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Conserved domains on  [gi|491954714|ref|WP_005689519|]
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GNAT family N-acetyltransferase [Lacticaseibacillus rhamnosus]

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, ...
11-174 3.02e-43

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: 141.68  E-value: 3.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714  11 TERLVLAPVTIDDAPDMFEYASNPENAYYVFETNKTLGDTKDIIQKI---FIENGLGKYGIFLNE--KLIGTIYFLNLDD 85
Cdd:COG1670    5 TERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLladWADGGALPFAIEDKEdgELIGVVGLYDIDR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714  86 RNKSAELSYVLNKKFEGHGYATEAAIKLRDIFFNELEGERLYARHTFDNLKSMNLMARIGMKIEGTLRKSYCFHGRQVDL 165
Cdd:COG1670   85 ANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164

                 ....*....
gi 491954714 166 AIWSMTRDD 174
Cdd:COG1670  165 VLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
11-174 3.02e-43

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: 141.68  E-value: 3.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714  11 TERLVLAPVTIDDAPDMFEYASNPENAYYVFETNKTLGDTKDIIQKI---FIENGLGKYGIFLNE--KLIGTIYFLNLDD 85
Cdd:COG1670    5 TERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLladWADGGALPFAIEDKEdgELIGVVGLYDIDR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714  86 RNKSAELSYVLNKKFEGHGYATEAAIKLRDIFFNELEGERLYARHTFDNLKSMNLMARIGMKIEGTLRKSYCFHGRQVDL 165
Cdd:COG1670   85 ANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164

                 ....*....
gi 491954714 166 AIWSMTRDD 174
Cdd:COG1670  165 VLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
13-147 2.72e-33

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 115.14  E-value: 2.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714   13 RLVLAPVTIDDAPDMFEYASNPENAYYVFETNKTLGDTKDIIQKIFIENGLGK---YGIFLNE-KLIGTIYFLNLDDRNK 88
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEAERgygWAIELKDtGFIGSIGLYDIDGEPE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 491954714   89 SAELSYVLNKKFEGHGYATEAAIKLRDIFFNELEGERLYARHTFDNLKSMNLMARIGMK 147
Cdd:pfam13302  81 RAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
75-160 3.56e-03

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 36.31  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714  75 IGTIYFLNLDDRNKSAELSYVLNKKFEGHGYATEAAIKLRDIFFNELEGERLYARHTFDNLKSMNLMARIGMKIEGTLRK 154
Cdd:PRK15130  69 AGLVELVEINHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIH 148

                 ....*.
gi 491954714 155 SYCFHG 160
Cdd:PRK15130 149 EFFING 154
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
11-174 3.02e-43

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: 141.68  E-value: 3.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714  11 TERLVLAPVTIDDAPDMFEYASNPENAYYVFETNKTLGDTKDIIQKI---FIENGLGKYGIFLNE--KLIGTIYFLNLDD 85
Cdd:COG1670    5 TERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLladWADGGALPFAIEDKEdgELIGVVGLYDIDR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714  86 RNKSAELSYVLNKKFEGHGYATEAAIKLRDIFFNELEGERLYARHTFDNLKSMNLMARIGMKIEGTLRKSYCFHGRQVDL 165
Cdd:COG1670   85 ANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164

                 ....*....
gi 491954714 166 AIWSMTRDD 174
Cdd:COG1670  165 VLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
13-147 2.72e-33

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 115.14  E-value: 2.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714   13 RLVLAPVTIDDAPDMFEYASNPENAYYVFETNKTLGDTKDIIQKIFIENGLGK---YGIFLNE-KLIGTIYFLNLDDRNK 88
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEAERgygWAIELKDtGFIGSIGLYDIDGEPE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 491954714   89 SAELSYVLNKKFEGHGYATEAAIKLRDIFFNELEGERLYARHTFDNLKSMNLMARIGMK 147
Cdd:pfam13302  81 RAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
66-164 4.36e-04

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 38.89  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714   66 YGIFLNEKLIGTIYFLNLDDR-NKSAELSYVLNKKFEgHGYATEAAIKLRDIFFNELEGERLYARHTFDNLKSMNLMARI 144
Cdd:pfam13420  52 FGVAESDRLIGYATLRQFDYVkTHKAELSFYVVKNND-EGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAI 130
                          90       100
                  ....*....|....*....|
gi 491954714  145 GMKIEGTLRKSYCFHGRQVD 164
Cdd:pfam13420 131 GFEWLGIERNAIKKNGRWID 150
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
75-160 3.56e-03

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 36.31  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714  75 IGTIYFLNLDDRNKSAELSYVLNKKFEGHGYATEAAIKLRDIFFNELEGERLYARHTFDNLKSMNLMARIGMKIEGTLRK 154
Cdd:PRK15130  69 AGLVELVEINHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIH 148

                 ....*.
gi 491954714 155 SYCFHG 160
Cdd:PRK15130 149 EFFING 154
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
66-168 4.62e-03

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 36.28  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954714  66 YGIFLNEKLIGTIYFLNLDDRNKSAELSYVLNKKFEGHGYATEAAIKLRDIFFNELEGERLYARHTFDNLKSMNLMARIG 145
Cdd:PRK10151  70 FMIFKEDELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNG 149
                         90       100
                 ....*....|....*....|...
gi 491954714 146 MKIEGTLRKSYCFHGRQVDLAIW 168
Cdd:PRK10151 150 FTLEGCLKQAEYLNGAYDDVNLY 172
 
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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