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Conserved domains on  [gi|16131313|ref|NP_417898|]
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N-acetyltransferase YhhY [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10013436)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate, similar to Escherichia coli AaaT/YhhY which catalyzes the N-acetylation of L-phenylalanine and L-methionine, and is also able to acetylate and thus detoxify several nonhydrolyzable aminoacyl adenylates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-162 1.53e-126

N-acetyltransferase;


:

Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 351.59  E-value: 1.53e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313    1 MSEIVIRHAETRDYEAIRQIHAQPEVYCNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313   81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 16131313  161 VK 162
Cdd:PRK10140 161 VK 162
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-162 1.53e-126

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 351.59  E-value: 1.53e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313    1 MSEIVIRHAETRDYEAIRQIHAQPEVYCNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313   81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 16131313  161 VK 162
Cdd:PRK10140 161 VK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-162 6.61e-32

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: 112.01  E-value: 6.61e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313   4 IVIRHAETRDYEAIRQIHAQPEVYCNTLQVPHPSDHMWQ-----ERLADRPGIKQLVACI--DGDVVGhlTIDVQQRPRR 76
Cdd:COG1670   8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAwlerlLADWADGGALPFAIEDkeDGELIG--VVGLYDIDRA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313  77 SHVADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAY 156
Cdd:COG1670  86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                ....*.
gi 16131313 157 YMARVK 162
Cdd:COG1670 166 LYSLLR 171
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-136 6.18e-15

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


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 66.77  E-value: 6.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313    25 EVYCNTLQVPHPSDHMW-QERLADRPGIKQLVACIDGDVVGHLTIdVQQRPRRSHVADFGICVDSRWKNRGVASALMREM 103
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDlLEDWDEDASEGFFVAEEDGELVGFASL-SIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQAL 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 16131313   104 IEMCDNWlRVDRIELTVFVDNAPAIKVYKKYGF 136
Cdd:pfam00583  85 LEWARER-GCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 54-158 1.35e-13

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


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 63.50  E-value: 1.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313    54 LVACIDGDVVGHLTIDVQqrPRRSHVadFGICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVFVDNAPAIKVYKK 133
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIV--LDEAHI--LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKK 108

                          90       100
                  ....*....|....*....|....*
gi 16131313   134 YGFEIEGTGKKYALRNGEyvDAYYM 158
Cdd:TIGR01575 109 LGFNEIAIRRNYYPDPGE--DAIVM 131
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-119 3.67e-05

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: 3.67e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131313  54 LVACIDGDVVGHLTIDVQQ-RPRRSHVADfgICVDSRWKNRGVASALMREMIEMCDNWlRVDRIELT 119
Cdd:cd04301   2 LVAEDDGEIVGFASLSPDGsGGDTAYIGD--LAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
 
Name Accession Description Interval E-value
PRK10140 PRK10140
N-acetyltransferase;
1-162 1.53e-126

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 351.59  E-value: 1.53e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313    1 MSEIVIRHAETRDYEAIRQIHAQPEVYCNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80
Cdd:PRK10140   1 MSEIVIRHAETRDYEAIRQIHAQPEVYHNTLQVPHPSDHMWQERLADRPGIKQLVACIDGDVVGHLTIDVQQRPRRSHVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313   81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160
Cdd:PRK10140  81 DFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMAR 160


                 ..
gi 16131313  161 VK 162
Cdd:PRK10140 161 VK 162
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 4-162 6.61e-32

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: 112.01  E-value: 6.61e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313   4 IVIRHAETRDYEAIRQIHAQPEVYCNTLQVPHPSDHMWQ-----ERLADRPGIKQLVACI--DGDVVGhlTIDVQQRPRR 76
Cdd:COG1670   8 LRLRPLRPEDAEALAELLNDPEVARYLPGPPYSLEEARAwlerlLADWADGGALPFAIEDkeDGELIG--VVGLYDIDRA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313  77 SHVADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAY 156
Cdd:COG1670  86 NRSAEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHV 165


