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Conserved domains on  [gi|2102610590|ref|WP_223914999|]
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MULTISPECIES: GNAT family N-acetyltransferase [Aeromonas]

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, ...
45-216 2.00e-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: 108.93  E-value: 2.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590  45 LHGWGCRLEPLDPErHLGDLWQAFSADsgAMWTYLTSGPFADETAMGvWLREVAT---KRDPQFYGIIDEGSGRALGLAS 121
Cdd:COG1670     3 LETERLRLRPLRPE-DAEALAELLNDP--EVARYLPGPPYSLEEARA-WLERLLAdwaDGGALPFAIEDKEDGELIGVVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590 122 YLRIDPLAGSIEVGWlHFSPAMQQSRLATAAMVLMMANAFA-LGYRRYEWKCNALNLPSRQAALRLGFHYEGTFRQARVD 200
Cdd:COG1670    79 LYDIDRANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEeLGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI 157
                         170
                  ....*....|....*.
gi 2102610590 201 KGHNRDTAWFSVIDSE 216
Cdd:COG1670   158 DGRYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
45-216 2.00e-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: 108.93  E-value: 2.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590  45 LHGWGCRLEPLDPErHLGDLWQAFSADsgAMWTYLTSGPFADETAMGvWLREVAT---KRDPQFYGIIDEGSGRALGLAS 121
Cdd:COG1670     3 LETERLRLRPLRPE-DAEALAELLNDP--EVARYLPGPPYSLEEARA-WLERLLAdwaDGGALPFAIEDKEDGELIGVVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590 122 YLRIDPLAGSIEVGWlHFSPAMQQSRLATAAMVLMMANAFA-LGYRRYEWKCNALNLPSRQAALRLGFHYEGTFRQARVD 200
Cdd:COG1670    79 LYDIDRANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEeLGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI 157
                         170
                  ....*....|....*.
gi 2102610590 201 KGHNRDTAWFSVIDSE 216
Cdd:COG1670   158 DGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
51-189 4.98e-09

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 53.50  E-value: 4.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590  51 RLEPLDPErHLGDLWQAFSadSGAMWTYLTSGPFADETAMGVWLREVATKRDPQFYG-IIDEGSGRALGLASYLRIDPLA 129
Cdd:pfam13302   3 LLRPLTEE-DAEALFELLS--DPEVMRYGVPWPLTLEEAREWLARIWAADEAERGYGwAIELKDTGFIGSIGLYDIDGEP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2102610590 130 GSIEVGWLhFSPAMQQSRLATAAMVLMMANAFA-LGYRRYEWKCNALNLPSRQAALRLGFH 189
Cdd:pfam13302  80 ERAELGYW-LGPDYWGKGYATEAVRALLEYAFEeLGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
114-197 2.66e-04

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 40.51  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590 114 GRALGLASYLRIDPLAGSIEVG-WLhfSPAMQQSRLATAAMVLMMANAFALG-YRRYEWKCNALNLPSRQAALRLGFHYE 191
Cdd:PRK10151   76 DELIGVLSFNRIEPLNKTAYIGyWL--DESHQGQGIISQALQALIHHYAQSGeLRRFVIKCRVDNPASNQVALRNGFTLE 153

                  ....*.
gi 2102610590 192 GTFRQA 197
Cdd:PRK10151  154 GCLKQA 159
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
45-216 2.00e-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: 108.93  E-value: 2.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590  45 LHGWGCRLEPLDPErHLGDLWQAFSADsgAMWTYLTSGPFADETAMGvWLREVAT---KRDPQFYGIIDEGSGRALGLAS 121
Cdd:COG1670     3 LETERLRLRPLRPE-DAEALAELLNDP--EVARYLPGPPYSLEEARA-WLERLLAdwaDGGALPFAIEDKEDGELIGVVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590 122 YLRIDPLAGSIEVGWlHFSPAMQQSRLATAAMVLMMANAFA-LGYRRYEWKCNALNLPSRQAALRLGFHYEGTFRQARVD 200
Cdd:COG1670    79 LYDIDRANRSAEIGY-WLAPAYWGKGYATEALRALLDYAFEeLGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVI 157
                         170
                  ....*....|....*.
gi 2102610590 201 KGHNRDTAWFSVIDSE 216
Cdd:COG1670   158 DGRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
51-189 4.98e-09

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 53.50  E-value: 4.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590  51 RLEPLDPErHLGDLWQAFSadSGAMWTYLTSGPFADETAMGVWLREVATKRDPQFYG-IIDEGSGRALGLASYLRIDPLA 129
Cdd:pfam13302   3 LLRPLTEE-DAEALFELLS--DPEVMRYGVPWPLTLEEAREWLARIWAADEAERGYGwAIELKDTGFIGSIGLYDIDGEP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2102610590 130 GSIEVGWLhFSPAMQQSRLATAAMVLMMANAFA-LGYRRYEWKCNALNLPSRQAALRLGFH 189
Cdd:pfam13302  80 ERAELGYW-LGPDYWGKGYATEAVRALLEYAFEeLGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
63-210 8.84e-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: 8.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590  63 DLWQAFSADSGAMWTYLTsgpfADETAMGVWLREVatkRDPQFYGIIDEGSGRALGLASYLRIDPLAGSIEVGWLHF--S 140
Cdd:COG1247    17 AIYNEAIAEGTATFETEP----PSEEEREAWFAAI---LAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAEESIyvD 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590 141 PAMQQSRLATAAMVLMMANAFALGYRRYEWKCNALNLPSRQAALRLGFHYEGTFRQARVDKGHNRDTAWF 210
Cdd:COG1247    90 PDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLM 159
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
114-197 2.66e-04

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 40.51  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2102610590 114 GRALGLASYLRIDPLAGSIEVG-WLhfSPAMQQSRLATAAMVLMMANAFALG-YRRYEWKCNALNLPSRQAALRLGFHYE 191
Cdd:PRK10151   76 DELIGVLSFNRIEPLNKTAYIGyWL--DESHQGQGIISQALQALIHHYAQSGeLRRFVIKCRVDNPASNQVALRNGFTLE 153

                  ....*.
gi 2102610590 192 GTFRQA 197
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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