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Conserved domains on  [gi|83754486|pdb|2C27|A]
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Chain A, MYCOTHIOL SYNTHASE

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11496873)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mycothiol_MshD TIGR03448
mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the ...
 5-308 2.61e-153

mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


:

Pssm-ID: 132489 [Multi-domain]  Cd Length: 292  Bit Score: 431.05  E-value: 2.61e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A          5 DWRSALTADEQRSVRALVTATTAVDGVAPVGEQVLREL---GQQRTEHLLVAGSRPggpIIGYLNLSPPRGAGGAMAELV 81
Cdd:TIGR03448   1 TWRAALDADLRRDVRELLAAATAVDGVAPVSEQVLRGLrepGAGHTRHLVAVDSDP---IVGYANLVPARGTDPAMAELV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A         82 VHPQSRRRGIGTAMARAALAKTAGRNQFWAHGTLDPARATASALGLVGVRELIQMRRPLRD--IPEPTIPDGVVIRTYAG 159
Cdd:TIGR03448  78 VHPAHRRRGIGRALIRALLAKGGGRLRVWAHGDLPAARALASRLGLVPTRELLQMRRPLRDleLPEPQVPDGVTVRAYVG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A        160 TSDDAELLRVNNAAFAGHPEQGGWTAVQLAERRGEAWFDPDGLILAFGDSprerPGRLLGFHWTKVHPDHPGLGEVYVLG 239
Cdd:TIGR03448 158 APDDAEWLRVNNAAFAWHPEQGGWTRADLAERRAEPWFDPAGLFLAFDDA----PGELLGFHWTKVHPDEPALGEVYVVG 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2C27_A        240 VDPAAQRRGLGQMLTSIGIVSLARRlggrktldpaVEPAVLLYVESDNVAAVRTYQSLGFTTYSVDTAY 308
Cdd:TIGR03448 234 VDPAAQGRGLGDALTLIGLHHLAAR----------GLPAVMLYVEADNEAAVRTYEKLGFTVAEVDVAY 292
 
Name Accession Description Interval E-value
mycothiol_MshD TIGR03448
mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the ...
 5-308 2.61e-153

mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 132489 [Multi-domain]  Cd Length: 292  Bit Score: 431.05  E-value: 2.61e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A          5 DWRSALTADEQRSVRALVTATTAVDGVAPVGEQVLREL---GQQRTEHLLVAGSRPggpIIGYLNLSPPRGAGGAMAELV 81
Cdd:TIGR03448   1 TWRAALDADLRRDVRELLAAATAVDGVAPVSEQVLRGLrepGAGHTRHLVAVDSDP---IVGYANLVPARGTDPAMAELV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A         82 VHPQSRRRGIGTAMARAALAKTAGRNQFWAHGTLDPARATASALGLVGVRELIQMRRPLRD--IPEPTIPDGVVIRTYAG 159
Cdd:TIGR03448  78 VHPAHRRRGIGRALIRALLAKGGGRLRVWAHGDLPAARALASRLGLVPTRELLQMRRPLRDleLPEPQVPDGVTVRAYVG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A        160 TSDDAELLRVNNAAFAGHPEQGGWTAVQLAERRGEAWFDPDGLILAFGDSprerPGRLLGFHWTKVHPDHPGLGEVYVLG 239
Cdd:TIGR03448 158 APDDAEWLRVNNAAFAWHPEQGGWTRADLAERRAEPWFDPAGLFLAFDDA----PGELLGFHWTKVHPDEPALGEVYVVG 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2C27_A        240 VDPAAQRRGLGQMLTSIGIVSLARRlggrktldpaVEPAVLLYVESDNVAAVRTYQSLGFTTYSVDTAY 308
Cdd:TIGR03448 234 VDPAAQGRGLGDALTLIGLHHLAAR----------GLPAVMLYVEADNEAAVRTYEKLGFTVAEVDVAY 292
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 219-312 1.17e-10

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 57.36  E-value: 1.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A      219 GFHWTKVHPDhPGLGEVYVLGVDPAAQRRGLGQMLTSIGIvSLARRLGGRKtldpavepaVLLYVESDNVAAVRTYQSLG 298
Cdd:COG0456   1 GFALLGLVDG-GDEAEIEDLAVDPEYRGRGIGRALLEAAL-ERARERGARR---------LRLEVREDNEAAIALYEKLG 69

