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Conserved domains on  [gi|1621947938|gb|THG57758|]
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GNAT family N-acetyltransferase [Bacillus sp. HUB-I-004]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 11441181)

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
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-166 3.27e-24

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 92.36  E-value: 3.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938   1 MEIRLLTTEDA----EIYLKVCMEGLTknpeafssSYEDVLKHEDPVAAMAKRLSNPDKYTLGVFKDNHLIGIATLEtkP 76
Cdd:COG1247     2 MTIRPATPEDApaiaAIYNEAIAEGTA--------TFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLG--P 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  77 FIKQEHKAKIG--SVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLDVVVGNEAAKKLYKSVGFQTYGVQERSLKHNG 154
Cdd:COG1247    72 FRPRPAYRGTAeeSIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFG 151

                         170
                  ....*....|..
gi 1621947938 155 QYWDEEHMVLFL 166
Cdd:COG1247   152 RWLDLVLMQKRL 163
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-166 3.27e-24

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 92.36  E-value: 3.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938   1 MEIRLLTTEDA----EIYLKVCMEGLTknpeafssSYEDVLKHEDPVAAMAKRLSNPDKYTLGVFKDNHLIGIATLEtkP 76
Cdd:COG1247     2 MTIRPATPEDApaiaAIYNEAIAEGTA--------TFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLG--P 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  77 FIKQEHKAKIG--SVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLDVVVGNEAAKKLYKSVGFQTYGVQERSLKHNG 154
Cdd:COG1247    72 FRPRPAYRGTAeeSIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFG 151

                         170
                  ....*....|..
gi 1621947938 155 QYWDEEHMVLFL 166
Cdd:COG1247   152 RWLDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 39-140 6.08e-16

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: 69.47  E-value: 6.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  39 HEDPVAAMAKRLSNPDKYTLGVFKDNHLIGIATLetKPFIKQEHKAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVE 118
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEEDGELVGFASL--SIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCE 94

                          90       100
                  ....*....|....*....|..
gi 1621947938 119 QLMLDVVVGNEAAKKLYKSVGF 140
Cdd:pfam00583  95 RIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 44-145 1.16e-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: 56.18  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  44 AAMAKRLSNPDKYTLGVFKDNHLIGIATLETKPFikqehKAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLD 123
Cdd:TIGR01575  20 AQFAEELANYHLCYLLARIGGKVVGYAGVQIVLD-----EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLE 94

                          90       100
                  ....*....|....*....|..
gi 1621947938 124 VVVGNEAAKKLYKSVGFQTYGV 145
Cdd:TIGR01575  95 VRVSNIAAQALYKKLGFNEIAI 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-123 5.32e-09

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: 49.97  E-value: 5.32e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621947938  58 LGVFKDNHLIGIATLETKPFikQEHKAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLD 123
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGS--GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK10140 PRK10140
N-acetyltransferase;
33-162 1.09e-08

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 51.52  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  33 YEDVLKHEDPVAAM-AKRLSN-PDKYTLGVFKDNHLIGIATLETKPFIKQEHKAKIGsVFVSPKARGLGAGRALIKAIIE 110
Cdd:PRK10140   27 YHNTLQVPHPSDHMwQERLADrPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVADFG-ICVDSRWKNRGVASALMREMIE 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1621947938 111 NADK-LHVEQLMLDVVVGNEAAKKLYKSVGFQTYGVQERSLKHNGQYWDEEHM 162
Cdd:PRK10140  106 MCDNwLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYM 158
 
Name Accession Description Interval E-value
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-166 3.27e-24

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 92.36  E-value: 3.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938   1 MEIRLLTTEDA----EIYLKVCMEGLTknpeafssSYEDVLKHEDPVAAMAKRLSNPDKYTLGVFKDNHLIGIATLEtkP 76
Cdd:COG1247     2 MTIRPATPEDApaiaAIYNEAIAEGTA--------TFETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLG--P 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  77 FIKQEHKAKIG--SVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLDVVVGNEAAKKLYKSVGFQTYGVQERSLKHNG 154
Cdd:COG1247    72 FRPRPAYRGTAeeSIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFG 151

