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Conserved domains on  [gi|500141444|ref|WP_011817447|]
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N-acetyltransferase [Yersinia enterocolitica]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10793418)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-151 2.59e-87

putative acetyltransferase; Provisional


:

Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 251.14  E-value: 2.59e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   1 MIRAYQPDDLDAVMQLWLTSTIAAHPFIAEQYWHESAPLVRNNYLPAARTWVYLHSKTIRdespiaGFISILAEQLVGAL 80
Cdd:PRK10562   1 MIREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVYLPAAQTWVWEEDGKLL------GFVSVLEGRFVGAL 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500141444  81 FVAQPFHGQGIGKALMEYVQQHYRALTLEVYQQNQRACHFYRKQGFTQIGKAYNAETKSTILTLHWQRPFN 151
Cdd:PRK10562  75 FVAPKAVRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQADQT 145
 
Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-151 2.59e-87

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 251.14  E-value: 2.59e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   1 MIRAYQPDDLDAVMQLWLTSTIAAHPFIAEQYWHESAPLVRNNYLPAARTWVYLHSKTIRdespiaGFISILAEQLVGAL 80
Cdd:PRK10562   1 MIREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVYLPAAQTWVWEEDGKLL------GFVSVLEGRFVGAL 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500141444  81 FVAQPFHGQGIGKALMEYVQQHYRALTLEVYQQNQRACHFYRKQGFTQIGKAYNAETKSTILTLHWQRPFN 151
Cdd:PRK10562  75 FVAPKAVRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQADQT 145
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 77-134 1.89e-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: 1.89e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500141444  77 VGALFVAQPFHGQGIGKALMEYVQQHYRA-----LTLEVYQQNQRACHFYRKQGFTQIGKAYN 134
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERARErgarrLRLEVREDNEAAIALYEKLGFEEVGERPN 78
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 10-126 1.41e-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: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   10 LDAVMQLWLTSTIAAHPFIAEQYWHESAPLvrnnylPAARTWVYLHSKTIrdespiAGFISILAEQL------VGALFVA 83
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDED------ASEGFFVAEEDGEL------VGFASLSIIDDeppvgeIEGLAVA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 500141444   84 QPFHGQGIGKALMEYVQQH-----YRALTLEVYQQNQRACHFYRKQGF 126
Cdd:pfam00583  69 PEYRGKGIGTALLQALLEWarergCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 53-133 1.98e-06

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: 44.24  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   53 YLHSKTIRDESPIAGFIS---ILAEQLVGALFVAQPFHGQGIGKALMEYVQQHY-----RALTLEVYQQNQRACHFYRKQ 124
Cdd:TIGR01575  30 HLCYLLARIGGKVVGYAGvqiVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAkgrgvNEIFLEVRVSNIAAQALYKKL 109

                          90
                  ....*....|.
gi 500141444  125 GFTQIG--KAY 133
Cdd:TIGR01575 110 GFNEIAirRNY 120
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-106 4.18e-05

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: 39.18  E-value: 4.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500141444  59 IRDESPIAGFISILAEQL------VGALFVAQPFHGQGIGKALMEYVQQHYRAL 106
Cdd:cd04301    4 AEDDGEIVGFASLSPDGSggdtayIGDLAVLPEYRGKGIGSALLEAAEEEARER 57
 
Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-151 2.59e-87

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 251.14  E-value: 2.59e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   1 MIRAYQPDDLDAVMQLWLTSTIAAHPFIAEQYWHESAPLVRNNYLPAARTWVYLHSKTIRdespiaGFISILAEQLVGAL 80
Cdd:PRK10562   1 MIREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVYLPAAQTWVWEEDGKLL------GFVSVLEGRFVGAL 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500141444  81 FVAQPFHGQGIGKALMEYVQQHYRALTLEVYQQNQRACHFYRKQGFTQIGKAYNAETKSTILTLHWQRPFN 151
Cdd:PRK10562  75 FVAPKAVRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQADQT 145
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-131 7.65e-20

