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Conserved domains on  [gi|1264335156|ref|WP_097949378.1|]
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GNAT family N-acetyltransferase

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, ...
 3-163 3.64e-30

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: 107.78  E-value: 3.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   3 IKVRAVEIKDARAIHRICIQDDVLPYMVFLPsMRVDAMENRIRNLA-----PNQFEFVAEF--DGEVVGFVGLTQSPgRR 75
Cdd:COG1670     8 LRLRPLRPEDAEALAELLNDPEVARYLPGPP-YSLEEARAWLERLLadwadGGALPFAIEDkeDGELIGVVGLYDID-RA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  76 SHSGDLFIGVDSEYHNKGIGKALLTKMLDLADNWLMLERVELGVLETNPKAKTLYEKFGFVEEGVKIGNLKAHGKFINEI 155
Cdd:COG1670    86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                  ....*...
gi 1264335156 156 MMSRFRPD 163
Cdd:COG1670   166 LYSLLREE 173
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-163 3.64e-30

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: 107.78  E-value: 3.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   3 IKVRAVEIKDARAIHRICIQDDVLPYMVFLPsMRVDAMENRIRNLA-----PNQFEFVAEF--DGEVVGFVGLTQSPgRR 75
Cdd:COG1670     8 LRLRPLRPEDAEALAELLNDPEVARYLPGPP-YSLEEARAWLERLLadwadGGALPFAIEDkeDGELIGVVGLYDID-RA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  76 SHSGDLFIGVDSEYHNKGIGKALLTKMLDLADNWLMLERVELGVLETNPKAKTLYEKFGFVEEGVKIGNLKAHGKFINEI 155
Cdd:COG1670    86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                  ....*...
gi 1264335156 156 MMSRFRPD 163
Cdd:COG1670   166 LYSLLREE 173
PRK10140 PRK10140
N-acetyltransferase;
3-161 1.65e-26

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 98.13  E-value: 1.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   3 IKVRAVEIKDARAIHRICIQDDVLPYMVFLPSMRVDAMENRIRNlAPNQFEFVAEFDGEVVGF--VGLTQSPgRRSHSGD 80
Cdd:PRK10140    4 IVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLAD-RPGIKQLVACIDGDVVGHltIDVQQRP-RRSHVAD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  81 LFIGVDSEYHNKGIGKALLTKMLDLADNWLMLERVELGVLETNPKAKTLYEKFGFVEEGVKIGNLKAHGKFINEIMMSRF 160
Cdd:PRK10140   82 FGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMARV 161


                  .
gi 1264335156 161 R 161
Cdd:PRK10140  162 K 162
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 54-135 1.03e-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: 74.09  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  54 FVAEFDGEVVGFVGLTQSPGRRSHSGDLFIGVDSEYHNKGIGKALLTKMLDLADNWLmLERVELGVLETNPKAKTLYEKF 133
Cdd:pfam00583  36 FVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERG-CERIFLEVAADNLAAIALYEKL 114


                  ..
gi 1264335156 134 GF 135
Cdd:pfam00583 115 GF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 55-140 1.91e-09

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: 53.10  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  55 VAEFDGEVVGFVGLTQSPgrrsHSGDLF-IGVDSEYHNKGIGKALLTKMLDLADNwLMLERVELGVLETNPKAKTLYEKF 133
Cdd:TIGR01575  35 LARIGGKVVGYAGVQIVL----DEAHILnIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKKL 109


                  ....*..
gi 1264335156 134 GFVEEGV 140
Cdd:TIGR01575 110 GFNEIAI 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-109 2.75e-08

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: 48.04  E-value: 2.75e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1264335156  54 FVAEFDGEVVGFVGLTQSPGRRsHSGDL-FIGVDSEYHNKGIGKALLTKMLDLADNW 109
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGG-DTAYIgDLAVLPEYRGKGIGSALLEAAEEEARER 57
 
Name Accession Description Interval E-value
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-163 3.64e-30

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: 107.78  E-value: 3.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   3 IKVRAVEIKDARAIHRICIQDDVLPYMVFLPsMRVDAMENRIRNLA-----PNQFEFVAEF--DGEVVGFVGLTQSPgRR 75
Cdd:COG1670     8 LRLRPLRPEDAEALAELLNDPEVARYLPGPP-YSLEEARAWLERLLadwadGGALPFAIEDkeDGELIGVVGLYDID-RA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  76 SHSGDLFIGVDSEYHNKGIGKALLTKMLDLADNWLMLERVELGVLETNPKAKTLYEKFGFVEEGVKIGNLKAHGKFINEI 155
Cdd:COG1670    86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                  ....*...
gi 1264335156 156 MMSRFRPD 163
Cdd:COG1670   166 LYSLLREE 173
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-159 4.90e-27