                         170
                  ....*....|..
gi 1621947938 155 QYWDEEHMVLFL 166
Cdd:COG1247   152 RWLDLVLMQKRL 163
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-168 4.98e-19

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: 79.27  E-value: 4.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938   1 MEIRLLTTEDAEIYLKvcmegLTKNPEA---FSSSYEDVLKHEDPVAAMAKRLSNPDKYTLGVFK--DNHLIGIATLetK 75
Cdd:COG1670     8 LRLRPLRPEDAEALAE-----LLNDPEVaryLPGPPYSLEEARAWLERLLADWADGGALPFAIEDkeDGELIGVVGL--Y 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  76 PFIKQEHKAKIGsVFVSPKARGLGAGRALIKAIIENA-DKLHVEQLMLDVVVGNEAAKKLYKSVGFQTYGVQERSLKHNG 154
Cdd:COG1670    81 DIDRANRSAEIG-YWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDG 159

                         170
                  ....*....|....
gi 1621947938 155 QYWDEEHMVLFLND 168
Cdd:COG1670   160 RYRDHVLYSLLREE 173
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 80-164 3.26e-17

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 72.00  E-value: 3.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  80 QEHKAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLDVVVGNEAAKKLYKSVGFQTYGVQERslkhngqYWDE 159
Cdd:COG0456    10 GGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPN-------YYGD 82


                  ....*
gi 1621947938 160 EHMVL 164
Cdd:COG0456    83 DALVM 87
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 39-140 6.08e-16

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: 69.47  E-value: 6.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  39 HEDPVAAMAKRLSNPDKYTLGVFKDNHLIGIATLetKPFIKQEHKAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVE 118
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEEDGELVGFASL--SIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGCE 94

                          90       100
                  ....*....|....*....|..
gi 1621947938 119 QLMLDVVVGNEAAKKLYKSVGF 140
Cdd:pfam00583  95 RIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
3-141 1.16e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 67.03  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938   3 IRLLTTEDAEIYLKVCMEgltknpeAFSSSYEdvlkhEDPVAAMakRLSNPDKYTLGVFKDNHLIGIATLETKPFIKQEH 82
Cdd:COG3153     1 IRPATPEDAEAIAALLRA-------AFGPGRE-----AELVDRL--REDPAAGLSLVAEDDGEIVGHVALSPVDIDGEGP 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621947938  83 KAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLdvvVGNEAAKKLYKSVGFQ 141
Cdd:COG3153    67 ALLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVL---LGDPSLLPFYERFGFR 122
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 42-141 3.86e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 65.46  E-value: 3.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  42 PVAAMAKRLSNPDK-----YTLGVFKDNHLIGIATLetkpFIKQEHKAKIGSVFVSPKARGLGAGRALIKAIIENADKLH 116
Cdd:COG0454    16 LIEALDAELKAMEGslagaEFIAVDDKGEPIGFAGL----RRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERG 91

                          90       100
                  ....*....|....*....|....*
gi 1621947938 117 VEQLMLDVVVGNEAAKKLYKSVGFQ 141
Cdd:COG0454    92 CTALELDTLDGNPAAIRFYERLGFK 116
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 63-167 5.64e-13

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: 62.32  E-value: 5.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  63 DNHLIGIATLETKPfikqEHKAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLDVvvgNEAAKKLYKSVGFQT 142
Cdd:COG1246    36 DGEIVGCAALHPLD----EDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLT---TSAAIHFYEKLGFEE 108

                          90       100
                  ....*....|....*....|....*
gi 1621947938 143 YGVQERSLkHNGQYWDEEHMVLFLN 167
Cdd:COG1246   109 IDKEDLPY-AKVWQRDSVVMEKDLE 132
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
86-144 3.13e-12

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 59.15  E-value: 3.13e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621947938  86 IGSVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLDVVVGNEAAKKLYKSVGFQTYG 144
Cdd:COG3393    18 ISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVG 76
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
3-159 4.01e-12

