NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|915779294|ref|WP_050887441|]
View 

GNAT family N-acetyltransferase [Klebsiella variicola]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11688059)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 83-132 5.97e-08

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 49.27  E-value: 5.97e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 915779294  83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGFTR 132
Cdd:COG0456   23 PEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEE 72
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 19-133 6.64e-05

N-Acyltransferase superfamily: Various enyzmes that characteristicly 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, 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 mechanism is an ordered Bi-Bi ternary complex kinetic mechanism for most GNATs: 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 then 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/ph enylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


The actual alignment was detected with superfamily member TIGR01575:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 131  Bit Score: 41.93  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779294   19 ILNACFE----AYLVPVT--QSVAGFAQRFSAEGMSLIDSRV------WLAGDEPAAIAIVARrgsaarlaafalrPAWR 86
Cdd:TIGR01575   1 DLKAVLEieaaAFAFPWTeaQFAEELANYHLCYLLARIGGKVvgyagvQIVLDEAHILNIAVK-------------PEYQ 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 915779294   87 GKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGFTRR 133
Cdd:TIGR01575  68 GQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 83-132 5.97e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 49.27  E-value: 5.97e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 915779294  83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGFTR 132
Cdd:COG0456   23 PEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEE 72
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 83-130 3.92e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 45.69  E-value: 3.92e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 915779294  83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGF 130
Cdd:PRK09491  73 PDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 83-130 5.79e-06

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: 44.43  E-value: 5.79e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 915779294   83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGF 130
Cdd:pfam00583  69 PEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 19-133 6.64e-05

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: 41.93  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779294   19 ILNACFE----AYLVPVT--QSVAGFAQRFSAEGMSLIDSRV------WLAGDEPAAIAIVARrgsaarlaafalrPAWR 86
Cdd:TIGR01575   1 DLKAVLEieaaAFAFPWTeaQFAEELANYHLCYLLARIGGKVvgyagvQIVLDEAHILNIAVK-------------PEYQ 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 915779294   87 GKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGFTRR 133
Cdd:TIGR01575  68 GQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
mycothiol_MshD TIGR03448
mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the ...
 83-132 3.42e-04

mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 132489 [Multi-domain]  Cd Length: 292  Bit Score: 41.23  E-value: 3.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 915779294   83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGFTR 132
Cdd:TIGR03448 236 PAAQGRGLGDALTLIGLHHLAARGLPAVMLYVEADNEAAVRTYEKLGFTV 285
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 83-132 5.97e-08

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 49.27  E-value: 5.97e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 915779294  83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGFTR 132
Cdd:COG0456   23 PEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEE 72
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
83-133 1.36e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 48.37  E-value: 1.36e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 915779294  83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGFTRR 133
Cdd:COG3393   25 PEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPV 75
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 83-130 3.92e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 45.69  E-value: 3.92e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 915779294  83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGF 130
Cdd:PRK09491  73 PDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 83-130 5.79e-06

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: 44.43  E-value: 5.79e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 915779294   83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGF 130
Cdd:pfam00583  69 PEYRGKGIGTALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
83-132 1.15e-05

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 44.60  E-value: 1.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 915779294  83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGFTR 132
Cdd:COG1247   90 PDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEE 139
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 19-133 6.64e-05

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: 41.93  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779294   19 ILNACFE----AYLVPVT--QSVAGFAQRFSAEGMSLIDSRV------WLAGDEPAAIAIVARrgsaarlaafalrPAWR 86
Cdd:TIGR01575   1 DLKAVLEieaaAFAFPWTeaQFAEELANYHLCYLLARIGGKVvgyagvQIVLDEAHILNIAVK-------------PEYQ 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 915779294   87 GKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGFTRR 133
Cdd:TIGR01575  68 GQGIGRALLRELIDEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEI 114
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 83-132 1.32e-04

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 41.19  E-value: 1.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 915779294  83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGFTR 132
Cdd:COG0454   68 PEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
mycothiol_MshD TIGR03448
mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the ...
 83-132 3.42e-04

mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 132489 [Multi-domain]  Cd Length: 292  Bit Score: 41.23  E-value: 3.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 915779294   83 PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVIRDNHAAVALYQTLGFTR 132
Cdd:TIGR03448 236 PAAQGRGLGDALTLIGLHHLAARGLPAVMLYVEADNEAAVRTYEKLGFTV 285
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 51-132 8.52e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 37.43  E-value: 8.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915779294   51 DSRVWLAGDEPAAIAIVARRGSAARLAAFALR----PAWRGKGLGRELMQDLLMLLQQQGVETVSLEVirdNHAAVALYQ 126
Cdd:pfam13508   2 GGRFFVAEDDGKIVGFAALLPLDDEGALAELRlavhPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYE 78


                  ....*.
gi 915779294  127 TLGFTR 132
Cdd:pfam13508  79 KLGFEE 84
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 106-132 9.00e-03

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 35.80  E-value: 9.00e-03
                          10        20
                  ....*....|....*....|....*..
gi 915779294  106 GVETVSLEVIRDNHAAVALYQTLGFTR 132
Cdd:TIGR03585 109 GLHKLSLEVLESNNKALKLYEKFGFER 135
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH