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Conserved domains on  [gi|490242715|ref|WP_004140943|]
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MULTISPECIES: GNAT family N-acetyltransferase [Klebsiella]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11447364)

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
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-166 1.79e-41

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: 137.05  E-value: 1.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242715   2 TTITTPRLSLTRFVTDDWPFFLRLRQDPQVMRFMGEV-LSEEALRSVFVSRCADP-----GVFVLRDKF-GEALGDIGLR 74
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPpYSLEEARAWLERLLADWadggaLPFAIEDKEdGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242715  75 ISPKNPHEADVGYALLPQAQGKGYASEALRAVCEYGFTTLGVQAINAWVLGENRGSSRLLEKQGFVRTQVLEKAYHLNGV 154
Cdd:COG1670   81 DIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160

                        170
                 ....*....|..
gi 490242715 155 DYDDWIYRLERE 166
Cdd:COG1670  161 YRDHVLYSLLRE 172
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-166 1.79e-41

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: 137.05  E-value: 1.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242715   2 TTITTPRLSLTRFVTDDWPFFLRLRQDPQVMRFMGEV-LSEEALRSVFVSRCADP-----GVFVLRDKF-GEALGDIGLR 74
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPpYSLEEARAWLERLLADWadggaLPFAIEDKEdGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242715  75 ISPKNPHEADVGYALLPQAQGKGYASEALRAVCEYGFTTLGVQAINAWVLGENRGSSRLLEKQGFVRTQVLEKAYHLNGV 154
Cdd:COG1670   81 DIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160

                        170
                 ....*....|..
gi 490242715 155 DYDDWIYRLERE 166
Cdd:COG1670  161 YRDHVLYSLLRE 172
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 8-140 1.04e-29

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 105.89  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242715    8 RLSLTRFVTDDWPFFLRLRQDPQVMRF-MGEVLSEEA----LRSVFVSRCADPG-VFVLRDKFGEALGDIGLRISPKNPH 81
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYgVPWPLTLEEarewLARIWAADEAERGyGWAIELKDTGFIGSIGLYDIDGEPE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490242715   82 EADVGYALLPQAQGKGYASEALRAVCEYGFTTLGVQAINAWVLGENRGSSRLLEKQGFV 140
Cdd:pfam13302  81 RAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 91-153 1.37e-04

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 40.55  E-value: 1.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490242715  91 PQAQGKGYASEALRAVCEYGFTTLGVQAINAWVLGENRGSSRLLEKQGFVRTQVLEKAYHLNG 153
Cdd:PRK15130  92 PEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFING 154
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-109 2.42e-03

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: 34.94  E-value: 2.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490242715  57 VFVLRDKfGEALGDIGLRISPKNPHEADVGY-ALLPQAQGKGYASEALRAVCEY 109
Cdd:cd04301    1 FLVAEDD-GEIVGFASLSPDGSGGDTAYIGDlAVLPEYRGKGIGSALLEAAEEE 53
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-166 1.79e-41

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: 137.05  E-value: 1.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242715   2 TTITTPRLSLTRFVTDDWPFFLRLRQDPQVMRFMGEV-LSEEALRSVFVSRCADP-----GVFVLRDKF-GEALGDIGLR 74
Cdd:COG1670    1 PTLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPpYSLEEARAWLERLLADWadggaLPFAIEDKEdGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242715  75 ISPKNPHEADVGYALLPQAQGKGYASEALRAVCEYGFTTLGVQAINAWVLGENRGSSRLLEKQGFVRTQVLEKAYHLNGV 154
Cdd:COG1670   81 DIDRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGR 160

                        170
                 ....*....|..
gi 490242715 155 DYDDWIYRLERE 166
Cdd:COG1670  161 YRDHVLYSLLRE 172
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 8-140 1.04e-29

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 105.89  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242715    8 RLSLTRFVTDDWPFFLRLRQDPQVMRF-MGEVLSEEA----LRSVFVSRCADPG-VFVLRDKFGEALGDIGLRISPKNPH 81
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEVMRYgVPWPLTLEEarewLARIWAADEAERGyGWAIELKDTGFIGSIGLYDIDGEPE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490242715   82 EADVGYALLPQAQGKGYASEALRAVCEYGFTTLGVQAINAWVLGENRGSSRLLEKQGFV 140
Cdd:pfam13302  81 RAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
17-163 5.52e-12

