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Conserved domains on  [gi|1241247918|gb|ASZ12775|]
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GNAT family N-acetyltransferase [Chitinophaga sp. MD30]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10006425)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate; similar to Escherichia coli uncharacterized protein YjdJ

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
3-89 3.41e-39

Predicted acetyltransferase, GNAT superfamily [General function prediction only];


:

Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 124.88  E-value: 3.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241247918  3 LNIKHNEKLHRFEAEIDGEF-AFIEYSRFPDGIIFNHTEVPQALEGQGIAAQLAKYVLEYARREHLRVVPLCPYVNAYVK 81
Cdd:COG2388    1 MEITHNEEKGRFELEVDGELaGELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAAYFE 80

                 ....*...
gi 1241247918 82 KHPEYNEL 89
Cdd:COG2388   81 RHPEYADL 88
 
Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
3-89 3.41e-39

Predicted acetyltransferase, GNAT superfamily [General function prediction only];


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 124.88  E-value: 3.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241247918  3 LNIKHNEKLHRFEAEIDGEF-AFIEYSRFPDGIIFNHTEVPQALEGQGIAAQLAKYVLEYARREHLRVVPLCPYVNAYVK 81
Cdd:COG2388    1 MEITHNEEKGRFELEVDGELaGELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAAYFE 80

                 ....*...
gi 1241247918 82 KHPEYNEL 89
Cdd:COG2388   81 RHPEYADL 88
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
13-89 1.99e-34

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 112.61  E-value: 1.99e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1241247918 13 RFEAEIDG--EFAFIEYSRFPDGIIFNHTEVPQALEGQGIAAQLAKYVLEYARREHLRVVPLCPYVNAYVKKHPEYNEL 89
Cdd:pfam14542  1 RFEIRVDGgaEVAFLTYRRGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
 
Name Accession Description Interval E-value
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
3-89 3.41e-39

Predicted acetyltransferase, GNAT superfamily [General function prediction only];


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 124.88  E-value: 3.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241247918  3 LNIKHNEKLHRFEAEIDGEF-AFIEYSRFPDGIIFNHTEVPQALEGQGIAAQLAKYVLEYARREHLRVVPLCPYVNAYVK 81
Cdd:COG2388    1 MEITHNEEKGRFELEVDGELaGELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERGLKVVPLCPFVAAYFE 80

                 ....*...
gi 1241247918 82 KHPEYNEL 89
Cdd:COG2388   81 RHPEYADL 88
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
13-89 1.99e-34

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 112.61  E-value: 1.99e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1241247918 13 RFEAEIDG--EFAFIEYSRFPDGIIFNHTEVPQALEGQGIAAQLAKYVLEYARREHLRVVPLCPYVNAYVKKHPEYNEL 89
Cdd:pfam14542  1 RFEIRVDGgaEVAFLTYRRGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIVPLCSYVAAYLEKHPEYADL 79
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
2-70 4.45e-03

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: 33.65  E-value: 4.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1241247918   2 ELNIKHNEKLHRFEAEIDGEF-AFIEYSRFPDGIIFNHTE---VPQALEGQGIAAQLAKYVLEYARREHLRVV 70
Cdd:pfam00583  24 LEDWDEDASEGFFVAEEDGELvGFASLSIIDDEPPVGEIEglaVAPEYRGKGIGTALLQALLEWARERGCERI 96
 
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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