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Conserved domains on  [gi|446392297|ref|WP_000470152|]
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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, ...
1-168 2.26e-48

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: 154.39  E-value: 2.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297   1 MFIKTERLLIRKFEFKDWQAVHEYTSDINVMKYIPEGVFTEENTRNFVNENIGENAKN----FPVVLINKDILIGHIVFH 76
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGgalpFAIEDKEDGELIGVVGLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297  77 KY-FGEHTYEIGWVFNPKYFNKGYASEAAQATLKYGFKEMKLHRIIATCQPQNIPSYRVMEKIGMRREGYFRKCIPHGNE 155
Cdd:COG1670   81 DIdRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160
                        170
                 ....*....|...
gi 446392297 156 WWDEYYYAILEEE 168
Cdd:COG1670  161 YRDHVLYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-168 2.26e-48

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: 154.39  E-value: 2.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297   1 MFIKTERLLIRKFEFKDWQAVHEYTSDINVMKYIPEGVFTEENTRNFVNENIGENAKN----FPVVLINKDILIGHIVFH 76
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGgalpFAIEDKEDGELIGVVGLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297  77 KY-FGEHTYEIGWVFNPKYFNKGYASEAAQATLKYGFKEMKLHRIIATCQPQNIPSYRVMEKIGMRREGYFRKCIPHGNE 155
Cdd:COG1670   81 DIdRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160
                        170
                 ....*....|...
gi 446392297 156 WWDEYYYAILEEE 168
Cdd:COG1670  161 YRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
7-141 1.04e-32

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 113.21  E-value: 1.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297    7 RLLIRKFEFKDWQAVHEYTSDINVMKYIPEGVFTEENTRNFVNE--NIGENAKNFP-VVLINKDILIGHIVFHKYFGE-H 82
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARiwAADEAERGYGwAIELKDTGFIGSIGLYDIDGEpE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446392297   83 TYEIGWVFNPKYFNKGYASEAAQATLKYGFKEMKLHRIIATCQPQNIPSYRVMEKIGMR 141
Cdd:pfam13302  81 RAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
82-168 7.33e-07

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 47.04  E-value: 7.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297  82 HTYEIGWVFNPKYFNKGYASEAAQATLKYGFKEMKLHRIIATCQPQNIPSYRVMEKIGMRREGYFRKCIPHGNEWWDEYY 161
Cdd:PRK10809 103 HACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVL 182

                 ....*..
gi 446392297 162 YAILEEE 168
Cdd:PRK10809 183 TALTTPE 189
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-168 2.26e-48

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: 154.39  E-value: 2.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297   1 MFIKTERLLIRKFEFKDWQAVHEYTSDINVMKYIPEGVFTEENTRNFVNENIGENAKN----FPVVLINKDILIGHIVFH 76
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAWLERLLADWADGgalpFAIEDKEDGELIGVVGLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297  77 KY-FGEHTYEIGWVFNPKYFNKGYASEAAQATLKYGFKEMKLHRIIATCQPQNIPSYRVMEKIGMRREGYFRKCIPHGNE 155
Cdd:COG1670   81 DIdRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160
                        170
                 ....*....|...
gi 446392297 156 WWDEYYYAILEEE 168
Cdd:COG1670  161 YRDHVLYSLLREE 173
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
7-141 1.04e-32

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 113.21  E-value: 1.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297    7 RLLIRKFEFKDWQAVHEYTSDINVMKYIPEGVFTEENTRNFVNE--NIGENAKNFP-VVLINKDILIGHIVFHKYFGE-H 82
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWLARiwAADEAERGYGwAIELKDTGFIGSIGLYDIDGEpE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446392297   83 TYEIGWVFNPKYFNKGYASEAAQATLKYGFKEMKLHRIIATCQPQNIPSYRVMEKIGMR 141
Cdd:pfam13302  81 RAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
33-140 4.99e-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: 48.67  E-value: 4.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297   33 YIPEGVFTEENTRNFVNENIGENAKNFPVVLINKDILIGHIVFHKYFGE--HTYEIGWVFNPKYFNKGYASEAAQATLKY 110
Cdd:pfam00583   8 LSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEppVGEIEGLAVAPEYRGKGIGTALLQALLEW 87
                          90       100       110
                  ....*....|....*....|....*....|
gi 446392297  111 GFKEmKLHRIIATCQPQNIPSYRVMEKIGM 140
Cdd:pfam00583  88 ARER-GCERIFLEVAADNLAAIALYEKLGF 116
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
82-168 7.33e-07

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 47.04  E-value: 7.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297  82 HTYEIGWVFNPKYFNKGYASEAAQATLKYGFKEMKLHRIIATCQPQNIPSYRVMEKIGMRREGYFRKCIPHGNEWWDEYY 161
Cdd:PRK10809 103 HACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVL 182

                 ....*..
gi 446392297 162 YAILEEE 168
Cdd:PRK10809 183 TALTTPE 189
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
10-144 3.76e-05

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 42.09  E-value: 3.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446392297  10 IRKFEFKDWQAVHEYTSDINVMKYI---PEGVFTE-----------ENTRNFVNENIGENAKNFPVVLINkdiligHIvf 75
Cdd:PRK15130   9 LRPLEREDLRFVHQLDNNASVMRYWfeePYEAFVElsdlydkhihdQSERRFVVECDGEKAGLVELVEIN------HV-- 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446392297  76 HKyfgehTYEIGWVFNPKYFNKGYASEAAQATLKYGFKEMKLHRIIATCQPQNIPSYRVMEKIGMRREG 144
Cdd:PRK15130  81 HR-----RAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEG 144
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
95-159 4.70e-03

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 35.81  E-value: 4.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446392297   95 FNKGYASEAAQATLKYGFKEMKLHRIIATCQPQNIPSYRVMEKIGMRREGYFRKCIPHGNEWWDE 159
Cdd:pfam13420  87 NDEGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDM 151
 
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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