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Conserved domains on  [gi|1264888692|gb|PGO24203|]
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ribosomal-protein-alanine N-acetyltransferase [Bacillus cereus]

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 ...
 10-141 2.43e-50

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: 157.11  E-value: 2.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  10 DIAQIVAIEEASFSTPWTADAFHRELTmNEHAHYIVLEKDGRVVGYCGLWIIIDESHITNIAILPEYRGQKLGDALLKAV 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELA-NYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLREL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1264888692  90 ISEAKELGVKTMTLEVRVSNEVAKQLYRKYGFQNGGIRKRYYADNQEDGLVM 141
Cdd:TIGR01575  80 IDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 10-141 2.43e-50

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: 157.11  E-value: 2.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  10 DIAQIVAIEEASFSTPWTADAFHRELTmNEHAHYIVLEKDGRVVGYCGLWIIIDESHITNIAILPEYRGQKLGDALLKAV 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELA-NYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLREL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1264888692  90 ISEAKELGVKTMTLEVRVSNEVAKQLYRKYGFQNGGIRKRYYADNQEDGLVM 141
Cdd:TIGR01575  80 IDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 10-141 2.72e-28

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 101.54  E-value: 2.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  10 DIAQIVAIEEASFSTPWTADAFhrelTMNEHAHYI--VLEKDGRVVGYCGLWIIIDESHITNIAILPEYRGQKLGDALLK 87
Cdd:PRK09491   11 DLPAAYHIEQRAHAFPWSEKTF----ASNQGERYLnlKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLE 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1264888692  88 AVISEAKELGVKTMTLEVRVSNEVAKQLYRKYGFQNGGIRKRYY--ADNQEDGLVM 141
Cdd:PRK09491   87 HLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYptADGREDAIIM 142
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-122 1.68e-25

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 94.00  E-value: 1.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   3 FRKMELDDIAQIVAIEEASFSTPWTADAFHRELTMNEHAHYIVLEKDGRVVGYCGLWIIIDES-----HITNIAILPEYR 77
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGegpalLLGPLAVDPEYR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1264888692  78 GQKLGDALLKAVISEAKELGVKTMTLevrVSNEVAKQLYRKYGFQ 122
Cdd:COG3153    81 GQGIGRALMRAALEAARERGARAVVL---LGDPSLLPFYERFGFR 122
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 11-121 7.05e-21

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: 81.41  E-value: 7.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  11 IAQIVAIEEASFSTPWTADAF--HRELTMNEHAHYIVLEKDGRVVGYCGLWIIIDES---HITNIAILPEYRGQKLGDAL 85
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLdlLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPpvgEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1264888692  86 LKAVISEAKELGVKTMTLEVRVSNEVAKQLYRKYGF 121
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 43-104 3.54e-14

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: 63.06  E-value: 3.54e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1264888692  43 YIVLEKDGRVVGYCGLWII---IDESHITNIAILPEYRGQKLGDALLKAVISEAKELGVKTMTLE 104
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDgsgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 10-141 2.43e-50

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: 157.11  E-value: 2.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  10 DIAQIVAIEEASFSTPWTADAFHRELTmNEHAHYIVLEKDGRVVGYCGLWIIIDESHITNIAILPEYRGQKLGDALLKAV 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELA-NYHLCYLLARIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLREL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1264888692  90 ISEAKELGVKTMTLEVRVSNEVAKQLYRKYGFQNGGIRKRYYADNQEDGLVM 141
Cdd:TIGR01575  80 IDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPGEDAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 10-141 2.72e-28

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 101.54  E-value: 2.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  10 DIAQIVAIEEASFSTPWTADAFhrelTMNEHAHYI--VLEKDGRVVGYCGLWIIIDESHITNIAILPEYRGQKLGDALLK 87
Cdd:PRK09491   11 DLPAAYHIEQRAHAFPWSEKTF----ASNQGERYLnlKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLE 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1264888692  88 AVISEAKELGVKTMTLEVRVSNEVAKQLYRKYGFQNGGIRKRYY--ADNQEDGLVM 141
Cdd:PRK09491   87 HLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYptADGREDAIIM 142
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-122 1.68e-25

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 94.00  E-value: 1.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   3 FRKMELDDIAQIVAIEEASFSTPWTADAFHRELTMNEHAHYIVLEKDGRVVGYCGLWIIIDES-----HITNIAILPEYR 77
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGegpalLLGPLAVDPEYR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1264888692  78 GQKLGDALLKAVISEAKELGVKTMTLevrVSNEVAKQLYRKYGFQ 122
Cdd:COG3153    81 GQGIGRALMRAALEAARERGARAVVL---LGDPSLLPFYERFGFR 122
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 54-142 1.21e-24

