd:PRK10975 107 RDASGQIQGF-VTLRELNdtDARIGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGANi 185


                 ...
gi 495777499 122 EAT 124
Cdd:PRK10975 186 EST 188
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 45-122 1.17e-04

Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.


Pssm-ID: 173920 [Multi-domain]  Cd Length: 297  Bit Score: 40.71  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499  45 LDVDGTMAAFAI-TQVV----LDEATLFNIAVDPAFQRRGLGRELLEHLIRELETRDVFTLWLEVRASNVaaiALYESLG 119
Cdd:cd02169    2 LSLDYTVGIFDDaGELIatgsIAGNVLKCVAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTKPKNA---KFFRGLG 78


                 ...
gi 495777499 120 FNE 122
Cdd:cd02169   79 FKE 81
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 69-97 1.36e-04

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 40.58  E-value: 1.36e-04
                         10        20
                 ....*....|....*....|....*....
gi 495777499  69 IAVDPAFQRRGLGRELLEHLIRELETRDV 97
Cdd:COG1444  491 IAVHPALQRRGLGSRLLAEIREEAKEEGL 519
PRK07922 PRK07922
amino-acid N-acetyltransferase;
69-104 4.52e-04

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 38.36  E-value: 4.52e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 495777499  69 IAVDPAFQRRGLGRELLEHLI---RELETRDVFTLWLEV 104
Cdd:PRK07922  76 VAVDPAARGRGVGHAIVERLLdvaRELGLSRVFVLTFEV 114
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 69-120 6.62e-04

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


Pssm-ID: 403833  Cd Length: 239  Bit Score: 38.41  E-value: 6.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 495777499   69 IAVDPAFQRRGLGRELLEHLIRELETRDVFTLWlevRASNVAAIALYESLGF 120
Cdd:pfam12746 182 IDTHPDYRGKGLATICAAALILECLKRGLYPSW---DAHNEASVALAEKLGY 230
PRK10514 PRK10514
putative acetyltransferase; Provisional
 16-121 7.22e-04

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 37.67  E-value: 7.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777499  16 FAIETRAHAF-PWSEKTFASNQGERYLNYRLDVDGTMAAfaitqvvldeatLFniaVDPAFQRRGLGRELLEH---LIRE 91
Cdd:PRK10514  36 AEIEELVRSFlPEAPLWVAVDERDQPVGFMLLSGGHMEA------------LF---VDPDVRGCGVGRMLVEHalsLHPE 100

                         90       100       110
                 ....*....|....*....|....*....|
gi 495777499  92 LETrdvftlwlEVRASNVAAIALYESLGFN 121
Cdd:PRK10514 101 LTT--------DVNEQNEQAVGFYKKMGFK 122
PRK10562 PRK10562
putative acetyltransferase; Provisional
 48-120 1.38e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 36.58  E-value: 1.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495777499  48 DGTMAAFAitqVVLDEATLFNIAVDPAFQRRGLGRELLEHLIRELEtrdvfTLWLEVRASNVAAIALYESLGF 120
Cdd:PRK10562  56 DGKLLGFV---SVLEGRFVGALFVAPKAVRRGIGKALMQHVQQRYP-----HLSLEVYQKNQRAVNFYHAQGF 120
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
43-96 2.92e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 34.75  E-value: 2.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495777499  43 YRLDVDGTMAAFAITQVVLDEATLFNIAVDPAFQRRGLGRELLEHLIRELETRD 96
Cdd:COG2388   12 FELEVDGELAGELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERG 65
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 75-129 5.66e-03

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: 35.03  E-value: 5.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 495777499   75 FQRRGLGRELLEHLIR-ELETRDVFTLWLEVRASNVAAIALYESLGFNEATIRRNY 129
Cdd:TIGR03585  87 FCKPGVGSVLEEAALEyAFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQG 142
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
78-130 9.27e-03

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 34.65  E-value: 9.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 495777499   78 RGLGRELLEHLIRELETR-DVFTLWLEVRASNVAAIALYESLGFNEATIRRNYY 130
Cdd:pfam13420  89 EGINRELINAIIQYARKNqNIENLEACIASNNINAIVFLKAIGFEWLGIERNAI 142
 
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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