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Conserved domains on  [gi|770923379|ref|WP_045143059|]
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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 4.87e-123

N-acetyltransferase;


:

Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 342.73  E-value: 4.87e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   1 MSEIVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSEQMWQERLSDQPGIKQLVACIDGHVAGHLCIVVAQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379  81 DFGICVGAQWQNRGVASALMRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGKRYALRNGEYVDAYYMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 770923379 161 MK 162
Cdd:PRK10140 161 VK 162
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-162 4.87e-123

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 342.73  E-value: 4.87e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   1 MSEIVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSEQMWQERLSDQPGIKQLVACIDGHVAGHLCIVVAQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379  81 DFGICVGAQWQNRGVASALMRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGKRYALRNGEYVDAYYMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 770923379 161 MK 162
Cdd:PRK10140 161 VK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-160 2.97e-34

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: 118.18  E-value: 2.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   4 IVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSEQMWQ-----ERLSDQPGIKQLVACI--DGHVAGHLCIVvaQRPRR 76
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAwlerlLADWADGGALPFAIEDkeDGELIGVVGLY--DIDRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379  77 SHVADFGICVGAQWQNRGVASALMRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGKRYALRNGEYVDAY 156
Cdd:COG1670   86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                 ....
gi 770923379 157 YMAR 160
Cdd:COG1670  166 LYSL 169
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 54-136 9.17e-15

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: 66.39  E-value: 9.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   54 LVACIDGHVAGHLCIVVaQRPRRSHVADFGICVGAQWQNRGVASALMRTMIDMCDNWlRVDRIELTVFVDNEPAIAVYKK 133
Cdd:pfam00583  36 FVAEEDGELVGFASLSI-IDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARER-GCERIFLEVAADNLAAIALYEK 113


                  ...
gi 770923379  134 HGF 136
Cdd:pfam00583 114 LGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 48-158 6.93e-14

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: 64.27  E-value: 6.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   48 QPGIKQLVACIDGHVAGHlcIVVAQRPRRSHVadFGICVGAQWQNRGVASALMRTMIDMCDNwLRVDRIELTVFVDNEPA 127
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGY--AGVQIVLDEAHI--LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAA 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 770923379  128 IAVYKKHGFEIEGTGKRYALRNGEyvDAYYM 158
Cdd:TIGR01575 103 QALYKKLGFNEIAIRRNYYPDPGE--DAIVM 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-119 2.29e-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: 2.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 770923379  54 LVACIDGHVAGhlCIVVAQRPRRSHVADFG-ICVGAQWQNRGVASALMRTMIDMCDNWlRVDRIELT 119
Cdd:cd04301    2 LVAEDDGEIVG--FASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-162 4.87e-123

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 342.73  E-value: 4.87e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   1 MSEIVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSEQMWQERLSDQPGIKQLVACIDGHVAGHLCIVVAQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379  81 DFGICVGAQWQNRGVASALMRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGKRYALRNGEYVDAYYMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 770923379 161 MK 162
Cdd:PRK10140 161 VK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-160 2.97e-34

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: 118.18  E-value: 2.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   4 IVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSEQMWQ-----ERLSDQPGIKQLVACI--DGHVAGHLCIVvaQRPRR 76
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAwlerlLADWADGGALPFAIEDkeDGELIGVVGLY--DIDRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379  77 SHVADFGICVGAQWQNRGVASALMRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGKRYALRNGEYVDAY 156
Cdd:COG1670   86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                 ....
gi 770923379 157 YMAR 160
Cdd:COG1670  166 LYSL 169
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-160 2.07e-29

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 105.46  E-value: 2.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   3 EIVIRHAEPKDYDAIRQIHAqpEVYHNTLQV---PHPSEQMWQERLSD--QPGIKQLVACIDGHVAGHLCIV-VAQRPRR 76
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYN--EAIAEGTATfetEPPSEEEREAWFAAilAPGRPVLVAEEDGEVVGFASLGpFRPRPAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379  77 SHVADFGICVGAQWQNRGVASALMRTMIDMCDNwLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGKRYALRNGEYVDAY 156
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARA-RGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLV 157


