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Conserved domains on  [gi|285809915|tpg|DAA06702|]
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TPA: peptide alpha-N-acetyltransferase complex A subunit ARD1 [Saccharomyces cerevisiae S288C]

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
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 ...
94-195 8.56e-17

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 72.77  E-value: 8.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285809915  94 GYVLVKMNDDPDqqneppNGHITSLSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLHVRQSNRAALHLYRdTLAFEV 173
Cdd:COG0456    1 GFALLGLVDGGD------EAEIEDLAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYE-KLGFEE 72
                         90       100
                 ....*....|....*....|..
gi 285809915 174 LSIEKSYYQDgeDAYAMKKVLK 195
Cdd:COG0456   73 VGERPNYYGD--DALVMEKELA 92
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
94-195 8.56e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 72.77  E-value: 8.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285809915  94 GYVLVKMNDDPDqqneppNGHITSLSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLHVRQSNRAALHLYRdTLAFEV 173
Cdd:COG0456    1 GFALLGLVDGGD------EAEIEDLAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYE-KLGFEE 72
                         90       100
                 ....*....|....*....|..
gi 285809915 174 LSIEKSYYQDgeDAYAMKKVLK 195
Cdd:COG0456   73 VGERPNYYGD--DALVMEKELA 92
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
89-190 2.65e-15

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: 70.05  E-value: 2.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285809915   89 GEKLVGYVLVKMndDPDqqneppNGHITSLSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLHVRQSNRAALHLYRdT 168
Cdd:TIGR01575  39 GGKVVGYAGVQI--VLD------EAHILNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYK-K 108
                          90       100
                  ....*....|....*....|...
gi 285809915  169 LAFEVLSIEKSYYQDG-EDAYAM 190
Cdd:TIGR01575 109 LGFNEIAIRRNYYPDPgEDAIVM 131
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
89-166 2.25e-13

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: 64.46  E-value: 2.25e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285809915   89 GEKLVGYVLVKMNDDpdqqnEPPNGHITSLSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLHVRQSNRAALHLYR 166
Cdd:pfam00583  41 DGELVGFASLSIIDD-----EPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARE-RGCERIFLEVAADNLAAIALYE 112
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
89-153 1.95e-06

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: 44.19  E-value: 1.95e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285809915  89 GEKLVGYVLVKMNDDpdqqnEPPNGHITSLSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLH 153
Cdd:cd04301    7 DGEIVGFASLSPDGS-----GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
118-190 1.55e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 40.68  E-value: 1.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285809915 118 LSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLHVRQSNRAALHLYrDTLAFEVLSIEKSYY--QDG-EDAYAM 190
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEK-RGVATLWLEVRASNAAAIALY-ESLGFNEVTIRRNYYptADGrEDAIIM 142
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
94-195 8.56e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 72.77  E-value: 8.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285809915  94 GYVLVKMNDDPDqqneppNGHITSLSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLHVRQSNRAALHLYRdTLAFEV 173
Cdd:COG0456    1 GFALLGLVDGGD------EAEIEDLAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYE-KLGFEE 72
                         90       100
                 ....*....|....*....|..
gi 285809915 174 LSIEKSYYQDgeDAYAMKKVLK 195
Cdd:COG0456   73 VGERPNYYGD--DALVMEKELA 92
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
89-190 2.65e-15

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: 70.05  E-value: 2.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285809915   89 GEKLVGYVLVKMndDPDqqneppNGHITSLSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLHVRQSNRAALHLYRdT 168
Cdd:TIGR01575  39 GGKVVGYAGVQI--VLD------EAHILNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYK-K 108
                          90       100
                  ....*....|....*....|...
gi 285809915  169 LAFEVLSIEKSYYQDG-EDAYAM 190
Cdd:TIGR01575 109 LGFNEIAIRRNYYPDPgEDAIVM 131
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
89-166 2.25e-13

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: 64.46  E-value: 2.25e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285809915   89 GEKLVGYVLVKMNDDpdqqnEPPNGHITSLSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLHVRQSNRAALHLYR 166
Cdd:pfam00583  41 DGELVGFASLSIIDD-----EPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARE-RGCERIFLEVAADNLAAIALYE 112
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
89-153 1.95e-06