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 99.68  E-value: 4.90e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   3 IKVRAVEIKDARAIHRIcIQDDVLPYMV--FLPSMRVDAMENRIRNLAPNQFE-FVAEFDGEVVGFVGLTQSPGR--RSH 77
Cdd:COG1247     2 MTIRPATPEDAPAIAAI-YNEAIAEGTAtfETEPPSEEEREAWFAAILAPGRPvLVAEEDGEVVGFASLGPFRPRpaYRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  78 SGDLFIGVDSEYHNKGIGKALLTKMLDLADNwLMLERVELGVLETNPKAKTLYEKFGFVEEGVKIGNLKAHGKFINEIMM 157
Cdd:COG1247    81 TAEESIYVDPDARGRGIGRALLEALIERARA-RGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLM 159


                  ..
gi 1264335156 158 SR 159
Cdd:COG1247   160 QK 161
PRK10140 PRK10140
N-acetyltransferase;
3-161 1.65e-26

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 98.13  E-value: 1.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   3 IKVRAVEIKDARAIHRICIQDDVLPYMVFLPSMRVDAMENRIRNlAPNQFEFVAEFDGEVVGF--VGLTQSPgRRSHSGD 80
Cdd:PRK10140    4 IVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLAD-RPGIKQLVACIDGDVVGHltIDVQQRP-RRSHVAD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  81 LFIGVDSEYHNKGIGKALLTKMLDLADNWLMLERVELGVLETNPKAKTLYEKFGFVEEGVKIGNLKAHGKFINEIMMSRF 160
Cdd:PRK10140   82 FGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMARV 161


                  .
gi 1264335156 161 R 161
Cdd:PRK10140  162 K 162
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
5-139 1.06e-18

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 77.43  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   5 VRAVEIKDARAIHRICIQddvlpymVFLPSMRVDAMEnRIRNLAPNQFEFVAEFDGEVVGFVGLTQSPgRRSHSGDLFIG 84
Cdd:COG3153     1 IRPATPEDAEAIAALLRA-------AFGPGREAELVD-RLREDPAAGLSLVAEDDGEIVGHVALSPVD-IDGEGPALLLG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1264335156  85 ---VDSEYHNKGIGKALLTKMLDLADNWlmleRVELGVLETNPKAKTLYEKFGFVEEG 139
Cdd:COG3153    72 plaVDPEYRGQGIGRALMRAALEAARER----GARAVVLLGDPSLLPFYERFGFRPAG 125
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 54-135 1.03e-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: 74.09  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  54 FVAEFDGEVVGFVGLTQSPGRRSHSGDLFIGVDSEYHNKGIGKALLTKMLDLADNWLmLERVELGVLETNPKAKTLYEKF 133
Cdd:pfam00583  36 FVAEEDGELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERG-CERIFLEVAADNLAAIALYEKL 114


                  ..
gi 1264335156 134 GF 135
Cdd:pfam00583 115 GF 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-137 3.37e-16

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 69.41  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  54 FVAEFDGEVVGFVGLTQSPGRRsHSGDLFIGVDSEYHNKGIGKALLtkmlDLADNWLMLERVELGVLETNPKAKTLYEKF 133
Cdd:pfam13508   6 FVAEDDGKIVGFAALLPLDDEG-ALAELRLAVHPEYRGQGIGRALL----EAAEAAAKEGGIKLLELETTNRAAAFYEKL 80


                  ....
gi 1264335156 134 GFVE 137
Cdd:pfam13508  81 GFEE 84
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 3-159 6.10e-16

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: 70.02  E-value: 6.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   3 IKVRAVEIKDARAIHRIciqddVLPYmvflpsmrvdAMENRIRNLapnqfeFVAEFDGEVVGFVGLTQSPGRRSHSGDLF 82
Cdd:COG1246     1 MTIRPATPDDVPAILEL-----IRPY----------ALEEEIGEF------WVAEEDGEIVGCAALHPLDEDLAELRSLA 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264335156  83 igVDSEYHNKGIGKALLTKMLDLADNwLMLERVElgvLETNPKAKTLYEKFGFVEegVKIGNLKAHGKFI-NEIMMSR 159
Cdd:COG1246    60 --VHPDYRGRGIGRRLLEALLAEARE-LGLKRLF---LLTTSAAIHFYEKLGFEE--IDKEDLPYAKVWQrDSVVMEK 129
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 30-140 3.17e-15

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: 68.07  E-value: 3.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  30 VFLPSMRVDAMENRIRNlaPNQFEFVAEFDGEVVGFVGLTqspgRRSHSGDLFigVDSEYHNKGIGKALLTKMLDLADNW 109
Cdd:pfam13673  12 TFYEFISPEALRERIDQ--GEYFFFVAFEGGQIVGVIALR----DRGHISLLF--VDPDYQGQGIGKALLEAVEDYAEKD 83

