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Conserved domains on  [gi|692317171|ref|WP_032128003|]
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MULTISPECIES: ribosomal protein S18-alanine N-acetyltransferase [Stenotrophomonas]

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 ...
 19-150 8.73e-51

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: 159.03  E-value: 8.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171   19 DLNAVMAIEVRGYPFPWTRGIFVDCLRAGYPGLAMER-DGQLIGYGVLSIAADEAHVLNVCIDPLTQSRGLGRQLLRALV 97
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARiGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 692317171   98 QLAGDRGAQRVFLEVRPSNTPALALYHSEGFNEIGRRPRYYPAAQgrEDAVVM 150
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPG--EDAIVM 131
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 19-150 8.73e-51

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: 159.03  E-value: 8.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171   19 DLNAVMAIEVRGYPFPWTRGIFVDCLRAGYPGLAMER-DGQLIGYGVLSIAADEAHVLNVCIDPLTQSRGLGRQLLRALV 97
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARiGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 692317171   98 QLAGDRGAQRVFLEVRPSNTPALALYHSEGFNEIGRRPRYYPAAQgrEDAVVM 150
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPG--EDAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 15-154 1.04e-44

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 143.92  E-value: 1.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  15 LRESDLNAVMAIEVRGYPFPWTRGIFVDCLRAGYPGLAMERDGQLIGYGVLSIAADEAHVLNVCIDPLTQSRGLGRQLLR 94
Cdd:PRK09491   7 LTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLE 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  95 ALVQLAGDRGAQRVFLEVRPSNTPALALYHSEGFNEIGRRPRYYPAAQGREDAVVMAIEL 154
Cdd:PRK09491  87 HLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAIIMALPL 146
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 61-154 1.72e-22

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 85.48  E-value: 1.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  61 GYGVLSI--AADEAHVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLEVRPSNTPALALYHSEGFNEIGRRPRYY 138
Cdd:COG0456    1 GFALLGLvdGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....*.
gi 692317171 139 PaaqgrEDAVVMAIEL 154
Cdd:COG0456   81 G-----DDALVMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 20-128 3.08e-18

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: 75.63  E-value: 3.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171   20 LNAVMAIEVRGYPFPWTRG----IFVDCLRAGYPGLAMERDGQLIGYGVLSIAADE---AHVLNVCIDPLTQSRGLGRQL 92
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEpldlLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEppvGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 692317171   93 LRALVQLAGDRGAQRVFLEVRPSNTPALALYHSEGF 128
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-111 1.26e-09

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 51.51  E-value: 1.26e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 692317171  51 LAMERDGQLIGYGVLSIA---ADEAHVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLE 111
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDgsgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 19-150 8.73e-51

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: 159.03  E-value: 8.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171   19 DLNAVMAIEVRGYPFPWTRGIFVDCLRAGYPGLAMER-DGQLIGYGVLSIAADEAHVLNVCIDPLTQSRGLGRQLLRALV 97
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARiGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 692317171   98 QLAGDRGAQRVFLEVRPSNTPALALYHSEGFNEIGRRPRYYPAAQgrEDAVVM 150
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPDPG--EDAIVM 131
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 15-154 1.04e-44

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 143.92  E-value: 1.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  15 LRESDLNAVMAIEVRGYPFPWTRGIFVDCLRAGYPGLAMERDGQLIGYGVLSIAADEAHVLNVCIDPLTQSRGLGRQLLR 94
Cdd:PRK09491   7 LTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLE 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  95 ALVQLAGDRGAQRVFLEVRPSNTPALALYHSEGFNEIGRRPRYYPAAQGREDAVVMAIEL 154
Cdd:PRK09491  87 HLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAIIMALPL 146
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 61-154 1.72e-22

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 85.48  E-value: 1.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  61 GYGVLSI--AADEAHVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLEVRPSNTPALALYHSEGFNEIGRRPRYY 138
Cdd:COG0456    1 GFALLGLvdGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....*.
gi 692317171 139 PaaqgrEDAVVMAIEL 154
Cdd:COG0456   81 G-----DDALVMEKEL 91
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
10-154 1.82e-20

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 82.35  E-value: 1.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  10 VSLRALRESDLNAVMAI---EVRGYPFPWT---------RGIFVDCLRAGYPGLAMERDGQLIGYGVLSI-----AADEA 72
Cdd:COG1247    2 MTIRPATPEDAPAIAAIyneAIAEGTATFEteppseeerEAWFAAILAPGRPVLVAEEDGEVVGFASLGPfrprpAYRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  73 HVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLEVRPSNTPALALYHSEGFNEIGRRPRYYPAAQGREDAVVMAI 152
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161


                 ..
gi 692317171 153 EL 154
Cdd:COG1247  162 RL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 20-128 3.08e-18