                        90
                ....*....|....
2C27_A      299 FTTYSVDTAYALAG 312
Cdd:COG0456  70 FEEVGERPNYYGDD 83
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 178-299 1.19e-08

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 52.52  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A        178 PEQGGWTAVQLAERRGEAWFDPDGLILAFGDsprerpGRLLGFHWTKVHPDHPGLGEVYVLGVDPAAQRRGLGQMLTSIg 257
Cdd:pfam00583  11 EFPEPWPDEPLDLLEDWDEDASEGFFVAEED------GELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQA- 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
2C27_A        258 IVSLARRLGGRKtldpavepaVLLYVESDNVAAVRTYQSLGF 299
Cdd:pfam00583  84 LLEWARERGCER---------IFLEVAADNLAAIALYEKLGF 116
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 215-304 8.23e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 41.84  E-value: 8.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A       215 GRLLGFHWTKVHPDHPGLgevYVLGVDPAAQRRGLGQMLTSIGIVSLARRlgGRKTLdpavepavLLYVESDNVAAVRTY 294
Cdd:PRK09491  49 GQMAAFAITQVVLDEATL---FNIAVDPDYQRQGLGRALLEHLIDELEKR--GVATL--------WLEVRASNAAAIALY 115

                         90
                 ....*....|
2C27_A       295 QSLGFTTYSV 304
Cdd:PRK09491 116 ESLGFNEVTI 125
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 212-269 1.17e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 39.57  E-value: 1.17e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
2C27_A      212 ERPGRLLGFHWTKVHPDHPGLGEVYVLGVDPAAQRRGLGQMLTSIgIVSLARRLGGRK 269
Cdd:cd04301   5 EDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEA-AEEEARERGAKR 61
 
Name Accession Description Interval E-value
mycothiol_MshD TIGR03448
mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the ...
 5-308 2.61e-153

mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 132489 [Multi-domain]  Cd Length: 292  Bit Score: 431.05  E-value: 2.61e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A          5 DWRSALTADEQRSVRALVTATTAVDGVAPVGEQVLREL---GQQRTEHLLVAGSRPggpIIGYLNLSPPRGAGGAMAELV 81
Cdd:TIGR03448   1 TWRAALDADLRRDVRELLAAATAVDGVAPVSEQVLRGLrepGAGHTRHLVAVDSDP---IVGYANLVPARGTDPAMAELV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A         82 VHPQSRRRGIGTAMARAALAKTAGRNQFWAHGTLDPARATASALGLVGVRELIQMRRPLRD--IPEPTIPDGVVIRTYAG 159
Cdd:TIGR03448  78 VHPAHRRRGIGRALIRALLAKGGGRLRVWAHGDLPAARALASRLGLVPTRELLQMRRPLRDleLPEPQVPDGVTVRAYVG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A        160 TSDDAELLRVNNAAFAGHPEQGGWTAVQLAERRGEAWFDPDGLILAFGDSprerPGRLLGFHWTKVHPDHPGLGEVYVLG 239
Cdd:TIGR03448 158 APDDAEWLRVNNAAFAWHPEQGGWTRADLAERRAEPWFDPAGLFLAFDDA----PGELLGFHWTKVHPDEPALGEVYVVG 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2C27_A        240 VDPAAQRRGLGQMLTSIGIVSLARRlggrktldpaVEPAVLLYVESDNVAAVRTYQSLGFTTYSVDTAY 308
Cdd:TIGR03448 234 VDPAAQGRGLGDALTLIGLHHLAAR----------GLPAVMLYVEADNEAAVRTYEKLGFTVAEVDVAY 292
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 219-312 1.17e-10

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 57.36  E-value: 1.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A      219 GFHWTKVHPDhPGLGEVYVLGVDPAAQRRGLGQMLTSIGIvSLARRLGGRKtldpavepaVLLYVESDNVAAVRTYQSLG 298
Cdd:COG0456   1 GFALLGLVDG-GDEAEIEDLAVDPEYRGRGIGRALLEAAL-ERARERGARR---------LRLEVREDNEAAIALYEKLG 69

                        90
                ....*....|....
2C27_A      299 FTTYSVDTAYALAG 312
Cdd:COG0456  70 FEEVGERPNYYGDD 83
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 178-299 1.19e-08

