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Conserved domains on  [gi|1067546601|gb|OEG08300|]
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GNAT family N-acetyltransferase [Aeromonas caviae]

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, ...
37-203 2.67e-29

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: 108.16  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601  37 CRLEPLDPErHLGDLWQAFSADsgAMWTYLTSGPFADEVAMGvWLREVAT---KRDPQFYGIIDEGSGRALGLASYLRID 113
Cdd:COG1670     8 LRLRPLRPE-DAEALAELLNDP--EVARYLPGPPYSLEEARA-WLERLLAdwaDGGALPFAIEDKEDGELIGVVGLYDID 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601 114 PLAGSIEVGWlHFSPAMQQSRLATAAMVLMMANAFA-LGYRRYEWKCNALNLPSRQAALRLGFHYEGTFRQARVDKGHNR 192
Cdd:COG1670    84 RANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEeLGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYR 162
                         170
                  ....*....|.
gi 1067546601 193 DTAWFSVIDSE 203
Cdd:COG1670   163 DHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
37-203 2.67e-29

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: 108.16  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601  37 CRLEPLDPErHLGDLWQAFSADsgAMWTYLTSGPFADEVAMGvWLREVAT---KRDPQFYGIIDEGSGRALGLASYLRID 113
Cdd:COG1670     8 LRLRPLRPE-DAEALAELLNDP--EVARYLPGPPYSLEEARA-WLERLLAdwaDGGALPFAIEDKEDGELIGVVGLYDID 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601 114 PLAGSIEVGWlHFSPAMQQSRLATAAMVLMMANAFA-LGYRRYEWKCNALNLPSRQAALRLGFHYEGTFRQARVDKGHNR 192
Cdd:COG1670    84 RANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEeLGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYR 162
                         170
                  ....*....|.
gi 1067546601 193 DTAWFSVIDSE 203
Cdd:COG1670   163 DHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
38-176 6.00e-09

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 53.12  E-value: 6.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601  38 RLEPLDPErHLGDLWQAFSadSGAMWTYLTSGPFADEVAMGVWLREVATKRDPQFYG-IIDEGSGRALGLASYLRIDPLA 116
Cdd:pfam13302   3 LLRPLTEE-DAEALFELLS--DPEVMRYGVPWPLTLEEAREWLARIWAADEAERGYGwAIELKDTGFIGSIGLYDIDGEP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067546601 117 GSIEVGWLhFSPAMQQSRLATAAMVLMMANAFA-LGYRRYEWKCNALNLPSRQAALRLGFH 176
Cdd:pfam13302  80 ERAELGYW-LGPDYWGKGYATEAVRALLEYAFEeLGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
101-184 2.96e-04

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 40.51  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601 101 GRALGLASYLRIDPLAGSIEVG-WLhfSPAMQQSRLATAAMVLMMANAFALG-YRRYEWKCNALNLPSRQAALRLGFHYE 178
Cdd:PRK10151   76 DELIGVLSFNRIEPLNKTAYIGyWL--DESHQGQGIISQALQALIHHYAQSGeLRRFVIKCRVDNPASNQVALRNGFTLE 153

                  ....*.
gi 1067546601 179 GTFRQA 184
Cdd:PRK10151  154 GCLKQA 159
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
37-203 2.67e-29

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: 108.16  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601  37 CRLEPLDPErHLGDLWQAFSADsgAMWTYLTSGPFADEVAMGvWLREVAT---KRDPQFYGIIDEGSGRALGLASYLRID 113
Cdd:COG1670     8 LRLRPLRPE-DAEALAELLNDP--EVARYLPGPPYSLEEARA-WLERLLAdwaDGGALPFAIEDKEDGELIGVVGLYDID 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601 114 PLAGSIEVGWlHFSPAMQQSRLATAAMVLMMANAFA-LGYRRYEWKCNALNLPSRQAALRLGFHYEGTFRQARVDKGHNR 192
Cdd:COG1670    84 RANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEeLGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYR 162
                         170
                  ....*....|.
gi 1067546601 193 DTAWFSVIDSE 203
Cdd:COG1670   163 DHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
38-176 6.00e-09

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 53.12  E-value: 6.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601  38 RLEPLDPErHLGDLWQAFSadSGAMWTYLTSGPFADEVAMGVWLREVATKRDPQFYG-IIDEGSGRALGLASYLRIDPLA 116
Cdd:pfam13302   3 LLRPLTEE-DAEALFELLS--DPEVMRYGVPWPLTLEEAREWLARIWAADEAERGYGwAIELKDTGFIGSIGLYDIDGEP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067546601 117 GSIEVGWLhFSPAMQQSRLATAAMVLMMANAFA-LGYRRYEWKCNALNLPSRQAALRLGFH 176
Cdd:pfam13302  80 ERAELGYW-LGPDYWGKGYATEAVRALLEYAFEeLGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
50-197 9.16e-08

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 50.38  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601  50 DLWQAFSADSGAmwTYLTSGPFADEVAmgVWLREVatkRDPQFYGIIDEGSGRALGLASYLRIDPLAGSIEVGWLHF--S 127
Cdd:COG1247    17 AIYNEAIAEGTA--TFETEPPSEEERE--AWFAAI---LAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAEESIyvD 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601 128 PAMQQSRLATAAMVLMMANAFALGYRRYEWKCNALNLPSRQAALRLGFHYEGTFRQARVDKGHNRDTAWF 197
Cdd:COG1247    90 PDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLM 159
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
101-184 2.96e-04

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 40.51  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067546601 101 GRALGLASYLRIDPLAGSIEVG-WLhfSPAMQQSRLATAAMVLMMANAFALG-YRRYEWKCNALNLPSRQAALRLGFHYE 178
Cdd:PRK10151   76 DELIGVLSFNRIEPLNKTAYIGyWL--DESHQGQGIISQALQALIHHYAQSGeLRRFVIKCRVDNPASNQVALRNGFTLE 153

                  ....*.
gi 1067546601 179 GTFRQA 184
Cdd:PRK10151  154 GCLKQA 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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