                ....*.
gi 16131313 157 YMARVK 162
Cdd:COG1670 166 LYSLLR 171
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
3-160 3.23e-29

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 105.08  E-value: 3.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313   3 EIVIRHAETRDYEAIRQIHAQ-PEVYCNTLQVPHPSDHMWQERLADR--PGIKQLVACIDGDVVGHLTI-DVQQRPRRSH 78
Cdd:COG1247   1 EMTIRPATPEDAPAIAAIYNEaIAEGTATFETEPPSEEEREAWFAAIlaPGRPVLVAEEDGEVVGFASLgPFRPRPAYRG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313  79 VADFGICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYM 158
Cdd:COG1247  81 TAEESIYVDPDARGRGIGRALLEALIERARA-RGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLM 159


                ..
gi 16131313 159 AR 160
Cdd:COG1247 160 QK 161
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 64-160 1.46e-15

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 67.76  E-value: 1.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313  64 GHLTIDVQQRPRRSHVADfgICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGK 143
Cdd:COG0456   1 GFALLGLVDGGDEAEIED--LAVDPEYRGRGIGRALLEAALERARE-RGARRLRLEVREDNEAAIALYEKLGFEEVGERP 77

                        90
                ....*....|....*..
gi 16131313 144 KYALRngeyvDAYYMAR 160
Cdd:COG0456  78 NYYGD-----DALVMEK 89
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 25-136 6.18e-15

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


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 66.77  E-value: 6.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313    25 EVYCNTLQVPHPSDHMW-QERLADRPGIKQLVACIDGDVVGHLTIdVQQRPRRSHVADFGICVDSRWKNRGVASALMREM 103
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDlLEDWDEDASEGFFVAEEDGELVGFASL-SIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQAL 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 16131313   104 IEMCDNWlRVDRIELTVFVDNAPAIKVYKKYGF 136
Cdd:pfam00583  85 LEWARER-GCERIFLEVAADNLAAIALYEKLGF 116
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
6-160 8.36e-14

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 64.34  E-value: 8.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313   6 IRHAETRDYEAIRQIHAQpeVYcntlqvPHPSDHMWQERLADRPGIKQ-LVACIDGDVVGHLTIDVQQRPRRSHVADFG- 83
Cdd:COG3153   1 IRPATPEDAEAIAALLRA--AF------GPGREAELVDRLREDPAAGLsLVAEDDGEIVGHVALSPVDIDGEGPALLLGp 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131313  84 ICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVFVDNAPaikVYKKYGFEIEGTGkkyalRNGEYVDAYYMAR 160
Cdd:COG3153  73 LAVDPEYRGQGIGRALMRAALEAARE-RGARAVVLLGDPSLLP---FYERFGFRPAGEL-----GLTLGPDEVFLAK 140
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 54-158 1.35e-13

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


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 63.50  E-value: 1.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313    54 LVACIDGDVVGHLTIDVQqrPRRSHVadFGICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVFVDNAPAIKVYKK 133
Cdd:TIGR01575  34 LLARIGGKVVGYAGVQIV--LDEAHI--LNIAVKPEYQGQGIGRALLRELIDEAKG-RGVNEIFLEVRVSNIAAQALYKK 108

                          90       100
                  ....*....|....*....|....*
gi 16131313   134 YGFEIEGTGKKYALRNGEyvDAYYM 158
Cdd:TIGR01575 109 LGFNEIAIRRNYYPDPGE--DAIVM 131
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 4-137 8.21e-12

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 59.28  E-value: 8.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313     4 IVIRHAETRDYEAIRQIHAQPEVycNTLQVPHPSD---------HMWQERLADRpGIKQLVACIDGDVVGhlTIDVQQRP 74
Cdd:pfam13302   2 LLLRPLTEEDAEALFELLSDPEV--MRYGVPWPLTleearewlaRIWAADEAER-GYGWAIELKDTGFIG--SIGLYDID 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131313    75 RRSHVADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFE 137
Cdd:pfam13302  77 GEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 37-137 1.48e-10