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 52.52  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A        178 PEQGGWTAVQLAERRGEAWFDPDGLILAFGDsprerpGRLLGFHWTKVHPDHPGLGEVYVLGVDPAAQRRGLGQMLTSIg 257
Cdd:pfam00583  11 EFPEPWPDEPLDLLEDWDEDASEGFFVAEED------GELVGFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQA- 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
2C27_A        258 IVSLARRLGGRKtldpavepaVLLYVESDNVAAVRTYQSLGF 299
Cdd:pfam00583  84 LLEWARERGCER---------IFLEVAADNLAAIALYEKLGF 116
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
225-311 2.25e-07

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 47.98  E-value: 2.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A      225 VHPDHPGLGEVYVLGVDPAAQRRGLGQMLTSiGIVSLARRLGGRKtldpavepaVLLYVESDNVAAVRTYQSLGFTTYSV 304
Cdd:COG3393   8 VRAESPGVAEISGVYTHPEYRGRGLASALVA-ALAREALARGART---------PFLYVDADNPAARRLYERLGFRPVGE 77


                ....*..
2C27_A      305 DTAYALA 311
Cdd:COG3393  78 YATVLFR 84
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 165-299 5.24e-06

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: 45.01  E-value: 5.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A        165 ELLRVNNAAFAgHPeqggWTAVQLAErrgEAWFDPDGLILAFGDsprerpGRLLGFHWTKVHPDHpglGEVYVLGVDPAA 244
Cdd:TIGR01575   4 AVLEIEAAAFA-FP----WTEAQFAE---ELANYHLCYLLARIG------GKVVGYAGVQIVLDE---AHILNIAVKPEY 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
2C27_A        245 QRRGLGQMLtsigIVSLARRLGGRKtldpAVEpaVLLYVESDNVAAVRTYQSLGF 299
Cdd:TIGR01575  67 QGQGIGRAL----LRELIDEAKGRG----VNE--IFLEVRVSNIAAQALYKKLGF 111
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
212-301 8.36e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 45.37  E-value: 8.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A      212 ERPGRLLGFHWTKVHPDHPGLGEVYV--LGVDPAAQRRGLGQMLTSiGIVSLARRLGGRKtldpavepaVLLYVESDNVA 289
Cdd:COG1247  58 EEDGEVVGFASLGPFRPRPAYRGTAEesIYVDPDARGRGIGRALLE-ALIERARARGYRR---------LVAVVLADNEA 127

                        90
                ....*....|..
2C27_A      290 AVRTYQSLGFTT 301
Cdd:COG1247 128 SIALYEKLGFEE 139
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 212-300 3.30e-05

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: 43.06  E-value: 3.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A      212 ERPGRLLGFhwTKVHPDHPGLGEVYVLGVDPAAQRRGLGQMLTSIgIVSLARRLGGRKtldpavepavlLYVESdNVAAV 291
Cdd:COG1246  34 EEDGEIVGC--AALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEA-LLAEARELGLKR-----------LFLLT-TSAAI 98


                ....*....
2C27_A      292 RTYQSLGFT 300
Cdd:COG1246  99 HFYEKLGFE 107
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 215-304 8.23e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 41.84  E-value: 8.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A       215 GRLLGFHWTKVHPDHPGLgevYVLGVDPAAQRRGLGQMLTSIGIVSLARRlgGRKTLdpavepavLLYVESDNVAAVRTY 294
Cdd:PRK09491  49 GQMAAFAITQVVLDEATL---FNIAVDPDYQRQGLGRALLEHLIDELEKR--GVATL--------WLEVRASNAAAIALY 115

                         90
                 ....*....|
2C27_A       295 QSLGFTTYSV 304
Cdd:PRK09491 116 ESLGFNEVTI 125
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 212-269 1.17e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 39.57  E-value: 1.17e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
2C27_A      212 ERPGRLLGFHWTKVHPDHPGLGEVYVLGVDPAAQRRGLGQMLTSIgIVSLARRLGGRK 269
Cdd:cd04301   5 EDDGEIVGFASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEA-AEEEARERGAKR 61
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-112 1.41e-04

