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Conserved domains on  [gi|764133625|ref|WP_044317888|]
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MULTISPECIES: GNAT family N-acetyltransferase [Pseudomonas syringae group]

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 ...
 7-167 1.63e-41

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: 136.65  E-value: 1.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   7 QILIQRMAETHLEGVTALYNEPAVCRQVLQMPYQSIEVWRKRLAASTERHvKLVALSGGEVIGSLGLEQYSRSRQSHVGA 86
Cdd:PRK10140   3 EIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIK-QLVACIDGDVVGHLTIDVQQRPRRSHVAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  87 IGMGVASAWHGKGIGSKLLAAALDIADNWMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNYAVRDGVFVDALSMARL 166
Cdd:PRK10140  82 FGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMARV 161


                 .
gi 764133625 167 R 167
Cdd:PRK10140 162 K 162
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
7-167 1.63e-41

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 136.65  E-value: 1.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   7 QILIQRMAETHLEGVTALYNEPAVCRQVLQMPYQSIEVWRKRLAASTERHvKLVALSGGEVIGSLGLEQYSRSRQSHVGA 86
Cdd:PRK10140   3 EIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIK-QLVACIDGDVVGHLTIDVQQRPRRSHVAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  87 IGMGVASAWHGKGIGSKLLAAALDIADNWMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNYAVRDGVFVDALSMARL 166
Cdd:PRK10140  82 FGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMARV 161


                 .
gi 764133625 167 R 167
Cdd:PRK10140 162 K 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 6-167 2.09e-34

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: 118.56  E-value: 2.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   6 PQILIQRMAETHLEGVTALYNEPAVCRQvLQMPYQSIEVWRKRLAASTERHVK-------LVALSGGEVIGSLGLeqYSR 78
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARY-LPGPPYSLEEARAWLERLLADWADggalpfaIEDKEDGELIGVVGL--YDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  79 SRQSHVGAIGMGVASAWHGKGIGSKLLAAALDIADNWMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNYAVRDGVFV 158
Cdd:COG1670   83 DRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYR 162


                 ....*....
gi 764133625 159 DALSMARLR 167
Cdd:COG1670  163 DHVLYSLLR 171
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 38-141 1.67e-15

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: 68.31  E-value: 1.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   38 PYQSIEVWRKRLAASTERHVKLVALSGGEVIGSLGLeqYSRSRQSHVGAI-GMGVASAWHGKGIGSKLLAAALDIADNWm 116
Cdd:pfam00583  15 PWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASL--SIIDDEPPVGEIeGLAVAPEYRGKGIGTALLQALLEWARER- 91

                          90       100
                  ....*....|....*....|....*
gi 764133625  117 NLHRVELTVFADNEAAKGLYRKYGF 141
Cdd:pfam00583  92 GCERIFLEVAADNLAAIALYEKLGF 116
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 98-164 1.22e-10

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 56.60  E-value: 1.22e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764133625   98 KGIGSKLLAAALDIADNWMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNYavrdGVFVDALSMA 164
Cdd:TIGR03585  90 PGVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQG----GEYYDVLLMY 152
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-124 6.67e-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: 41.88  E-value: 6.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764133625  59 LVALSGGEVIGSLGLEQYSRSRqsHVGAIG-MGVASAWHGKGIGSKLLAAALDIADNWmNLHRVELT 124
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGG--DTAYIGdLAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
7-167 1.63e-41

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 136.65  E-value: 1.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   7 QILIQRMAETHLEGVTALYNEPAVCRQVLQMPYQSIEVWRKRLAASTERHvKLVALSGGEVIGSLGLEQYSRSRQSHVGA 86
Cdd:PRK10140   3 EIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIK-QLVACIDGDVVGHLTIDVQQRPRRSHVAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  87 IGMGVASAWHGKGIGSKLLAAALDIADNWMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNYAVRDGVFVDALSMARL 166
Cdd:PRK10140  82 FGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMARV 161