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 60.39  E-value: 5.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242715  17 DDWPFFLRLRQD---PQVMRFMGEVLSEEALRSVFVSRCADPG-VFVLRDKfGEALGDIGL---RISPKNPHEADVGYAL 89
Cdd:COG1247   10 EDAPAIAAIYNEaiaEGTATFETEPPSEEEREAWFAAILAPGRpVLVAEED-GEVVGFASLgpfRPRPAYRGTAEESIYV 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490242715  90 LPQAQGKGYASEALRAVCEYgFTTLGVQAINAWVLGENRGSSRLLEKQGFVRTQVLEKAYHLNGVDYDDWIYRL 163
Cdd:COG1247   89 DPDARGRGIGRALLEALIER-ARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQK 161
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 32-139 2.16e-08

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: 49.82  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242715   32 MRFMGEVLSEEALRSVFVSRCADPGVFVLRDKFGEALGDIGLRISPKNPHEADV-GYALLPQAQGKGYASEALRAVCEYG 110
Cdd:pfam00583   9 SEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPPVGEIeGLAVAPEYRGKGIGTALLQALLEWA 88

                          90       100
                  ....*....|....*....|....*....
gi 490242715  111 FtTLGVQAINAWVLGENRGSSRLLEKQGF 139
Cdd:pfam00583  89 R-ERGCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 88-156 7.34e-05

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: 7.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490242715  88 ALLPQAQGKGYASEALRAVCEYgFTTLGVQAINAWVLGENRGSSRLLEKQGFVRTQVLEKAYHLNGVDY 156
Cdd:COG0456   20 AVDPEYRGRGIGRALLEAALER-ARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVM 87
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 91-153 1.37e-04

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 40.55  E-value: 1.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490242715  91 PQAQGKGYASEALRAVCEYGFTTLGVQAINAWVLGENRGSSRLLEKQGFVRTQVLEKAYHLNG 153
Cdd:PRK15130  92 PEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFING 154
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 57-141 3.00e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 37.82  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242715   57 VFVLRDKfGEALGDIGLRISPKNPHEADVGYALLPQAQGKGYASEALRAVCEYgfttLGVQAINAWVLGENRGSSRLLEK 136
Cdd:pfam13508   5 FFVAEDD-GKIVGFAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAA----AKEGGIKLLELETTNRAAAFYEK 79


                  ....*
gi 490242715  137 QGFVR 141
Cdd:pfam13508  80 LGFEE 84
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
58-109 5.61e-04

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 38.74  E-value: 5.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490242715  58 FVLRDKFGEALGDIGLRISPkNPHEADV----GYALLPQAQGKGYASEALRAVCEY 109
Cdd:COG3981   65 YWLVDEDGRIVGAINLRHEL-NEFLLRVgghiGYGVRPSERGKGYATEMLRLALEE 119
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-109 2.42e-03

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: 34.94  E-value: 2.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490242715  57 VFVLRDKfGEALGDIGLRISPKNPHEADVGY-ALLPQAQGKGYASEALRAVCEY 109
Cdd:cd04301    1 FLVAEDD-GEIVGFASLSPDGSGGDTAYIGDlAVLPEYRGKGIGSALLEAAEEE 53
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
81-141 6.71e-03

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 35.87  E-value: 6.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490242715  81 HEADVGYALLPQAQGKGYASEALRAVCEYGFTTLGVQAINAWVLGENRGSSRLLEKQGFVR 141
Cdd:PRK10809 103 HACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEK 163
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 91-141 7.67e-03

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 35.19  E-value: 7.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490242715   91 PQAQGKGYASEALRAVCEYGFTTLGVQAinawVLGE----NRGSSRLLEKQGFVR 141
Cdd:pfam13523  89 PAFRGRGFTTALLRALVHYLFADPRTRR----VVVEpdvrNERAIRLLERAGFRK 139
 
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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