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Conserved domains on  [gi|446416807|ref|WP_000494662|]
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MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

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, ...
8-177 2.70e-34

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: 118.95  E-value: 2.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807   8 DEIELQLLEKHHKEELYQLINqnRNHLRRWLPWVDgmKSADAYNEICPMWLKKFAEGDGFESGIRYK--GKLVGMVGIHP 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLN--DPEVARYLPGPP--YSLEEARAWLERLLADWADGGALPFAIEDKedGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807  86 VSWGKKAASLGYYLAEDAGGKGIMTRSVKAVLHYAFENLKLNKMEIRCGVENVKSRAIPERLEFKLDGILRDEEWLYDHF 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 446416807 166 HDIAVYSLLASE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
8-177 2.70e-34

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: 118.95  E-value: 2.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807   8 DEIELQLLEKHHKEELYQLINqnRNHLRRWLPWVDgmKSADAYNEICPMWLKKFAEGDGFESGIRYK--GKLVGMVGIHP 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLN--DPEVARYLPGPP--YSLEEARAWLERLLADWADGGALPFAIEDKedGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807  86 VSWGKKAASLGYYLAEDAGGKGIMTRSVKAVLHYAFENLKLNKMEIRCGVENVKSRAIPERLEFKLDGILRDEEWLYDHF 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 446416807 166 HDIAVYSLLASE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
10-150 4.32e-20

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 81.62  E-value: 4.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807   10 IELQLLEKHHKEELYQlINQNRNHLRRWLPWVDGMKSADAYneICPMWlKKFAEGDGFESGIRYKG-KLVGMVGIHPVSW 88
Cdd:pfam13302   2 LLLRPLTEEDAEALFE-LLSDPEVMRYGVPWPLTLEEAREW--LARIW-AADEAERGYGWAIELKDtGFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446416807   89 GKKAASLGYYLAEDAGGKGIMTRSVKAVLHYAFENLKLNKMEIRCGVENVKSRAIPERLEFK 150
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
3-171 7.90e-18

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 76.72  E-value: 7.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807   3 TLRVDDEIELQLLEKHHKEELYQLINQNRNHLRRWLPWVDGMKSADAyneicpmwLKKFAEGD------GFESG--IRYK 74
Cdd:PRK10151   4 IIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEED--------TRKTVQGNvmlhqrGYAKMfmIFKE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807  75 GKLVGMVGIHPVSWGKKAASLGYYLAEDAGGKGIMTRSVKAVLHYAFENLKLNKMEIRCGVENVKSRAIPERLEFKLDGI 154
Cdd:PRK10151  76 DELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGC 155
                        170
                 ....*....|....*..
gi 446416807 155 LRDEEWLYDHFHDIAVY 171
Cdd:PRK10151 156 LKQAEYLNGAYDDVNLY 172
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
8-177 2.70e-34

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: 118.95  E-value: 2.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807   8 DEIELQLLEKHHKEELYQLINqnRNHLRRWLPWVDgmKSADAYNEICPMWLKKFAEGDGFESGIRYK--GKLVGMVGIHP 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLN--DPEVARYLPGPP--YSLEEARAWLERLLADWADGGALPFAIEDKedGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807  86 VSWGKKAASLGYYLAEDAGGKGIMTRSVKAVLHYAFENLKLNKMEIRCGVENVKSRAIPERLEFKLDGILRDEEWLYDHF 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 446416807 166 HDIAVYSLLASE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
10-150 4.32e-20

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 81.62  E-value: 4.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807   10 IELQLLEKHHKEELYQlINQNRNHLRRWLPWVDGMKSADAYneICPMWlKKFAEGDGFESGIRYKG-KLVGMVGIHPVSW 88
Cdd:pfam13302   2 LLLRPLTEEDAEALFE-LLSDPEVMRYGVPWPLTLEEAREW--LARIW-AADEAERGYGWAIELKDtGFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446416807   89 GKKAASLGYYLAEDAGGKGIMTRSVKAVLHYAFENLKLNKMEIRCGVENVKSRAIPERLEFK 150
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
3-171 7.90e-18

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 76.72  E-value: 7.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807   3 TLRVDDEIELQLLEKHHKEELYQLINQNRNHLRRWLPWVDGMKSADAyneicpmwLKKFAEGD------GFESG--IRYK 74
Cdd:PRK10151   4 IIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEED--------TRKTVQGNvmlhqrGYAKMfmIFKE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807  75 GKLVGMVGIHPVSWGKKAASLGYYLAEDAGGKGIMTRSVKAVLHYAFENLKLNKMEIRCGVENVKSRAIPERLEFKLDGI 154
Cdd:PRK10151  76 DELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGC 155
                        170
                 ....*....|....*..
gi 446416807 155 LRDEEWLYDHFHDIAVY 171
Cdd:PRK10151 156 LKQAEYLNGAYDDVNLY 172
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
71-149 6.83e-07

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 45.97  E-value: 6.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807   71 IRYKGKLVGMVGIHPVSWGKKAASL-GYYLAEDAGGKGIMTRSVKAVLHYAFEnLKLNKMEIRCGVENVKSRAIPERLEF 149
Cdd:pfam00583  38 AEEDGELVGFASLSIIDDEPPVGEIeGLAVAPEYRGKGIGTALLQALLEWARE-RGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
75-174 1.23e-04

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 40.75  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807  75 GKLVGMVGIHPVSWGKKAASLGY---YLAEDAGGKGIMTRSVKAVLHYAfENLKLNKMEIRCGVENVKSRAIPERLEFKL 151
Cdd:COG1247   61 GEVVGFASLGPFRPRPAYRGTAEesiYVDPDARGRGIGRALLEALIERA-RARGYRRLVAVVLADNEASIALYEKLGFEE 139
                         90       100
                 ....*....|....*....|...
gi 446416807 152 DGILRDEEWLYDHFHDIAVYSLL 174
Cdd:COG1247  140 VGTLPEVGFKFGRWLDLVLMQKR 162
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
6-158 1.43e-03

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 37.85  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416807   6 VDDEIELQLLEKHHKEELYQLINqNRNHLRRWLPwvdgmKSADAYNEICPMWLKKFAEGDGFESGIRYKGKLVGMVGIHP 85
Cdd:PRK15130   3 SAHSVKLRPLEREDLRFVHQLDN-NASVMRYWFE-----EPYEAFVELSDLYDKHIHDQSERRFVVECDGEKAGLVELVE 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446416807  86 VSWGKKAASLGYYLAEDAGGKGIMTRSVKAVLHYAFENLKLNKMEIRCGVENVKSRAIPERLEFKLDGILRDE 158
Cdd:PRK15130  77 INHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHE 149
 
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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