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Conserved domains on  [gi|1330017218|ref|WP_102270858|]
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GNAT family N-acetyltransferase, partial [Vibrio lentus]

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, ...
8-118 2.87e-15

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: 67.72  E-value: 2.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330017218   8 DEGSEWFAIYFK--NQFGGVFGIKSIDFDSKACELGYWLSDNARGNRVIGQVLDVVIPYLLNDHAVRVVEFHCLESNSAS 85
Cdd:COG1670    57 DGGALPFAIEDKedGELIGVVGLYDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTAS 136
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1330017218  86 IKIVKRAGATLKRKICNTLDVPNKEQLMCIYAL 118
Cdd:COG1670   137 IRVLEKLGFRLEGTLRDALVIDGRYRDHVLYSL 169
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
8-118 2.87e-15

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: 67.72  E-value: 2.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330017218   8 DEGSEWFAIYFK--NQFGGVFGIKSIDFDSKACELGYWLSDNARGNRVIGQVLDVVIPYLLNDHAVRVVEFHCLESNSAS 85
Cdd:COG1670    57 DGGALPFAIEDKedGELIGVVGLYDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTAS 136
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1330017218  86 IKIVKRAGATLKRKICNTLDVPNKEQLMCIYAL 118
Cdd:COG1670   137 IRVLEKLGFRLEGTLRDALVIDGRYRDHVLYSL 169
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
1-95 1.51e-11

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 57.36  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330017218   1 SRSHPGGDEGSEWFAIYFKNQ-FGGVFGIKSIDFDSKACELGYWLSDNARGNRVIGQVLDVVIPYLLNDHAVRVVEFHCL 79
Cdd:pfam13302  44 RIWAADEAERGYGWAIELKDTgFIGSIGLYDIDGEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARID 123
                          90
                  ....*....|....*.
gi 1330017218  80 ESNSASIKIVKRAGAT 95
Cdd:pfam13302 124 PENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
14-96 5.41e-05

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 40.51  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330017218  14 FAIYFKNQFGGVFGIKSIDFDSKACELGYWLSDNARGNRVIGQVLDVVIPYLLNDHAVRVVEFHCLESNSASIKIVKRAG 93
Cdd:PRK10151   70 FMIFKEDELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNG 149

                  ...
gi 1330017218  94 ATL 96
Cdd:PRK10151  150 FTL 152
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
8-118 2.87e-15

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: 67.72  E-value: 2.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330017218   8 DEGSEWFAIYFK--NQFGGVFGIKSIDFDSKACELGYWLSDNARGNRVIGQVLDVVIPYLLNDHAVRVVEFHCLESNSAS 85
Cdd:COG1670    57 DGGALPFAIEDKedGELIGVVGLYDIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTAS 136
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1330017218  86 IKIVKRAGATLKRKICNTLDVPNKEQLMCIYAL 118
Cdd:COG1670   137 IRVLEKLGFRLEGTLRDALVIDGRYRDHVLYSL 169
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
1-95 1.51e-11

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 57.36  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330017218   1 SRSHPGGDEGSEWFAIYFKNQ-FGGVFGIKSIDFDSKACELGYWLSDNARGNRVIGQVLDVVIPYLLNDHAVRVVEFHCL 79
Cdd:pfam13302  44 RIWAADEAERGYGWAIELKDTgFIGSIGLYDIDGEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARID 123
                          90
                  ....*....|....*.
gi 1330017218  80 ESNSASIKIVKRAGAT 95
Cdd:pfam13302 124 PENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
14-96 5.41e-05

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 40.51  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330017218  14 FAIYFKNQFGGVFGIKSIDFDSKACELGYWLSDNARGNRVIGQVLDVVIPYLLNDHAVRVVEFHCLESNSASIKIVKRAG 93
Cdd:PRK10151   70 FMIFKEDELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNG 149

                  ...
gi 1330017218  94 ATL 96
Cdd:PRK10151  150 FTL 152
 
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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