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Conserved domains on  [gi|666885830|gb|AIG33654|]
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GNAT family acetyltransferase [Flavobacterium psychrophilum]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-143 2.71e-25

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 94.68  E-value: 2.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830   1 MIVRKGEKKDMSAVLNLIKE-----LAIFEKEPQAVEvtandLLRDGFSD--NPLFYTFIAEVEGEIIGMAlYYYRYSTW 73
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSEE-----EREAWFAAilAPGRPVLVAEEDGEVVGFA-SLGPFRPR 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 666885830  74 KG-KTIHLEDLIVQEKSRGTGAGYALYTAIISQGKKDNVRRIEWNVLNWNTLAINFYNKSGAKLLQDWRVV 143
Cdd:COG1247   76 PAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEV 146
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-143 2.71e-25

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 94.68  E-value: 2.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830   1 MIVRKGEKKDMSAVLNLIKE-----LAIFEKEPQAVEvtandLLRDGFSD--NPLFYTFIAEVEGEIIGMAlYYYRYSTW 73
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSEE-----EREAWFAAilAPGRPVLVAEEDGEVVGFA-SLGPFRPR 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 666885830  74 KG-KTIHLEDLIVQEKSRGTGAGYALYTAIISQGKKDNVRRIEWNVLNWNTLAINFYNKSGAKLLQDWRVV 143
Cdd:COG1247   76 PAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEV 146
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
23-133 6.44e-16

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: 69.08  E-value: 6.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830   23 IFEKEPQAVEVTANDLLRDGFSDNPLFYTFIAEVEGEIIGMALYYYRYSTWKgkTIHLEDLIVQEKSRGTGAGYALYTAI 102
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP--VGEIEGLAVAPEYRGKGIGTALLQAL 84
                          90       100       110
                  ....*....|....*....|....*....|.
gi 666885830  103 ISQGKKDNVRRIEWNVLNWNTLAINFYNKSG 133
Cdd:pfam00583  85 LEWARERGCERIFLEVAADNLAAIALYEKLG 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
52-115 4.14e-07

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: 44.96  E-value: 4.14e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 666885830  52 FIAEVEGEIIGMALYYYRYstWKGKTIHLEDLIVQEKSRGTGAGYALYTAIISQGKKDNVRRIE 115
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-143 2.71e-25

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 94.68  E-value: 2.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830   1 MIVRKGEKKDMSAVLNLIKE-----LAIFEKEPQAVEvtandLLRDGFSD--NPLFYTFIAEVEGEIIGMAlYYYRYSTW 73
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEaiaegTATFETEPPSEE-----EREAWFAAilAPGRPVLVAEEDGEVVGFA-SLGPFRPR 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 666885830  74 KG-KTIHLEDLIVQEKSRGTGAGYALYTAIISQGKKDNVRRIEWNVLNWNTLAINFYNKSGAKLLQDWRVV 143
Cdd:COG1247   76 PAyRGTAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEV 146
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
23-133 6.44e-16

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: 69.08  E-value: 6.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830   23 IFEKEPQAVEVTANDLLRDGFSDNPLFYTFIAEVEGEIIGMALYYYRYSTWKgkTIHLEDLIVQEKSRGTGAGYALYTAI 102
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP--VGEIEGLAVAPEYRGKGIGTALLQAL 84
                          90       100       110
                  ....*....|....*....|....*....|.
gi 666885830  103 ISQGKKDNVRRIEWNVLNWNTLAINFYNKSG 133
Cdd:pfam00583  85 LEWARERGCERIFLEVAADNLAAIALYEKLG 115
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-142 2.14e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 60.87  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830   3 VRKGEKKDMSAVLNLIKELAIFEKEPQAVEvtanDLLRDGfsdnPLFYTFIAEVEGEIIGMALYYYRYSTWKGKTIHLED 82
Cdd:COG3153    1 IRPATPEDAEAIAALLRAAFGPGREAELVD----RLREDP----AAGLSLVAEDDGEIVGHVALSPVDIDGEGPALLLGP 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830  83 LIVQEKSRGTGAGYALYTAIISQGKKDNVRRIewnVLNWNTLAINFYNKSGAKLLQDWRV 142
Cdd:COG3153   73 LAVDPEYRGQGIGRALMRAALEAARERGARAV---VLLGDPSLLPFYERFGFRPAGELGL 129
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
1-142 4.45e-11