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 80.05  E-value: 7.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   2 IRAYQPDDLDAVMQLWLTSTIAAHPFIAEQYWHESAPLVRNnYLPAARTWVylhSKTIRDEsPIaGFIsILAEQLVGALF 81
Cdd:PRK10514   4 IRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRS-FLPEAPLWV---AVDERDQ-PV-GFM-LLSGGHMEALF 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 500141444  82 VAQPFHGQGIGKALMEYVQQHYRALTLEVYQQNQRACHFYRKQGFTQIGK 131
Cdd:PRK10514  77 VDPDVRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTGR 126
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 77-134 1.89e-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: 1.89e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500141444  77 VGALFVAQPFHGQGIGKALMEYVQQHYRA-----LTLEVYQQNQRACHFYRKQGFTQIGKAYN 134
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERARErgarrLRLEVREDNEAAIALYEKLGFEEVGERPN 78
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-130 4.26e-14

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 65.40  E-value: 4.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   1 MIRAYQPDDLDAVMQLW---LTSTIAAHPFIAEQYWHESApLVRNNYLPAARTWVylhsktIRDESPIAGFISI------ 71
Cdd:COG1247    3 TIRPATPEDAPAIAAIYneaIAEGTATFETEPPSEEEREA-WFAAILAPGRPVLV------AEEDGEVVGFASLgpfrpr 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500141444  72 LAEQLVG--ALFVAQPFHGQGIGKALMEYV-----QQHYRALTLEVYQQNQRACHFYRKQGFTQIG 130
Cdd:COG1247   76 PAYRGTAeeSIYVDPDARGRGIGRALLEALierarARGYRRLVAVVLADNEASIALYEKLGFEEVG 141
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-138 1.31e-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: 60.78  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   1 MIRAYQPDDLDAVMQLWLTSTIaahpfiaeqywhesaplvrnnYLPAARTWVylhsktIRDESPIAGFISI------LAE 74
Cdd:COG1246    2 TIRPATPDDVPAILELIRPYAL---------------------EEEIGEFWV------AEEDGEIVGCAALhpldedLAE 54

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500141444  75 qlVGALFVAQPFHGQGIGKALMEYV-----QQHYRALTLEVYqqnQRACHFYRKQGFTQIGKAYNAETK 138
Cdd:COG1246   55 --LRSLAVHPDYRGRGIGRRLLEALlaearELGLKRLFLLTT---SAAIHFYEKLGFEEIDKEDLPYAK 118
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 10-126 1.41e-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: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   10 LDAVMQLWLTSTIAAHPFIAEQYWHESAPLvrnnylPAARTWVYLHSKTIrdespiAGFISILAEQL------VGALFVA 83
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDED------ASEGFFVAEEDGEL------VGFASLSIIDDeppvgeIEGLAVA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 500141444   84 QPFHGQGIGKALMEYVQQH-----YRALTLEVYQQNQRACHFYRKQGF 126
Cdd:pfam00583  69 PEYRGKGIGTALLQALLEWarergCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-132 3.15e-11

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 57.40  E-value: 3.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   2 IRAYQPDDLDAVMQLWLtstiAAHPfiaEQYWHESAPLVRNNyLPAARTWVylhsktIRDESPIAGFISILAEQL----- 76
Cdd:COG3153    1 IRPATPEDAEAIAALLR----AAFG---PGREAELVDRLRED-PAAGLSLV------AEDDGEIVGHVALSPVDIdgegp 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500141444  77 ---VGALFVAQPFHGQGIGKALMEYV-----QQHYRALTLEVyqqNQRACHFYRKQGFTQIGKA 132
Cdd:COG3153   67 allLGPLAVDPEYRGQGIGRALMRAAleaarERGARAVVLLG---DPSLLPFYERFGFRPAGEL 127
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 46-128 3.83e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.92  E-value: 3.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   46 PAARTWVylhsktIRDESPIAGFISIL-----AEQLVGALFVAQPFHGQGIGKALMEYVQQHYRALTLEVYQ--QNQRAC 118
Cdd:pfam13508   1 PGGRFFV------AEDDGKIVGFAALLplddeGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEleTTNRAA 74

                          90
                  ....*....|
gi 500141444  119 HFYRKQGFTQ 128
Cdd:pfam13508  75 AFYEKLGFEE 84
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 60-130 1.71e-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: 1.71e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500141444   60 RDESPIAGFISILAEQLVGALFVAQPFHGQGIGKALMEYV-----QQHYRALTLEVYQQNQrACHFYRKQGFTQIG 130
Cdd:pfam13673  37 FEGGQIVGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVedyaeKDGIKLSELTVNASPY-AVPFYEKLGFRATG 111
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 77-130 5.77e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 53.90  E-value: 5.77e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 500141444  77 VGALFVAQPFHGQGIGKALMEYV-----QQHYRALTLEVYQQNQRACHFYRKQGFTQIG 130
Cdd:COG0454   61 LKRLYVLPEYRGKGIGKALLEALlewarERGCTALELDTLDGNPAAIRFYERLGFKEIE 119
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-130 5.42e-07

