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Conserved domains on  [gi|656016165|ref|WP_029056074|]
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MULTISPECIES: ribosomal protein S18-alanine N-acetyltransferase [Staphylococcus]

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 ...
 18-148 5.61e-32

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: 110.88  E-value: 5.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165   18 DVPSVFDIERNSFNdSSWTIDAFYHEIeKNEFANYFVIEFDNTIIGYLGLWIVIDQAQITTIAITEKFRGYGLGQLLLKY 97
Cdd:TIGR01575   1 DLKAVLEIEAAAFA-FPWTEAQFAEEL-ANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 656016165   98 VMNYA-SHKCEMMSLEVRIDNIVAQHVYQNLGFQYGGKRKNYYGEGQ-DALVM 148
Cdd:TIGR01575  79 LIDEAkGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAIVM 131
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 18-148 5.61e-32

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: 110.88  E-value: 5.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165   18 DVPSVFDIERNSFNdSSWTIDAFYHEIeKNEFANYFVIEFDNTIIGYLGLWIVIDQAQITTIAITEKFRGYGLGQLLLKY 97
Cdd:TIGR01575   1 DLKAVLEIEAAAFA-FPWTEAQFAEEL-ANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 656016165   98 VMNYA-SHKCEMMSLEVRIDNIVAQHVYQNLGFQYGGKRKNYYGEGQ-DALVM 148
Cdd:TIGR01575  79 LIDEAkGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-153 1.43e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 77.77  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  63 GYLGLWIVIDQ--AQITTIAITEKFRGYGLGQLLLKYVMNYA-SHKCEMMSLEVRIDNIVAQHVYQNLGFQYGGKRKNYY 139
Cdd:COG0456    1 GFALLGLVDGGdeAEIEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....
gi 656016165 140 GEgqDALVMWVNLS 153
Cdd:COG0456   81 GD--DALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 19-129 5.10e-16

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: 69.47  E-value: 5.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165   19 VPSVFDIERNSFNDSsWTIDAFYHEIEKNEFAN--YFVIEFDNTIIGYLGLWIV---IDQAQITTIAITEKFRGYGLGQL 93
Cdd:pfam00583   1 LEALYELLSEEFPEP-WPDEPLDLLEDWDEDASegFFVAEEDGELVGFASLSIIddePPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 656016165   94 LLKYVMNYA-SHKCEMMSLEVRIDNIVAQHVYQNLGF 129
Cdd:pfam00583  80 LLQALLEWArERGCERIFLEVAADNLAAIALYEKLGF 116
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 10-148 3.47e-13

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 62.64  E-value: 3.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  10 NIRKMSIDDVPSVFDIERNS--FndsSWTIDAFYheieKNEFANY--FVIEFDNTIIGYLGLWIVIDQAQITTIAITEKF 85
Cdd:PRK09491   3 TISSLTPADLPAAYHIEQRAhaF---PWSEKTFA----SNQGERYlnLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDY 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 656016165  86 RGYGLGQLLLKYVMNYASHKCEM-MSLEVRIDNIVAQHVYQNLGFQYGGKRKNYY--GEG-QDALVM 148
Cdd:PRK09491  76 QRQGLGRALLEHLIDELEKRGVAtLWLEVRASNAAAIALYESLGFNEVTIRRNYYptADGrEDAIIM 142
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-112 1.01e-08

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: 48.81  E-value: 1.01e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 656016165  52 YFVIEFDNTIIGYLGLWI---VIDQAQITTIAITEKFRGYGLGQLLLKYVMNYA-SHKCEMMSLE 112
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEArERGAKRLRLE 65
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
11-95 1.32e-03

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 36.44  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  11 IRKMSIDDVPSVFDIERNSFNdssWTidafYHEIEKNEFANYFVIE--------------------------FDNTIIGY 64
Cdd:NF041158   4 IRKLSAEDVDALIEVARESWK---WT----YRDIYSNEFIESWISEkyskekllneiirsqsnldiiflgafVNSALIGF 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 656016165  65 LGLWIVIDQAQITTIAITEKFRGYGLGQLLL 95
Cdd:NF041158  77 IELKIIADKAELLRLYLKPEYTHRGIGKLLL 107
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 18-148 5.61e-32

