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Conserved domains on  [gi|488981188|ref|WP_002892021|]
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MULTISPECIES: GNAT family N-acetyltransferase [Klebsiella]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
28-201 5.11e-37

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: 127.81  E-value: 5.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981188  28 VLQGSRCRLEPLTLAHASDLFAAHQlapDARSWTWLLREPESnLAEFSAWVEQVATLA---DPIHFAVVDQQRGKAVGSL 104
Cdd:COG1670    2 TLETERLRLRPLRPEDAEALAELLN---DPEVARYLPGPPYS-LEEARAWLERLLADWadgGALPFAIEDKEDGELIGVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981188 105 ALMRIDIAHGVVEVGhVHFSPLLSRTAMATEAHWLLMQYVFDTLGYRRYEWKCNSLNIPSARAARRLGFQYEGRFRQALV 184
Cdd:COG1670   78 GLYDIDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
                        170
                 ....*....|....*..
gi 488981188 185 SKGHNRDTDWFSVIDGE 201
Cdd:COG1670  157 IDGRYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
28-201 5.11e-37

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: 127.81  E-value: 5.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981188  28 VLQGSRCRLEPLTLAHASDLFAAHQlapDARSWTWLLREPESnLAEFSAWVEQVATLA---DPIHFAVVDQQRGKAVGSL 104
Cdd:COG1670    2 TLETERLRLRPLRPEDAEALAELLN---DPEVARYLPGPPYS-LEEARAWLERLLADWadgGALPFAIEDKEDGELIGVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981188 105 ALMRIDIAHGVVEVGhVHFSPLLSRTAMATEAHWLLMQYVFDTLGYRRYEWKCNSLNIPSARAARRLGFQYEGRFRQALV 184
Cdd:COG1670   78 GLYDIDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
                        170
                 ....*....|....*..
gi 488981188 185 SKGHNRDTDWFSVIDGE 201
Cdd:COG1670  157 IDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
33-174 2.61e-14

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 67.37  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981188   33 RCRLEPLTLAHASDLFaahQLAPDARSWTWLLREPeSNLAEFSAWVE---QVATLADPIHFAVVDQQRGkAVGSLALMRI 109
Cdd:pfam13302   1 RLLLRPLTEEDAEALF---ELLSDPEVMRYGVPWP-LTLEEAREWLAriwAADEAERGYGWAIELKDTG-FIGSIGLYDI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488981188  110 DIAHGVVEVGHVhFSPLLSRTAMATEAHWLLMQYVFDTLGYRRYEWKCNSLNIPSARAARRLGFQ 174
Cdd:pfam13302  76 DGEPERAELGYW-LGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
28-201 5.11e-37

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: 127.81  E-value: 5.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981188  28 VLQGSRCRLEPLTLAHASDLFAAHQlapDARSWTWLLREPESnLAEFSAWVEQVATLA---DPIHFAVVDQQRGKAVGSL 104
Cdd:COG1670    2 TLETERLRLRPLRPEDAEALAELLN---DPEVARYLPGPPYS-LEEARAWLERLLADWadgGALPFAIEDKEDGELIGVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981188 105 ALMRIDIAHGVVEVGhVHFSPLLSRTAMATEAHWLLMQYVFDTLGYRRYEWKCNSLNIPSARAARRLGFQYEGRFRQALV 184
Cdd:COG1670   78 GLYDIDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
                        170
                 ....*....|....*..
gi 488981188 185 SKGHNRDTDWFSVIDGE 201
Cdd:COG1670  157 IDGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
33-174 2.61e-14

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 67.37  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981188   33 RCRLEPLTLAHASDLFaahQLAPDARSWTWLLREPeSNLAEFSAWVE---QVATLADPIHFAVVDQQRGkAVGSLALMRI 109
Cdd:pfam13302   1 RLLLRPLTEEDAEALF---ELLSDPEVMRYGVPWP-LTLEEAREWLAriwAADEAERGYGWAIELKDTG-FIGSIGLYDI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488981188  110 DIAHGVVEVGHVhFSPLLSRTAMATEAHWLLMQYVFDTLGYRRYEWKCNSLNIPSARAARRLGFQ 174
Cdd:pfam13302  76 DGEPERAELGYW-LGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
35-195 1.36e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 43.83  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981188  35 RLEPLTLAHASDLFAAHQLAPDARSWTWLLREPEsnLAEFSAWVEQVATLADPIHFAVVDqqrgkavgslalmridiahG 114
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGTATFETEPPS--EEEREAWFAAILAPGRPVLVAEED-------------------G 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981188 115 VVeVGHVHFSPLLSRTAMATEAHW---------------LLMQYVFD---TLGYRRYEWKCNSLNIPSARAARRLGFQYE 176
Cdd:COG1247   62 EV-VGFASLGPFRPRPAYRGTAEEsiyvdpdargrgigrALLEALIErarARGYRRLVAVVLADNEASIALYEKLGFEEV 140
                        170
                 ....*....|....*....
gi 488981188 177 GRFRQALVSKGHNRDTDWF 195
Cdd:COG1247  141 GTLPEVGFKFGRWLDLVLM 159
 
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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