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 90.49  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  54 GYCGLWIII--DESHITNIAILPEYRGQKLGDALLKAVISEAKELGVKTMTLEVRVSNEVAKQLYRKYGFQNGGIRKRYY 131
Cdd:COG0456     1 GFALLGLVDggDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                          90
                  ....*....|.
gi 1264888692 132 ADnqeDGLVMW 142
Cdd:COG0456    81 GD---DALVME 88
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-142 2.74e-24

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 91.59  E-value: 2.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   1 MIFRKMELDDIAQIVAI-------EEASFST-PWTADAFHRELT--MNEHAHYIVLEKDGRVVGYCGLWIII-----DES 65
Cdd:COG1247     2 MTIRPATPEDAPAIAAIyneaiaeGTATFETePPSEEEREAWFAaiLAPGRPVLVAEEDGEVVGFASLGPFRprpayRGT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264888692  66 HITNIAILPEYRGQKLGDALLKAVISEAKELGVKTMTLEVRVSNEVAKQLYRKYGFQ-NGGIRKRYYADNQEDGLVMW 142
Cdd:COG1247    82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEeVGTLPEVGFKFGRWLDLVLM 159
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-143 3.23e-23

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: 88.13  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   1 MIFRKMELDDIAQIVAIEEasfstPWTADafhreltmNEHAHYIVLEKDGRVVGYCGLWIIIDES-HITNIAILPEYRGQ 79
Cdd:COG1246     1 MTIRPATPDDVPAILELIR-----PYALE--------EEIGEFWVAEEDGEIVGCAALHPLDEDLaELRSLAVHPDYRGR 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1264888692  80 KLGDALLKAVISEAKELGVKTMTLEvrvSNEVAKQLYRKYGFQNGGIRKRYYADNQEDGLVMWV 143
Cdd:COG1246    68 GIGRRLLEALLAEARELGLKRLFLL---TTSAAIHFYEKLGFEEIDKEDLPYAKVWQRDSVVME 128
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 1-122 4.58e-21

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 82.79  E-value: 4.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   1 MIFRKMELDDIAQIVAIEEasfstpWTADAFHREltMNEH-AHYIVLEKDGRVVGYCGLWIIIDES-HITNIAILPEYRG 78
Cdd:COG0454     1 MSIRKATPEDINFILLIEA------LDAELKAME--GSLAgAEFIAVDDKGEPIGFAGLRRLDDKVlELKRLYVLPEYRG 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1264888692  79 QKLGDALLKAVISEAKELGVKTMTLEVRVSNEVAKQLYRKYGFQ 122
Cdd:COG0454    73 KGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFK 116
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 11-121 7.05e-21

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: 81.41  E-value: 7.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  11 IAQIVAIEEASFSTPWTADAF--HRELTMNEHAHYIVLEKDGRVVGYCGLWIIIDES---HITNIAILPEYRGQKLGDAL 85
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLdlLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPpvgEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1264888692  86 LKAVISEAKELGVKTMTLEVRVSNEVAKQLYRKYGF 121
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 27-127 1.85e-18

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: 75.77  E-value: 1.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  27 TADAFHRELtMNEHAHYIVLEKDGRVVGYCGLwiiIDESHITNIAILPEYRGQKLGDALLKAVISEAKELGVKTMTLEVR 106
Cdd:pfam13673  18 SPEALRERI-DQGEYFFFVAFEGGQIVGVIAL---RDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVN 93

                          90       100
                  ....*....|....*....|....*...
gi 1264888692 107 VSNEvAKQLYRKYGFQN-------GGIR 127
Cdd:pfam13673  94 ASPY-AVPFYEKLGFRAtgpeqefNGIR 120
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 39-122 4.50e-18

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 73.64  E-value: 4.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  39 EHAHYIVLEKDGRVVGYCGLWIIIDESHIT--NIAILPEYRGQKLGDALLKAVISEAKELGVKTMTLEVRVSnevAKQLY 116
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AAAFY 77


                  ....*.
gi 1264888692 117 RKYGFQ 122
Cdd:pfam13508  78 EKLGFE 83
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-134 1.91e-16

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: 71.57  E-value: 1.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   1 MIFRKMELDDIAQIVA------IEEASFSTPWTADAFHRELTM-------NEHAHYIVLEK-DGRVVGYCGLWIIIDESH 66
Cdd:COG1670     8 LRLRPLRPEDAEALAEllndpeVARYLPGPPYSLEEARAWLERlladwadGGALPFAIEDKeDGELIGVVGLYDIDRANR 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264888692  67 ITNIA--ILPEYRGQKLGDALLKAVISEA-KELGVKTMTLEVRVSNEVAKQLYRKYGFQNGGIRKRYYADN 134
Cdd:COG1670    88 SAEIGywLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVID 158
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
39-122 5.86e-16

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 69.44  E-value: 5.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  39 EHAHYIVLEKDGRVVGYCGLWII-IDESHITNIAILPEYRGQKLGDALLKAVISEAKELGVKTMTLEVRVSnevAKQLYR 117
Cdd:COG2153    32 EDARHLLAYDDGELVATARLLPPgDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYE 108


                  ....*
gi 1264888692 118 KYGFQ 122
Cdd:COG2153   109 KLGFV 113
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 43-104 3.54e-14

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: 63.06  E-value: 3.54e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1264888692  43 YIVLEKDGRVVGYCGLWII---IDESHITNIAILPEYRGQKLGDALLKAVISEAKELGVKTMTLE 104
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPDgsgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
51-122 5.01e-13

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 60.31  E-value: 5.01e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1264888692  51 RVVGYCGLWIIIDE-SHITNIAILPEYRGQKLGDALLKAVISEAKELGVKTMTLEVRVSNEVAKQLYRKYGFQ 122
Cdd:COG3393     1 ELVAMAGVRAESPGvAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFR 73
PRK07757 PRK07757
N-acetyltransferase;
43-122 4.93e-12

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 59.44  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  43 YIVLEKDGRVVGYCGLWII-IDESHITNIAILPEYRGQKLGDALLKAVISEAKELGVK---TMTLEVRvsnevakqLYRK 118
Cdd:PRK07757   43 FYVAEEEGEIVGCCALHILwEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKrvfALTYQPE--------FFEK 114


                  ....
gi 1264888692 119 YGFQ 122
Cdd:PRK07757  115 LGFR 118
Eis COG4552
Predicted acetyltransferase [General function prediction only];
1-130 8.33e-12

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 61.07  E-value: 8.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   1 MIFRKMELDDIAQIVAIEEASFSTPWTADAFHRELTMNEHAHYIVLEKDGRVVGYCGLW--------IIIDESHITNIAI 72
Cdd:COG4552     1 MEIRPLTEDDLDAFARLLAYAFGPEPDDEELEAYRPLLEPGRVLGVFDDGELVGTLALYpftlnvggARVPMAGITGVAV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1264888692  73 LPEYRGQKLGDALLKAVISEAKELGvktmtleVRVSN----EVAkqLYRKYGFQNGGIRKRY 130
Cdd:COG4552    81 APEHRRRGVARALLREALAELRERG-------QPLSAlypfEPG--FYRRFGYELAGDRRRY 133
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 2-122 1.11e-09

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 53.12  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   2 IFRKMELDDIAQIVAI------EEASFSTPWTADAFHRELTMNEHAH-------YIVLEKDGRVVGYCGLWIIIDESHIT 68
Cdd:pfam13302   3 LLRPLTEEDAEALFELlsdpevMRYGVPWPLTLEEAREWLARIWAADeaergygWAIELKDTGFIGSIGLYDIDGEPERA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1264888692  69 NIA--ILPEYRGQKLGDALLKAVISEA-KELGVKTMTLEVRVSNEVAKQLYRKYGFQ 122
Cdd:pfam13302  83 ELGywLGPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 33-100 5.30e-09

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 53.23  E-value: 5.30e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1264888692  33 RELTMNEHAHYIVLEKDGRVVGyCGLWIIIDESHITNIAIL---PEYRGQKLGDALLKAVISEAKELGVKT 100
Cdd:PRK05279  326 REQLEREIDKFTVIERDGLIIG-CAALYPFPEEKMGEMACLavhPDYRGSGRGERLLKRIEQRARQLGLKR 395
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-121 1.68e-07

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 46.80  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   3 FRKMELDDIAQIVAIEEASFstPWTADAFHRELTMN--EHAHYIVLEKDGRVVGYCGLWI--------IIDESHITNIAI 72
Cdd:pfam13527   1 IRPLTEDEFDEVLRLLEYAF--QDEDSPELREYFRPllEEGRVLGAFDDGELVSTLALYPfelnvpgkTLPAAGITGVAT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1264888692  73 LPEYRGQKLGDALLKAVISEAKELGVktmTLEVRVSNEVAkqLYRKYGF 121
Cdd:pfam13527  79 YPEYRGRGVMSRLLRRSLEEMRERGV---PLSFLYPSSYP--IYRRFGY 122
PRK10146 PRK10146
aminoalkylphosphonate N-acetyltransferase;
29-127 1.89e-06

aminoalkylphosphonate N-acetyltransferase;