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: 75.63  E-value: 3.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171   20 LNAVMAIEVRGYPFPWTRG----IFVDCLRAGYPGLAMERDGQLIGYGVLSIAADE---AHVLNVCIDPLTQSRGLGRQL 92
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEpldlLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEppvGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 692317171   93 LRALVQLAGDRGAQRVFLEVRPSNTPALALYHSEGF 128
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 10-137 1.73e-16

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 71.62  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  10 VSLRALRESDLNAVMAIEvrgypfPWTRGIFV-DCLRAGYPGLAMERDGQLIGYGVLSIAADE-AHVLNVCIDPLTQSRG 87
Cdd:COG0454    1 MSIRKATPEDINFILLIE------ALDAELKAmEGSLAGAEFIAVDDKGEPIGFAGLRRLDDKvLELKRLYVLPEYRGKG 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 692317171  88 LGRQLLRALVQLAGDRGAQRVFLEVRPSNTPALALYHSEGFNEIGRRPRY 137
Cdd:COG0454   75 IGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVAY 124
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 10-152 1.22e-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: 70.03  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  10 VSLRALRESDLNAVMAI----EVRGYPFPWTRGI-----FVDCLRAGYP-------GLAMERDGQLIGYGVLSIAADEAH 73
Cdd:COG1670    8 LRLRPLRPEDAEALAELlndpEVARYLPGPPYSLeearaWLERLLADWAdggalpfAIEDKEDGELIGVVGLYDIDRANR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  74 VLNV--CIDPLTQSRGLGRQLLRALVQLA-GDRGAQRVFLEVRPSNTPALALYHSEGFNEIGRRPRYYPAAQGREDAVVM 150
Cdd:COG1670   88 SAEIgyWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVLY 167


                 ..
gi 692317171 151 AI 152
Cdd:COG1670  168 SL 169
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
12-154 4.28e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.80  E-value: 4.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  12 LRALRESDLNAVMAIEVRGYPFPWTRGIfVDCLRAGYPG---LAMERDGQLIGYGVLSIAADEAHVLNVCIDPLT----- 83
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAEL-VDRLREDPAAglsLVAEDDGEIVGHVALSPVDIDGEGPALLLGPLAvdpey 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 692317171  84 QSRGLGRQLLRALVQLAGDRGAQRVFLEVRPSNtpaLALYHSEGFNEIGRRPRYYPaaqgrEDAVVMAIEL 154
Cdd:COG3153   80 RGQGIGRALMRAALEAARERGARAVVLLGDPSL---LPFYERFGFRPAGELGLTLG-----PDEVFLAKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 10-154 8.97e-15

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: 66.94  E-value: 8.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  10 VSLRALRESDLNAVMAIeVRGYPFPWTRGIFvdclragypgLAMERDGQLIGYGVLSI-AADEAHVLNVCIDPLTQSRGL 88
Cdd:COG1246    1 MTIRPATPDDVPAILEL-IRPYALEEEIGEF----------WVAEEDGEIVGCAALHPlDEDLAELRSLAVHPDYRGRGI 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692317171  89 GRQLLRALVQLAGDRGAQRVFLEvrpSNTPALALYHSEGFNEIGRRPRYYPAAQGReDAVVMAIEL 154
Cdd:COG1246   70 GRRLLEALLAEARELGLKRLFLL---TTSAAIHFYEKLGFEEIDKEDLPYAKVWQR-DSVVMEKDL 131
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
63-137 1.43e-12

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 59.92  E-value: 1.43e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692317171  63 GVLSIAADEAHVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLEVRPSNTPALALYHSEGFNEIGRRPRY 137
Cdd:COG3393    7 GVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-130 4.10e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 55.92  E-value: 4.10e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 692317171   54 ERDGQLIGYGVLSIAADEAHV--LNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLEVRPsntPALALYHSEGFNE 130
Cdd:pfam13508   9 EDDGKIVGFAALLPLDDEGALaeLRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTN---RAAAFYEKLGFEE 84
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
54-132 5.29e-10

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 54.42  E-value: 5.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  54 ERDGQLIGYG-VLSIAADEAHVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLEVRpsnTPALALYHSEGFNEIG 132
Cdd:COG2153   40 YDDGELVATArLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQ---AHAVGFYEKLGFVPVG 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-111 1.26e-09

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 51.51  E-value: 1.26e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 692317171  51 LAMERDGQLIGYGVLSIA---ADEAHVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLE 111
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDgsgGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 43-133 1.53e-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: 53.04  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171   43 CLRAGYPGLAMERDGQLIGYGVLSiaaDEAHVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLEVRPSNTpALAL 122
Cdd:pfam13673  26 IDQGEYFFFVAFEGGQIVGVIALR---DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPY-AVPF 101