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: 46.53  E-value: 5.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   2 IRAYQPDDLDAVMQLW----LTSTIAAHPFIAEQYWHESAPLVRNNYLPAARTWVYLHsktiRDESPIAGFISILAEQLV 77
Cdd:COG1670   10 LRPLRPEDAEALAELLndpeVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIED----KEDGELIGVVGLYDIDRA 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500141444  78 G-----ALFVAQPFHGQGIG----KALMEYVQQH--YRALTLEVYQQNQRACHFYRKQGFTQIG 130
Cdd:COG1670   86 NrsaeiGYWLAPAYWGKGYAtealRALLDYAFEElgLHRVEAEVDPDNTASIRVLEKLGFRLEG 149
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
77-130 1.50e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 43.74  E-value: 1.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 500141444  77 VGALFVAQPFHGQGIGKALMEYV-----QQHYRALTLEVYQQNQRACHFYRKQGFTQIG 130
Cdd:COG3393   18 ISGVYTHPEYRGRGLASALVAALarealARGARTPFLYVDADNPAARRLYERLGFRPVG 76
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 53-133 1.98e-06

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: 44.24  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444   53 YLHSKTIRDESPIAGFIS---ILAEQLVGALFVAQPFHGQGIGKALMEYVQQHY-----RALTLEVYQQNQRACHFYRKQ 124
Cdd:TIGR01575  30 HLCYLLARIGGKVVGYAGvqiVLDEAHILNIAVKPEYQGQGIGRALLRELIDEAkgrgvNEIFLEVRVSNIAAQALYKKL 109

                          90
                  ....*....|.
gi 500141444  125 GFTQIG--KAY 133
Cdd:TIGR01575 110 GFNEIAirRNY 120
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
77-133 1.15e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 42.48  E-value: 1.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500141444  77 VGALFVAQPFHGQGIGKALMEYV-----QQHYRALTLEVyQqnQRACHFYRKQGFTQIGKAY 133
Cdd:COG2153   61 IGRVAVLPEYRGQGLGRALMEAAieearERGARRIVLSA-Q--AHAVGFYEKLGFVPVGEEF 119
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-106 4.18e-05

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: 39.18  E-value: 4.18e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 500141444  59 IRDESPIAGFISILAEQL------VGALFVAQPFHGQGIGKALMEYVQQHYRAL 106
Cdd:cd04301    4 AEDDGEIVGFASLSPDGSggdtayIGDLAVLPEYRGKGIGSALLEAAEEEARER 57
PRK07757 PRK07757
N-acetyltransferase;
58-133 7.32e-05

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 40.56  E-value: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444  58 TIRD------ESPIAGF--ISILAEQL--VGALFVAQPFHGQGIGKALMEYVQQHYRALTL-EV----YQQNqrachFYR 122
Cdd:PRK07757  39 NIRDfyvaeeEGEIVGCcaLHILWEDLaeIRSLAVSEDYRGQGIGRMLVEACLEEARELGVkRVfaltYQPE-----FFE 113

                         90
                 ....*....|.
gi 500141444 123 KQGFTQIGKAY 133
Cdd:PRK07757 114 KLGFREVDKEA 124
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 2-127 7.92e-03

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 34.63  E-value: 7.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500141444    2 IRAYQPDDLDAVMQLW----LTSTIAAHPFIAEQYWHESAPLVRNNYLPAARTWVylhskTIRDESPIAGFISILAEQLV 77
Cdd:pfam13302   4 LRPLTEEDAEALFELLsdpeVMRYGVPWPLTLEEAREWLARIWAADEAERGYGWA-----IELKDTGFIGSIGLYDIDGE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500141444   78 GALF-----VAQPFHGQGIG----KALMEYVQQHYRALTLE--VYQQNQRACHFYRKQGFT 127
Cdd:pfam13302  79 PERAelgywLGPDYWGKGYAteavRALLEYAFEELGLPRLVarIDPENTASRRVLEKLGFK 139
 
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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