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Conserved domains on  [gi|501085214|ref|WP_012135683|]
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MULTISPECIES: N-acetyltransferase [Citrobacter]

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
 1-143 9.23e-98

putative acetyltransferase; Provisional


:

Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 277.33  E-value: 9.23e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   1 MIRESRTDDMASILTLWMESTIYAHPFIEARYWRESEAIVRDVYLPAAQTWVWEEAGSLKGFASVMEARFLGALFVTPDA 80
Cdd:PRK10562   1 MIREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVYLPAAQTWVWEEDGKLLGFVSVLEGRFVGALFVAPKA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085214  81 IRSGIGKALVQHVQQRFTALSLEVYQKNQSAVNFYHALGFRIEDSAWQEDTQHPTWIMGWQAD 143
Cdd:PRK10562  81 VRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQAD 143
 
Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-143 9.23e-98

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 277.33  E-value: 9.23e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   1 MIRESRTDDMASILTLWMESTIYAHPFIEARYWRESEAIVRDVYLPAAQTWVWEEAGSLKGFASVMEARFLGALFVTPDA 80
Cdd:PRK10562   1 MIREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVYLPAAQTWVWEEDGKLLGFVSVLEGRFVGALFVAPKA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085214  81 IRSGIGKALVQHVQQRFTALSLEVYQKNQSAVNFYHALGFRIEDSAWQEDTQHPTWIMGWQAD 143
Cdd:PRK10562  81 VRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQAD 143
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-137 1.89e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 60.78  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   1 MIRESRTDDMASILTlwmestIYAHPFIE--ARYWRES------EAIVRDVYLPAAQTWVWEEAGSLKGFASVMEAR--- 69
Cdd:COG1247    3 TIRPATPEDAPAIAA------IYNEAIAEgtATFETEPpseeerEAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRprp 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085214  70 -----FLGALFVTPDAIRSGIGKALVQHVQQR-----FTALSLEVYQKNQSAVNFYHALGFRIEDSAWQEDTQHPTWI 137
Cdd:COG1247   77 ayrgtAEESIYVDPDARGRGIGRALLEALIERarargYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWL 154
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 10-120 1.43e-10

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: 54.83  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   10 MASILTLWMESTIYAHPFIEARYWRESEAIvrdvylPAAQTWVWEEAGSLKGFASVMEAR------FLGALFVTPDAIRS 83
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDED------ASEGFFVAEEDGELVGFASLSIIDdeppvgEIEGLAVAPEYRGK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 501085214   84 GIGKALVQHV-----QQRFTALSLEVYQKNQSAVNFYHALGF 120
Cdd:pfam00583  75 GIGTALLQALlewarERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 19-138 2.59e-05

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: 41.16  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   19 ESTIYAHPFIEArywreseAIVRDVYLPAAQTWVWEEAGSLKGFASVMEARFLGALF---VTPDAIRSGIGKALVQHVQQ 95
Cdd:TIGR01575   9 EAAAFAFPWTEA-------QFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILniaVKPEYQGQGIGRALLRELID 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 501085214   96 RF-----TALSLEVYQKNQSAVNFYHALGFRIED--SAWQEDTQHPTWIM 138
Cdd:TIGR01575  82 EAkgrgvNEIFLEVRVSNIAAQALYKKLGFNEIAirRNYYPDPGEDAIVM 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-97 1.53e-04

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: 37.64  E-value: 1.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501085214  51 WVWEEAGSLKGFASVMEAR------FLGALFVTPDAIRSGIGKALVQHVQQRF 97
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGsggdtaYIGDLAVLPEYRGKGIGSALLEAAEEEA 54
 
Name Accession Description Interval E-value
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-143 9.23e-98

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 277.33  E-value: 9.23e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   1 MIRESRTDDMASILTLWMESTIYAHPFIEARYWRESEAIVRDVYLPAAQTWVWEEAGSLKGFASVMEARFLGALFVTPDA 80
Cdd:PRK10562   1 MIREYQPSDLPAILQLWLESTIWAHPFIKEQYWRESAPLVRDVYLPAAQTWVWEEDGKLLGFVSVLEGRFVGALFVAPKA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501085214  81 IRSGIGKALVQHVQQRFTALSLEVYQKNQSAVNFYHALGFRIEDSAWQEDTQHPTWIMGWQAD 143
Cdd:PRK10562  81 VRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIVDSAWQEETQHPTWIMSWQAD 143
PRK10514 PRK10514
putative acetyltransferase; Provisional
 2-122 7.75e-18