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: 110.88  E-value: 5.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165   18 DVPSVFDIERNSFNdSSWTIDAFYHEIeKNEFANYFVIEFDNTIIGYLGLWIVIDQAQITTIAITEKFRGYGLGQLLLKY 97
Cdd:TIGR01575   1 DLKAVLEIEAAAFA-FPWTEAQFAEEL-ANYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 656016165   98 VMNYA-SHKCEMMSLEVRIDNIVAQHVYQNLGFQYGGKRKNYYGEGQ-DALVM 148
Cdd:TIGR01575  79 LIDEAkGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGeDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-153 1.43e-19

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 77.77  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  63 GYLGLWIVIDQ--AQITTIAITEKFRGYGLGQLLLKYVMNYA-SHKCEMMSLEVRIDNIVAQHVYQNLGFQYGGKRKNYY 139
Cdd:COG0456    1 GFALLGLVDGGdeAEIEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....
gi 656016165 140 GEgqDALVMWVNLS 153
Cdd:COG0456   81 GD--DALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 19-129 5.10e-16

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: 69.47  E-value: 5.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165   19 VPSVFDIERNSFNDSsWTIDAFYHEIEKNEFAN--YFVIEFDNTIIGYLGLWIV---IDQAQITTIAITEKFRGYGLGQL 93
Cdd:pfam00583   1 LEALYELLSEEFPEP-WPDEPLDLLEDWDEDASegFFVAEEDGELVGFASLSIIddePPVGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 656016165   94 LLKYVMNYA-SHKCEMMSLEVRIDNIVAQHVYQNLGF 129
Cdd:pfam00583  80 LLQALLEWArERGCERIFLEVAADNLAAIALYEKLGF 116
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 7-148 4.90e-15

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: 68.10  E-value: 4.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165   7 EQLNIRKMSIDDVPSVFDIERN------------SFNDSSWTIDAFYHEIEKNEFANYFVIE-FDNTIIGYLGLWIVIDQ 73
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDpevarylpgppySLEEARAWLERLLADWADGGALPFAIEDkEDGELIGVVGLYDIDRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  74 AQITTIAIT--EKFRGYGLGQLLLKYVMNYA--SHKCEMMSLEVRIDNIVAQHVYQNLGFQYGGKRKNYY---GEGQDAL 146
Cdd:COG1670   86 NRSAEIGYWlaPAYWGKGYATEALRALLDYAfeELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALvidGRYRDHV 165


                 ..
gi 656016165 147 VM 148
Cdd:COG1670  166 LY 167
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
9-152 1.57e-14

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 66.56  E-value: 1.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165   9 LNIRKMSIDDVPSVFDIERNSFNDSSWT----------IDAFYHEIEKNEFAnYFVIEFDNTIIGY--LGLWIVIDQAQI 76
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATfeteppseeeREAWFAAILAPGRP-VLVAEEDGEVVGFasLGPFRPRPAYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  77 T---TIAITEKFRGYGLGQLLLKYVMNYA-SHKCEMMSLEVRIDNIVAQHVYQNLGFQYGGKRKNYY---GEGQDALVMW 149
Cdd:COG1247   81 TaeeSIYVDPDARGRGIGRALLEALIERArARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGfkfGRWLDLVLMQ 160


                 ...
gi 656016165 150 VNL 152
Cdd:COG1247  161 KRL 163
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 11-153 5.28e-14

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: 64.63  E-value: 5.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  11 IRKMSIDDVPSVFDIernsfndsswtIDAFYHEIEKNEFanyFVIEFDNTIIGYLGLWIVI-DQAQITTIAITEKFRGYG 89
Cdd:COG1246    3 IRPATPDDVPAILEL-----------IRPYALEEEIGEF---WVAEEDGEIVGCAALHPLDeDLAELRSLAVHPDYRGRG 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 656016165  90 LGQLLLKYVMNYA-SHKCEMMSLEVRIDnivAQHVYQNLGFQYGGKRKNYYGEGQ--DALVMWVNLS 153
Cdd:COG1246   69 IGRRLLEALLAEArELGLKRLFLLTTSA---AIHFYEKLGFEEIDKEDLPYAKVWqrDSVVMEKDLE 132
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 10-148 3.47e-13

