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Conserved domains on  [gi|495004548|ref|WP_007730562|]
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N-acetyltransferase [Cronobacter dublinensis]

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 ...
 1-163 9.01e-93

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 PRK10140:

Pssm-ID: 473072 [Multi-domain]  Cd Length: 162  Bit Score: 266.46  E-value: 9.01e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   1 MNEIVVRHAEAEDAQALQQIHTMSEIIHNTLQIPHPSLAMWRDRLgAPQPGRRQLVACIGEQVVGHLALTVEQNPRRSHV 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERL-ADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548  81 ATFGMSVHPAWRNRGVASALIREMVNLCDNWLRIERIELTVFVDNAPALAVYRKFGFETEGTGRRYALRDGEYVDAYFMA 160
Cdd:PRK10140  80 ADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMA 159


                 ...
gi 495004548 161 RMK 163
Cdd:PRK10140 160 RVK 162
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-163 9.01e-93

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 266.46  E-value: 9.01e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   1 MNEIVVRHAEAEDAQALQQIHTMSEIIHNTLQIPHPSLAMWRDRLgAPQPGRRQLVACIGEQVVGHLALTVEQNPRRSHV 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERL-ADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548  81 ATFGMSVHPAWRNRGVASALIREMVNLCDNWLRIERIELTVFVDNAPALAVYRKFGFETEGTGRRYALRDGEYVDAYFMA 160
Cdd:PRK10140  80 ADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMA 159


                 ...
gi 495004548 161 RMK 163
Cdd:PRK10140 160 RVK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-161 3.95e-29

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: 105.08  E-value: 3.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   4 IVVRHAEAEDAQALQQIHTMSEIIHNTLQIPHpSLAMWRDRL-----GAPQPGRRQLVACIGE--QVVGHLALTveQNPR 76
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPY-SLEEARAWLerllaDWADGGALPFAIEDKEdgELIGVVGLY--DIDR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548  77 RSHVATFGMSVHPAWRNRGVASALIREMVNLCDNWLRIERIELTVFVDNAPALAVYRKFGFETEGTGRRYALRDGEYVDA 156
Cdd:COG1670   85 ANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164


                 ....*
gi 495004548 157 YFMAR 161
Cdd:COG1670  165 VLYSL 169
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 20-137 4.18e-17

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: 72.55  E-value: 4.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   20 IHTMSEIIHNTLQIPHPSLAMWRDRLGAPQPGRRQLVACIGEQVVGHLALTVEQNPRRsHVATFGMSVHPAWRNRGVASA 99
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP-VGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 495004548  100 LIREMVNLCDNWlRIERIELTVFVDNAPALAVYRKFGF 137
Cdd:pfam00583  80 LLQALLEWARER-GCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 55-159 1.14e-13

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 63.89  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   55 LVACIGEQVVGHLalTVEQNPRRSHVATFGmsVHPAWRNRGVASALIREMVNLCDNwLRIERIELTVFVDNAPALAVYRK 134
Cdd:TIGR01575  34 LLARIGGKVVGYA--GVQIVLDEAHILNIA--VKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKK 108

                          90       100
                  ....*....|....*....|....*
gi 495004548  135 FGFETEGTGRRYALRDGEyvDAYFM 159
Cdd:TIGR01575 109 LGFNEIAIRRNYYPDPGE--DAIVM 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 55-120 2.32e-06

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: 43.03  E-value: 2.32e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495004548  55 LVACIGEQVVGHLALTV-EQNPRRSHVATFGmsVHPAWRNRGVASALIREMVNLCDNWlRIERIELT 120
Cdd:cd04301    2 LVAEDDGEIVGFASLSPdGSGGDTAYIGDLA--VLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-163 9.01e-93

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 266.46  E-value: 9.01e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   1 MNEIVVRHAEAEDAQALQQIHTMSEIIHNTLQIPHPSLAMWRDRLgAPQPGRRQLVACIGEQVVGHLALTVEQNPRRSHV 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERL-ADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548  81 ATFGMSVHPAWRNRGVASALIREMVNLCDNWLRIERIELTVFVDNAPALAVYRKFGFETEGTGRRYALRDGEYVDAYFMA 160
Cdd:PRK10140  80 ADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMA 159


                 ...
gi 495004548 161 RMK 163
Cdd:PRK10140 160 RVK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-161 3.95e-29

