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Conserved domains on  [gi|1172869192|gb|OQQ04077|]
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GNAT family N-acetyltransferase [Vibrio anguillarum]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11418877)

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
PubMed:  27367672|26818562|15581578|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 69-139 1.27e-11

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


:

Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 57.36  E-value: 1.27e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172869192  69 LICFKPYDQAFHIHLLIIFPDHQKKKLGFKVINHIHQLAAEANRNLITLSSFKSNKSAIGFYSSLGYQITD 139
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVG 74
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 69-139 1.27e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 57.36  E-value: 1.27e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172869192  69 LICFKPYDQAFHIHLLIIFPDHQKKKLGFKVINHIHQLAAEANRNLITLSSFKSNKSAIGFYSSLGYQITD 139
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVG 74
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 34-135 1.28e-11

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: 57.91  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172869192  34 EPVYGWDDEYQYHRLTTEYQHSWYYWVTYRNQR-VGLICFKPYDQAF---HIHLLIIFPDHQKKKLGFKVINHIHQLAAE 109
Cdd:pfam00583  11 EFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGElVGFASLSIIDDEPpvgEIEGLAVAPEYRGKGIGTALLQALLEWARE 90

                          90       100
                  ....*....|....*....|....*.
gi 1172869192 110 ANRNLITLSSFKSNKSAIGFYSSLGY 135
Cdd:pfam00583  91 RGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-118 4.00e-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: 39.57  E-value: 4.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172869192  58 YWVTYRNQR-VGLICFKPYDQA---FHIHLLIIFPDHQKKKLGFKVINHIHQLAAEANRNLITLS 118
Cdd:cd04301     1 FLVAEDDGEiVGFASLSPDGSGgdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 61-152 6.56e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 40.68  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172869192  61 TYRNQRVGL-ICFKPYDQA--FHIhllIIFPDHQKKKLGFKVINH-IHQLAAeanRNLITL--SSFKSNKSAIGFYSSLG 134
Cdd:PRK09491   46 TVNGQMAAFaITQVVLDEAtlFNI---AVDPDYQRQGLGRALLEHlIDELEK---RGVATLwlEVRASNAAAIALYESLG 119

                          90       100
                  ....*....|....*....|....*..
gi 1172869192 135 ---------YQITDSGDENFVSMACEI 152
Cdd:PRK09491  120 fnevtirrnYYPTADGREDAIIMALPL 146
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 69-139 1.27e-11

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 57.36  E-value: 1.27e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172869192  69 LICFKPYDQAFHIHLLIIFPDHQKKKLGFKVINHIHQLAAEANRNLITLSSFKSNKSAIGFYSSLGYQITD 139
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVG 74
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 34-135 1.28e-11

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: 57.91  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172869192  34 EPVYGWDDEYQYHRLTTEYQHSWYYWVTYRNQR-VGLICFKPYDQAF---HIHLLIIFPDHQKKKLGFKVINHIHQLAAE 109
Cdd:pfam00583  11 EFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGElVGFASLSIIDDEPpvgEIEGLAVAPEYRGKGIGTALLQALLEWARE 90

                          90       100
                  ....*....|....*....|....*.
gi 1172869192 110 ANRNLITLSSFKSNKSAIGFYSSLGY 135
Cdd:pfam00583  91 RGCERIFLEVAADNLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 57-139 8.39e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 53.52  E-value: 8.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172869192  57 YYWVTYRNQRVGLICFKPYDQ-AFHIHLLIIFPDHQKKKLGFKVINHIHQLAAEANRNLITLSSFKSNKSAIGFYSSLGY 135
Cdd:COG0454    36 FIAVDDKGEPIGFAGLRRLDDkVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGF 115


                  ....
gi 1172869192 136 QITD 139
Cdd:COG0454   116 KEIE 119
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 57-137 4.02e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 50.53  E-value: 4.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172869192  57 YYWVTYRN-QRVGLICFKPYDQAFHIHLLIIF--PDHQKKKLGFKVINHIHQLAAEANRNLITLSSfksNKSAIGFYSSL 133
Cdd:pfam13508   4 RFFVAEDDgKIVGFAALLPLDDEGALAELRLAvhPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAAAFYEKL 80


