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Conserved domains on  [gi|2495844912|ref|WP_280061173|]
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MULTISPECIES: GNAT family N-acetyltransferase [Empedobacter]

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, ...
1-143 6.33e-24

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: 91.60  E-value: 6.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495844912   1 MEDELIYFRELLDTDVTRLFEIYSNAEAMKYRETTPMkTIEDSYKMLERDKEKKNSGYEFRFAVIEKSSETLIGTVMFQ- 79
Cdd:COG1670     3 LETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPY-SLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLYd 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495844912  80 --PVHDKAIIGYSIDEQFWNKGYATR----IINLISKELKSRKymlIEAWVKKENIASSKALLKNNFQQI 143
Cdd:COG1670    82 idRANRSAEIGYWLAPAYWGKGYATEalraLLDYAFEELGLHR---VEAEVDPDNTASIRVLEKLGFRLE 148
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-143 6.33e-24

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: 91.60  E-value: 6.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495844912   1 MEDELIYFRELLDTDVTRLFEIYSNAEAMKYRETTPMkTIEDSYKMLERDKEKKNSGYEFRFAVIEKSSETLIGTVMFQ- 79
Cdd:COG1670     3 LETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPY-SLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLYd 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495844912  80 --PVHDKAIIGYSIDEQFWNKGYATR----IINLISKELKSRKymlIEAWVKKENIASSKALLKNNFQQI 143
Cdd:COG1670    82 idRANRSAEIGYWLAPAYWGKGYATEalraLLDYAFEELGLHR---VEAEVDPDNTASIRVLEKLGFRLE 148
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
6-141 3.85e-21

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 83.55  E-value: 3.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495844912   6 IYFRELLDTDVTRLFEIYSNAEAMKYRETTPmKTIEDSYKMLERDKEKKNSGYEFRFAVIEKSSEtLIGTVMFQPVHD-- 83
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWP-LTLEEAREWLARIWAADEAERGYGWAIELKDTG-FIGSIGLYDIDGep 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495844912  84 -KAIIGYSIDEQFWNKGYAT----RIINLISKELKSRKymlIEAWVKKENIASSKALLKNNFQ 141
Cdd:pfam13302  80 eRAELGYWLGPDYWGKGYATeavrALLEYAFEELGLPR---LVARIDPENTASRRVLEKLGFK 139
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-143 6.33e-24

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: 91.60  E-value: 6.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495844912   1 MEDELIYFRELLDTDVTRLFEIYSNAEAMKYRETTPMkTIEDSYKMLERDKEKKNSGYEFRFAVIEKSSETLIGTVMFQ- 79
Cdd:COG1670     3 LETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPY-SLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLYd 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495844912  80 --PVHDKAIIGYSIDEQFWNKGYATR----IINLISKELKSRKymlIEAWVKKENIASSKALLKNNFQQI 143
Cdd:COG1670    82 idRANRSAEIGYWLAPAYWGKGYATEalraLLDYAFEELGLHR---VEAEVDPDNTASIRVLEKLGFRLE 148
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
6-141 3.85e-21

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 83.55  E-value: 3.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495844912   6 IYFRELLDTDVTRLFEIYSNAEAMKYRETTPmKTIEDSYKMLERDKEKKNSGYEFRFAVIEKSSEtLIGTVMFQPVHD-- 83
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWP-LTLEEAREWLARIWAADEAERGYGWAIELKDTG-FIGSIGLYDIDGep 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2495844912  84 -KAIIGYSIDEQFWNKGYAT----RIINLISKELKSRKymlIEAWVKKENIASSKALLKNNFQ 141
Cdd:pfam13302  80 eRAELGYWLGPDYWGKGYATeavrALLEYAFEELGLPR---LVARIDPENTASRRVLEKLGFK 139
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
87-158 9.66e-06

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 43.36  E-value: 9.66e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2495844912  87 IGYSIDEQFWNKGYATRIINLISKELKSRKymLIEAWV--KKENIASSKALLKNNFQQISQTIYPKNHLFQLRF 158
Cdd:COG3981    95 IGYGVRPSERGKGYATEMLRLALEEARELG--LDRVLItcDKDNIASRKVIEANGGVLEDEVVDEEDGRPVRRY 166
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
6-143 9.19e-04

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 37.67  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495844912   6 IYFRELLDTDVTRLFEIYsnAEAMKYR----ETTPMkTIEDsykMLERDKEKKNSGYEFRFAVIEkssETLIGTVMFQPV 81
Cdd:COG1247     2 MTIRPATPEDAPAIAAIY--NEAIAEGtatfETEPP-SEEE---REAWFAAILAPGRPVLVAEED---GEVVGFASLGPF 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495844912  82 HDKAiiGYS--------IDEQFWNKGYATRIINLISKELKSRKYMLIEAWVKKENIASSKALLKNNFQQI 143
Cdd:COG1247    73 RPRP--AYRgtaeesiyVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEV 140
 
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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