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: 105.08  E-value: 3.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   4 IVVRHAEAEDAQALQQIHTMSEIIHNTLQIPHpSLAMWRDRL-----GAPQPGRRQLVACIGE--QVVGHLALTveQNPR 76
Cdd:COG1670    8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPY-SLEEARAWLerllaDWADGGALPFAIEDKEdgELIGVVGLY--DIDR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548  77 RSHVATFGMSVHPAWRNRGVASALIREMVNLCDNWLRIERIELTVFVDNAPALAVYRKFGFETEGTGRRYALRDGEYVDA 156
Cdd:COG1670   85 ANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDH 164


                 ....*
gi 495004548 157 YFMAR 161
Cdd:COG1670  165 VLYSL 169
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-161 6.11e-28

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 101.61  E-value: 6.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   3 EIVVRHAEAEDAQALQQIHTmsEIIHNTLQ---IPHPSLAMWRDRLGA-PQPGRRQLVACIGEQVVGHLALT-VEQNPRR 77
Cdd:COG1247    1 EMTIRPATPEDAPAIAAIYN--EAIAEGTAtfeTEPPSEEEREAWFAAiLAPGRPVLVAEEDGEVVGFASLGpFRPRPAY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548  78 SHVATFGMSVHPAWRNRGVASALIREMVNLCDNwLRIERIELTVFVDNAPALAVYRKFGFETEGTGRRYALRDGEYVDAY 157
Cdd:COG1247   79 RGTAEESIYVDPDARGRGIGRALLEALIERARA-RGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLV 157


                 ....
gi 495004548 158 FMAR 161
Cdd:COG1247  158 LMQK 161
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 20-137 4.18e-17

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: 72.55  E-value: 4.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   20 IHTMSEIIHNTLQIPHPSLAMWRDRLGAPQPGRRQLVACIGEQVVGHLALTVEQNPRRsHVATFGMSVHPAWRNRGVASA 99
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEPP-VGEIEGLAVAPEYRGKGIGTA 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 495004548  100 LIREMVNLCDNWlRIERIELTVFVDNAPALAVYRKFGF 137
Cdd:pfam00583  80 LLQALLEWARER-GCERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 65-161 4.96e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 68.91  E-value: 4.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548  65 GHLALTVEQNPRRSHVATFGmsVHPAWRNRGVASALIREMVNLCDNwLRIERIELTVFVDNAPALAVYRKFGFETEGTGR 144
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLA--VDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                         90
                 ....*....|....*..
gi 495004548 145 RYALRdgeyvDAYFMAR 161
Cdd:COG0456   78 NYYGD-----DALVMEK 89
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-161 6.47e-15

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.42  E-value: 6.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   6 VRHAEAEDAQALQQIHTmseiihntLQIPHPSLAMWRDRLGAPQPGRRQLVACIGEQVVGHLALTVEQNPRRSHVATFG- 84
Cdd:COG3153    1 IRPATPEDAEAIAALLR--------AAFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGPALLLGp 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495004548  85 MSVHPAWRNRGVASALIREMVNLCDNwLRIERIELTVfvdNAPALAVYRKFGFETEGTGRRYAlrdgeYVDAYFMAR 161
Cdd:COG3153   73 LAVDPEYRGQGIGRALMRAALEAARE-RGARAVVLLG---DPSLLPFYERFGFRPAGELGLTL-----GPDEVFLAK 140
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 55-159 1.14e-13

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 63.89  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   55 LVACIGEQVVGHLalTVEQNPRRSHVATFGmsVHPAWRNRGVASALIREMVNLCDNwLRIERIELTVFVDNAPALAVYRK 134
Cdd:TIGR01575  34 LLARIGGKVVGYA--GVQIVLDEAHILNIA--VKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKK 108

                          90       100
                  ....*....|....*....|....*
gi 495004548  135 FGFETEGTGRRYALRDGEyvDAYFM 159
Cdd:TIGR01575 109 LGFNEIAIRRNYYPDPGE--DAIVM 131
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 50-138 2.39e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 56.69  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   50 PGRRQLVACIGEQVVGHLALTVEqnPRRSHVATFGMSVHPAWRNRGVASALIREmvnlCDNWLRIERIELTVFVDNAPAL 129
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPL--DDEGALAELRLAVHPEYRGQGIGRALLEA----AEAAAKEGGIKLLELETTNRAA 74