                 .
gi 764133625 167 R 167
Cdd:PRK10140 162 K 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 6-167 2.09e-34

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: 118.56  E-value: 2.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   6 PQILIQRMAETHLEGVTALYNEPAVCRQvLQMPYQSIEVWRKRLAASTERHVK-------LVALSGGEVIGSLGLeqYSR 78
Cdd:COG1670    6 ERLRLRPLRPEDAEALAELLNDPEVARY-LPGPPYSLEEARAWLERLLADWADggalpfaIEDKEDGELIGVVGL--YDI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  79 SRQSHVGAIGMGVASAWHGKGIGSKLLAAALDIADNWMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNYAVRDGVFV 158
Cdd:COG1670   83 DRANRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYR 162


                 ....*....
gi 764133625 159 DALSMARLR 167
Cdd:COG1670  163 DHVLYSLLR 171
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
8-166 5.14e-26

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 96.99  E-value: 5.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   8 ILIQRMAETHLEGVTALYNEPAVCRQVL-QMPYQSIEVWRKRLAA-STERHVKLVALSGGEVIGSLGLEQYS-RSRQSHV 84
Cdd:COG1247    2 MTIRPATPEDAPAIAAIYNEAIAEGTATfETEPPSEEEREAWFAAiLAPGRPVLVAEEDGEVVGFASLGPFRpRPAYRGT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  85 GAIGMGVASAWHGKGIGSKLLAAALDIADNwMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNYAVRDGVFVDALSMA 164
Cdd:COG1247   82 AEESIYVDPDARGRGIGRALLEALIERARA-RGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQ 160


                 ..
gi 764133625 165 RL 166
Cdd:COG1247  161 KR 162
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 69-157 9.43e-16

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 68.53  E-value: 9.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  69 GSLGLEQYSRSRQSHVGAIGmgVASAWHGKGIGSKLLAAALDIADNwMNLHRVELTVFADNEAAKGLYRKYGFELEGRLR 148
Cdd:COG0456    1 GFALLGLVDGGDEAEIEDLA--VDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77


                 ....*....
gi 764133625 149 NYAVRDGVF 157
Cdd:COG0456   78 NYYGDDALV 86
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 38-141 1.67e-15

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: 68.31  E-value: 1.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   38 PYQSIEVWRKRLAASTERHVKLVALSGGEVIGSLGLeqYSRSRQSHVGAI-GMGVASAWHGKGIGSKLLAAALDIADNWm 116
Cdd:pfam00583  15 PWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASL--SIIDDEPPVGEIeGLAVAPEYRGKGIGTALLQALLEWARER- 91

                          90       100
                  ....*....|....*....|....*
gi 764133625  117 NLHRVELTVFADNEAAKGLYRKYGF 141
Cdd:pfam00583  92 GCERIFLEVAADNLAAIALYEKLGF 116
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 8-142 8.24e-13

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 61.98  E-value: 8.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625    8 ILIQRMAETHLEGVTALYNEPAVCRQVLQMPY---QSIEVWRKRLAASTERH--VKLVALSGGEVIGSLGLeqYSRSRQS 82
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEVMRYGVPWPLtleEAREWLARIWAADEAERgyGWAIELKDTGFIGSIGL--YDIDGEP 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   83 HVGAIGMGVASAWHGKGIGSKLLAAALDIADNWMNLHRVELTVFADNEAAKGLYRKYGFE 142
Cdd:pfam13302  80 ERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
10-157 9.04e-13

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 62.03  E-value: 9.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  10 IQRMAETHLEGVTALYNEpavcrqvlQMPYQSIEVWRKRLAASTERHVKLVALSGGEVIGSLGLEQYSRSRQSHVGAIG- 88
Cdd:COG3153    1 IRPATPEDAEAIAALLRA--------AFGPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGPALLLGp 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764133625  89 MGVASAWHGKGIGSKLLAAALDIADNwMNLHRVELTVFADNEAakgLYRKYGFELEGRLRNYAVRDGVF 157
Cdd:COG3153   73 LAVDPEYRGQGIGRALMRAALEAARE-RGARAVVLLGDPSLLP---FYERFGFRPAGELGLTLGPDEVF 137
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 39-156 1.17e-12

