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Conserved domains on  [gi|515716943|ref|WP_017149543|]
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GNAT family N-acetyltransferase [Bacillus bingmayongensis]

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 ...
21-132 2.78e-12

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: 62.59  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515716943   21 FQLFEEVFRIPAQTLQNFesngFWDTTYKPFSYL---QEGQVIANVSMFSLPMFVNGEQIHAAGIQSVMTHPEYRRKGLM 97
Cdd:pfam13527  13 LRLLEYAFQDEDSPELRE----YFRPLLEEGRVLgafDDGELVSTLALYPFELNVPGKTLPAAGITGVATYPEYRGRGVM 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 515716943   98 KQLFCKVLQEIDTQYEC-TVLFTEKPELYEPFGFRV 132
Cdd:pfam13527  89 SRLLRRSLEEMRERGVPlSFLYPSSYPIYRRFGYEI 124
 
Name Accession Description Interval E-value
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
21-132 2.78e-12

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 62.59  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515716943   21 FQLFEEVFRIPAQTLQNFesngFWDTTYKPFSYL---QEGQVIANVSMFSLPMFVNGEQIHAAGIQSVMTHPEYRRKGLM 97
Cdd:pfam13527  13 LRLLEYAFQDEDSPELRE----YFRPLLEEGRVLgafDDGELVSTLALYPFELNVPGKTLPAAGITGVATYPEYRGRGVM 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 515716943   98 KQLFCKVLQEIDTQYEC-TVLFTEKPELYEPFGFRV 132
Cdd:pfam13527  89 SRLLRRSLEEMRERGVPlSFLYPSSYPIYRRFGYEI 124
Eis COG4552
Predicted acetyltransferase [General function prediction only];
24-130 5.63e-10

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 59.53  E-value: 5.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515716943  24 FEEVFRIPAQTLQNFESNGFWDTT---YKPFSYL---QEGQVIANVSMFSLPMFVNGEQIHAAGIQSVMTHPEYRRKGLM 97
Cdd:COG4552   11 LDAFARLLAYAFGPEPDDEELEAYrplLEPGRVLgvfDDGELVGTLALYPFTLNVGGARVPMAGITGVAVAPEHRRRGVA 90
                         90       100       110
                 ....*....|....*....|....*....|....
gi 515716943  98 KQLFCKVLQEI-DTQYECTVLFTEKPELYEPFGF 130
Cdd:COG4552   91 RALLREALAELrERGQPLSALYPFEPGFYRRFGY 124
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
51-107 9.16e-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: 36.87  E-value: 9.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515716943  51 FSYLQEGQVIANVSMFslpmfVNGEQIHAAGIQSVMTHPEYRRKGLMKQLFCKVLQE 107
Cdd:cd04301    2 LVAEDDGEIVGFASLS-----PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
 
Name Accession Description Interval E-value
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
21-132 2.78e-12

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 62.59  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515716943   21 FQLFEEVFRIPAQTLQNFesngFWDTTYKPFSYL---QEGQVIANVSMFSLPMFVNGEQIHAAGIQSVMTHPEYRRKGLM 97
Cdd:pfam13527  13 LRLLEYAFQDEDSPELRE----YFRPLLEEGRVLgafDDGELVSTLALYPFELNVPGKTLPAAGITGVATYPEYRGRGVM 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 515716943   98 KQLFCKVLQEIDTQYEC-TVLFTEKPELYEPFGFRV 132
Cdd:pfam13527  89 SRLLRRSLEEMRERGVPlSFLYPSSYPIYRRFGYEI 124
Eis COG4552
Predicted acetyltransferase [General function prediction only];
24-130 5.63e-10