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 60.46  E-value: 4.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938   3 IRLLTTEDAEIYLKVCMEGltKNPEAFSSSYEdvlkhEDPVAAMAKRLSN---PDKYTLGVFKDNHLIGIATLETKPFIk 79
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAED--RVNPAFTQEYA-----HSSIEEFETFLAAylsPGEIVFGVAESDRLIGYATLRQFDYV- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  80 QEHKAKIGSVFVSPKARGLGagRALIKAIIENADK-LHVEQLMLDVVVGNEAAKKLYKSVGFQTYGVQERSLKHNGQYWD 158
Cdd:pfam13420  73 KTHKAELSFYVVKNNDEGIN--RELINAIIQYARKnQNIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150


                  .
gi 1621947938 159 E 159
Cdd:pfam13420 151 M 151
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
58-144 4.10e-11

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 57.50  E-value: 4.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  58 LGVFKDNHLIGIATLetkpFIKQEHKAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLDVvvgNEAAKKLYKS 137
Cdd:COG2153    37 LLAYDDGELVATARL----LPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSA---QAHAVGFYEK 109


                  ....*..
gi 1621947938 138 VGFQTYG 144
Cdd:COG2153   110 LGFVPVG 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 44-145 1.16e-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: 56.18  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  44 AAMAKRLSNPDKYTLGVFKDNHLIGIATLETKPFikqehKAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLD 123
Cdd:TIGR01575  20 AQFAEELANYHLCYLLARIGGKVVGYAGVQIVLD-----EAHILNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLE 94

                          90       100
                  ....*....|....*....|..
gi 1621947938 124 VVVGNEAAKKLYKSVGFQTYGV 145
Cdd:TIGR01575  95 VRVSNIAAQALYKKLGFNEIAI 116
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 44-148 2.91e-10

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


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 54.97  E-value: 2.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  44 AAMAKRLSNPDKYTLGVFKDNHLIGIATLETKPfikqehkaKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEqlmLD 123
Cdd:pfam13673  20 EALRERIDQGEYFFFVAFEGGQIVGVIALRDRG--------HISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIK---LS 88

                          90       100
                  ....*....|....*....|....*...
gi 1621947938 124 VVVGNEA--AKKLYKSVGFQTYG-VQER 148
Cdd:pfam13673  89 ELTVNASpyAVPFYEKLGFRATGpEQEF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 58-123 5.32e-09

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: 49.97  E-value: 5.32e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621947938  58 LGVFKDNHLIGIATLETKPFikQEHKAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLD 123
Cdd:cd04301     2 LVAEDDGEIVGFASLSPDGS--GGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
PRK10140 PRK10140
N-acetyltransferase;
33-162 1.09e-08

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 51.52  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  33 YEDVLKHEDPVAAM-AKRLSN-PDKYTLGVFKDNHLIGIATLETKPFIKQEHKAKIGsVFVSPKARGLGAGRALIKAIIE 110
Cdd:PRK10140   27 YHNTLQVPHPSDHMwQERLADrPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVADFG-ICVDSRWKNRGVASALMREMIE 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1621947938 111 NADK-LHVEQLMLDVVVGNEAAKKLYKSVGFQTYGVQERSLKHNGQYWDEEHM 162
Cdd:PRK10140  106 MCDNwLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYM 158
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 53-141 1.59e-08

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 49.38  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  53 PDKYTLGVFKDNHLIGIATLEtkpFIKQEHKAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEQLMLDVvvgNEAAK 132
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALL---PLDDEGALAELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELET---TNRAA 74


                  ....*....
gi 1621947938 133 KLYKSVGFQ 141
Cdd:pfam13508  75 AFYEKLGFE 83
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 86-149 2.93e-06

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: 43.47  E-value: 2.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621947938  86 IGSVFVSPKARGLGAGRALIKAIIENADKLHvEQLMLDVVVGNEAAKKLYKSVGFQTYGVQERS 149
Cdd:pfam08445  24 LGALQTLPEHRRRGLGSRLVAALARGIAERG-ITPFAVVVAGNTPSRRLYEKLGFRKIDETYWV 86
PRK10514 PRK10514
putative acetyltransferase; Provisional
 77-144 1.50e-05

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 42.68  E-value: 1.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621947938  77 FIKQEHkakIGSVFVSPKARGLGAGRALikaiIENADKLHVEqLMLDVVVGNEAAKKLYKSVGFQTYG 144
Cdd:PRK10514   66 LLSGGH---MEALFVDPDVRGCGVGRML----VEHALSLHPE-LTTDVNEQNEQAVGFYKKMGFKVTG 125
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 51-158 1.77e-05

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: 42.35  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  51 SNPDKYTLGVFKDNHLIGIATLETkpfIKQEHKAKIGSVFVSPKARGlGAGRALIKAIIENAD-KLHVEQLMLDVVVGNE 129
Cdd:TIGR03585  47 QDPNRRYWIVCQESRPIGVISFTD---INLVHKSAFWGIYANPFCKP-GVGSVLEEAALEYAFeHLGLHKLSLEVLESNN 122

                          90       100
                  ....*....|....*....|....*....
gi 1621947938 130 AAKKLYKSVGFQTYGVqersLKHNGQYWD 158
Cdd:TIGR03585 123 KALKLYEKFGFEREGV----FRQGGEYYD 147
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 3-141 3.22e-05

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 41.56  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938   3 IRLLTTEDAEIYLKvcmegLTKNPEAFSSSYEDVLKHEDPVAAMAKRLSNPDK---YTLGVF-KDNHLIGIATLEtkPFI 78
Cdd:pfam13302   4 LRPLTEEDAEALFE-----LLSDPEVMRYGVPWPLTLEEAREWLARIWAADEAergYGWAIElKDTGFIGSIGLY--DID 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621947938  79 KQEHKAKIGSVFvSPKARGLGAGRALIKAIIENA-DKLHVEQLMLDVVVGNEAAKKLYKSVGFQ 141
Cdd:pfam13302  77 GEPERAELGYWL-GPDYWGKGYATEAVRALLEYAfEELGLPRLVARIDPENTASRRVLEKLGFK 139
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 91-140 5.74e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 41.07  E-value: 5.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1621947938  91 VSPKARGLGAGRALIKAIIENADKLHVEQLMLDVVVGNEAAKKLYKSVGF 140
Cdd:PRK09491   71 VDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
PRK10562 PRK10562
putative acetyltransferase; Provisional
 73-141 8.65e-05

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 40.44  E-value: 8.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1621947938  73 ETKPFIKQEHKAKIGSVFVSPKARGLGAGRALIKaiienadklHVEQ----LMLDVVVGNEAAKKLYKSVGFQ 141
Cdd:PRK10562   58 KLLGFVSVLEGRFVGALFVAPKAVRRGIGKALMQ---------HVQQryphLSLEVYQKNQRAVNFYHAQGFR 121
Acetyltransf_18 pfam18014
Acetyltransferase (GNAT) domain; This entry represents a likely acetyltransferase enzyme that ...
 48-141 9.24e-05

Acetyltransferase (GNAT) domain; This entry represents a likely acetyltransferase enzyme that is related to pfam06852.


Pssm-ID: 436212  Cd Length: 123  Bit Score: 39.96  E-value: 9.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  48 KRLSNPDKYTLGVFKDNHLIGIATLetkpfIKQEHKAKIGSVFvspkARGLGAGRALIKAIIENADklhvEQLMLDVVVG 127
Cdd:pfam18014  19 RRLKQADQVAVVRNEDGEIRGYGLA-----RRCPAGLKIGPLV----ANNEEIALALIRALAANHE----GPVRIDVPEE 85