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: 61.13  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   39 YQSIEVWRKRLAASTERHvkLVALSGGEVIGSLGLeqysrSRQSHVGaiGMGVASAWHGKGIGSKLLAAALDIADNWmNL 118
Cdd:pfam13673  16 FISPEALRERIDQGEYFF--FVAFEGGQIVGVIAL-----RDRGHIS--LLFVDPDYQGQGIGKALLEAVEDYAEKD-GI 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 764133625  119 HRVELTVFADNeAAKGLYRKYGFELEGRLRnyaVRDGV 156
Cdd:pfam13673  86 KLSELTVNASP-YAVPFYEKLGFRATGPEQ---EFNGI 119
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 59-142 2.58e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 56.69  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   59 LVALSGGEVIGSLGLEQYSRSRqsHVGAIGMGVASAWHGKGIGSKLLAAALDIADNwmnlHRVELTVFADNEAAKGLYRK 138
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEG--ALAELRLAVHPEYRGQGIGRALLEAAEAAAKE----GGIKLLELETTNRAAAFYEK 79


                  ....
gi 764133625  139 YGFE 142
Cdd:pfam13508  80 LGFE 83
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 98-164 1.22e-10

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 56.60  E-value: 1.22e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764133625   98 KGIGSKLLAAALDIADNWMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNYavrdGVFVDALSMA 164
Cdd:TIGR03585  90 PGVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQG----GEYYDVLLMY 152
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 59-142 1.71e-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: 55.77  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  59 LVALSGGEVIGSLGLEQYSrsrqSHVGAIG-MGVASAWHGKGIGSKLLAAALDIADNwMNLHRVELTVfadNEAAKGLYR 137
Cdd:COG1246   31 WVAEEDGEIVGCAALHPLD----EDLAELRsLAVHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLLT---TSAAIHFYE 102


                 ....*
gi 764133625 138 KYGFE 142
Cdd:COG1246  103 KLGFE 107
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 42-150 2.34e-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: 2.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  42 IEVWRKRLAA--STERHVKLVALS-GGEVIGSLGLEQYSrSRQSHVGaiGMGVASAWHGKGIGSKLLAAALDIADNwMNL 118
Cdd:COG0454   17 IEALDAELKAmeGSLAGAEFIAVDdKGEPIGFAGLRRLD-DKVLELK--RLYVLPEYRGKGIGKALLEALLEWARE-RGC 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 764133625 119 HRVELTVFADNEAAKGLYRKYGFELEGRLRNY 150
Cdd:COG0454   93 TALELDTLDGNPAAIRFYERLGFKEIERYVAY 124
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 59-163 6.77e-10

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: 54.26  E-value: 6.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   59 LVALSGGEVIGSLG----LEQYsrsrqsHVGAIGmgVASAWHGKGIGSKLLAAALDIADNwMNLHRVELTVFADNEAAKG 134
Cdd:TIGR01575  34 LLARIGGKVVGYAGvqivLDEA------HILNIA--VKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQA 104

                          90       100
                  ....*....|....*....|....*....
gi 764133625  135 LYRKYGFELEGRLRNYaVRDGVfVDALSM 163
Cdd:TIGR01575 105 LYKKLGFNEIAIRRNY-YPDPG-EDAIVM 131
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
78-153 2.38e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 48.75  E-value: 2.38e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764133625  78 RSRQSHVGAI-GMGVASAWHGKGIGSKLLAAALDIADNwMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNYAVR 153
Cdd:COG3393    9 RAESPGVAEIsGVYTHPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFRPVGEYATVLFR 84
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
18-150 1.68e-07

