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Conserved domains on  [gi|556425669|ref|WP_023310596|]
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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, ...
27-201 7.08e-37

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: 127.42  E-value: 7.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669  27 VVLQGHYCRLEPLRVEHAHALFSAYSLAEDTRSWTWLLREPDATAEEFAEWVASVSElSDPIHFTVMDNRTQSPVGTLSL 106
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWAD-GGALPFAIEDKEDGELIGVVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669 107 MRIDPKNGVVEVGhVHFSPLLSRTPGSTEAQYLLMRYVFDTLGYRRYEWKCNSLNEPSRKAALRLGFQFEGRFRQALVIK 186
Cdd:COG1670   80 YDIDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVID 158
                        170
                 ....*....|....*
gi 556425669 187 GRNRDTDWFSILDKE 201
Cdd:COG1670  159 GRYRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
27-201 7.08e-37

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: 127.42  E-value: 7.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669  27 VVLQGHYCRLEPLRVEHAHALFSAYSLAEDTRSWTWLLREPDATAEEFAEWVASVSElSDPIHFTVMDNRTQSPVGTLSL 106
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWAD-GGALPFAIEDKEDGELIGVVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669 107 MRIDPKNGVVEVGhVHFSPLLSRTPGSTEAQYLLMRYVFDTLGYRRYEWKCNSLNEPSRKAALRLGFQFEGRFRQALVIK 186
Cdd:COG1670   80 YDIDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVID 158
                        170
                 ....*....|....*
gi 556425669 187 GRNRDTDWFSILDKE 201
Cdd:COG1670  159 GRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
35-174 1.23e-11

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 60.44  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669   35 RLEPLRVEHAHALFSAYSLAEDTRSWTWLLREPDATAEEFAEWVASVSElSDPIHFTVMDnRTQSPVGTLSLMRIDPKNG 114
Cdd:pfam13302   3 LLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEA-ERGYGWAIEL-KDTGFIGSIGLYDIDGEPE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556425669  115 VVEVGHVhfspLLSRTPGS---TEAQYLLMRYVFDTLGYRRYEWKCNSLNEPSRKAALRLGFQ 174
Cdd:pfam13302  81 RAELGYW----LGPDYWGKgyaTEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
101-191 5.02e-05

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 42.44  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669 101 VGTLSLMRIDPKNGVVEVGH-----VHFSPLLSRtpgSTEAqylLMRYVFDTLGYRRYEWKCNSLNEPSRKAALRLGFQF 175
Cdd:PRK10151  79 IGVLSFNRIEPLNKTAYIGYwldesHQGQGIISQ---ALQA---LIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTL 152
                         90
                 ....*....|....*.
gi 556425669 176 EGRFRQALVIKGRNRD 191
Cdd:PRK10151 153 EGCLKQAEYLNGAYDD 168
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
27-201 7.08e-37

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: 127.42  E-value: 7.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669  27 VVLQGHYCRLEPLRVEHAHALFSAYSLAEDTRSWTWLLREPDATAEEFAEWVASVSElSDPIHFTVMDNRTQSPVGTLSL 106
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWAD-GGALPFAIEDKEDGELIGVVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669 107 MRIDPKNGVVEVGhVHFSPLLSRTPGSTEAQYLLMRYVFDTLGYRRYEWKCNSLNEPSRKAALRLGFQFEGRFRQALVIK 186
Cdd:COG1670   80 YDIDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVID 158
                        170
                 ....*....|....*
gi 556425669 187 GRNRDTDWFSILDKE 201
Cdd:COG1670  159 GRYRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
35-174 1.23e-11

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 60.44  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669   35 RLEPLRVEHAHALFSAYSLAEDTRSWTWLLREPDATAEEFAEWVASVSElSDPIHFTVMDnRTQSPVGTLSLMRIDPKNG 114
Cdd:pfam13302   3 LLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARIWAADEA-ERGYGWAIEL-KDTGFIGSIGLYDIDGEPE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556425669  115 VVEVGHVhfspLLSRTPGS---TEAQYLLMRYVFDTLGYRRYEWKCNSLNEPSRKAALRLGFQ 174
Cdd:pfam13302  81 RAELGYW----LGPDYWGKgyaTEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
35-195 6.23e-07

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 47.68  E-value: 6.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669  35 RLEPLRVEHAHALFSAYSLAEDTRSWTWLLREPdaTAEEFAEWVASVSELSDPIHFTVMDNRtqsPVGTLSLMRI---DP 111
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGTATFETEPP--SEEEREAWFAAILAPGRPVLVAEEDGE---VVGFASLGPFrprPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669 112 KNGVVEVGhVHFSPllsrtpgstEAQ-----YLLMRYVFD---TLGYRRYEWKCNSLNEPSRKAALRLGFQFEGRFRQAL 183
Cdd:COG1247   78 YRGTAEES-IYVDP---------DARgrgigRALLEALIErarARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVG 147
                        170
                 ....*....|..
gi 556425669 184 VIKGRNRDTDWF 195
Cdd:COG1247  148 FKFGRWLDLVLM 159
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
101-191 5.02e-05

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 42.44  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556425669 101 VGTLSLMRIDPKNGVVEVGH-----VHFSPLLSRtpgSTEAqylLMRYVFDTLGYRRYEWKCNSLNEPSRKAALRLGFQF 175
Cdd:PRK10151  79 IGVLSFNRIEPLNKTAYIGYwldesHQGQGIISQ---ALQA---LIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTL 152
                         90
                 ....*....|....*.
gi 556425669 176 EGRFRQALVIKGRNRD 191
Cdd:PRK10151 153 EGCLKQAEYLNGAYDD 168
 
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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