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Conserved domains on  [gi|507046868|ref|WP_016117903|]
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MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

Protein Classification

GNAT family protein( domain architecture ID 106742)

GNAT (Gcn5-related N-acetyltransferase) family protein similar to N-acetyltransferases that catalyze the transfer of an acetyl group from acetyl-CoA to a substrate

PubMed:  15581578

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAT_SF super family cl17182
N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of ...
 18-132 9.32e-15

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 pfam13527:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 124  Bit Score: 69.14  E-value: 9.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507046868   18 EQLFPLFEEVLGITTQTLNDFSDKGYWDDTyKALSFLQEDKVIANVAAFSLPLLINGEKINAAGIQSVMTHPNFRRQGLM 97
Cdd:pfam13527  10 DEVLRLLEYAFQDEDSPELREYFRPLLEEG-RVLGAFDDGELVSTLALYPFELNVPGKTLPAAGITGVATYPEYRGRGVM 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 507046868   98 TQLMSKMIEEIDKKCEC-ALLFTEKPELYTTFGFKV 132
Cdd:pfam13527  89 SRLLRRSLEEMRERGVPlSFLYPSSYPIYRRFGYEI 124
 
Name Accession Description Interval E-value
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 18-132 9.32e-15

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 69.14  E-value: 9.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507046868   18 EQLFPLFEEVLGITTQTLNDFSDKGYWDDTyKALSFLQEDKVIANVAAFSLPLLINGEKINAAGIQSVMTHPNFRRQGLM 97
Cdd:pfam13527  10 DEVLRLLEYAFQDEDSPELREYFRPLLEEG-RVLGAFDDGELVSTLALYPFELNVPGKTLPAAGITGVATYPEYRGRGVM 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 507046868   98 TQLMSKMIEEIDKKCEC-ALLFTEKPELYTTFGFKV 132
Cdd:pfam13527  89 SRLLRRSLEEMRERGVPlSFLYPSSYPIYRRFGYEI 124
Eis COG4552
Predicted acetyltransferase [General function prediction only];
55-130 1.34e-09

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 58.37  E-value: 1.34e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507046868  55 QEDKVIANVAAFSLPLLINGEKINAAGIQSVMTHPNFRRQGLMTQLMSKMIEEI-DKKCECALLFTEKPELYTTFGF 130
Cdd:COG4552   48 DDGELVGTLALYPFTLNVGGARVPMAGITGVAVAPEHRRRGVARALLREALAELrERGQPLSALYPFEPGFYRRFGY 124
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-107 7.33e-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: 37.26  E-value: 7.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 507046868  53 FLQEDKVIANVAafslpLLINGEKINAAGIQSVMTHPNFRRQGLMTQLMSKMIEE 107
Cdd:cd04301    4 AEDDGEIVGFAS-----LSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
 
Name Accession Description Interval E-value
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 18-132 9.32e-15

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 69.14  E-value: 9.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507046868   18 EQLFPLFEEVLGITTQTLNDFSDKGYWDDTyKALSFLQEDKVIANVAAFSLPLLINGEKINAAGIQSVMTHPNFRRQGLM 97
Cdd:pfam13527  10 DEVLRLLEYAFQDEDSPELREYFRPLLEEG-RVLGAFDDGELVSTLALYPFELNVPGKTLPAAGITGVATYPEYRGRGVM 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 507046868   98 TQLMSKMIEEIDKKCEC-ALLFTEKPELYTTFGFKV 132
Cdd:pfam13527  89 SRLLRRSLEEMRERGVPlSFLYPSSYPIYRRFGYEI 124
Eis COG4552
Predicted acetyltransferase [General function prediction only];
55-130 1.34e-09

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 58.37  E-value: 1.34e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507046868  55 QEDKVIANVAAFSLPLLINGEKINAAGIQSVMTHPNFRRQGLMTQLMSKMIEEI-DKKCECALLFTEKPELYTTFGF 130
Cdd:COG4552   48 DDGELVGTLALYPFTLNVGGARVPMAGITGVAVAPEHRRRGVARALLREALAELrERGQPLSALYPFEPGFYRRFGY 124
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
78-138 3.82e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 49.91  E-value: 3.82e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507046868  78 NAAGIQSVMTHPNFRRQGLMTQLMSKMIEEI-DKKCECALLFTEK--PE---LYTTFGFKVVQEYLM 138
Cdd:COG3393   14 GVAEISGVYTHPEYRGRGLASALVAALAREAlARGARTPFLYVDAdnPAarrLYERLGFRPVGEYAT 80
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
56-143 2.21e-06

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 46.23  E-value: 2.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507046868  56 EDKVIANVAAFslPLLINGEkINAAGIQSVMTHPNFRRQGLMTQLMSKMIEEIDKK-CECALLFTEKP--ELYTTFGFKV 132
Cdd:COG3153   47 DGEIVGHVALS--PVDIDGE-GPALLLGPLAVDPEYRGQGIGRALMRAALEAARERgARAVVLLGDPSllPFYERFGFRP 123

                         90
                 ....*....|.
gi 507046868 133 VQEYLMTIPYD 143
Cdd:COG3153  124 AGELGLTLGPD 134
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-130 2.78e-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: 45.59  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507046868   18 EQLFPLFEEVLGITTQTLNDFSDKGYWDDTYKALSFLQEDKVIANVAAFSlpllINGEKINAAGIQSVMTHPNFRRQGLM 97
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLS----IIDDEPPVGEIEGLAVAPEYRGKGIG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 507046868   98 TQLMSKMIEE-IDKKCECALLFTEKP-----ELYTTFGF 130
Cdd:pfam00583  78 TALLQALLEWaRERGCERIFLEVAADnlaaiALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 78-155 8.90e-05

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: 8.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507046868  78 NAAGIQSVMTHPNFRRQGLMTQLMSKMIEE-IDKKCECALLFT--EKPELYTTFGFKVVQEYlmTIPYDKNINNNDSLLK 154
Cdd:COG1246   51 DLAELRSLAVHPDYRGRGIGRRLLEALLAEaRELGLKRLFLLTtsAAIHFYEKLGFEEIDKE--DLPYAKVWQRDSVVME 128


                 .
gi 507046868 155 K 155
Cdd:COG1246  129 K 129
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 79-132 1.15e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 40.13  E-value: 1.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 507046868   79 AAGIQSVMTHPNFRRQGLMTQLMsKMIEEIDKKCECALLFTEKPE----LYTTFGFKV 132
Cdd:pfam13508  28 ALAELRLAVHPEYRGQGIGRALL-EAAEAAAKEGGIKLLELETTNraaaFYEKLGFEE 84
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 82-135 2.00e-04

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 39.64  E-value: 2.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 507046868  82 IQSVMTHPNFRRQGLMTQLMSKMIEEI-DKKCECALLFTEKP-----ELYTTFGFKVVQE 135
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEVREDneaaiALYEKLGFEEVGE 75
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-107 7.33e-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: 37.26  E-value: 7.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 507046868  53 FLQEDKVIANVAafslpLLINGEKINAAGIQSVMTHPNFRRQGLMTQLMSKMIEE 107
Cdd:cd04301    4 AEDDGEIVGFAS-----LSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
 
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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