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Conserved domains on  [gi|505384361|ref|WP_015571463|]
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MULTISPECIES: N-acetyltransferase [Enterobacter]

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 1.14e-120

N-acetyltransferase;


:

Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 336.57  E-value: 1.14e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   1 MSEIVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSMEMWQMRLGEQPGIKQLVACIDDIVVGHLTIDVAQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361  81 DFGICVGAQWHNRGVASALIRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGRRYALRNGEYVDAYYMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 505384361 161 MK 162
Cdd:PRK10140 161 VK 162
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-162 1.14e-120

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 336.57  E-value: 1.14e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   1 MSEIVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSMEMWQMRLGEQPGIKQLVACIDDIVVGHLTIDVAQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361  81 DFGICVGAQWHNRGVASALIRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGRRYALRNGEYVDAYYMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 505384361 161 MK 162
Cdd:PRK10140 161 VK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-160 3.64e-32

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: 112.79  E-value: 3.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   4 IVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSMEMWQM-----RLGEQPGIKQLVACI--DDIVVGhlTIDVAQRPRR 76
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWlerllADWADGGALPFAIEDkeDGELIG--VVGLYDIDRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361  77 SHVADFGICVGAQWHNRGVASALIRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGRRYALRNGEYVDAY 156
Cdd:COG1670   86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                 ....
gi 505384361 157 YMAR 160
Cdd:COG1670  166 LYSL 169
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 4-137 3.10e-13

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 63.13  E-value: 3.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361    4 IVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSMEMWQM------RLGEQPGIKQLVACIDDIVVGhlTIDVAQRPRRS 77
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWlariwaADEAERGYGWAIELKDTGFIG--SIGLYDIDGEP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   78 HVADFGICVGAQWHNRGVASALIRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFE 137
Cdd:pfam13302  80 ERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 48-158 8.90e-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: 61.58  E-value: 8.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   48 QPGIKQLVACIDDIVVGHLTIDVAqrPRRSHVadFGICVGAQWHNRGVASALIRTMIDMCDNwLRVDRIELTVFVDNEPA 127
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGYAGVQIV--LDEAHI--LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAA 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 505384361  128 IAVYKKHGFEIEGTGRRYALRNGEyvDAYYM 158
Cdd:TIGR01575 103 QALYKKLGFNEIAIRRNYYPDPGE--DAIVM 131
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-162 1.14e-120

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 336.57  E-value: 1.14e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   1 MSEIVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSMEMWQMRLGEQPGIKQLVACIDDIVVGHLTIDVAQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361  81 DFGICVGAQWHNRGVASALIRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGRRYALRNGEYVDAYYMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 505384361 161 MK 162
Cdd:PRK10140 161 VK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-160 3.64e-32

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: 112.79  E-value: 3.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   4 IVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSMEMWQM-----RLGEQPGIKQLVACI--DDIVVGhlTIDVAQRPRR 76
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWlerllADWADGGALPFAIEDkeDGELIG--VVGLYDIDRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361  77 SHVADFGICVGAQWHNRGVASALIRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGRRYALRNGEYVDAY 156
Cdd:COG1670   86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                 ....
gi 505384361 157 YMAR 160
Cdd:COG1670  166 LYSL 169
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-160 1.26e-27

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 100.84  E-value: 1.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   3 EIVIRHAEPKDYDAIRQIHAqpEVYHNTLQV---PHPSMEMWQMRLGE--QPGIKQLVACIDDIVVGHLTI-DVAQRPRR 76
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYN--EAIAEGTATfetEPPSEEEREAWFAAilAPGRPVLVAEEDGEVVGFASLgPFRPRPAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361  77 SHVADFGICVGAQWHNRGVASALIRTMIDMCDNwLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGRRYALRNGEYVDAY 156
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARA-RGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLV 157


                 ....
gi 505384361 157 YMAR 160
Cdd:COG1247  158 LMQK 161
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 64-160 2.87e-14

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 64.29  E-value: 2.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361  64 GHLTIDVAQRPRRSHVADfgICVGAQWHNRGVASALIRTMIDMCDNwLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGR 143
Cdd:COG0456    1 GFALLGLVDGGDEAEIED--LAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                         90
                 ....*....|....*..
gi 505384361 144 RYALRngeyvDAYYMAR 160
Cdd:COG0456   78 NYYGD-----DALVMEK 89
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 4-137 3.10e-13

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 63.13  E-value: 3.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361    4 IVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSMEMWQM------RLGEQPGIKQLVACIDDIVVGhlTIDVAQRPRRS 77
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWlariwaADEAERGYGWAIELKDTGFIG--SIGLYDIDGEP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   78 HVADFGICVGAQWHNRGVASALIRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFE 137
Cdd:pfam13302  80 ERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 48-158 8.90e-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: 61.58  E-value: 8.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   48 QPGIKQLVACIDDIVVGHLTIDVAqrPRRSHVadFGICVGAQWHNRGVASALIRTMIDMCDNwLRVDRIELTVFVDNEPA 127
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGYAGVQIV--LDEAHI--LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAA 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 505384361  128 IAVYKKHGFEIEGTGRRYALRNGEyvDAYYM 158
Cdd:TIGR01575 103 QALYKKLGFNEIAIRRNYYPDPGE--DAIVM 131
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-160 1.05e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 61.64  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   6 IRHAEPKDYDAIRQIHAQ---PEVYHNTLQvphpsmemwqmRLGEQPGIKQ-LVACIDDIVVGHLTIDVAQRPRRSHVAD 81
Cdd:COG3153    1 IRPATPEDAEAIAALLRAafgPGREAELVD-----------RLREDPAAGLsLVAEDDGEIVGHVALSPVDIDGEGPALL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361  82 FG-ICVGAQWHNRGVASALIRTMIDMCDNwLRVDRIELTVfvdNEPAIAVYKKHGFEIEGTGRRYAlrngeYVDAYYMAR 160
Cdd:COG3153   70 LGpLAVDPEYRGQGIGRALMRAALEAARE-RGARAVVLLG---DPSLLPFYERFGFRPAGELGLTL-----GPDEVFLAK 140
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 54-136 3.01e-12

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: 59.84  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   54 LVACIDDIVVGHLTIDVaQRPRRSHVADFGICVGAQWHNRGVASALIRTMIDMCDNWlRVDRIELTVFVDNEPAIAVYKK 133
Cdd:pfam00583  36 FVAEEDGELVGFASLSI-IDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARER-GCERIFLEVAADNLAAIALYEK 113


                  ...
gi 505384361  134 HGF 136
Cdd:pfam00583 114 LGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 6-147 1.39e-09

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 53.13  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   6 IRHAEPKDYDAIRQIHAQpevyHNTLQVphpsmemwqmRLGEQPGIKQLVACIDDIVVGHLTIdvaqrprrSHVADFGIC 85
Cdd:COG0454    3 IRKATPEDINFILLIEAL----DAELKA----------MEGSLAGAEFIAVDDKGEPIGFAGL--------RRLDDKVLE 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361  86 VGA-----QWHNRGVASALIRTMIDmcdnWLR---VDRIELTVFVDNEPAIAVYKKHGFEIEGTGRRYAL 147
Cdd:COG0454   61 LKRlyvlpEYRGKGIGKALLEALLE----WARergCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVG 126
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
6-154 5.75e-09

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 51.98  E-value: 5.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361    6 IRHAEPKDYDAIRQIHAQPevYHNTLQVP---HPSMEMWQMRLGEQPGIKQLVACID--DIVVGHLTIdVAQRPRRSHVA 80
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAED--RVNPAFTQeyaHSSIEEFETFLAAYLSPGEIVFGVAesDRLIGYATL-RQFDYVKTHKA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505384361   81 DFGICVGAQwHNRGVasalIRTMIDMCDNWLR----VDRIELTVFVDNEPAIAVYKKHGFEIEGTGRRYALRNGEYVD 154
Cdd:pfam13420  78 ELSFYVVKN-NDEGI----NRELINAIIQYARknqnIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 47-137 5.11e-08

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: 48.81  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   47 EQPGIKQLVACIDDIVVGHLTIDvaqrpRRSHVADFgiCVGAQWHNRGVASALIRTMIDMCDNWlRVDRIELTVFVDNeP 126
Cdd:pfam13673  27 DQGEYFFFVAFEGGQIVGVIALR-----DRGHISLL--FVDPDYQGQGIGKALLEAVEDYAEKD-GIKLSELTVNASP-Y 97

                          90
                  ....*....|.
gi 505384361  127 AIAVYKKHGFE 137
Cdd:pfam13673  98 AVPFYEKLGFR 108
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-138 6.84e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 47.45  E-value: 6.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   54 LVACIDDIVVGhlTIDVAQRPRRSHVADFGICVGAQWHNRGVASALIRTmidmCDNWLRVDRIELTVFVDNEPAIAVYKK 133
Cdd:pfam13508   6 FVAEDDGKIVG--FAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEA----AEAAAKEGGIKLLELETTNRAAAFYEK 79


                  ....*
gi 505384361  134 HGFEI 138
Cdd:pfam13508  80 LGFEE 84
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
70-148 5.64e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.59  E-value: 5.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361  70 VAQRPRRSHVA-DFGICVGAQWHNRGVASALIRTMIDmcdnWLR---VDRIELTVFVDNEPAIAVYKKHGFEIEGTGRRY 145
Cdd:COG3393    6 AGVRAESPGVAeISGVYTHPEYRGRGLASALVAALAR----EALargARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81


                 ...
gi 505384361 146 ALR 148
Cdd:COG3393   82 LFR 84
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 44-141 1.56e-05

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 42.51  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   44 RLGEQPGIKQLVACIDDIVVGHLTIDvaqRPRRSHVA--------DFGI--CVGAQWH-NRGVASALIRTMIDMCDNWLR 112
Cdd:pfam13523  37 RLAADPHSHPYIGLLDGEPFGYFEIY---WAKEDRLGeyydarpgDRGIhlLIGEPAFrGRGFTTALLRALVHYLFADPR 113

                          90       100       110
                  ....*....|....*....|....*....|..
gi 505384361  113 VDRIeltVF---VDNEPAIAVYKKHGFEIEGT 141
Cdd:pfam13523 114 TRRV---VVepdVRNERAIRLLERAGFRKVKE 142
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 80-158 2.10e-05

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 42.48  E-value: 2.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505384361  80 ADFGICVGAQWHNRGVASALIRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGRRYALRNGEYVDAYYM 158
Cdd:PRK15130  84 AEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTIRM 162
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 4-137 3.64e-05

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: 41.13  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361   4 IVIRHAEPKDYDAIRQIHAQPEVYHNTLQVphpsmemwqmrlgeqpgikqLVACIDDIVVGHLTIDVaQRPRRSHVADFG 83
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALEEEIGEF--------------------WVAEEDGEIVGCAALHP-LDEDLAELRSLA 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 505384361  84 icVGAQWHNRGVASALIRTMIDMCDNwLRVDRIELTVfvdNEPAIAVYKKHGFE 137
Cdd:COG1246   60 --VHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLLT---TSAAIHFYEKLGFE 107
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
54-140 2.73e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 35.93  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384361  54 LVACIDDIVVGHLTIdvaqRPRRSHVADFG-ICVGAQWHNRGVASALIRTMIDMCDNwLRVDRIELTVfvdNEPAIAVYK 132
Cdd:COG2153   37 LLAYDDGELVATARL----LPPGDGEAKIGrVAVLPEYRGQGLGRALMEAAIEEARE-RGARRIVLSA---QAHAVGFYE 108


                 ....*...
gi 505384361 133 KHGFEIEG 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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