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Conserved domains on  [gi|1168799880|ref|WP_080369820|]
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N-acetyltransferase [Vibrio cholerae]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 2-60 6.82e-12

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.43  E-value: 6.82e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168799880  2 FIHHLYVATEYQGQGVGSMLLN-----GAKMKYGNLSLKCMVQNQKALNFYLSQGFEIVSQVDD 60
Cdd:COG0456   15 EIEDLAVDPEYRGRGIGRALLEaalerARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 2-60 6.82e-12

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.43  E-value: 6.82e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168799880  2 FIHHLYVATEYQGQGVGSMLLN-----GAKMKYGNLSLKCMVQNQKALNFYLSQGFEIVSQVDD 60
Cdd:COG0456   15 EIEDLAVDPEYRGRGIGRALLEaalerARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
PRK10562 PRK10562
putative acetyltransferase; Provisional
 2-55 2.93e-11

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 54.69  E-value: 2.93e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1168799880   2 FIHHLYVATEYQGQGVGSMLLNGAKMKYGNLSLKCMVQNQKALNFYLSQGFEIV 55
Cdd:PRK10562   70 FVGALFVAPKAVRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIV 123
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 2-52 7.54e-10

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: 50.59  E-value: 7.54e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1168799880   2 FIHHLYVATEYQGQGVGSMLLN-----GAKMKYGNLSLKCMVQNQKALNFYLSQGF 52
Cdd:pfam00583  61 EIEGLAVAPEYRGKGIGTALLQallewARERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 3-66 4.52e-07

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 43.86  E-value: 4.52e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168799880   3 IHHLYVATEYQGQGVGSMLLNGAKMKYGNLSLKCM-----VQNQKALNFYLSQGFEIVsqvdDELGGYY 66
Cdd:TIGR01575  57 ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIflevrVSNIAAQALYKKLGFNEI----AIRRNYY 121
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 2-23 1.87e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 35.71  E-value: 1.87e-04
                         10        20
                 ....*....|....*....|..
gi 1168799880  2 FIHHLYVATEYQGQGVGSMLLN 23
Cdd:cd04301   27 YIGDLAVLPEYRGKGIGSALLE 48
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 2-60 6.82e-12

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.43  E-value: 6.82e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168799880  2 FIHHLYVATEYQGQGVGSMLLN-----GAKMKYGNLSLKCMVQNQKALNFYLSQGFEIVSQVDD 60
Cdd:COG0456   15 EIEDLAVDPEYRGRGIGRALLEaalerARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN 78
PRK10562 PRK10562
putative acetyltransferase; Provisional
 2-55 2.93e-11

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 54.69  E-value: 2.93e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1168799880   2 FIHHLYVATEYQGQGVGSMLLNGAKMKYGNLSLKCMVQNQKALNFYLSQGFEIV 55
Cdd:PRK10562   70 FVGALFVAPKAVRRGIGKALMQHVQQRYPHLSLEVYQKNQRAVNFYHAQGFRIV 123
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 1-70 1.38e-10

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 52.75  E-value: 1.38e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168799880   1 MFIHHLYVATEYQGQGVGSMLLNGAkMK------YGNLSLKCMVQNQKALNFYLSQGFEIVSQVDDELGGYYYMSF 70
Cdd:COG0454    59 LELKRLYVLPEYRGKGIGKALLEAL-LEwarergCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVGGEFEKEL 133
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 2-52 7.54e-10

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: 50.59  E-value: 7.54e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1168799880   2 FIHHLYVATEYQGQGVGSMLLN-----GAKMKYGNLSLKCMVQNQKALNFYLSQGF 52
Cdd:pfam00583  61 EIEGLAVAPEYRGKGIGTALLQallewARERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
4-55 3.84e-09

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 49.61  E-value: 3.84e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1168799880   4 HHLYVATEYQGQGVGSMLLN-----GAKMKYGNLSLKCMVQNQKALNFYLSQGFEIV 55
Cdd:COG1247    84 ESIYVDPDARGRGIGRALLEalierARARGYRRLVAVVLADNEASIALYEKLGFEEV 140
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-54 6.55e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 47.45  E-value: 6.55e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1168799880  3 IHHLYVATEYQGQGVGSMLLNGAK--MKYGNLSLKCMVQNQKALNFYLSQGFEI 54
Cdd:pfam13508 31 ELRLAVHPEYRGQGIGRALLEAAEaaAKEGGIKLLELETTNRAAAFYEKLGFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
1-68 2.39e-07