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1264335156 110 LmLERVELGVlETNPKAKTLYEKFGFVEEGV 140
Cdd:pfam13673  84 G-IKLSELTV-NASPYAVPFYEKLGFRATGP 112
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 35-137 4.21e-15

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 68.16  E-value: 4.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  35 MRVDAMENRIRNLAPNQFE---FVAEFDGEVVGFVGLTQSPGRRSHSGDLFigVDSEYHNKGIGKALLTKMLDLADNwLM 111
Cdd:COG0454    15 LLIEALDAELKAMEGSLAGaefIAVDDKGEPIGFAGLRRLDDKVLELKRLY--VLPEYRGKGIGKALLEALLEWARE-RG 91

                          90       100
                  ....*....|....*....|....*.
gi 1264335156 112 LERVELGVLETNPKAKTLYEKFGFVE 137
Cdd:COG0454    92 CTALELDTLDGNPAAIRFYERLGFKE 117
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 64-140 1.05e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 63.14  E-value: 1.05e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264335156  64 GFVGLTQSPGRrsHSGDLF-IGVDSEYHNKGIGKALLTKMLDLADNwLMLERVELGVLETNPKAKTLYEKFGFVEEGV 140
Cdd:COG0456     1 GFALLGLVDGG--DEAEIEdLAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGE 75
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 6-136 3.23e-10

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 55.04  E-value: 3.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   6 RAVEIKDARAIHRICIQDDVLPYMVFLPSMRVDA---MENRIRNLAPNQ-FEF-VAEFDGEVVGFVGLTqSPGRRSHSGD 80
Cdd:pfam13302   5 RPLTEEDAEALFELLSDPEVMRYGVPWPLTLEEArewLARIWAADEAERgYGWaIELKDTGFIGSIGLY-DIDGEPERAE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1264335156  81 LFIGVDSEYHNKGIGKALLTKMLDLADNWLMLERVELGVLETNPKAKTLYEKFGFV 136
Cdd:pfam13302  84 LGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 55-140 1.91e-09

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: 53.10  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  55 VAEFDGEVVGFVGLTQSPgrrsHSGDLF-IGVDSEYHNKGIGKALLTKMLDLADNwLMLERVELGVLETNPKAKTLYEKF 133
Cdd:TIGR01575  35 LARIGGKVVGYAGVQIVL----DEAHILnIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKKL 109


                  ....*..
gi 1264335156 134 GFVEEGV 140
Cdd:TIGR01575 110 GFNEIAI 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-109 2.75e-08

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: 48.04  E-value: 2.75e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1264335156  54 FVAEFDGEVVGFVGLTQSPGRRsHSGDL-FIGVDSEYHNKGIGKALLTKMLDLADNW 109
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGSGG-DTAYIgDLAVLPEYRGKGIGSALLEAAEEEARER 57
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 54-157 8.05e-08

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: 48.89  E-value: 8.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  54 FVAEFDGEVVGFVGLTQSPGRRSHSgdlFIGVDSE-YHNKGIGKALLTKMLDLADNWLMLERVELGVLETNPKAKTLYEK 132
Cdd:TIGR03585  54 WIVCQESRPIGVISFTDINLVHKSA---FWGIYANpFCKPGVGSVLEEAALEYAFEHLGLHKLSLEVLESNNKALKLYEK 130

                          90       100
                  ....*....|....*....|....*
gi 1264335156 133 FGFVEEGVkignLKAHGKFINEIMM 157
Cdd:TIGR03585 131 FGFEREGV----FRQGGEYYDVLLM 151
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
5-156 7.95e-07

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 46.21  E-value: 7.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   5 VRAVEIKDARAIHRICIQDDVLPYMVF---LPSmrVDAMENRIRN-LAPNQFEFVAEFDGEVVGFVGLTQSPGRRSHSGD 80
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVNPAFTQeyaHSS--IEEFETFLAAyLSPGEIVFGVAESDRLIGYATLRQFDYVKTHKAE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1264335156  81 LFIGVDSEyHNKGIGKALLTKMLDLADNWLMLERVELGVLETNPKAKTLYEKFGFVEEGVKIGNLKAHGKFINEIM 156
Cdd:pfam13420  79 LSFYVVKN-NDEGINRELINAIIQYARKNQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWIDMMW 153
PRK03624 PRK03624
putative acetyltransferase; Provisional
 54-138 1.07e-06

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 45.69  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  54 FVAEFDGEVVGfvglTQSPGRRSHSGDLF-IGVDSEYHNKGIGKALLTKmldlADNWLM---LERVELGVLETNPKAKTL 129
Cdd:PRK03624   48 LVAEVGGEVVG----TVMGGYDGHRGWAYyLAVHPDFRGRGIGRALVAR----LEKKLIargCPKINLQVREDNDAVLGF 119


                  ....*....
gi 1264335156 130 YEKFGFVEE 138
Cdd:PRK03624  120 YEALGYEEQ 128
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 1-168 1.41e-06

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 45.94  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   1 MGIKVRAVEIKDARAIHRICIQDDVL------PYMVFLPsmRVDAMENRIRNLAPNQFefVAEFDGEVVGFVGLTQ--SP 72
Cdd:PRK15130    5 HSVKLRPLEREDLRFVHQLDNNASVMrywfeePYEAFVE--LSDLYDKHIHDQSERRF--VVECDGEKAGLVELVEinHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  73 GRRShsgDLFIGVDSEYHNKGIGKALLTKMLDLADNWLMLERVELGVLETNPKAKTLYEKFGFVEEGVKIGNLKAHGKFI 152
Cdd:PRK15130   81 HRRA---EFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYR 157

                         170
                  ....*....|....*.
gi 1264335156 153 NEIMMSRFRPDGLIVH 168
Cdd:PRK15130  158 NTIRMCIFQHQYLAEH 173
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
61-139 4.99e-06

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.59  E-value: 4.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1264335156  61 EVVGFVGLTQSPGRRSHSGDLFigVDSEYHNKGIGKALLTKMLDLADNwLMLERVELGVLETNPKAKTLYEKFGFVEEG 139
Cdd:COG3393     1 ELVAMAGVRAESPGVAEISGVY--THPEYRGRGLASALVAALAREALA-RGARTPFLYVDADNPAARRLYERLGFRPVG 76
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
54-139 5.84e-06

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 43.63  E-value: 5.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  54 FVAEFDGEVVGFVGLtqspgRRSHSGDLFIG---VDSEYHNKGIGKALLTKMLDLADNwLMLERVELGVLETnpkAKTLY 130
Cdd:COG2153    37 LLAYDDGELVATARL-----LPPGDGEAKIGrvaVLPEYRGQGLGRALMEAAIEEARE-RGARRIVLSAQAH---AVGFY 107


                  ....*....
gi 1264335156 131 EKFGFVEEG 139
Cdd:COG2153   108 EKLGFVPVG 116
PRK10562 PRK10562
putative acetyltransferase; Provisional
 49-139 1.31e-05

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 42.75  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156  49 PNQFEFVAEFDGEVVGFVGLTQSPgrrshsgdlFIG---VDSEYHNKGIGKALLTKMLDLADnWLMLErvelgVLETNPK 125
Cdd:PRK10562   46 PAAQTWVWEEDGKLLGFVSVLEGR---------FVGalfVAPKAVRRGIGKALMQHVQQRYP-HLSLE-----VYQKNQR 110

                          90
                  ....*....|....
gi 1264335156 126 AKTLYEKFGFVEEG 139
Cdd:PRK10562  111 AVNFYHAQGFRIVD 124
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 81-137 8.30e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 40.68  E-value: 8.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1264335156  81 LF-IGVDSEYHNKGIGKALLTKMLDLAD----NWLMLErvelgVLETNPKAKTLYEKFGFVE 137
Cdd:PRK09491   66 LFnIAVDPDYQRQGLGRALLEHLIDELEkrgvATLWLE-----VRASNAAAIALYESLGFNE 122
PRK07757 PRK07757
N-acetyltransferase;
3-137 8.52e-05

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 40.56  E-value: 8.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1264335156   3 IKVRAVEIKDARAIHRIciqddVLPYM---VFLPSMRVDAMENrIRNLapnqfeFVAEFDGEVVGFVGLTqspgrrSHSG 79
Cdd:PRK07757    2 MEIRKARLSDVKAIHAL-----INVYAkkgLMLPRSLDELYEN-IRDF------YVAEEEGEIVGCCALH------ILWE 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1264335156  80 DLF----IGVDSEYHNKGIGKALLTKMLDladnwlmlERVELGVletnPKAKTL------YEKFGFVE 137
Cdd:PRK07757   64 DLAeirsLAVSEDYRGQGIGRMLVEACLE--------EARELGV----KRVFALtyqpefFEKLGFRE 119
PRK10514 PRK10514
putative acetyltransferase; Provisional
 63-139 2.28e-03

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 36.52  E-value: 2.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1264335156  63 VGFVGLTQSpgrrsHSGDLFigVDSEYHNKGIGKALLTKMLDLADNwlmlerVELGVLETNPKAKTLYEKFGFVEEG 139
Cdd:PRK10514   62 VGFMLLSGG-----HMEALF--VDPDVRGCGVGRMLVEHALSLHPE------LTTDVNEQNEQAVGFYKKMGFKVTG 125
 
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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