                          90
                  ....*....|....
gi 1621947938 128 NEAAKKLYKSVGFQ 141
Cdd:pfam18014  86 NPALIALLESLGFE 99
ectoine_EctA TIGR02406
diaminobutyrate acetyltransferase; This enzyme family is the EctA of ectoine biosynthesis. ...
 89-139 9.58e-05

diaminobutyrate acetyltransferase; This enzyme family is the EctA of ectoine biosynthesis. Ectoine is a compatible solute, analagous to trehalose, betaines, etc., found often in halotolerant organisms. EctA is L-2,4-diaminobutyric acid acetyltransferase, also called DABA acetyltransferase. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 131459  Cd Length: 157  Bit Score: 40.47  E-value: 9.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1621947938  89 VFVSPKARGLGAGRALIKAIIENADKLHVEQLMLDVVVGNEAAKKLYKSVG 139
Cdd:TIGR02406  72 VAVDPRARGKGLARRLLEALLERVACERVRHLETTITPDNQASRALFKALA 122
PRK03624 PRK03624
putative acetyltransferase; Provisional
 82-148 4.39e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 38.37  E-value: 4.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621947938  82 HKAKIGSVFVSPKARGLGAGRALI----KAIIEnadkLHVEQLMLDVVVGNEAAKKLYKSVGfqtYGVQER 148
Cdd:PRK03624   67 HRGWAYYLAVHPDFRGRGIGRALVarleKKLIA----RGCPKINLQVREDNDAVLGFYEALG---YEEQDR 130
Eis COG4552
Predicted acetyltransferase [General function prediction only];
1-112 1.10e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 38.34  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938   1 MEIRLLTTEDAEIYLKVCMEgltknpeAFSSSYEDvlkheDPVAAMAKRLSNPDkyTLGVFKDNHLIGIATL-------- 72
Cdd:COG4552     1 MEIRPLTEDDLDAFARLLAY-------AFGPEPDD-----EELEAYRPLLEPGR--VLGVFDDGELVGTLALypftlnvg 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1621947938  73 -ETKPFikqehkAKIGSVFVSPKARGLGAGRALIKAIIENA 112
Cdd:COG4552    67 gARVPM------AGITGVAVAPEHRRRGVARALLREALAEL 101
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
62-141 1.20e-03

dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;


Pssm-ID: 182877  Cd Length: 194  Bit Score: 37.60  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938  62 KDNHLIGIATLETKpfikQEHKAKIGSVFVSPKARGLGAGRALIKAII-----ENADKLHVE-QLmldvvvGNEAAKKLY 135
Cdd:PRK10975  109 ASGQIQGFVTLREL----NDTDARIGLLAVFPGAQGRGIGARLMQAALnwcqaRGLTRLRVAtQM------GNLAALRLY 178


                  ....*.
gi 1621947938 136 KSVGFQ 141
Cdd:PRK10975  179 IRSGAN 184
COG3981 COG3981
Predicted acetyltransferase [General function prediction only];
1-133 3.27e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443180  Cd Length: 170  Bit Score: 36.43  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621947938   1 MEIRLLTTEDAEIYLK---------VCMEGLTKNPEAFSSSYEDVLKHEDPVAAMAKRLsnPDKYTLGVFKDNHLIGIAT 71
Cdd:COG3981     2 MELVRPTLEDEESYLEylaeflkehIDGSGYLVSFEDFEAWLERLLDEEKGEELPEGWV--PATTYWLVDEDGRIVGAIN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621947938  72 L--ETKPFIKQE--HkakIG-SVfvSPKARGLGAGRALIKAIIENADKLHVEQLMLDVVVGNEAAKK 133
Cdd:COG3981    80 LrhELNEFLLRVggH---IGyGV--RPSERGKGYATEMLRLALEEARELGLDRVLITCDKDNIASRK 141
PRK07757 PRK07757
N-acetyltransferase;
60-120 4.98e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 35.56  E-value: 4.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621947938  60 VFKDNHLIGIATLEtkpfIKQEHKAKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEQL 120
Cdd:PRK07757   46 AEEEGEIVGCCALH----ILWEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKRV 102
PRK07922 PRK07922
amino-acid N-acetyltransferase;
84-120 5.70e-03

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 35.67  E-value: 5.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1621947938  84 AKIGSVFVSPKARGLGAGRALIKAIIENADKLHVEQL 120
Cdd:PRK07922   71 AEIRTVAVDPAARGRGVGHAIVERLLDVARELGLSRV 107
 
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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