                  ....*....
gi 495004548  130 AVYRKFGFE 138
Cdd:pfam13508  75 AFYEKLGFE 83
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 55-141 1.28e-10

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: 55.74  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   55 LVACIGEQVVGHLALTveqnpRRSHVAtfGMSVHPAWRNRGVASALIREMVNLCDNWlRIERIELTVFVDNaPALAVYRK 134
Cdd:pfam13673  34 FVAFEGGQIVGVIALR-----DRGHIS--LLFVDPDYQGQGIGKALLEAVEDYAEKD-GIKLSELTVNASP-YAVPFYEK 104


                  ....*..
gi 495004548  135 FGFETEG 141
Cdd:pfam13673 105 LGFRATG 111
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 6-148 1.88e-10

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 55.44  E-value: 1.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   6 VRHAEAEDAQALQQIHTMSEIIHNTLQIPHpslamwrdrlgapqpGRRQLVACIGEQVVGHLALTVEqNPRRSHVAtfGM 85
Cdd:COG0454    3 IRKATPEDINFILLIEALDAELKAMEGSLA---------------GAEFIAVDDKGEPIGFAGLRRL-DDKVLELK--RL 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495004548  86 SVHPAWRNRGVASALIREMVNlcdnWLR---IERIELTVFVDNAPALAVYRKFGFETEGTGRRYAL 148
Cdd:COG0454   65 YVLPEYRGKGIGKALLEALLE----WARergCTALELDTLDGNPAAIRFYERLGFKEIERYVAYVG 126
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
84-149 8.18e-10

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.60  E-value: 8.18e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495004548  84 GMSVHPAWRNRGVASALIREMVNLCDNwLRIERIELTVFVDNAPALAVYRKFGFETEGTGRRYALR 149
Cdd:COG3393   20 GVYTHPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLFR 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 4-138 2.80e-08

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: 49.61  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   4 IVVRHAEAEDAQALQQIHTMSEIIhntlqiphpslamwrdrlgapQPGRRQLVACIGEQVVGHLALTVEqNPRRSHVATf 83
Cdd:COG1246    1 MTIRPATPDDVPAILELIRPYALE---------------------EEIGEFWVAEEDGEIVGCAALHPL-DEDLAELRS- 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495004548  84 gMSVHPAWRNRGVASALIREMVNLCDNwLRIERIELTVfvdNAPALAVYRKFGFE 138
Cdd:COG1246   58 -LAVHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLLT---TSAAIHFYEKLGFE 107
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 4-138 5.82e-07

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 46.18  E-value: 5.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548    4 IVVRHAEAEDAQALQQIHTMSEIIHNTLQIPHPSLAMWRD-----RLGAPQPGRRQLVACIGEQVVGhlALTVEQNPRRS 78
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEAREWlariwAADEAERGYGWAIELKDTGFIG--SIGLYDIDGEP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   79 HVATFGMSVHPAWRNRGVASALIREMVNLCDNWLRIERIELTVFVDNAPALAVYRKFGFE 138
Cdd:pfam13302  80 ERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 55-120 2.32e-06

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: 43.03  E-value: 2.32e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495004548  55 LVACIGEQVVGHLALTV-EQNPRRSHVATFGmsVHPAWRNRGVASALIREMVNLCDNWlRIERIELT 120
Cdd:cd04301    2 LVAEDDGEIVGFASLSPdGSGGDTAYIGDLA--VLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
6-155 2.99e-06

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 44.66  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548    6 VRHAEAEDAQALQQIhtMSEIIHNTLQIP---HPSLAMWRDRLGA-PQPGRRQLVACIGEQVVGHLALtVEQNPRRSHVA 81
Cdd:pfam13420   1 IRALTQNDLKEIRRW--YAEDRVNPAFTQeyaHSSIEEFETFLAAyLSPGEIVFGVAESDRLIGYATL-RQFDYVKTHKA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495004548   82 TFGMSVHpAWRNRGVasalIREMVNLCDNWLR----IERIELTVFVDNAPALAVYRKFGFETEGTGRRYALRDGEYVD 155
Cdd:pfam13420  78 ELSFYVV-KNNDEGI----NRELINAIIQYARknqnIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
53-141 4.81e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 43.63  E-value: 4.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548  53 RQLVACIGEQVVGHLALTVEQNPrrshVATFG-MSVHPAWRNRGVASALIREMVNLCDNwLRIERIELTVfvdNAPALAV 131
Cdd:COG2153   35 RHLLAYDDGELVATARLLPPGDG----EAKIGrVAVLPEYRGQGLGRALMEAAIEEARE-RGARRIVLSA---QAHAVGF 106