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: 44.19  E-value: 1.95e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285809915  89 GEKLVGYVLVKMNDDpdqqnEPPNGHITSLSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLH 153
Cdd:cd04301    7 DGEIVGFASLSPDGS-----GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARE-RGAKRLRLE 65
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
89-194 1.64e-05

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 43.54  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285809915  89 GEKLVGYVLVKMNDDPDqqnEPPNGHITSLSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLHvrqSNRAALHLYRDt 168
Cdd:COG3153   47 DGEIVGHVALSPVDIDG---EGPALLLGPLAVDPEYRGQGIGRALMRAALEAARE-RGARAVVLL---GDPSLLPFYER- 118
                         90       100
                 ....*....|....*....|....*.
gi 285809915 169 LAFEVlsIEKSYYQDGEDAYAMKKVL 194
Cdd:COG3153  119 FGFRP--AGELGLTLGPDEVFLAKEL 142
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
110-166 3.20e-05

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 41.43  E-value: 3.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 285809915 110 PPNGHITSLSVMRTYRRMGIAENLMRQALFALREVHqAEYVSLHVRQSNRAALHLYR 166
Cdd:COG3393   13 PGVAEISGVYTHPEYRGRGLASALVAALAREALARG-ARTPFLYVDADNPAARRLYE 68
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
118-190 1.55e-04

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 40.68  E-value: 1.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 285809915 118 LSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLHVRQSNRAALHLYrDTLAFEVLSIEKSYY--QDG-EDAYAM 190
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEK-RGVATLWLEVRASNAAAIALY-ESLGFNEVTIRRNYYptADGrEDAIIM 142
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
89-166 1.56e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 39.36  E-value: 1.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 285809915   89 GEKLVGYVLVKMNDDPDqqneppNGHITSLSVMRTYRRMGIAENLMRQALFALREvhqaEYVSLHVRQSNRAALHLYR 166
Cdd:pfam13508  11 DGKIVGFAALLPLDDEG------ALAELRLAVHPEYRGQGIGRALLEAAEAAAKE----GGIKLLELETTNRAAAFYE 78
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
89-195 9.01e-04

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: 38.43  E-value: 9.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285809915  89 GEKLVGYVLVKMNDDPdqqneppNGHITSLSVMRTYRRMGIAENLMRQALFALREvHQAEYVSLHvrqSNRAALHLYRdT 168
Cdd:COG1246   36 DGEIVGCAALHPLDED-------LAELRSLAVHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLL---TTSAAIHFYE-K 103
                         90       100
                 ....*....|....*....|....*....
gi 285809915 169 LAFEVLSIEKSYYQDGEDAY--AMKKVLK 195
Cdd:COG1246  104 LGFEEIDKEDLPYAKVWQRDsvVMEKDLE 132
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
83-194 1.56e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 38.05  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285809915  83 PTYLA-PGEKLVGYVLVKMNddpdqQNEPPNGHITSLSVM--RTYRRMGIAENLMRQALFALREvHQAEYVSLHVRQSNR 159
Cdd:COG1247   53 PVLVAeEDGEVVGFASLGPF-----RPRPAYRGTAEESIYvdPDARGRGIGRALLEALIERARA-RGYRRLVAVVLADNE 126
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 285809915 160 AALHLYRDtLAFEVL-SIEKSYYQDGE--DAYAMKKVL 194
Cdd:COG1247  127 ASIALYEK-LGFEEVgTLPEVGFKFGRwlDLVLMQKRL 163
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
110-174 4.74e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 35.38  E-value: 4.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285809915  110 PPNGHITSLSVMRTYRRMGIAENLMRQALFALREvhQAEYVSLHVRQSNRAALHLYrDTLAFEVL 174
Cdd:pfam08445  19 LPGGELGALQTLPEHRRRGLGSRLVAALARGIAE--RGITPFAVVVAGNTPSRRLY-EKLGFRKI 80
 
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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