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 44.69  E-value: 2.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168799880   1 MFIHHLYVATEYQGQGVGSMLLNGA-----KMKYGNLSLkcmVQNQKALNFYLSQGFEIVSQVDDELGGYYYM 68
Cdd:COG3153    68 LLLGPLAVDPEYRGQGIGRALMRAAleaarERGARAVVL---LGDPSLLPFYERFGFRPAGELGLTLGPDEVF 137
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 3-66 4.52e-07

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 43.86  E-value: 4.52e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168799880   3 IHHLYVATEYQGQGVGSMLLNGAKMKYGNLSLKCM-----VQNQKALNFYLSQGFEIVsqvdDELGGYY 66
Cdd:TIGR01575  57 ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIflevrVSNIAAQALYKKLGFNEI----AIRRNYY 121
PRK10514 PRK10514
putative acetyltransferase; Provisional
 1-60 5.99e-07

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 43.45  E-value: 5.99e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168799880   1 MFIH--H---LYVATEYQGQGVGSMLLNGAKMKYGNLSLKCMVQNQKALNFYLSQGFEIV--SQVDD 60
Cdd:PRK10514   65 MLLSggHmeaLFVDPDVRGCGVGRMLVEHALSLHPELTTDVNEQNEQAVGFYKKMGFKVTgrSEVDD 131
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 3-58 2.93e-06

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 41.49  E-value: 2.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168799880   3 IHHLYVATEYQGQGVGSMLLNGA-----KMKYGNLSLKCMVQNQkALNFYLSQGFEIVSQV 58
Cdd:pfam13673  54 ISLLFVDPDYQGQGIGKALLEAVedyaeKDGIKLSELTVNASPY-AVPFYEKLGFRATGPE 113
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 3-59 3.60e-06

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 41.52  E-value: 3.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1168799880   3 IHHLYVATEYQGQGVGSMLLNGAKMKYGNLSLKCMV--QNQKALNFYLSQGFEIVSQVD 59
Cdd:COG1246    55 LRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFllTTSAAIHFYEKLGFEEIDKED 113
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
3-63 6.05e-06

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 40.55  E-value: 6.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168799880   3 IHHLYVATEYQGQGVGSMLLNGAkMKY----GNLSLKCMVQNQkALNFYLSQGFEIVSQVDDELG 63
Cdd:COG2153    61 IGRVAVLPEYRGQGLGRALMEAA-IEEarerGARRIVLSAQAH-AVGFYEKLGFVPVGEEFLEAG 123
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 2-23 1.87e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 35.71  E-value: 1.87e-04
                         10        20
                 ....*....|....*....|..
gi 1168799880  2 FIHHLYVATEYQGQGVGSMLLN 23
Cdd:cd04301   27 YIGDLAVLPEYRGKGIGSALLE 48
PRK13688 PRK13688
N-acetyltransferase;
6-61 1.53e-03

N-acetyltransferase;


Pssm-ID: 237470  Cd Length: 156  Bit Score: 34.60  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1168799880   6 LYVATEYQGQGVGSMLLNGAKMKygNLSLKCMVQNQKAlNFYLSQGFEIVSQVDDE 61
Cdd:PRK13688   85 LEVLPKYQNRGYGEMLVDFAKSF--QLPIKTIARNKSK-DFWLKLGFTPVEYKNDE 137
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
1-25 2.26e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 33.20  E-value: 2.26e-03
                         10        20
                 ....*....|....*....|....*
gi 1168799880  1 MFIHHLYVATEYQGQGVGSMLLNGA 25
Cdd:COG2388   33 IIITHTEVPPALRGQGIASALVEAA 57
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 1-25 2.82e-03

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: 32.88  E-value: 2.82e-03
                         10        20
                 ....*....|....*....|....*
gi 1168799880  1 MFIHHLYVATEYQGQGVGSMLLNGA 25
Cdd:pfam14542 24 LIITHTEVPPALRGQGIASKLVKAA 48
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 7-62 7.77e-03

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: 32.66  E-value: 7.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168799880   7 YVATEYQGQGVGSMLLNGAkMKYG-------NLSLKCMVQNQKALNFYLSQGFEIVSQVDDEL 62
Cdd:COG1670    94 WLAPAYWGKGYATEALRAL-LDYAfeelglhRVEAEVDPDNTASIRVLEKLGFRLEGTLRDAL 155
 
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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