                         90
                 ....*....|
gi 495004548 132 YRKFGFETEG 141
Cdd:COG2153  107 YEKLGFVPVG 116
Eis COG4552
Predicted acetyltransferase [General function prediction only];
6-152 8.70e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 41.42  E-value: 8.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   6 VRHAEAEDAQALQQIhtmseiIHNTLQIPHP--SLAMWRDRLGapqpGRRQLVACIGEQVVGHLAL-TVEQNPRRSHVAT 82
Cdd:COG4552    3 IRPLTEDDLDAFARL------LAYAFGPEPDdeELEAYRPLLE----PGRVLGVFDDGELVGTLALyPFTLNVGGARVPM 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548  83 FGMS---VHPAWRNRGVASALIREMvnlcdnwlrierieLTVFVDNAPALAV--------YRKFGFETEGTGRRYALRDG 151
Cdd:COG4552   73 AGITgvaVAPEHRRRGVARALLREA--------------LAELRERGQPLSAlypfepgfYRRFGYELAGDRRRYTIPPE 138


                 .
gi 495004548 152 E 152
Cdd:COG4552  139 S 139
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 49-159 1.34e-04

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 40.55  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548  49 QPGRRQLVACIGEQVvgHLALTVEQNprrsHV---ATFGMSVHPAWRNRGVASALIREMVNLCDNWLRIERIELTVFVDN 125
Cdd:PRK15130  55 QSERRFVVECDGEKA--GLVELVEIN----HVhrrAEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKEN 128

                         90       100       110
                 ....*....|....*....|....*....|....
gi 495004548 126 APALAVYRKFGFETEGTGRRYALRDGEYVDAYFM 159
Cdd:PRK15130 129 EKAIHIYRKLGFEVEGELIHEFFINGEYRNTIRM 162
PRK03624 PRK03624
putative acetyltransferase; Provisional
 55-140 1.57e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 39.53  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548  55 LVACIGEQVVGhlALTVEQNPRRSHVATFGmsVHPAWRNRGVASALIREMvnlcDNWLR---IERIELTVFVDNAPALAV 131
Cdd:PRK03624  48 LVAEVGGEVVG--TVMGGYDGHRGWAYYLA--VHPDFRGRGIGRALVARL----EKKLIargCPKINLQVREDNDAVLGF 119


                 ....*....
gi 495004548 132 YRKFGFETE 140
Cdd:PRK03624 120 YEALGYEEQ 128
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
84-131 1.43e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 37.20  E-value: 1.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 495004548  84 GMSVHPAWRNRGVASALIREMVNLCDNwLRIERIELTVFVDNAPALAV 131
Cdd:COG3981   96 GYGVRPSERGKGYATEMLRLALEEARE-LGLDRVLITCDKDNIASRKV 142
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 41-139 3.28e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 35.62  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004548   41 WRDRLGApqpgRRQLVACIGEQVVGHLALtveqNPRRSHV--ATF------GMSVHPAWRNRGVASALIREMvnLCDnwL 112
Cdd:pfam13527  32 FRPLLEE----GRVLGAFDDGELVSTLAL----YPFELNVpgKTLpaagitGVATYPEYRGRGVMSRLLRRS--LEE--M 99

                          90       100
                  ....*....|....*....|....*..
gi 495004548  113 RIERIELTVFVDNAPALavYRKFGFET 139
Cdd:pfam13527 100 RERGVPLSFLYPSSYPI--YRRFGYEI 124
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 89-142 4.25e-03

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 35.57  E-value: 4.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 495004548   89 PAWRNRGVASALIREMVNLCDNWLRIERIeltVF---VDNAPALAVYRKFGFETEGT 142
Cdd:pfam13523  89 PAFRGRGFTTALLRALVHYLFADPRTRRV---VVepdVRNERAIRLLERAGFRKVKE 142
 
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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