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 62.64  E-value: 3.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  10 NIRKMSIDDVPSVFDIERNS--FndsSWTIDAFYheieKNEFANY--FVIEFDNTIIGYLGLWIVIDQAQITTIAITEKF 85
Cdd:PRK09491   3 TISSLTPADLPAAYHIEQRAhaF---PWSEKTFA----SNQGERYlnLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDY 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 656016165  86 RGYGLGQLLLKYVMNYASHKCEM-MSLEVRIDNIVAQHVYQNLGFQYGGKRKNYY--GEG-QDALVM 148
Cdd:PRK09491  76 QRQGLGRALLEHLIDELEKRGVAtLWLEVRASNAAAIALYESLGFNEVTIRRNYYptADGrEDAIIM 142
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
11-148 6.20e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 62.03  E-value: 6.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  11 IRKMSIDDVPSVFDIERNSFNDSsWTIDAFYHEIEKNEFANYFVIEFDNTIIGYLGLWIV-----IDQAQITTIAITEKF 85
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPG-REAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVdidgeGPALLLGPLAVDPEY 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 656016165  86 RGYGLGQLLLKYVMNYA-SHKCEMMSLEVRIDNIvaqHVYQNLGFQYGGKRKNYYGEGQDALVM 148
Cdd:COG3153   80 RGQGIGRALMRAALEAArERGARAVVLLGDPSLL---PFYERFGFRPAGELGLTLGPDEVFLAK 140
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 50-130 6.03e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.15  E-value: 6.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165   50 ANYFVIEFDNTIIGYLGLWIVIDQAQIT--TIAITEKFRGYGLGQLLLKYVMNYA-SHKCEMMSLEVRIDnivAQHVYQN 126
Cdd:pfam13508   3 GRFFVAEDDGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIGRALLEAAEAAAkEGGIKLLELETTNR---AAAFYEK 79


                  ....
gi 656016165  127 LGFQ 130
Cdd:pfam13508  80 LGFE 83
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 11-130 8.84e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 50.82  E-value: 8.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  11 IRKMSIDDVPSVFDIErnsfndsswTIDAFYHEIEKNEFANYFVI-EFDNTIIGYLGLWIVIDQ-AQITTIAITEKFRGY 88
Cdd:COG0454    3 IRKATPEDINFILLIE---------ALDAELKAMEGSLAGAEFIAvDDKGEPIGFAGLRRLDDKvLELKRLYVLPEYRGK 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 656016165  89 GLGQLLLKYVMNYASHK-CEMMSLEVRIDNIVAQHVYQNLGFQ 130
Cdd:COG0454   74 GIGKALLEALLEWARERgCTALELDTLDGNPAAIRFYERLGFK 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 52-112 1.01e-08

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: 48.81  E-value: 1.01e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 656016165  52 YFVIEFDNTIIGYLGLWI---VIDQAQITTIAITEKFRGYGLGQLLLKYVMNYA-SHKCEMMSLE 112
Cdd:cd04301    1 FLVAEDDGEIVGFASLSPdgsGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEArERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
74-133 7.45e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 47.21  E-value: 7.45e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 656016165  74 AQITTIAITEKFRGYGLGQLLLKYVMNYA-SHKCEMMSLEVRIDNIVAQHVYQNLGFQYGG 133
Cdd:COG3393   16 AEISGVYTHPEYRGRGLASALVAALAREAlARGARTPFLYVDADNPAARRLYERLGFRPVG 76
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
41-130 2.80e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 46.72  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  41 YHEI-EKNEFANYFVIEFDNTIIGYLGL-WIVIDQAQITTIAITEKFRGYGLGQLLLKYVMNYA-SHKCEMMSLEVRIDn 117
Cdd:COG2153   24 YLELdGKDEDARHLLAYDDGELVATARLlPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEArERGARRIVLSAQAH- 102

                         90
                 ....*....|...
gi 656016165 118 ivAQHVYQNLGFQ 130
Cdd:COG2153  103 --AVGFYEKLGFV 113
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 9-130 3.13e-07

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 46.96  E-value: 3.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165    9 LNIRKMSIDDVPSVF------DIERNSFN-----DSSWT-IDAFYHEIEKNEFANYFVIEFDNTIIGYLGLWIVIDQAQI 76
Cdd:pfam13302   2 LLLRPLTEEDAEALFellsdpEVMRYGVPwpltlEEAREwLARIWAADEAERGYGWAIELKDTGFIGSIGLYDIDGEPER 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 656016165   77 TTIA--ITEKFRGYGLGQLLLKYVMNYASHKCEMMSLEVRID--NIVAQHVYQNLGFQ 130
Cdd:pfam13302  82 AELGywLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDpeNTASRRVLEKLGFK 139
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 38-130 2.59e-04

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: 38.79  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165   38 DAFYHEIEKNEFaNYFVIEFDNTIIGYLGLwivIDQAQITTIAITEKFRGYGLGQLLLKYVMNYAS-HKCEMMSLEVRID 116
Cdd:pfam13673  20 EALRERIDQGEY-FFFVAFEGGQIVGVIAL---RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEkDGIKLSELTVNAS 95

                          90
                  ....*....|....
gi 656016165  117 NiVAQHVYQNLGFQ 130
Cdd:pfam13673  96 P-YAVPFYEKLGFR 108
PRK07757 PRK07757
N-acetyltransferase;
51-102 4.82e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 38.25  E-value: 4.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 656016165  51 NYFVIEFDNTIIGYLGLWIV-IDQAQITTIAITEKFRGYGLGQLLLKYVMNYA 102
Cdd:PRK07757  42 DFYVAEEEGEIVGCCALHILwEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEA 94
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 52-148 7.10e-04

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: 37.72  E-value: 7.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165   52 YFVIEFDNTIIGYLGLWIVIDQAQITTIAI-TEKFRGYGLGQLLLKYVMNYA--SHKCEMMSLEVRIDNIVAQHVYQNLG 128
Cdd:TIGR03585  53 YWIVCQESRPIGVISFTDINLVHKSAFWGIyANPFCKPGVGSVLEEAALEYAfeHLGLHKLSLEVLESNNKALKLYEKFG 132

                          90       100
                  ....*....|....*....|
gi 656016165  129 FQYGGKRKNyYGEGQDALVM 148
Cdd:TIGR03585 133 FEREGVFRQ-GGEYYDVLLM 151
Spm_actase_Thplmales NF041158
spermidine N(1)-acetyltransferase;
11-95 1.32e-03

spermidine N(1)-acetyltransferase;


Pssm-ID: 469070  Cd Length: 115  Bit Score: 36.44  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 656016165  11 IRKMSIDDVPSVFDIERNSFNdssWTidafYHEIEKNEFANYFVIE--------------------------FDNTIIGY 64
Cdd:NF041158   4 IRKLSAEDVDALIEVARESWK---WT----YRDIYSNEFIESWISEkyskekllneiirsqsnldiiflgafVNSALIGF 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 656016165  65 LGLWIVIDQAQITTIAITEKFRGYGLGQLLL 95
Cdd:NF041158  77 IELKIIADKAELLRLYLKPEYTHRGIGKLLL 107
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
43-102 1.86e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 35.52  E-value: 1.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 656016165  43 EIEKNEFANYFVIEFDNTIIGYLGlWIVIDQaqitTIAIT-----EKFRGYGLGQLLLKYVMNYA 102
Cdd:COG2388    2 EITHNEEKGRFELEVDGELAGELT-YRLEGG----VIIIThtevpPALRGQGIASALVEAALDDA 61
 
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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