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Conserved domains on  [gi|15241925|ref|NP_200485|]
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histone acetyltransferase of the GNAT family 2 [Arabidopsis thaliana]

Protein Classification

histone acetyltransferase type B catalytic subunit( domain architecture ID 10564069)

histone acetyltransferase type B (HAT-B) catalytic subunit (HAT1) which acetylates K5 and K12 of histone H4, and is involved in telomeric silencing and DNA double-strand break repair; similar to Cryptococcus neoformans HAT1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hat1_N pfam10394
Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the ...
 29-195 5.36e-37

Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the structure of histone acetyl transferase HAT1. It is often found in association with the C-terminal part of the GNAT Acetyltransf_1 (pfam00583) domain. It seems to be motifs C and D of the structure. Histone acetyltransferases (HATs) catalyze the transfer of an acetyl group from acetyl-CoA to the lysine E-amino groups on the N-terminal tails of histones. HATs are involved in transcription since histones tend to be hyper-acetylated in actively transcribed regions of chromatin, whereas in transcriptionally silent regions histones are hypo-acetylated.


:

Pssm-ID: 463071  Cd Length: 158  Bit Score: 133.05  E-value: 5.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241925    29 GVEANECIKIYLVSSKEEVDSsDISSVKPVDLNDFFDGDGKIYGYQGLKINVWINSISLHSYADITYQSTIN--GDKGIT 106
Cdd:pfam10394   2 TSDANEALKISLVRPEEDVES-DDTSFHPEFTYQIFGEEETIFGYKDLKINLYFSAGSLRPYLDISYSEKLDsvGDTGAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241925   107 DLKSALQNIFAETIVDTKDEFLQTFStQRDFIRNMVsnGEVMHAGATDGSsknaevvpSDPQVIRMEIGSPNAGLLYSRL 186
Cdd:pfam10394  81 DVEKKLKEFLPEDLFTDKDEFLKALE-EKEKSFKPP--GELIHSYTREGK--------STFEIYKGSLADPAFRELHRRL 149


                  ....*....
gi 15241925   187 VPLVLLFVD 195
Cdd:pfam10394 150 QIFVLLFIE 158
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 225-283 2.36e-05

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: 41.88  E-value: 2.36e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15241925 225 RIVGFTAIYKFYRYPDRLRmrLSQILVLPSFQGKGLGSYLMEVVNNVAITENVYDLTVE 283
Cdd:cd04301   9 EIVGFASLSPDGSGGDTAY--IGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
Hat1_N pfam10394
Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the ...
 29-195 5.36e-37

Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the structure of histone acetyl transferase HAT1. It is often found in association with the C-terminal part of the GNAT Acetyltransf_1 (pfam00583) domain. It seems to be motifs C and D of the structure. Histone acetyltransferases (HATs) catalyze the transfer of an acetyl group from acetyl-CoA to the lysine E-amino groups on the N-terminal tails of histones. HATs are involved in transcription since histones tend to be hyper-acetylated in actively transcribed regions of chromatin, whereas in transcriptionally silent regions histones are hypo-acetylated.


Pssm-ID: 463071  Cd Length: 158  Bit Score: 133.05  E-value: 5.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241925    29 GVEANECIKIYLVSSKEEVDSsDISSVKPVDLNDFFDGDGKIYGYQGLKINVWINSISLHSYADITYQSTIN--GDKGIT 106
Cdd:pfam10394   2 TSDANEALKISLVRPEEDVES-DDTSFHPEFTYQIFGEEETIFGYKDLKINLYFSAGSLRPYLDISYSEKLDsvGDTGAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241925   107 DLKSALQNIFAETIVDTKDEFLQTFStQRDFIRNMVsnGEVMHAGATDGSsknaevvpSDPQVIRMEIGSPNAGLLYSRL 186
Cdd:pfam10394  81 DVEKKLKEFLPEDLFTDKDEFLKALE-EKEKSFKPP--GELIHSYTREGK--------STFEIYKGSLADPAFRELHRRL 149


                  ....*....
gi 15241925   187 VPLVLLFVD 195
Cdd:pfam10394 150 QIFVLLFIE 158
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 225-283 2.36e-05