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 39.18  E-value: 1.41e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
2C27_A       58 GGPIIGYLNLSPPRGAGGA--MAELVVHPQSRRRGIGTAMARAAL--AKTAGRNQFWAH 112
Cdd:cd04301   7 DGEIVGFASLSPDGSGGDTayIGDLAVLPEYRGKGIGSALLEAAEeeARERGAKRLRLE 65
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 48-120 2.01e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 39.36  E-value: 2.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2C27_A         48 EHLLVAgsRPGGPIIGYLNLSP-PRGAGGAMAELVVHPQSRRRGIGTA-MARAALAKTAGRNQFWAHGTLDPARA 120
Cdd:pfam13508   3 GRFFVA--EDDGKIVGFAALLPlDDEGALAELRLAVHPEYRGQGIGRAlLEAAEAAAKEGGIKLLELETTNRAAA 75
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 44-120 2.12e-04

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: 40.36  E-value: 2.12e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2C27_A       44 QQRTEHLLVAgsRPGGPIIGYLNLSPPRGAGGAMAELVVHPQSRRRGIGTAMARAAL--AKTAGRNQFWAHgTLDPARA 120
Cdd:COG1246  24 EEEIGEFWVA--EEDGEIVGCAALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLaeARELGLKRLFLL-TTSAAIH 99
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 36-126 2.25e-04

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: 40.19  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A         36 EQVLRELGQQRTEHLLVAgsRPGGPIIGYLNLSPPRGAG--GAMAELVVHPQSRRRGIGTAMARAAL--AKTAGRNQFWA 111
Cdd:pfam00583  21 LDLLEDWDEDASEGFFVA--EEDGELVGFASLSIIDDEPpvGEIEGLAVAPEYRGKGIGTALLQALLewARERGCERIFL 98

                          90
                  ....*....|....*..
2C27_A        112 HGTLD--PARATASALG 126
Cdd:pfam00583  99 EVAADnlAAIALYEKLG 115
PRK03624 PRK03624
putative acetyltransferase; Provisional
 233-301 3.41e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 39.91  E-value: 3.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2C27_A       233 GEVYVLGVDPAAQRRGLGQMLtsigIVSLARRLGGRKTldpavePAVLLYVESDNVAAVRTYQSLGFTT 301
Cdd:PRK03624  69 GWAYYLAVHPDFRGRGIGRAL----VARLEKKLIARGC------PKINLQVREDNDAVLGFYEALGYEE 127
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 212-300 4.18e-04

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 38.59  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A        212 ERPGRLLGFHWTKVHPDHPGLGEVYvLGVDPAAQRRGLGQMLtsIGIVSLARRLGGrktldpavepAVLLYVESDNvAAV 291
Cdd:pfam13508   9 EDDGKIVGFAALLPLDDEGALAELR-LAVHPEYRGQGIGRAL--LEAAEAAAKEGG----------IKLLELETTN-RAA 74


                  ....*....
2C27_A        292 RTYQSLGFT 300
Cdd:pfam13508  75 AFYEKLGFE 83
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
18-101 4.41e-04

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 40.36  E-value: 4.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A       18 VRALVTATTAVDGVAPVGEQVLREL---GQQRTEHLLVAgsRPGGPIIGYLNLSP--PRGAGGAMAE--LVVHPQSRRRG 90
Cdd:COG1247  19 YNEAIAEGTATFETEPPSEEEREAWfaaILAPGRPVLVA--EEDGEVVGFASLGPfrPRPAYRGTAEesIYVDPDARGRG 96

                        90
                ....*....|.
2C27_A       91 IGTAMARAALA 101
Cdd:COG1247  97 IGRALLEALIE 107
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 36-112 5.08e-04

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 39.65  E-value: 5.08e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2C27_A       36 EQVLRELGQQRTEHLLVAGSRpgGPIIGYLNLSPPRGAGGAMAELVVHPQSRRRGIGTAMARAAL--AKTAGRNQFWAH 112
Cdd:COG0454  22 AELKAMEGSLAGAEFIAVDDK--GEPIGFAGLRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLewARERGCTALELD 98
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 63-110 5.62e-04

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 38.48  E-value: 5.62e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
2C27_A       63 GYLNLSPPRGAGGA-MAELVVHPQSRRRGIGTAMARAAL--AKTAGRNQFW 110
Cdd:COG0456   1 GFALLGLVDGGDEAeIEDLAVDPEYRGRGIGRALLEAALerARERGARRLR 51
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
9-107 5.98e-04