                 ....
gi 770923379 157 YMAR 160
Cdd:COG1247  158 LMQK 161
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 64-160 1.18e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 68.14  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379  64 GHLCIVVAQRPRRSHVADfgICVGAQWQNRGVASALMRTMIDMCDNwLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGK 143
Cdd:COG0456    1 GFALLGLVDGGDEAEIED--LAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                         90
                 ....*....|....*..
gi 770923379 144 RYALRngeyvDAYYMAR 160
Cdd:COG0456   78 NYYGD-----DALVMEK 89
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-160 1.37e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 69.34  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   6 IRHAEPKDYDAIRQIHAQpeVYhntlqvPHPSEQMWQERLSDQPGIKQ-LVACIDGHVAGHLCIVVAQRPRRSHVADFG- 83
Cdd:COG3153    1 IRPATPEDAEAIAALLRA--AF------GPGREAELVDRLREDPAAGLsLVAEDDGEIVGHVALSPVDIDGEGPALLLGp 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 770923379  84 ICVGAQWQNRGVASALMRTMIDMCDNwLRVDRIELTVfvdNEPAIAVYKKHGFEIEGTGkryalRNGEYVDAYYMAR 160
Cdd:COG3153   73 LAVDPEYRGQGIGRALMRAALEAARE-RGARAVVLLG---DPSLLPFYERFGFRPAGEL-----GLTLGPDEVFLAK 140
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 54-136 9.17e-15

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: 66.39  E-value: 9.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   54 LVACIDGHVAGHLCIVVaQRPRRSHVADFGICVGAQWQNRGVASALMRTMIDMCDNWlRVDRIELTVFVDNEPAIAVYKK 133
Cdd:pfam00583  36 FVAEEDGELVGFASLSI-IDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARER-GCERIFLEVAADNLAAIALYEK 113


                  ...
gi 770923379  134 HGF 136
Cdd:pfam00583 114 LGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 48-158 6.93e-14

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: 64.27  E-value: 6.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   48 QPGIKQLVACIDGHVAGHlcIVVAQRPRRSHVadFGICVGAQWQNRGVASALMRTMIDMCDNwLRVDRIELTVFVDNEPA 127
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGY--AGVQIVLDEAHI--LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAA 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 770923379  128 IAVYKKHGFEIEGTGKRYALRNGEyvDAYYM 158
Cdd:TIGR01575 103 QALYKKLGFNEIAIRRNYYPDPGE--DAIVM 131
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 4-137 7.13e-14

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 64.67  E-value: 7.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379    4 IVIRHAEPKDYDAIRQIHAQPEVYHNTLQVPHPSEQMWQ------ERLSDQPGIKQLVACIDGHVAGhlCIVVAQRPRRS 77
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREwlariwAADEAERGYGWAIELKDTGFIG--SIGLYDIDGEP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   78 HVADFGICVGAQWQNRGVASALMRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFE 137
Cdd:pfam13302  80 ERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-138 1.06e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 52.46  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   54 LVACIDGHVAGhlCIVVAQRPRRSHVADFGICVGAQWQNRGVASALMRTmidmCDNWLRVDRIELTVFVDNEPAIAVYKK 133
Cdd:pfam13508   6 FVAEDDGKIVG--FAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEA----AEAAAKEGGIKLLELETTNRAAAFYEK 79


                  ....*
gi 770923379  134 HGFEI 138
Cdd:pfam13508  80 LGFEE 84
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 6-138 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 770923379   6 IRHAEPKDYDAIRQIHAQpevyhntlqvphpsEQMWQERLSDQPGIKQLVACIDGHVAGHLCIvvaqrprrSHVADFGIC 85
Cdd:COG0454    3 IRKATPEDINFILLIEAL--------------DAELKAMEGSLAGAEFIAVDDKGEPIGFAGL--------RRLDDKVLE 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 770923379  86 VGA-----QWQNRGVASALMRTMIDmcdnWLR---VDRIELTVFVDNEPAIAVYKKHGFEI 138
Cdd:COG0454   61 LKRlyvlpEYRGKGIGKALLEALLE----WARergCTALELDTLDGNPAAIRFYERLGFKE 117
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 37-137 1.73e-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: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   37 SEQMWQERLsDQPGIKQLVACIDGHVAGHLCIvvaqrPRRSHVADFgiCVGAQWQNRGVASALMRTMIDMCDNWlRVDRI 116
Cdd:pfam13673  18 SPEALRERI-DQGEYFFFVAFEGGQIVGVIAL-----RDRGHISLL--FVDPDYQGQGIGKALLEAVEDYAEKD-GIKLS 88

                          90       100
                  ....*....|....*....|.
gi 770923379  117 ELTVFVDNePAIAVYKKHGFE 137
Cdd:pfam13673  89 ELTVNASP-YAVPFYEKLGFR 108
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
6-154 1.02e-08