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: 41.88  E-value: 2.36e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15241925 225 RIVGFTAIYKFYRYPDRLRmrLSQILVLPSFQGKGLGSYLMEVVNNVAITENVYDLTVE 283
Cdd:cd04301   9 EIVGFASLSPDGSGGDTAY--IGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 225-283 2.68e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.44  E-value: 2.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15241925   225 RIVGFTAIYKFYRYPDRLRMRLSqilVLPSFQGKGLGSYLMEVVNNVAITENVYDLTVE 283
Cdd:pfam13508  13 KIVGFAALLPLDDEGALAELRLA---VHPEYRGQGIGRALLEAAEAAAKEGGIKLLELE 68
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
225-266 1.14e-04

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 41.99  E-value: 1.14e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15241925 225 RIVGFTAIYKFYRYPDRLRMRLSQILVLPSFQGKGLGSYLME 266
Cdd:COG3153  49 EIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMR 90
 
Name Accession Description Interval E-value
Hat1_N pfam10394
Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the ...
 29-195 5.36e-37

Histone acetyl transferase HAT1 N-terminus; This domain is the N-terminal half of the structure of histone acetyl transferase HAT1. It is often found in association with the C-terminal part of the GNAT Acetyltransf_1 (pfam00583) domain. It seems to be motifs C and D of the structure. Histone acetyltransferases (HATs) catalyze the transfer of an acetyl group from acetyl-CoA to the lysine E-amino groups on the N-terminal tails of histones. HATs are involved in transcription since histones tend to be hyper-acetylated in actively transcribed regions of chromatin, whereas in transcriptionally silent regions histones are hypo-acetylated.


Pssm-ID: 463071  Cd Length: 158  Bit Score: 133.05  E-value: 5.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241925    29 GVEANECIKIYLVSSKEEVDSsDISSVKPVDLNDFFDGDGKIYGYQGLKINVWINSISLHSYADITYQSTIN--GDKGIT 106
Cdd:pfam10394   2 TSDANEALKISLVRPEEDVES-DDTSFHPEFTYQIFGEEETIFGYKDLKINLYFSAGSLRPYLDISYSEKLDsvGDTGAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241925   107 DLKSALQNIFAETIVDTKDEFLQTFStQRDFIRNMVsnGEVMHAGATDGSsknaevvpSDPQVIRMEIGSPNAGLLYSRL 186
Cdd:pfam10394  81 DVEKKLKEFLPEDLFTDKDEFLKALE-EKEKSFKPP--GELIHSYTREGK--------STFEIYKGSLADPAFRELHRRL 149


                  ....*....
gi 15241925   187 VPLVLLFVD 195
Cdd:pfam10394 150 QIFVLLFIE 158
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 225-283 2.36e-05

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: 41.88  E-value: 2.36e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15241925 225 RIVGFTAIYKFYRYPDRLRmrLSQILVLPSFQGKGLGSYLMEVVNNVAITENVYDLTVE 283
Cdd:cd04301   9 EIVGFASLSPDGSGGDTAY--IGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 225-283 2.68e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 42.44  E-value: 2.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15241925   225 RIVGFTAIYKFYRYPDRLRMRLSqilVLPSFQGKGLGSYLMEVVNNVAITENVYDLTVE 283
Cdd:pfam13508  13 KIVGFAALLPLDDEGALAELRLA---VHPEYRGQGIGRALLEAAEAAAKEGGIKLLELE 68
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
225-266 1.14e-04

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 41.99  E-value: 1.14e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15241925 225 RIVGFTAIYKFYRYPDRLRMRLSQILVLPSFQGKGLGSYLME 266
Cdd:COG3153  49 EIVGHVALSPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMR 90
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 225-266 1.18e-04

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: 41.35  E-value: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15241925   225 RIVGFTAIYKFYRYPDRlrMRLSQILVLPSFQGKGLGSYLME 266
Cdd:pfam00583  43 ELVGFASLSIIDDEPPV--GEIEGLAVAPEYRGKGIGTALLQ 82
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
225-266 2.55e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 38.44  E-value: 2.55e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15241925 225 RIVGFTAIYKFYRYPDRLRMRLSQILVLPSFQGKGLGSYLME 266
Cdd:COG1247  62 EVVGFASLGPFRPRPAYRGTAEESIYVDPDARGRGIGRALLE 103
 
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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