                          90
                  ....*....|.
gi 692317171  123 YHSEGFNEIGR 133
Cdd:pfam13673 102 YEKLGFRATGP 112
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 77-131 1.52e-06

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: 43.86  E-value: 1.52e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 692317171   77 VCIDPLTQSRGLGRQLLRALVQLAGDRGaQRVFLEVRPSNTPALALYHSEGFNEI 131
Cdd:pfam08445  27 LQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGFRKI 80
PRK10140 PRK10140
N-acetyltransferase;
45-151 1.80e-05

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 42.66  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  45 RAGYPGLAMERDGQLIGYgvLSIAADE----AHV--LNVCIDPLTQSRGLGRQLLRALVQLAGD-RGAQRVFLEVRPSNT 117
Cdd:PRK10140  48 RPGIKQLVACIDGDVVGH--LTIDVQQrprrSHVadFGICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVFVDNA 125

                         90       100       110
                 ....*....|....*....|....*....|....
gi 692317171 118 PALALYHSEGFNEIGRRPRYYPAAQGREDAVVMA 151
Cdd:PRK10140 126 PAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMA 159
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-128 2.54e-05

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 41.95  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171   12 LRALRESDLNAVMAI----EVRGYPFPW------TRGIFVDCLRAGYPGLAM-----ERDGQLIGYGVLSIAADEAHVLN 76
Cdd:pfam13302   4 LRPLTEEDAEALFELlsdpEVMRYGVPWpltleeAREWLARIWAADEAERGYgwaieLKDTGFIGSIGLYDIDGEPERAE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 692317171   77 V--CIDPLTQSRGLGRQLLRALVQLAGDR-GAQRVFLEVRPSNTPALALYHSEGF 128
Cdd:pfam13302  84 LgyWLGPDYWGKGYATEAVRALLEYAFEElGLPRLVARIDPENTASRRVLEKLGF 138
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
37-129 3.03e-05

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 42.22  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  37 RGIFVD-CLragypgLAMERDGQLIGYGVLSIAAD-EAHVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLEVRP 114
Cdd:PRK10975  96 RGTFDHqCL------LLRDASGQIQGFVTLRELNDtDARIGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQM 169

                         90
                 ....*....|....*
gi 692317171 115 SNTPALALYHSEGFN 129
Cdd:PRK10975 170 GNLAALRLYIRSGAN 184
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 86-132 5.47e-05

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 40.97  E-value: 5.47e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 692317171   86 RGLGRQLLRALVQLA-GDRGAQRVFLEVRPSNTPALALYHSEGFNEIG 132
Cdd:pfam13523  94 RGFTTALLRALVHYLfADPRTRRVVVEPDVRNERAIRLLERAGFRKVK 141
PRK07922 PRK07922
amino-acid N-acetyltransferase;
52-135 7.30e-05

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 41.06  E-value: 7.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692317171  52 AMERDGQLIGYGVLSIA-ADEAHVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVF---LEVrpsntpalALYHSEG 127
Cdd:PRK07922  50 AEHLDGEVVGCGALHVMwEDLAEIRTVAVDPAARGRGVGHAIVERLLDVARELGLSRVFvltFEV--------EFFARHG 121


                 ....*...
gi 692317171 128 FNEIGRRP 135
Cdd:PRK07922 122 FVEIDGTP 129
PRK07757 PRK07757
N-acetyltransferase;
53-109 2.30e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 39.41  E-value: 2.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 692317171  53 MERDGQLIGYGVLSI-AADEAHVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVF 109
Cdd:PRK07757  46 AEEEGEIVGCCALHIlWEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRVF 103
PLN02706 PLN02706
glucosamine 6-phosphate N-acetyltransferase
 73-118 2.92e-04

glucosamine 6-phosphate N-acetyltransferase


Pssm-ID: 178308 [Multi-domain]  Cd Length: 150  Bit Score: 38.92  E-value: 2.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 692317171  73 HVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLEVRPSNTP 118
Cdd:PLN02706  87 HIEDVVVDSAARGKGLGKKIIEALTEHARSAGCYKVILDCSEENKA 132
PRK03624 PRK03624
putative acetyltransferase; Provisional
 77-130 4.79e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 38.37  E-value: 4.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 692317171  77 VCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLEVRPSNTPALALYHSEGFNE 130
Cdd:PRK03624  74 LAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEE 127
PTZ00330 PTZ00330
acetyltransferase; Provisional
 73-136 6.70e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 35.20  E-value: 6.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 692317171  73 HVLNVCIDPLTQSRGLGRQLLRALVQLAGDRGAQRVFLEvrpSNTPALALYHSEGFNEIGRRPR 136
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILD---CTEDMVAFYKKLGFRACERQMR 144
 
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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