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 51.21  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379    6 IRHAEPKDYDAIRQIHAQPevYHNTLQVP---HPSEQMWQERLSDQPGIKQLVACID--GHVAGHlCIVVAQRPRRSHVA 80
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAED--RVNPAFTQeyaHSSIEEFETFLAAYLSPGEIVFGVAesDRLIGY-ATLRQFDYVKTHKA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 770923379   81 DFGICVGAQwQNRGVAsalmRTMIDMCDNWLR----VDRIELTVFVDNEPAIAVYKKHGFEIEGTGKRYALRNGEYVD 154
Cdd:pfam13420  78 ELSFYVVKN-NDEGIN----RELINAIIQYARknqnIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
69-148 7.84e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 47.21  E-value: 7.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379  69 VVAQRPRRSHVA-DFGICVGAQWQNRGVASALMRTMIDmcdnWLR---VDRIELTVFVDNEPAIAVYKKHGFEIEGTGKR 144
Cdd:COG3393    5 MAGVRAESPGVAeISGVYTHPEYRGRGLASALVAALAR----EALargARTPFLYVDADNPAARRLYERLGFRPVGEYAT 80


                 ....
gi 770923379 145 YALR 148
Cdd:COG3393   81 VLFR 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 4-137 1.61e-07

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: 47.68  E-value: 1.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   4 IVIRHAEPKDYDAIRQIHAQPEVYHNTLQVphpseqmwqerlsdqpgikqLVACIDGHVAGhlCIVVAQRPRRS-HVADF 82
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALEEEIGEF--------------------WVAEEDGEIVG--CAALHPLDEDLaELRSL 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 770923379  83 GicVGAQWQNRGVASALMRTMIDMCDNwLRVDRIELTVfvdNEPAIAVYKKHGFE 137
Cdd:COG1246   59 A--VHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLLT---TSAAIHFYEKLGFE 107
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 80-158 1.02e-06

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 46.33  E-value: 1.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 770923379  80 ADFGICVGAQWQNRGVASALMRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGKRYALRNGEYVDAYYM 158
Cdd:PRK15130  84 AEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTIRM 162
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 41-141 2.87e-06

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 44.43  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379   41 WQERLSDQPGIKQLVACIDGHVAGHLCIVvaqRPRRSHVA--------DFGI--CVGAQWQ-NRGVASALMRTMIDMCDN 109
Cdd:pfam13523  34 YLARLAADPHSHPYIGLLDGEPFGYFEIY---WAKEDRLGeyydarpgDRGIhlLIGEPAFrGRGFTTALLRALVHYLFA 110

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 770923379  110 WLRVDRIeltVF---VDNEPAIAVYKKHGFEIEGT 141
Cdd:pfam13523 111 DPRTRRV---VVepdVRNERAIRLLERAGFRKVKE 142
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-119 2.29e-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: 2.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 770923379  54 LVACIDGHVAGhlCIVVAQRPRRSHVADFG-ICVGAQWQNRGVASALMRTMIDMCDNWlRVDRIELT 119
Cdd:cd04301    2 LVAEDDGEIVG--FASLSPDGSGGDTAYIGdLAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
84-140 3.66e-04

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 38.63  E-value: 3.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 770923379  84 ICVGAQWQNRGVASALMRTMIDMCDNwLRVDRIELTVfvdNEPAIAVYKKHGFEIEG 140
Cdd:COG2153   64 VAVLPEYRGQGLGRALMEAAIEEARE-RGARRIVLSA---QAHAVGFYEKLGFVPVG 116
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 6-138 1.66e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 36.40  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379    6 IRHAEPKDYDAIRQIHAqpEVYHNTlqvphPSEQMWQERlsdQPGIKQ---LVACIDGHVAGHLCIVvaqrPRRSHV--A 80
Cdd:pfam13527   1 IRPLTEDEFDEVLRLLE--YAFQDE-----DSPELREYF---RPLLEEgrvLGAFDDGELVSTLALY----PFELNVpgK 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 770923379   81 DF------GICVGAQWQNRGVASALMRTMIDMCdnwlRVDRIELTVFVDNEPAIavYKKHGFEI 138
Cdd:pfam13527  67 TLpaagitGVATYPEYRGRGVMSRLLRRSLEEM----RERGVPLSFLYPSSYPI--YRRFGYEI 124
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
78-159 5.96e-03

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 35.48  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 770923379  78 HVADFGICVGAQWQNRGVASALMRTMIDMCDNWLRVDRIELTVFVDNEPAIAVYKKHGFEIEGTGKRYALRNGEYVDAYY 157
Cdd:PRK10809 103 HACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVL 182


                 ..
gi 770923379 158 MA 159
Cdd:PRK10809 183 TA 184
 
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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