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 48.13  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625   18 LEGVTALYNEPAVCRQVLQMPYQSIEVWRKRLAASTERHVKLV--ALSGGEVIGSLGLEQYsRSRQSHVGAIGMGVAsAW 95
Cdd:pfam13420   9 LKEIRRWYAEDRVNPAFTQEYAHSSIEEFETFLAAYLSPGEIVfgVAESDRLIGYATLRQF-DYVKTHKAELSFYVV-KN 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 764133625   96 HGKGIGSKLLAAALDIADNWMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNY 150
Cdd:pfam13420  87 NDEGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNA 141
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
59-145 1.98e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 47.49  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  59 LVALSGGEVIGslgleqYSRSRQ--SHVGAIG-MGVASAWHGKGIGSKLLAAALDIADNwMNLHRVELTVfadNEAAKGL 135
Cdd:COG2153   37 LLAYDDGELVA------TARLLPpgDGEAKIGrVAVLPEYRGQGLGRALMEAAIEEARE-RGARRIVLSA---QAHAVGF 106

                         90
                 ....*....|
gi 764133625 136 YRKYGFELEG 145
Cdd:COG2153  107 YEKLGFVPVG 116
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 18-163 2.67e-06

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 45.17  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  18 LEGVTALYNEPAVCRQVLQMPYQSI----EVWRKRLAASTERhvKLVALSGGEVIGSLGLEQYSR-SRQSHVGAIgmgVA 92
Cdd:PRK15130  17 LRFVHQLDNNASVMRYWFEEPYEAFvelsDLYDKHIHDQSER--RFVVECDGEKAGLVELVEINHvHRRAEFQII---IS 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764133625  93 SAWHGKGIGSKLLAAALDIADNWMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNYAVRDGVFVDALSM 163
Cdd:PRK15130  92 PEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTIRM 162
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 59-124 6.67e-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: 41.88  E-value: 6.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764133625  59 LVALSGGEVIGSLGLEQYSRSRqsHVGAIG-MGVASAWHGKGIGSKLLAAALDIADNWmNLHRVELT 124
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGG--DTAYIGdLAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
64-133 3.62e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 41.82  E-value: 3.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764133625  64 GGEVIGSLGLEQYSRSRQSHVGA-IGMGVASAWHGKGIGSKLLAAALDIADNwMNLHRVELTVFADNEAAK 133
Cdd:COG3981   71 DGRIVGAINLRHELNEFLLRVGGhIGYGVRPSERGKGYATEMLRLALEEARE-LGLDRVLITCDKDNIASR 140
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
83-164 8.26e-04

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 38.18  E-value: 8.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  83 HVGAIGMGVASAWHGKGIGSKLLAAALDIADNWMNLHRVELTVFADNEAAKGLYRKYGFELEGRLRNYAVRDGVFVDALS 162
Cdd:PRK10809 103 HACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEGYAKDYLLIDGQWRDHVL 182


                 ..
gi 764133625 163 MA 164
Cdd:PRK10809 183 TA 184
PRK03624 PRK03624
putative acetyltransferase; Provisional
 59-147 3.68e-03

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 35.67  E-value: 3.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764133625  59 LVALSGGEVIGSLgLEQYSRSRQShvgAIGMGVASAWHGKGIGSKLLAAAldiaDNWMnLHR----VELTVFADNEAAKG 134
Cdd:PRK03624  48 LVAEVGGEVVGTV-MGGYDGHRGW---AYYLAVHPDFRGRGIGRALVARL----EKKL-IARgcpkINLQVREDNDAVLG 118

                         90
                 ....*....|...
gi 764133625 135 LYRKYGFELEGRL 147
Cdd:PRK03624 119 FYEALGYEEQDRI 131
PRK10514 PRK10514
putative acetyltransferase; Provisional
 91-146 6.81e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 34.98  E-value: 6.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 764133625  91 VASAWHGKGIGSKLLAAALDIADnwmnlhrvELT--VFADNEAAKGLYRKYGFELEGR 146
Cdd:PRK10514  77 VDPDVRGCGVGRMLVEHALSLHP--------ELTtdVNEQNEQAVGFYKKMGFKVTGR 126
 
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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