NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|507038261|ref|WP_016109943|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.17e-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: 71.83  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507038261   18 EQLFPLFEEVFGITTQTLNDFSDKGYWDDTyKALSFLQEDKVIANVSAFSLPLLINGEKINAAGIQSVMTHPNFRRQGLM 97
Cdd:pfam13527  10 DEVLRLLEYAFQDEDSPELREYFRPLLEEG-RVLGAFDDGELVSTLALYPFELNVPGKTLPAAGITGVATYPEYRGRGVM 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 507038261   98 TQLMSKMIEEIDKKCEC-ALLFTEKPELYTAFGFKV 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 1.17e-15

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 71.83  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507038261   18 EQLFPLFEEVFGITTQTLNDFSDKGYWDDTyKALSFLQEDKVIANVSAFSLPLLINGEKINAAGIQSVMTHPNFRRQGLM 97
Cdd:pfam13527  10 DEVLRLLEYAFQDEDSPELREYFRPLLEEG-RVLGAFDDGELVSTLALYPFELNVPGKTLPAAGITGVATYPEYRGRGVM 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 507038261   98 TQLMSKMIEEIDKKCEC-ALLFTEKPELYTAFGFKV 132
Cdd:pfam13527  89 SRLLRRSLEEMRERGVPlSFLYPSSYPIYRRFGYEI 124
Eis COG4552
Predicted acetyltransferase [General function prediction only];
17-130 4.56e-10

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 59.91  E-value: 4.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507038261  17 REQLFPLFEEVFG--ITTQTLNDFSDKGYWDDTYKALsflQEDKVIANVSAFSLPLLINGEKINAAGIQSVMTHPNFRRQ 94
Cdd:COG4552   11 LDAFARLLAYAFGpePDDEELEAYRPLLEPGRVLGVF---DDGELVGTLALYPFTLNVGGARVPMAGITGVAVAPEHRRR 87

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 507038261  95 GLMTQLMSKMIEEI-DKKCECALLFTEKPELYTAFGF 130
Cdd:COG4552   88 GVARALLREALAELrERGQPLSALYPFEPGFYRRFGY 124
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-107 5.90e-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: 37.64  E-value: 5.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 507038261  53 FLQEDKVIANVSafslpLLINGEKINAAGIQSVMTHPNFRRQGLMTQLMSKMIEE 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 1.17e-15

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 71.83  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507038261   18 EQLFPLFEEVFGITTQTLNDFSDKGYWDDTyKALSFLQEDKVIANVSAFSLPLLINGEKINAAGIQSVMTHPNFRRQGLM 97
Cdd:pfam13527  10 DEVLRLLEYAFQDEDSPELREYFRPLLEEG-RVLGAFDDGELVSTLALYPFELNVPGKTLPAAGITGVATYPEYRGRGVM 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 507038261   98 TQLMSKMIEEIDKKCEC-ALLFTEKPELYTAFGFKV 132
Cdd:pfam13527  89 SRLLRRSLEEMRERGVPlSFLYPSSYPIYRRFGYEI 124
Eis COG4552
Predicted acetyltransferase [General function prediction only];
17-130 4.56e-10

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 59.91  E-value: 4.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507038261  17 REQLFPLFEEVFG--ITTQTLNDFSDKGYWDDTYKALsflQEDKVIANVSAFSLPLLINGEKINAAGIQSVMTHPNFRRQ 94
Cdd:COG4552   11 LDAFARLLAYAFGpePDDEELEAYRPLLEPGRVLGVF---DDGELVGTLALYPFTLNVGGARVPMAGITGVAVAPEHRRR 87

