NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446416794|ref|WP_000494649|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.18e-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: 1.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794   8 DEIELQLLEKHHKEELYELLdqNRNHLRRWLPWVDgtKSADAYDEIFPMWLKKFAEGDGFESGIRYK--GKLVGMVGIHP 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELL--NDPEVARYLPGPP--YSLEEARAWLERLLADWADGGALPFAIEDKedGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794  86 VSWGKKATSLGYYLTEDAGGKGIMTRSVKAVLHYAFENLKLNKVEIRCGVENVKSRAIPERLGFKLDGILRDDEWIYDHF 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 446416794 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 1.18e-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: 1.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794   8 DEIELQLLEKHHKEELYELLdqNRNHLRRWLPWVDgtKSADAYDEIFPMWLKKFAEGDGFESGIRYK--GKLVGMVGIHP 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELL--NDPEVARYLPGPP--YSLEEARAWLERLLADWADGGALPFAIEDKedGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794  86 VSWGKKATSLGYYLTEDAGGKGIMTRSVKAVLHYAFENLKLNKVEIRCGVENVKSRAIPERLGFKLDGILRDDEWIYDHF 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 446416794 166 HDIAVYSLLASE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
10-150 1.71e-22

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 87.79  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794   10 IELQLLEKHHKEELYELLdQNRNHLRRWLPWVdgTKSADAYDEIFPMWlKKFAEGDGFESGIRYKG-KLVGMVGIHPVSW 88
Cdd:pfam13302   2 LLLRPLTEEDAEALFELL-SDPEVMRYGVPWP--LTLEEAREWLARIW-AADEAERGYGWAIELKDtGFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446416794   89 GKKATSLGYYLTEDAGGKGIMTRSVKAVLHYAFENLKLNKVEIRCGVENVKSRAIPERLGFK 150
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
3-171 2.39e-16

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 72.87  E-value: 2.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794   3 TLRVDDEIELQLLEKHHKEELYELLDQNRNHLRRWLPWVDGTKSAD---------------AYDEIFPMWLKkfaegdgf 67
Cdd:PRK10151   4 IIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEdtrktvqgnvmlhqrGYAKMFMIFKE-------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794  68 esgirykGKLVGMVGIHPVSWGKKATSLGYYLTEDAGGKGIMTRSVKAVLHYAFENLKLNKVEIRCGVENVKSRAIPERL 147
Cdd:PRK10151  76 -------DELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRN 148
                        170       180
                 ....*....|....*....|....
gi 446416794 148 GFKLDGILRDDEWIYDHFHDIAVY 171
Cdd:PRK10151 149 GFTLEGCLKQAEYLNGAYDDVNLY 172
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
8-177 1.18e-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: 1.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794   8 DEIELQLLEKHHKEELYELLdqNRNHLRRWLPWVDgtKSADAYDEIFPMWLKKFAEGDGFESGIRYK--GKLVGMVGIHP 85
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELL--NDPEVARYLPGPP--YSLEEARAWLERLLADWADGGALPFAIEDKedGELIGVVGLYD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794  86 VSWGKKATSLGYYLTEDAGGKGIMTRSVKAVLHYAFENLKLNKVEIRCGVENVKSRAIPERLGFKLDGILRDDEWIYDHF 165
Cdd:COG1670   82 IDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRY 161
                        170
                 ....*....|..
gi 446416794 166 HDIAVYSLLASE 177
Cdd:COG1670  162 RDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
10-150 1.71e-22

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 87.79  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794   10 IELQLLEKHHKEELYELLdQNRNHLRRWLPWVdgTKSADAYDEIFPMWlKKFAEGDGFESGIRYKG-KLVGMVGIHPVSW 88
Cdd:pfam13302   2 LLLRPLTEEDAEALFELL-SDPEVMRYGVPWP--LTLEEAREWLARIW-AADEAERGYGWAIELKDtGFIGSIGLYDIDG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446416794   89 GKKATSLGYYLTEDAGGKGIMTRSVKAVLHYAFENLKLNKVEIRCGVENVKSRAIPERLGFK 150
Cdd:pfam13302  78 EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
3-171 2.39e-16

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 72.87  E-value: 2.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794   3 TLRVDDEIELQLLEKHHKEELYELLDQNRNHLRRWLPWVDGTKSAD---------------AYDEIFPMWLKkfaegdgf 67
Cdd:PRK10151   4 IIPVSESLELHAVDESHVTPLHQLVCKNKTWLQQSLNWPQFVQSEEdtrktvqgnvmlhqrGYAKMFMIFKE-------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794  68 esgirykGKLVGMVGIHPVSWGKKATSLGYYLTEDAGGKGIMTRSVKAVLHYAFENLKLNKVEIRCGVENVKSRAIPERL 147
Cdd:PRK10151  76 -------DELIGVLSFNRIEPLNKTAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRN 148
                        170       180
                 ....*....|....*....|....
gi 446416794 148 GFKLDGILRDDEWIYDHFHDIAVY 171
Cdd:PRK10151 149 GFTLEGCLKQAEYLNGAYDDVNLY 172
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
34-149 2.07e-08

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: 50.21  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794   34 LRRWLPWVDGTKSADAYDEIFPMWLKKFAEGDGFESGIRYKGKLVGMVGIHPVSWGKKATSL-GYYLTEDAGGKGIMTRS 112
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIeGLAVAPEYRGKGIGTAL 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446416794  113 VKAVLHYAFEnLKLNKVEIRCGVENVKSRAIPERLGF 149
Cdd:pfam00583  81 LQALLEWARE-RGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
75-174 7.67e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 41.13  E-value: 7.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794  75 GKLVGMVGIHPVSWGKKATSLGY---YLTEDAGGKGIMTRSVKAVLHYAfENLKLNKVEIRCGVENVKSRAIPERLGFKL 151
Cdd:COG1247   61 GEVVGFASLGPFRPRPAYRGTAEesiYVDPDARGRGIGRALLEALIERA-RARGYRRLVAVVLADNEASIALYEKLGFEE 139
                         90       100
                 ....*....|....*....|...
gi 446416794 152 DGILRDDEWIYDHFHDIAVYSLL 174
Cdd:COG1247  140 VGTLPEVGFKFGRWLDLVLMQKR 162
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
6-161 2.32e-03

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 37.08  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446416794   6 VDDEIELQLLEKHHKEELYELlDQNRNHLRRWL--PWVDGTKSADAYDE-IFPMWLKKFAegdgfesgIRYKGKLVGMVG 82
Cdd:PRK15130   3 SAHSVKLRPLEREDLRFVHQL-DNNASVMRYWFeePYEAFVELSDLYDKhIHDQSERRFV--------VECDGEKAGLVE 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446416794  83 IHPVSWGKKATSLGYYLTEDAGGKGIMTRSVKAVLHYAFENLKLNKVEIRCGVENVKSRAIPERLGFKLDGILRDDEWI 161
Cdd:PRK15130  74 LVEINHVHRRAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFI 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH