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Conserved domains on  [gi|983222632|gb|KWU62845|]
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GNAT family acetyltransferase [Bacillus cereus]

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, ...
9-179 2.87e-36

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: 124.34  E-value: 2.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222632   9 ETERLMIRPFQNDDYESWLDGFNKrlPSQYKYDDGYQVmassTKEWFTEWIRGFDEAAHRDEMYVLGIFRKEDGANIGKL 88
Cdd:COG1670    4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPY----SLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222632  89 ELIKILRMDyQWAMMGYSIHNQYWKNGYGMESVKAAVSLFFNRLHFHRIELHIRVDNEPSVRLAERAGFSFECKREAFSL 168
Cdd:COG1670   78 GLYDIDRAN-RSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
                        170
                 ....*....|.
gi 983222632 169 ENGKWMDFLIY 179
Cdd:COG1670  157 IDGRYRDHVLY 167
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
9-179 2.87e-36

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: 124.34  E-value: 2.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222632   9 ETERLMIRPFQNDDYESWLDGFNKrlPSQYKYDDGYQVmassTKEWFTEWIRGFDEAAHRDEMYVLGIFRKEDGANIGKL 88
Cdd:COG1670    4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPY----SLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222632  89 ELIKILRMDyQWAMMGYSIHNQYWKNGYGMESVKAAVSLFFNRLHFHRIELHIRVDNEPSVRLAERAGFSFECKREAFSL 168
Cdd:COG1670   78 GLYDIDRAN-RSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
                        170
                 ....*....|.
gi 983222632 169 ENGKWMDFLIY 179
Cdd:COG1670  157 IDGRYRDHVLY 167
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
12-157 9.05e-22

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 85.86  E-value: 9.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222632   12 RLMIRPFQNDDYESWLDGFNKrlPSQYKYddgyQVMASSTKEWFTEWIRGFDEAAHRDEMYVLGIFRKEDGAnIGKLELI 91
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSD--PEVMRY----GVPWPLTLEEAREWLARIWAADEAERGYGWAIELKDTGF-IGSIGLY 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983222632   92 KILRmDYQWAMMGYSIHNQYWKNGYGMESVKAAVSLFFNRLHFHRIELHIRVDNEPSVRLAERAGF 157
Cdd:pfam13302  74 DIDG-EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGF 138
PRK10140 PRK10140
N-acetyltransferase;
112-175 7.58e-06

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 44.20  E-value: 7.58e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983222632 112 WKN-GYGMESVKAAVSLFFNRLHFHRIELHIRVDNEPSVRLAERAGFSFECKREAFSLENGKWMD 175
Cdd:PRK10140  90 WKNrGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVD 154
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
9-179 2.87e-36

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: 124.34  E-value: 2.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222632   9 ETERLMIRPFQNDDYESWLDGFNKrlPSQYKYDDGYQVmassTKEWFTEWIRGFDEAAHRDEMYVLGIFRKEDGANIGKL 88
Cdd:COG1670    4 ETERLRLRPLRPEDAEALAELLND--PEVARYLPGPPY----SLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222632  89 ELIKILRMDyQWAMMGYSIHNQYWKNGYGMESVKAAVSLFFNRLHFHRIELHIRVDNEPSVRLAERAGFSFECKREAFSL 168
Cdd:COG1670   78 GLYDIDRAN-RSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV 156
                        170
                 ....*....|.
gi 983222632 169 ENGKWMDFLIY 179
Cdd:COG1670  157 IDGRYRDHVLY 167
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
12-157 9.05e-22

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 85.86  E-value: 9.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222632   12 RLMIRPFQNDDYESWLDGFNKrlPSQYKYddgyQVMASSTKEWFTEWIRGFDEAAHRDEMYVLGIFRKEDGAnIGKLELI 91
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSD--PEVMRY----GVPWPLTLEEAREWLARIWAADEAERGYGWAIELKDTGF-IGSIGLY 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983222632   92 KILRmDYQWAMMGYSIHNQYWKNGYGMESVKAAVSLFFNRLHFHRIELHIRVDNEPSVRLAERAGF 157
Cdd:pfam13302  74 DIDG-EPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGF 138
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
47-157 3.54e-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: 49.44  E-value: 3.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222632   47 MASSTKEWFTEWIRGFDEAAHRDEMYVLGIfrKEDGANIGKLELIKILRMDYQWAMMGYSIHNQYWKNGYGMESVKAAVS 126
Cdd:pfam00583   9 SEEFPEPWPDEPLDLLEDWDEDASEGFFVA--EEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLE 86
                          90       100       110
                  ....*....|....*....|....*....|.
gi 983222632  127 LFFNRlHFHRIELHIRVDNEPSVRLAERAGF 157
Cdd:pfam00583  87 WARER-GCERIFLEVAADNLAAIALYEKLGF 116
PRK10140 PRK10140
N-acetyltransferase;
112-175 7.58e-06

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 44.20  E-value: 7.58e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983222632 112 WKN-GYGMESVKAAVSLFFNRLHFHRIELHIRVDNEPSVRLAERAGFSFECKREAFSLENGKWMD 175
Cdd:PRK10140  90 WKNrGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVD 154
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
131-181 1.51e-04

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 40.36  E-value: 1.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 983222632 131 RLHFHRIELHIRVDNEPSVRLAERAGFSFECKREAFSLENGKWMDFLIYFK 181
Cdd:COG1247  111 ARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
50-178 2.27e-04

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 39.66  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222632   50 STKEWFTEWIrgfdEAAHRDEMYVLGIFRKEDGANIGKLELIKILRMDYQWAMMGYSIHNqywKNGYGMESVKAAVSLFF 129
Cdd:pfam13420  32 SSIEEFETFL----AAYLSPGEIVFGVAESDRLIGYATLRQFDYVKTHKAELSFYVVKNN---DEGINRELINAIIQYAR 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 983222632  130 NRLHFHRIELHIRVDNEPSVRLAERAGFSFECKREAFSLENGKWMDFLI 178
Cdd:pfam13420 105 KNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDMMW 153
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
93-175 5.36e-03

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 36.26  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222632  93 ILRMDYQWAMMGYSIHNQYWKNGYGMESVKAAVSLFFNRLHFHRIELHIRVDNEPSVRLAERAGFSFECKREAFSLENGK 172
Cdd:PRK10809  97 VVRGSFHACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQ 176

                 ...
gi 983222632 173 WMD 175
Cdd:PRK10809 177 WRD 179
 
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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