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 74.65  E-value: 7.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   2 IRESRTDDMASILTLWMESTIYAHPFIEARYWRESEAIVRDvYLPAAQTWVW-EEAGSLKGFASVMEARfLGALFVTPDA 80
Cdd:PRK10514   4 IRRSRHEEGERLVAIWRRSVDATHDFLSAEDRAEIEELVRS-FLPEAPLWVAvDERDQPVGFMLLSGGH-MEALFVDPDV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 501085214  81 IRSGIGKALVQHVQQRFTALSLEVYQKNQSAVNFYHALGFRI 122
Cdd:PRK10514  82 RGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKV 123
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-137 1.89e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 60.78  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   1 MIRESRTDDMASILTlwmestIYAHPFIE--ARYWRES------EAIVRDVYLPAAQTWVWEEAGSLKGFASVMEAR--- 69
Cdd:COG1247    3 TIRPATPEDAPAIAA------IYNEAIAEgtATFETEPpseeerEAWFAAILAPGRPVLVAEEDGEVVGFASLGPFRprp 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501085214  70 -----FLGALFVTPDAIRSGIGKALVQHVQQR-----FTALSLEVYQKNQSAVNFYHALGFRIEDSAWQEDTQHPTWI 137
Cdd:COG1247   77 ayrgtAEESIYVDPDARGRGIGRALLEALIERarargYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWL 154
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 61-124 7.16e-12

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 57.74  E-value: 7.16e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501085214  61 GFASVMEAR-----FLGALFVTPDAIRSGIGKALVQHVQQR-----FTALSLEVYQKNQSAVNFYHALGFRIED 124
Cdd:COG0456    1 GFALLGLVDggdeaEIEDLAVDPEYRGRGIGRALLEAALERarergARRLRLEVREDNEAAIALYEKLGFEEVG 74
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 10-120 1.43e-10

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: 54.83  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   10 MASILTLWMESTIYAHPFIEARYWRESEAIvrdvylPAAQTWVWEEAGSLKGFASVMEAR------FLGALFVTPDAIRS 83
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDED------ASEGFFVAEEDGELVGFASLSIIDdeppvgEIEGLAVAPEYRGK 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 501085214   84 GIGKALVQHV-----QQRFTALSLEVYQKNQSAVNFYHALGF 120
Cdd:pfam00583  75 GIGTALLQALlewarERGCERIFLEVAADNLAAIALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 1-121 2.11e-10

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: 54.61  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   1 MIRESRTDDMASILTLWMESTIYAhpfiearywreseaivrdvylPAAQTWVWEEAGSLKGFASV--MEARF--LGALFV 76
Cdd:COG1246    2 TIRPATPDDVPAILELIRPYALEE---------------------EIGEFWVAEEDGEIVGCAALhpLDEDLaeLRSLAV 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 501085214  77 TPDAIRSGIGKALVQHV-----QQRFTALSLEVYqknQSAVNFYHALGFR 121
Cdd:COG1246   61 HPDYRGRGIGRRLLEALlaearELGLKRLFLLTT---SAAIHFYEKLGFE 107
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 37-121 1.14e-09

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: 52.66  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   37 EAIVRDVYLPAAQTWVWEEAGSLKGFASVMEARFLGALFVTPDAIRSGIGKALVQHV-----QQRFTALSLEVyqkNQS- 110
Cdd:pfam13673  20 EALRERIDQGEYFFFVAFEGGQIVGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVedyaeKDGIKLSELTV---NASp 96

                          90
                  ....*....|..
gi 501085214  111 -AVNFYHALGFR 121
Cdd:pfam13673  97 yAVPFYEKLGFR 108
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-121 6.00e-09