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 56.99  E-value: 4.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830   1 MIVRKGEKKDMSAVLN---LIKELAIFEKEPQAVEVtandllrdgfsdnplfytFIAEVEGEIIGmalyYYRYSTWKGKT 77
Cdd:COG0454    1 MSIRKATPEDINFILLieaLDAELKAMEGSLAGAEF------------------IAVDDKGEPIG----FAGLRRLDDKV 58
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 666885830  78 IHLEDLIVQEKSRGTGAGYALYTAIISQGKKDNVRRIEWNVLNWNTLAINFYNKSGAKLLQDWRV 142
Cdd:COG0454   59 LELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIERYVA 123
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
62-133 9.88e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 55.05  E-value: 9.88e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 666885830  62 GMALYYYRYStwkGKTIHLEDLIVQEKSRGTGAGYALYTAIISQGKKDNVRRIEWNVLNWNTLAINFYNKSG 133
Cdd:COG0456    1 GFALLGLVDG---GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLG 69
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
1-133 4.00e-10

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: 54.61  E-value: 4.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830   1 MIVRKGEKKDMSAVLNLIKELAIFEKEPQavevtandllrdgfsdnplfyTFIAEVEGEIIGMAlyyyRYSTWKGKTIHL 80
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALEEEIGE---------------------FWVAEEDGEIVGCA----ALHPLDEDLAEL 55
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 666885830  81 EDLIVQEKSRGTGAGYALYTAIISQGKKDNVRRIEWNVlnwNTLAINFYNKSG 133
Cdd:COG1246   56 RSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLG 105
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
52-115 4.14e-07

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: 44.96  E-value: 4.14e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 666885830  52 FIAEVEGEIIGMALYYYRYstWKGKTIHLEDLIVQEKSRGTGAGYALYTAIISQGKKDNVRRIE 115
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDG--SGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
25-133 1.48e-06

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 44.95  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830   25 EKEPQAVEVTANDLLRDGFS---DNPLFYTFIAEVEGEIIGMAlyyyRYSTwkgkTIHLEDLIVQEKSRGTGAGYALYTA 101
Cdd:pfam13673   4 DYSEEGIETFYEFISPEALReriDQGEYFFFVAFEGGQIVGVI----ALRD----RGHISLLFVDPDYQGQGIGKALLEA 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 666885830  102 IISQGKKDNVRRIEWNVlNWNTLAINFYNKSG 133
Cdd:pfam13673  76 VEDYAEKDGIKLSELTV-NASPYAVPFYEKLG 106
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
1-136 2.22e-05

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 42.29  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830   1 MIVRKGEKKDMSAVLNLIKELAIFE------KEPQAVEVTANDLLRDGFSDNPLFYTFIAEVEGEIIGMALYYYRysTWK 74
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARylpgppYSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVVGLYDI--DRA 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 666885830  75 GKTIHLeDLIVQEKSRGTGAGYALYTAIISQGKKD-NVRRIEWNVLNWNTLAINFYNKSGAKL 136
Cdd:COG1670   86 NRSAEI-GYWLAPAYWGKGYATEALRALLDYAFEElGLHRVEAEVDPDNTASIRVLEKLGFRL 147
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
47-133 2.33e-05

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 40.52  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 666885830   47 PLFYTFIAEVEGEIIGMALYYYRYSTWkgkTIHLEDLIVQEKSRGTGAGYALYTAIISQGKKDNVRRIEWNVLNWntlAI 126
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEG---ALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNR---AA 74

                  ....*..
gi 666885830  127 NFYNKSG 133
Cdd:pfam13508  75 AFYEKLG 81
 
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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