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Conserved domains on  [gi|16766832|ref|NP_462447|]
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putative transferase [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10013436)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate, similar to Escherichia coli AaaT/YhhY which catalyzes the N-acetylation of L-phenylalanine and L-methionine, and is also able to acetylate and thus detoxify several nonhydrolyzable aminoacyl adenylates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-162 6.88e-121

N-acetyltransferase;


:

Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 337.34  E-value: 6.88e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832    1 MSEIVIRHAEPKDYDAIRQIHAQPEVYHNMLQVPHPSLEMWQARLTEQAGVKQLVACIDDIVVGHLSIQVTQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832   81 DFGICVDARWHNRGIASALIRTMIDMCDNWLRVDRIELTVFVDNEPAVAVYKKYGFEIEGTGKKYGLRNGEYVDAYFMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 16766832  161 VK 162
Cdd:PRK10140 161 VK 162
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-162 6.88e-121

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 337.34  E-value: 6.88e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832    1 MSEIVIRHAEPKDYDAIRQIHAQPEVYHNMLQVPHPSLEMWQARLTEQAGVKQLVACIDDIVVGHLSIQVTQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832   81 DFGICVDARWHNRGIASALIRTMIDMCDNWLRVDRIELTVFVDNEPAVAVYKKYGFEIEGTGKKYGLRNGEYVDAYFMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 16766832  161 VK 162
Cdd:PRK10140 161 VK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-162 7.75e-33

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: 114.33  E-value: 7.75e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832   4 IVIRHAEPKDYDAIRQIHAQPEVYHNMLQVPHpSLEMWQARLTEQAGVKQ--------LVACIDDIVVGHlsIQVTQRPR 75
Cdd:COG1670   8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPY-SLEEARAWLERLLADWAdggalpfaIEDKEDGELIGV--VGLYDIDR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832  76 RSHVADFGICVDARWHNRGIASALIRTMIDMCDNWLRVDRIELTVFVDNEPAVAVYKKYGFEIEGTGKKYGLRNGEYVDA 155
Cdd:COG1670  85 ANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164


                ....*..
gi 16766832 156 YFMARVK 162
Cdd:COG1670 165 VLYSLLR 171
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 4-137 5.65e-14

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 65.06  E-value: 5.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832     4 IVIRHAEPKDYDAIRQIHAQPEVYHNMLQVPHP--SLEMWQARLTEQAGVKQ----LVACIDDIVVGhlSIQVTQRPRRS 77
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTleEAREWLARIWAADEAERgygwAIELKDTGFIG--SIGLYDIDGEP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832    78 HVADFGICVDARWHNRGIASALIRTMIDMCDNWLRVDRIELTVFVDNEPAVAVYKKYGFE 137
Cdd:pfam13302  80 ERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 54-158 4.47e-13

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: 62.35  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832    54 LVACIDDIVVGHLSIQVTqrPRRSHVadFGICVDARWHNRGIASALIRTMIDMCDNwLRVDRIELTVFVDNEPAVAVYKK 133
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIV--LDEAHI--LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKK 108

                          90       100
                  ....*....|....*....|....*
gi 16766832   134 YGFEIEGTGKKYGLRNGEyvDAYFM 158
Cdd:TIGR01575 109 LGFNEIAIRRNYYPDPGE--DAIVM 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-119 3.45e-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: 37.26  E-value: 3.45e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16766832  54 LVACIDDIVVGHLSI-QVTQRPRRSHVADfgICVDARWHNRGIASALIRTMIDMCDNWlRVDRIELT 119
Cdd:cd04301   2 LVAEDDGEIVGFASLsPDGSGGDTAYIGD--LAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-162 6.88e-121

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 337.34  E-value: 6.88e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832    1 MSEIVIRHAEPKDYDAIRQIHAQPEVYHNMLQVPHPSLEMWQARLTEQAGVKQLVACIDDIVVGHLSIQVTQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832   81 DFGICVDARWHNRGIASALIRTMIDMCDNWLRVDRIELTVFVDNEPAVAVYKKYGFEIEGTGKKYGLRNGEYVDAYFMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 16766832  161 VK 162
Cdd:PRK10140 161 VK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-162 7.75e-33

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: 114.33  E-value: 7.75e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832   4 IVIRHAEPKDYDAIRQIHAQPEVYHNMLQVPHpSLEMWQARLTEQAGVKQ--------LVACIDDIVVGHlsIQVTQRPR 75
Cdd:COG1670   8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPY-SLEEARAWLERLLADWAdggalpfaIEDKEDGELIGV--VGLYDIDR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832  76 RSHVADFGICVDARWHNRGIASALIRTMIDMCDNWLRVDRIELTVFVDNEPAVAVYKKYGFEIEGTGKKYGLRNGEYVDA 155
Cdd:COG1670  85 ANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164


                ....*..
gi 16766832 156 YFMARVK 162
Cdd:COG1670 165 VLYSLLR 171
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-160 1.03e-28