Pssm-ID: 182266 [Multi-domain]  Cd Length: 144  Bit Score: 44.52  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  29 DAFHRELTMN---EHAHYIVLEKDGRVVGYCGL----------WIiideSHITNIAILPEYRGQKLGDALLKAVISEAKE 95
Cdd:PRK10146   32 QAFRVGFNANlrdPNMRYHLALLDGEVVGMIGLhlqfhlhhvnWI----GEIQELVVMPQARGLNVGSKLLAWAEEEARQ 107

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1264888692  96 LGVKTMTLEVRVSNEVAKQLYRKYGFQNGGIR 127
Cdd:PRK10146  108 AGAEMTELSTNVKRHDAHRFYLREGYEQSHFR 139
PRK03624 PRK03624
putative acetyltransferase; Provisional
 1-122 7.65e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 42.99  E-value: 7.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   1 MIFRKMELDDIAQIVAI-EEASFSTPWT---ADaFHRELTMnEHAHYIVLEKDGRVV-----GYCGlwiiidesH---IT 68
Cdd:PRK03624    3 MEIRVFRQADFEAVIALwERCDLTRPWNdpeMD-IERKLNH-DPSLFLVAEVGGEVVgtvmgGYDG--------HrgwAY 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1264888692  69 NIAILPEYRGQKLGDALLKAVISEAKELGVKTMTLEVRVSNEVAKQLYRKYGFQ 122
Cdd:PRK03624   73 YLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYE 126
PRK10140 PRK10140
N-acetyltransferase;
7-136 2.53e-05

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 41.89  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   7 ELDDIAQIVAIEEASFST---PWTADAFHRE-LTMNEHAHYIVLEKDGRVVGYCGLWIIID--ESHITNIAILPEYRGQK 80
Cdd:PRK10140   13 DYEAIRQIHAQPEVYHNTlqvPHPSDHMWQErLADRPGIKQLVACIDGDVVGHLTIDVQQRprRSHVADFGICVDSRWKN 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1264888692  81 LG--DALLKAVISEAKE-LGVKTMTLEVRVSNEVAKQLYRKYGFQNGGIRKRYYADNQE 136
Cdd:PRK10140   93 RGvaSALMREMIEMCDNwLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGE 151
PRK07922 PRK07922
amino-acid N-acetyltransferase;
49-119 3.33e-05

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 41.44  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  49 DGRVVGyCG----LWIIIDEshITNIAILPEYRGQKLGDALLKAVISEAKELGVK---TMTLEVR--------------V 107
Cdd:PRK07922   54 DGEVVG-CGalhvMWEDLAE--IRTVAVDPAARGRGVGHAIVERLLDVARELGLSrvfVLTFEVEffarhgfveidgtpV 130

                          90
                  ....*....|..
gi 1264888692 108 SNEVAKQLYRKY 119
Cdd:PRK07922  131 TPEVYAELLRSY 142
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 4-131 7.81e-05

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 40.07  E-value: 7.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   4 RKMELDDIAQ--IVAIEEASFSTPWTADAFH---RELTMNEHAHYIVLEKD---GRVVGY------------CGLwiiid 63
Cdd:PLN02706   10 RRLEISDKSKgfLELLQQLTVVGDVTEEEFEarfQELASLGDDHLICVIEDaasGRIIATgsvfverkfirnCGK----- 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264888692  64 ESHITNIAILPEYRGQKLGDALLKAVISEAKELGVKTMTLEVRVSNevaKQLYRKYGFQNGGIRKRYY 131
Cdd:PLN02706   85 VGHIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEEN---KAFYEKCGYVRKEIQMVKY 149
PLN02825 PLN02825
amino-acid N-acetyltransferase
 4-103 8.73e-05

amino-acid N-acetyltransferase


Pssm-ID: 215441 [Multi-domain]  Cd Length: 515  Bit Score: 41.30  E-value: 8.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   4 RKMELDDIAQIV-AIEEASFSTPWTADAFHRELTmnehaHYIVLEKDGRVVGYCGLWIIIDE--SHITNIAILPEYRGQK 80
Cdd:PLN02825  374 RVEDLAGIRQIIrPLEESGILVRRTDEELLRALD-----SFVVVEREGSIIACAALFPFFEEkcGEVAAIAVSPECRGQG 448