                  ....
gi 1172869192 134 GYQI 137
Cdd:pfam13508  81 GFEE 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 40-142 4.92e-07

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: 46.14  E-value: 4.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172869192  40 DDEYQYHRLTTEY---QHSWYYWVTYRN-QRVGLICFKPYDQAF-HIHLLIIFPDHQKKKLGFKVINHIHQLAAEANRNL 114
Cdd:COG1246     9 DDVPAILELIRPYaleEEIGEFWVAEEDgEIVGCAALHPLDEDLaELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKR 88

                          90       100
                  ....*....|....*....|....*...
gi 1172869192 115 ITLSSfksNKSAIGFYSSLGYQITDSGD 142
Cdd:COG1246    89 LFLLT---TSAAIHFYEKLGFEEIDKED 113
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
59-142 5.41e-07

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 46.23  E-value: 5.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172869192  59 WVTYRNQR-VGLICFKPYD-----QAFHIHLLIIFPDHQKKKLGFKVINHIHQLAAEANRNLITLSSfksNKSAIGFYSS 132
Cdd:COG3153    42 LVAEDDGEiVGHVALSPVDidgegPALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLG---DPSLLPFYER 118

                          90
                  ....*....|
gi 1172869192 133 LGYQITDSGD 142
Cdd:COG3153   119 FGFRPAGELG 128
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 57-152 1.15e-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: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172869192  57 YYWVTYRNQR-VGLICFKpydQAFHIHLLIIFPDHQKKKLGFKVINHIHQLAAEANRNLITLsSFKSNKSAIGFYSSLGY 135
Cdd:pfam13673  32 FFFVAFEGGQiVGVIALR---DRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSEL-TVNASPYAVPFYEKLGF 107

                          90       100
                  ....*....|....*....|..
gi 1172869192 136 QITDS-----GDEnFVSMACEI 152
Cdd:pfam13673 108 RATGPeqefnGIR-FVPMEKEL 128
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-118 4.00e-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: 39.57  E-value: 4.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172869192  58 YWVTYRNQR-VGLICFKPYDQA---FHIHLLIIFPDHQKKKLGFKVINHIHQLAAEANRNLITLS 118
Cdd:cd04301     1 FLVAEDDGEiVGFASLSPDGSGgdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 61-152 6.56e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 40.68  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172869192  61 TYRNQRVGL-ICFKPYDQA--FHIhllIIFPDHQKKKLGFKVINH-IHQLAAeanRNLITL--SSFKSNKSAIGFYSSLG 134
Cdd:PRK09491   46 TVNGQMAAFaITQVVLDEAtlFNI---AVDPDYQRQGLGRALLEHlIDELEK---RGVATLwlEVRASNAAAIALYESLG 119

                          90       100
                  ....*....|....*....|....*..
gi 1172869192 135 ---------YQITDSGDENFVSMACEI 152
Cdd:PRK09491  120 fnevtirrnYYPTADGREDAIIMALPL 146
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
72-143 1.26e-04

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 39.40  E-value: 1.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172869192  72 FKPYDQAFHIHLLIIFPDHQKKKLGFKVINHIHQLAAEANRNLITLSSfksNKSAIGFYSSLGYQITdsGDE 143
Cdd:COG2153    52 LPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA---QAHAVGFYEKLGFVPV--GEE 118
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
46-139 1.03e-03

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 37.28  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172869192  46 HRLTTEYQHSWYYWV-TYRNQRVGLICFKPY--DQAF-HIHLLIIF--PDHQKKKLGFKVINHIHQLAAEANRNLITLSS 119
Cdd:COG1247    42 AWFAAILAPGRPVLVaEEDGEVVGFASLGPFrpRPAYrGTAEESIYvdPDARGRGIGRALLEALIERARARGYRRLVAVV 121

                          90       100
                  ....*....|....*....|
gi 1172869192 120 FKSNKSAIGFYSSLGYQITD 139
Cdd:COG1247   122 LADNEASIALYEKLGFEEVG 141
 
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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