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 39.30  E-value: 5.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A        9 ALTADEQRSVRALVTATTAVDGVAPVGEQVLRELGQqrtEHLLVAgsRPGGPIIGYLNLSPPRGAGGA----MAELVVHP 84
Cdd:COG3153   3 PATPEDAEAIAALLRAAFGPGREAELVDRLREDPAA---GLSLVA--EDDGEIVGHVALSPVDIDGEGpallLGPLAVDP 77

                        90       100
                ....*....|....*....|...
2C27_A       85 QSRRRGIGTAMARAALAKTAGRN 107
Cdd:COG3153  78 EYRGQGIGRALMRAALEAARERG 100
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
154-300 2.09e-03

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 37.76  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A      154 IRTyAGTSDDAELLRVNNAAFAGHPEQggwtavQLAERRGEAWFDPDGLILafgdsprERPGRLLGF--HWTKVHPDHPG 231
Cdd:COG3153   1 IRP-ATPEDAEAIAALLRAAFGPGREA------ELVDRLREDPAAGLSLVA-------EDDGEIVGHvaLSPVDIDGEGP 66

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2C27_A      232 LGEVYVLGVDPAAQRRGLGQMLTSIGIvSLARRLGgrktldpavEPAVLLYVESDNVAAvrtYQSLGFT 300
Cdd:COG3153  67 ALLLGPLAVDPEYRGQGIGRALMRAAL-EAARERG---------ARAVVLLGDPSLLPF---YERFGFR 122
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 39-101 2.52e-03

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: 38.06  E-value: 2.52e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
2C27_A       39 LRELGQQRTEHLLVAGSRPGGPIIGYLNLSPPRGAGGAmAEL--VVHPQSRRRGIGTAMARAALA 101
Cdd:COG1670  51 LLADWADGGALPFAIEDKEDGELIGVVGLYDIDRANRS-AEIgyWLAPAYWGKGYATEALRALLD 114
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 215-312 4.05e-03

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 36.96  E-value: 4.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A      215 GRLLGFHWTKVHPDhpGLGEVYVLGVDPAAQRRGLGQMLTsIGIVSLARRLG-GRKTLDpavepavllyVESDNVAAVRT 293
Cdd:COG0454  43 GEPIGFAGLRRLDD--KVLELKRLYVLPEYRGKGIGKALL-EALLEWARERGcTALELD----------TLDGNPAAIRF 109

                        90
                ....*....|....*....
2C27_A      294 YQSLGFTTYSVDTAYALAG 312
Cdd:COG0454 110 YERLGFKEIERYVAYVGGE 128
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 229-302 4.23e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 35.77  E-value: 4.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2C27_A        229 HPGLGEVYVLGVDPAAQRRGLGQMLTSigivSLARRLGGRktldpavEPAVLLYVESDNVAAVRTYQSLGFTTY 302
Cdd:pfam08445  18 RLPGGELGALQTLPEHRRRGLGSRLVA----ALARGIAER-------GITPFAVVVAGNTPSRRLYEKLGFRKI 80
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 160-300 5.92e-03

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: 36.90  E-value: 5.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2C27_A      160 TSDDAELLrvnnAAFAGHPEQGGWT---------AVQLAERRGEAWFDPDGLILAFGDSPRERP-GRLlGFHWTKVHPDH 229
Cdd:COG1670  14 RPEDAEAL----AELLNDPEVARYLpgppysleeARAWLERLLADWADGGALPFAIEDKEDGELiGVV-GLYDIDRANRS 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2C27_A      230 PGLGevyvLGVDPAAQRRGLGQMLTSiGIVSLARRLGGRKTldpavepaVLLYVESDNVAAVRTYQSLGFT 300
Cdd:COG1670  89 AEIG----YWLAPAYWGKGYATEALR-ALLDYAFEELGLHR--------VEAEVDPDNTASIRVLEKLGFR 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 36-107 6.84e-03

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: 36.15  E-value: 6.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2C27_A         36 EQVLRELGQQRTeHLLVAGSrpGGPIIGYLNLSPPRGAGGAMAeLVVHPQSRRRGIGTAMARAALAKTAGRN 107
Cdd:TIGR01575  20 AQFAEELANYHL-CYLLARI--GGKVVGYAGVQIVLDEAHILN-IAVKPEYQGQGIGRALLRELIDEAKGRG 87
 
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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