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 507038261  95 GLMTQLMSKMIEEI-DKKCECALLFTEKPELYTAFGF 130
Cdd:COG4552   88 GVARALLREALAELrERGQPLSALYPFEPGFYRRFGY 124
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
78-138 1.07e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 51.45  E-value: 1.07e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507038261  78 NAAGIQSVMTHPNFRRQGLMTQLMSKMIEEI-DKKCECALLFTEK--PE---LYTAFGFKVVQEYLM 138
Cdd:COG3393   14 GVAEISGVYTHPEYRGRGLASALVAALAREAlARGARTPFLYVDAdnPAarrLYERLGFRPVGEYAT 80
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
18-143 5.10e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 48.16  E-value: 5.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507038261  18 EQLFPLFEEVFGITTQTlnDFSDKgYWDDTYKALSF--LQEDKVIANVSAFslPLLINGEkINAAGIQSVMTHPNFRRQG 95
Cdd:COG3153   10 EAIAALLRAAFGPGREA--ELVDR-LREDPAAGLSLvaEDDGEIVGHVALS--PVDIDGE-GPALLLGPLAVDPEYRGQG 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 507038261  96 LMTQLMSKMIEEIDKK-CECALLFTEKP--ELYTAFGFKVVQEYLMTIPYD 143
Cdd:COG3153   84 IGRALMRAALEAARERgARAVVLLGDPSllPFYERFGFRPAGELGLTLGPD 134
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 18-130 8.39e-07

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: 47.13  E-value: 8.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507038261   18 EQLFPLFEEVFGITTQTLNDFSDKGYWDDT-YKALSFLQEDKVIANVSAFslpllINGEKINAAGIQSVMTHPNFRRQGL 96
Cdd:pfam00583   2 EALYELLSEEFPEPWPDEPLDLLEDWDEDAsEGFFVAEEDGELVGFASLS-----IIDDEPPVGEIEGLAVAPEYRGKGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 507038261   97 MTQLMSKMIEE-IDKKCECALLFTEKP-----ELYTAFGF 130
Cdd:pfam00583  77 GTALLQALLEWaRERGCERIFLEVAADnlaaiALYEKLGF 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 78-155 3.08e-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: 42.67  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507038261  78 NAAGIQSVMTHPNFRRQGLMTQLMSKMIEE-IDKKCECALLFT--EKPELYTAFGFKVVQEYlmTIPYDKNINNNDSLLK 154
Cdd:COG1246   51 DLAELRSLAVHPDYRGRGIGRRLLEALLAEaRELGLKRLFLLTtsAAIHFYEKLGFEEIDKE--DLPYAKVWQRDSVVME 128


                 .
gi 507038261 155 K 155
Cdd:COG1246  129 K 129
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 79-132 5.42e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 40.90  E-value: 5.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 507038261   79 AAGIQSVMTHPNFRRQGLMTQLMsKMIEEIDKKCECALLFTEKPE----LYTAFGFKV 132
Cdd:pfam13508  28 ALAELRLAVHPEYRGQGIGRALL-EAAEAAAKEGGIKLLELETTNraaaFYEKLGFEE 84
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 82-135 7.90e-05

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 40.79  E-value: 7.90e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 507038261  82 IQSVMTHPNFRRQGLMTQLMSKMIEEI-DKKCECALLFTEKP-----ELYTAFGFKVVQE 135
Cdd:COG0456   16 IEDLAVDPEYRGRGIGRALLEAALERArERGARRLRLEVREDneaaiALYEKLGFEEVGE 75
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 53-107 5.90e-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: 37.64  E-value: 5.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 507038261  53 FLQEDKVIANVSafslpLLINGEKINAAGIQSVMTHPNFRRQGLMTQLMSKMIEE 107
Cdd:cd04301    4 AEDDGEIVGFAS-----LSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEE 53
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
84-133 6.82e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 36.51  E-value: 6.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 507038261  84 SVMTHPNFRRQGLMTQLMSKMIEE-IDKKCECALLFTEKP-----ELYTAFGFKVV 133
Cdd:COG1247   85 SIYVDPDARGRGIGRALLEALIERaRARGYRRLVAVVLADneasiALYEKLGFEEV 140
 
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