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 51.24  E-value: 6.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   2 IRESRTDDMASILTLWMEStiyahpFIEARYWRESEAIVRDvyLPAAQTWVWEEAGSLKGFASVMEAR--------FLGA 73
Cdd:COG3153    1 IRPATPEDAEAIAALLRAA------FGPGREAELVDRLRED--PAAGLSLVAEDDGEIVGHVALSPVDidgegpalLLGP 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501085214  74 LFVTPDAIRSGIGKALVQHV-----QQRFTALSLEVyqkNQSAVNFYHALGFR 121
Cdd:COG3153   73 LAVDPEYRGQGIGRALMRAAleaarERGARAVVLLG---DPSLLPFYERFGFR 122
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 46-122 1.22e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 48.99  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   46 PAAQTWVWEEAGSLKGFASVM-----EARFLGALFVTPDAIRSGIGKALVQHVQQRFTALSLEVYQ--KNQSAVNFYHAL 118
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLplddeGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLEleTTNRAAAFYEKL 80


                  ....
gi 501085214  119 GFRI 122
Cdd:pfam13508  81 GFEE 84
PRK03624 PRK03624
putative acetyltransferase; Provisional
 2-125 2.58e-08

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 49.54  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   2 IRESRTDDMASILTLWMESTIyahpfieARYWRESEA-IVRDVYLPAAQTWVWEEAGSLKGfaSVMeARFLG------AL 74
Cdd:PRK03624   5 IRVFRQADFEAVIALWERCDL-------TRPWNDPEMdIERKLNHDPSLFLVAEVGGEVVG--TVM-GGYDGhrgwayYL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501085214  75 FVTPDAIRSGIGKALVQHVQQRFTA-----LSLEVYQKNQSAVNFYHALGFRIEDS 125
Cdd:PRK03624  75 AVHPDFRGRGIGRALVARLEKKLIArgcpkINLQVREDNDAVLGFYEALGYEEQDR 130
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 34-122 1.73e-07

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 46.97  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214  34 RESEAIVRD-VYLPAAQTWVW-EEAGSLKGFASVM----EARFLGALFVTPDAIRSGIGKALVQHV-----QQRFTALSL 102
Cdd:COG0454   18 EALDAELKAmEGSLAGAEFIAvDDKGEPIGFAGLRrlddKVLELKRLYVLPEYRGKGIGKALLEALlewarERGCTALEL 97

                         90       100
                 ....*....|....*....|
gi 501085214 103 EVYQKNQSAVNFYHALGFRI 122
Cdd:COG0454   98 DTLDGNPAAIRFYERLGFKE 117
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 19-138 2.59e-05

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: 41.16  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501085214   19 ESTIYAHPFIEArywreseAIVRDVYLPAAQTWVWEEAGSLKGFASVMEARFLGALF---VTPDAIRSGIGKALVQHVQQ 95
Cdd:TIGR01575   9 EAAAFAFPWTEA-------QFAEELANYHLCYLLARIGGKVVGYAGVQIVLDEAHILniaVKPEYQGQGIGRALLRELID 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 501085214   96 RF-----TALSLEVYQKNQSAVNFYHALGFRIED--SAWQEDTQHPTWIM 138
Cdd:TIGR01575  82 EAkgrgvNEIFLEVRVSNIAAQALYKKLGFNEIAirRNYYPDPGEDAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 74-120 6.05e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 40.30  E-value: 6.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 501085214  74 LF---VTPDAIRSGIGKALVQHVQQRFTA-----LSLEVYQKNQSAVNFYHALGF 120
Cdd:PRK09491  66 LFniaVDPDYQRQGLGRALLEHLIDELEKrgvatLWLEVRASNAAAIALYESLGF 120
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
71-121 8.96e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 38.74  E-value: 8.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501085214  71 LGALFVTPDAIRSGIGKALVQHVQQRFTA-----LSLEVYQKNQSAVNFYHALGFR 121
Cdd:COG3393   18 ISGVYTHPEYRGRGLASALVAALAREALArgartPFLYVDADNPAARRLYERLGFR 73
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-97 1.53e-04

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: 37.64  E-value: 1.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501085214  51 WVWEEAGSLKGFASVMEAR------FLGALFVTPDAIRSGIGKALVQHVQQRF 97
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGsggdtaYIGDLAVLPEYRGKGIGSALLEAAEEEA 54
 
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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