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Conserved domains on  [gi|516290119|ref|WP_017693426|]
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MULTISPECIES: GNAT family N-acetyltransferase [Enterobacter]

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, ...
4-175 2.59e-25

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: 95.84  E-value: 2.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516290119   4 PTLTTERLLLKPLVAADAAQIQQRYPRWEIVRYMVasvPWPYPENGAENYVNNvALPDMAKGIAWFWTIRRREApDELMG 83
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLP---GPPYSLEEARAWLER-LLADWADGGALPFAIEDKED-GELIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516290119  84 LICLYDVEDNNR----GFWLAPEFQGQGYMREASIAATDYWFNTLNKPVLRAPKAAANSRSRRISDSSGMRLIRTEKKAY 159
Cdd:COG1670   76 VVGLYDIDRANRsaeiGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155
                        170
                 ....*....|....*...
gi 516290119 160 VSG--LLDSELWEITRDE 175
Cdd:COG1670  156 VIDgrYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
4-175 2.59e-25

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: 95.84  E-value: 2.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516290119   4 PTLTTERLLLKPLVAADAAQIQQRYPRWEIVRYMVasvPWPYPENGAENYVNNvALPDMAKGIAWFWTIRRREApDELMG 83
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLP---GPPYSLEEARAWLER-LLADWADGGALPFAIEDKED-GELIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516290119  84 LICLYDVEDNNR----GFWLAPEFQGQGYMREASIAATDYWFNTLNKPVLRAPKAAANSRSRRISDSSGMRLIRTEKKAY 159
Cdd:COG1670   76 VVGLYDIDRANRsaeiGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155
                        170
                 ....*....|....*...
gi 516290119 160 VSG--LLDSELWEITRDE 175
Cdd:COG1670  156 VIDgrYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
10-137 8.18e-23

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 88.56  E-value: 8.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516290119   10 RLLLKPLVAADAAQIQQRYPRWEIVRYMVasvPWPYPENGAENYVNNvALPDMAKGIAWFWTIRRREapDELMGLICLYD 89
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGV---PWPLTLEEAREWLAR-IWAADEAERGYGWAIELKD--TGFIGSIGLYD 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 516290119   90 VEDNNR----GFWLAPEFQGQGYMREASIAATDYWFNTLNKPVLRAPKAAAN 137
Cdd:pfam13302  75 IDGEPEraelGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPEN 126
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
4-175 2.59e-25

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: 95.84  E-value: 2.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516290119   4 PTLTTERLLLKPLVAADAAQIQQRYPRWEIVRYMVasvPWPYPENGAENYVNNvALPDMAKGIAWFWTIRRREApDELMG 83
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLP---GPPYSLEEARAWLER-LLADWADGGALPFAIEDKED-GELIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516290119  84 LICLYDVEDNNR----GFWLAPEFQGQGYMREASIAATDYWFNTLNKPVLRAPKAAANSRSRRISDSSGMRLIRTEKKAY 159
Cdd:COG1670   76 VVGLYDIDRANRsaeiGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155
                        170
                 ....*....|....*...
gi 516290119 160 VSG--LLDSELWEITRDE 175
Cdd:COG1670  156 VIDgrYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
10-137 8.18e-23

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 88.56  E-value: 8.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516290119   10 RLLLKPLVAADAAQIQQRYPRWEIVRYMVasvPWPYPENGAENYVNNvALPDMAKGIAWFWTIRRREapDELMGLICLYD 89
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGV---PWPLTLEEAREWLAR-IWAADEAERGYGWAIELKD--TGFIGSIGLYD 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 516290119   90 VEDNNR----GFWLAPEFQGQGYMREASIAATDYWFNTLNKPVLRAPKAAAN 137
Cdd:pfam13302  75 IDGEPEraelGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPEN 126
 
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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