                          90       100
                  ....*....|....*....|...
gi 1264888692  81 LGDALLKAVISEAKELGVKTMTL 103
Cdd:PLN02825  449 QGDKLLDYIEKKAASLGLEKLFL 471
PHA01807 PHA01807
hypothetical protein
 16-118 2.43e-04

hypothetical protein


Pssm-ID: 222839  Cd Length: 153  Bit Score: 38.76  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  16 AIEEASFSTPWT-----ADAFHRELTMNEHAHYIVLeKDGRVVGYCGLwIIIDESHITNIA------ILPEYRGQKLGDA 84
Cdd:PHA01807   24 AIQELEEFTLFRskeeaLERILDSTESNDRTELLVF-RDGKLAGIAVL-VFEDDPHVGPCLgvqwqyVLPEYRNAGVARE 101

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1264888692  85 LLKAVISEAKELGVKTMTLEVRVSNEVAKQLYRK 118
Cdd:PHA01807  102 FLRELIRLAGEGNLPLIAFSHREGEGRYTIHYRR 135
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 29-130 4.02e-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: 38.11  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  29 DAFHRELTMNEHAHYIVLEKDGRVVGYCGLWIIIDESHITNIAIL--PEYRGQKlGDALLKAVISEAKE-LGVKTMTLEV 105
Cdd:TIGR03585  39 LHFIEALKQDPNRRYWIVCQESRPIGVISFTDINLVHKSAFWGIYanPFCKPGV-GSVLEEAALEYAFEhLGLHKLSLEV 117

                          90       100
                  ....*....|....*....|....*
gi 1264888692 106 RVSNEVAKQLYRKYGFQNGGIRKRY 130
Cdd:TIGR03585 118 LESNNKALKLYEKFGFEREGVFRQG 142
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 44-122 8.65e-04

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: 36.15  E-value: 8.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264888692  44 IVLEKDGRVVGYCglwIIIDESHITNIAILPEYRGQKLGDALLKAVISEAKELGvKTMTLEVRVSNEVAKQLYRKYGFQ 122
Cdd:pfam08445   4 IYRGDTGELAAWC---LRLPGGELGALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGFR 78
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
7-122 4.01e-03

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 35.68  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692   7 ELDDIAQIVAIEEASFS-----TPWTADA----FHRELTMN------EHAHYIVLEKDGRVVGYCGLWIIIDES-HITNI 70
Cdd:PRK10975   53 TETDIPALRQLAAQAFAqsrfrAPWYAPDdsgrFYAQWIENavrgtfDHQCLLLRDASGQIQGFVTLRELNDTDaRIGLL 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1264888692  71 AILPEYRGQKLGDALLKAVISEAKELGVKTMTLEVRVSNEVAKQLYRKYGFQ 122
Cdd:PRK10975  133 AVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGAN 184
Acetyltransf_6 pfam13480
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 22-101 5.06e-03

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions.


Pssm-ID: 433244 [Multi-domain]  Cd Length: 143  Bit Score: 34.94  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264888692  22 FSTPWTADaFHREL--TMNEH--AHYIVLEKDGRVVGYCGLWIIIDESHITNIAILPEYRGQKLGDALLKAVISEAKELG 97
Cdd:pfam13480  50 FAPPWTRA-FLRDLlaALAARgaLRLYVLRLDGRPVAALLGLRSGDRLYYWFGGYDPEYARLSPGLLLLWELIEHAAEEG 128


                  ....
gi 1264888692  98 VKTM 101
Cdd:pfam13480 129 LRRF 132
PRK10514 PRK10514
putative acetyltransferase; Provisional
 62-135 5.72e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 34.98  E-value: 5.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1264888692  62 IDESHITNIAILPEYRGQKLGDALLKAVISEAKELgvktmTLEVRVSNEVAKQLYRKYGFQNGGirkRYYADNQ 135
Cdd:PRK10514   67 LSGGHMEALFVDPDVRGCGVGRMLVEHALSLHPEL-----TTDVNEQNEQAVGFYKKMGFKVTG---RSEVDDQ 132
PRK09831 PRK09831
GNAT family N-acetyltransferase;
64-122 7.82e-03

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 34.55  E-value: 7.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1264888692  64 ESHITNIAILPEYRGQKLGDALLKAVISEAKELGVKtmtlevrvSNEVAKQLYRKYGFQ 122
Cdd:PRK09831   72 EHYIDMLFVDPEYTRRGVASALLKPLIKSESELTVD--------ASITAKPFFERYGFQ 122
 
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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