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 103.54  E-value: 1.03e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832   3 EIVIRHAEPKDYDAIRQIHAQ-----PEVYHNMLqvphPSLEMWQARLTE--QAGVKQLVACIDDIVVGHLSI-QVTQRP 74
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIYNEaiaegTATFETEP----PSEEEREAWFAAilAPGRPVLVAEEDGEVVGFASLgPFRPRP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832  75 RRSHVADFGICVDARWHNRGIASALIRTMIDMCDNwLRVDRIELTVFVDNEPAVAVYKKYGFEIEGTGKKYGLRNGEYVD 154
Cdd:COG1247  77 AYRGTAEESIYVDPDARGRGIGRALLEALIERARA-RGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLD 155


                ....*.
gi 16766832 155 AYFMAR 160
Cdd:COG1247 156 LVLMQK 161
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 64-160 2.60e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.99  E-value: 2.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832  64 GHLSIQVTQRPRRSHVADfgICVDARWHNRGIASALIRTMIDMCDNwLRVDRIELTVFVDNEPAVAVYKKYGFEIEGTGK 143
Cdd:COG0456   1 GFALLGLVDGGDEAEIED--LAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                        90
                ....*....|....*..
gi 16766832 144 KYGLRngeyvDAYFMAR 160
Cdd:COG0456  78 NYYGD-----DALVMEK 89
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 4-137 5.65e-14

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 65.06  E-value: 5.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832     4 IVIRHAEPKDYDAIRQIHAQPEVYHNMLQVPHP--SLEMWQARLTEQAGVKQ----LVACIDDIVVGhlSIQVTQRPRRS 77
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTleEAREWLARIWAADEAERgygwAIELKDTGFIG--SIGLYDIDGEP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832    78 HVADFGICVDARWHNRGIASALIRTMIDMCDNWLRVDRIELTVFVDNEPAVAVYKKYGFE 137
Cdd:pfam13302  80 ERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-160 6.35e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 64.72  E-value: 6.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832   6 IRHAEPKDYDAIRQIHAQpeVYhnmlqvPHPSLEMWQARLTEQAGVKQ-LVACIDDIVVGHLSIQVTQRPRRSHVADFG- 83
Cdd:COG3153   1 IRPATPEDAEAIAALLRA--AF------GPGREAELVDRLREDPAAGLsLVAEDDGEIVGHVALSPVDIDGEGPALLLGp 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16766832  84 ICVDARWHNRGIASALIRTMIDMCDNwLRVDRIELTVfvdNEPAVAVYKKYGFEIEGTGkkyglRNGEYVDAYFMAR 160
Cdd:COG3153  73 LAVDPEYRGQGIGRALMRAALEAARE-RGARAVVLLG---DPSLLPFYERFGFRPAGEL-----GLTLGPDEVFLAK 140
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 54-136 3.80e-13

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: 62.15  E-value: 3.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832    54 LVACIDDIVVGHLSIqVTQRPRRSHVADFGICVDARWHNRGIASALIRTMIDMCDNWlRVDRIELTVFVDNEPAVAVYKK 133
Cdd:pfam00583  36 FVAEEDGELVGFASL-SIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARER-GCERIFLEVAADNLAAIALYEK 113


                  ...
gi 16766832   134 YGF 136
Cdd:pfam00583 114 LGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 54-158 4.47e-13

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: 62.35  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832    54 LVACIDDIVVGHLSIQVTqrPRRSHVadFGICVDARWHNRGIASALIRTMIDMCDNwLRVDRIELTVFVDNEPAVAVYKK 133
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIV--LDEAHI--LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKK 108

                          90       100
                  ....*....|....*....|....*
gi 16766832   134 YGFEIEGTGKKYGLRNGEyvDAYFM 158
Cdd:TIGR01575 109 LGFNEIAIRRNYYPDPGE--DAIVM 131
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 39-137 4.82e-11

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: 56.90  E-value: 4.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832    39 EMWQARLTEQAgVKQLVACIDDIVVGHLSIQvtqrpRRSHVADFgiCVDARWHNRGIASALIRTMIDMCDNWlRVDRIEL 118
Cdd:pfam13673  20 EALRERIDQGE-YFFFVAFEGGQIVGVIALR-----DRGHISLL--FVDPDYQGQGIGKALLEAVEDYAEKD-GIKLSEL 90

                          90
                  ....*....|....*....
gi 16766832   119 TVFVDNePAVAVYKKYGFE 137
Cdd:pfam13673  91 TVNASP-YAVPFYEKLGFR 108
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 6-162 2.59e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 55.06  E-value: 2.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832   6 IRHAEPKDYDAIRQIHAQpevyHNMLQvphpslemwqARLTEQAGVKQLVACIDDIVVGHLSIQVTQRPRrSHVADfgIC 85
Cdd:COG0454   3 IRKATPEDINFILLIEAL----DAELK----------AMEGSLAGAEFIAVDDKGEPIGFAGLRRLDDKV-LELKR--LY 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832  86 VDARWHNRGIASALIRTMIDmcdnWLR---VDRIELTVFVDNEPAVAVYKKYGFEIEGtgkkyglRNGEYVDAYFMARVK 162
Cdd:COG0454  66 VLPEYRGKGIGKALLEALLE----WARergCTALELDTLDGNPAAIRFYERLGFKEIE-------RYVAYVGGEFEKELS 134
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
6-154 8.59e-09

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 51.60  E-value: 8.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832     6 IRHAEPKDYDAIRQIHAQPevYHNMLQVP---HPSLEMWQARLTEQAGVKQLVACID--DIVVGHLSIQVTqRPRRSHVA 80
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAED--RVNPAFTQeyaHSSIEEFETFLAAYLSPGEIVFGVAesDRLIGYATLRQF-DYVKTHKA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16766832    81 DFGICVDARwHNRGIasalIRTMIDMCDNWLR----VDRIELTVFVDNEPAVAVYKKYGFEIEGTGKKYGLRNGEYVD 154
Cdd:pfam13420  78 ELSFYVVKN-NDEGI----NRELINAIIQYARknqnIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-138 1.06e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.76  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832    54 LVACIDDIVVGhlSIQVTQRPRRSHVADFGICVDARWHNRGIASALIRTmidmCDNWLRVDRIELTVFVDNEPAVAVYKK 133
Cdd:pfam13508   6 FVAEDDGKIVG--FAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEA----AEAAAKEGGIKLLELETTNRAAAFYEK 79


                  ....*
gi 16766832   134 YGFEI 138
Cdd:pfam13508  80 LGFEE 84
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
83-141 1.88e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 43.74  E-value: 1.88e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16766832  83 GICVDARWHNRGIASALIRTMIDmcdnWLR---VDRIELTVFVDNEPAVAVYKKYGFEIEGT 141
Cdd:COG3393  20 GVYTHPEYRGRGLASALVAALAR----EALargARTPFLYVDADNPAARRLYERLGFRPVGE 77
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 4-137 2.80e-06

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: 44.21  E-value: 2.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832   4 IVIRHAEPKDYDAIRQIHAQPEVYHNMLQVphpslemwqarlteqagvkqLVACIDDIVVGHLSIQVTqRPRRSHVADFG 83
Cdd:COG1246   1 MTIRPATPDDVPAILELIRPYALEEEIGEF--------------------WVAEEDGEIVGCAALHPL-DEDLAELRSLA 59

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 16766832  84 icVDARWHNRGIASALIRTMIDMCDNwLRVDRIELTVfvdNEPAVAVYKKYGFE 137
Cdd:COG1246  60 --VHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLLT---TSAAIHFYEKLGFE 107
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 80-158 5.95e-06

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 44.02  E-value: 5.95e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16766832   80 ADFGICVDARWHNRGIASALIRTMIDMCDNWLRVDRIELTVFVDNEPAVAVYKKYGFEIEGTGKKYGLRNGEYVDAYFM 158
Cdd:PRK15130  84 AEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTIRM 162
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 21-141 1.91e-05

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 42.12  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832    21 HAQPEVYH-NMLQVPHPSLEMWQARLTEQAGVKQLVACIDDIVVGHLSIQvtqRPRRSHVA--------DFGICV---DA 88
Cdd:pfam13523  13 MNDPRVAFwWMLAGPLEQVREYLARLAADPHSHPYIGLLDGEPFGYFEIY---WAKEDRLGeyydarpgDRGIHLligEP 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16766832    89 RWHNRGIASALIRTMIDMCDNWLRVDRIeltVF---VDNEPAVAVYKKYGFEIEGT 141
Cdd:pfam13523  90 AFRGRGFTTALLRALVHYLFADPRTRRV---VVepdVRNERAIRLLERAGFRKVKE 142
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-119 3.45e-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: 37.26  E-value: 3.45e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16766832  54 LVACIDDIVVGHLSI-QVTQRPRRSHVADfgICVDARWHNRGIASALIRTMIDMCDNWlRVDRIELT 119
Cdd:cd04301   2 LVAEDDGEIVGFASLsPDGSGGDTAYIGD--LAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
54-140 3.93e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 38.24  E-value: 3.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766832  54 LVACIDDIVVGHLSIqvtqRPRRSHVADFG-ICVDARWHNRGIASALIRTMIDMCDNwLRVDRIELTVfvdNEPAVAVYK 132
Cdd:COG2153  37 LLAYDDGELVATARL----LPPGDGEAKIGrVAVLPEYRGQGLGRALMEAAIEEARE-RGARRIVLSA---QAHAVGFYE 108


                ....*...
gi 16766832 133 KYGFEIEG 140
Cdd:COG2153 109 KLGFVPVG 116
 
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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