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Conserved domains on  [gi|1390927797|gb|PWL06201|]
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N-acetyltransferase [Staphylococcus aureus]

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, ...
1-154 4.21e-20

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: 81.97  E-value: 4.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390927797   1 MINTERLNLMIPSSSHLIELYNICSHPQANIYTPkGLHNSKLDTQRWIEKWRNHWQQYQFGYFVLVKKIDCSVIGICGYE 80
Cdd:COG1670     2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLP-GPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390927797  81 YRQLKQETVlNLFYKLHPSFEGQGYACEAITAITNFV-NYIDQETVkVIRTNKCNQRSINLAERLKFKRDKAMDD 154
Cdd:COG1670    81 DIDRANRSA-EIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRV-EAEVDPDNTASIRVLEKLGFRLEGTLRD 153
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-154 4.21e-20

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: 81.97  E-value: 4.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390927797   1 MINTERLNLMIPSSSHLIELYNICSHPQANIYTPkGLHNSKLDTQRWIEKWRNHWQQYQFGYFVLVKKIDCSVIGICGYE 80
Cdd:COG1670     2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLP-GPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390927797  81 YRQLKQETVlNLFYKLHPSFEGQGYACEAITAITNFV-NYIDQETVkVIRTNKCNQRSINLAERLKFKRDKAMDD 154
Cdd:COG1670    81 DIDRANRSA-EIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRV-EAEVDPDNTASIRVLEKLGFRLEGTLRD 153
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
6-147 3.48e-15

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 68.14  E-value: 3.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390927797   6 RLNLMIPSSSHLIELYNICSHPQANIYTPKGlHNSKLDTQRWIEK-WRNHWQQYQFGYFVLVKkiDCSVIGICGYEYRQL 84
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPW-PLTLEEAREWLARiWAADEAERGYGWAIELK--DTGFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390927797  85 KQETVlNLFYKLHPSFEGQGYACEAITAITNFV-NYIDQETVkVIRTNKCNQRSINLAERLKFK 147
Cdd:pfam13302  78 EPERA-ELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRL-VARIDPENTASRRVLEKLGFK 139
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-154 4.21e-20

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: 81.97  E-value: 4.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390927797   1 MINTERLNLMIPSSSHLIELYNICSHPQANIYTPkGLHNSKLDTQRWIEKWRNHWQQYQFGYFVLVKKIDCSVIGICGYE 80
Cdd:COG1670     2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLP-GPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390927797  81 YRQLKQETVlNLFYKLHPSFEGQGYACEAITAITNFV-NYIDQETVkVIRTNKCNQRSINLAERLKFKRDKAMDD 154
Cdd:COG1670    81 DIDRANRSA-EIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRV-EAEVDPDNTASIRVLEKLGFRLEGTLRD 153
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
6-147 3.48e-15

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 68.14  E-value: 3.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390927797   6 RLNLMIPSSSHLIELYNICSHPQANIYTPKGlHNSKLDTQRWIEK-WRNHWQQYQFGYFVLVKkiDCSVIGICGYEYRQL 84
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPW-PLTLEEAREWLARiWAADEAERGYGWAIELK--DTGFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390927797  85 KQETVlNLFYKLHPSFEGQGYACEAITAITNFV-NYIDQETVkVIRTNKCNQRSINLAERLKFK 147
Cdd:pfam13302  78 EPERA-ELGYWLGPDYWGKGYATEAVRALLEYAfEELGLPRL-VARIDPENTASRRVLEKLGFK 139
 
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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