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 59.53  E-value: 5.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515716943  24 FEEVFRIPAQTLQNFESNGFWDTT---YKPFSYL---QEGQVIANVSMFSLPMFVNGEQIHAAGIQSVMTHPEYRRKGLM 97
Cdd:COG4552   11 LDAFARLLAYAFGPEPDDEELEAYrplLEPGRVLgvfDDGELVGTLALYPFTLNVGGARVPMAGITGVAVAPEHRRRGVA 90
                         90       100       110
                 ....*....|....*....|....*....|....
gi 515716943  98 KQLFCKVLQEI-DTQYECTVLFTEKPELYEPFGF 130
Cdd:COG4552   91 RALLREALAELrERGQPLSALYPFEPGFYRRFGY 124
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
18-140 1.36e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 49.70  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515716943  18 ELLFQLFEEVFRIP--AQTLQNFESNGFWDTTykpFSYLQEGQVIANVSMFslPMFVNGEqIHAAGIQSVMTHPEYRRKG 95
Cdd:COG3153   10 EAIAALLRAAFGPGreAELVDRLREDPAAGLS---LVAEDDGEIVGHVALS--PVDIDGE-GPALLLGPLAVDPEYRGQG 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515716943  96 LMKQLFCKVLQEIDTQ-YECTVLFTEKP--ELYEPFGFRVVQEHLMTL 140
Cdd:COG3153   84 IGRALMRAALEAARERgARAVVLLGDPSllPFYERFGFRPAGELGLTL 131
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
78-135 8.63e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 46.06  E-value: 8.63e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515716943  78 HAAGIQSVMTHPEYRRKGLMKQLFCKVLQEI-DTQYECTVLFTEK--PE---LYEPFGFRVVQE 135
Cdd:COG3393   14 GVAEISGVYTHPEYRGRGLASALVAALAREAlARGARTPFLYVDAdnPAarrLYERLGFRPVGE 77
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
20-130 4.31e-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: 39.42  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515716943   20 LFQLFEEVFRIPAQTLQNFESNGFW-DTTYKPFSYLQEGQVIANVSMFslpmfVNGEQIHAAGIQSVMTHPEYRRKGLMK 98
Cdd:pfam00583   4 LYELLSEEFPEPWPDEPLDLLEDWDeDASEGFFVAEEDGELVGFASLS-----IIDDEPPVGEIEGLAVAPEYRGKGIGT 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 515716943   99 QLFCKVLQE-IDTQYECTVLFTEKP-----ELYEPFGF 130
Cdd:pfam00583  79 ALLQALLEWaRERGCERIFLEVAADnlaaiALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
51-107 9.16e-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: 36.87  E-value: 9.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515716943  51 FSYLQEGQVIANVSMFslpmfVNGEQIHAAGIQSVMTHPEYRRKGLMKQLFCKVLQE 107
Cdd:cd04301    2 LVAEDDGEIVGFASLS-----PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
51-132 1.25e-03

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 37.05  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515716943   51 FSYLQEGQVIANVsmfslpMFVNGEQIHAAGIQSVMTHPEYRRKGLMKQLFcKVLQEIDTQYECTVLFTEKPE----LYE 126
Cdd:pfam13508   6 FVAEDDGKIVGFA------ALLPLDDEGALAELRLAVHPEYRGQGIGRALL-EAAEAAAKEGGIKLLELETTNraaaFYE 78

                  ....*.
gi 515716943  127 PFGFRV 132
Cdd:pfam13508  79 KLGFEE 84
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
78-136 2.02e-03

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 36.56  E-value: 2.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515716943  78 HAAGIQSVMTHPEYRRKGLMKQLFCKVLQEI-DTQYECTVLFTEKP-----ELYEPFGFRVVQEH 136
Cdd:COG0456   12 DEAEIEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEVREDneaaiALYEKLGFEEVGER 76
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
82-135 2.79e-03

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: 37.28  E-value: 2.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515716943  82 IQSVMTHPEYRRKGLMKQLFCKVLQEIDTQ-YECTVLFT--EKPELYEPFGFRVVQE 135
Cdd:COG1246   55 LRSLAVHPDYRGRGIGRRLLEALLAEARELgLKRLFLLTtsAAIHFYEKLGFEEIDK 111
 
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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