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


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 55.74  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313    37 SDHMWQERLaDRPGIKQLVACIDGDVVGHLTIDvqqrpRRSHVADFgiCVDSRWKNRGVASALMREMIEMCDNWlRVDRI 116
Cdd:pfam13673  18 SPEALRERI-DQGEYFFFVAFEGGQIVGVIALR-----DRGHISLL--FVDPDYQGQGIGKALLEAVEDYAEKD-GIKLS 88

                          90       100
                  ....*....|....*....|.
gi 16131313   117 ELTVFVDNaPAIKVYKKYGFE 137
Cdd:pfam13673  89 ELTVNASP-YAVPFYEKLGFR 108
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
6-154 1.58e-09

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 53.52  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313     6 IRHAETRDYEAIRQIHAQPEV-YCNTLQVPHPSDHMWQERLADRPGIKQLVACID--GDVVGHLTIdVQQRPRRSHVADF 82
Cdd:pfam13420   1 IRALTQNDLKEIRRWYAEDRVnPAFTQEYAHSSIEEFETFLAAYLSPGEIVFGVAesDRLIGYATL-RQFDYVKTHKAEL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131313    83 GICVDSRwKNRGVAsalmREMIEMCDNWLR----VDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVD 154
Cdd:pfam13420  80 SFYVVKN-NDEGIN----RELINAIIQYARknqnIENLEACIASNNINAIVFLKAIGFEWLGIERNAIKKNGRWID 150
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 54-138 2.47e-09

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 51.30  E-value: 2.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313    54 LVACIDGDVVGhlTIDVQQRPRRSHVADFGICVDSRWKNRGVASALMREMIEmcdnWLRVDRIELTVFVDNAPAIKVYKK 133
Cdd:pfam13508   6 FVAEDDGKIVG--FAALLPLDDEGALAELRLAVHPEYRGQGIGRALLEAAEA----AAKEGGIKLLELETTNRAAAFYEK 79


                  ....*
gi 16131313   134 YGFEI 138
Cdd:pfam13508  80 LGFEE 84
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 39-162 3.63e-08

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 49.28  E-value: 3.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313  39 HMWQERLADRPGIK----QLVACIDGDVVGHLTIdvqqrprrSHVAD-----FGICVDSRWKNRGVASALMREMIEmcdn 109
Cdd:COG0454  18 EALDAELKAMEGSLagaeFIAVDDKGEPIGFAGL--------RRLDDkvlelKRLYVLPEYRGKGIGKALLEALLE---- 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131313 110 WLR---VDRIELTVFVDNAPAIKVYKKYGFEIEGtgkkyalRNGEYVDAYYMARVK 162
Cdd:COG0454  86 WARergCTALELDTLDGNPAAIRFYERLGFKEIE-------RYVAYVGGEFEKELS 134
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
83-141 8.89e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 47.21  E-value: 8.89e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131313  83 GICVDSRWKNRGVASALMREMIEmcdnWLR---VDRIELTVFVDNAPAIKVYKKYGFEIEGT 141
Cdd:COG3393  20 GVYTHPEYRGRGLASALVAALAR----EALargARTPFLYVDADNPAARRLYERLGFRPVGE 77
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 4-137 2.45e-06

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: 44.60  E-value: 2.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313   4 IVIRHAETRDYEAIRQIHAQPEVYcntlqvpHPSDHMWqerladrpgikqlVACIDGDVVGHLTIDVQQrPRRSHVADFG 83
Cdd:COG1246   1 MTIRPATPDDVPAILELIRPYALE-------EEIGEFW-------------VAEEDGEIVGCAALHPLD-EDLAELRSLA 59

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 16131313  84 icVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVfvdNAPAIKVYKKYGFE 137
Cdd:COG1246  60 --VHPDYRGRGIGRRLLEALLAEARE-LGLKRLFLLT---TSAAIHFYEKLGFE 107
Acetyltransf_8 pfam13523
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 41-141 1.49e-05

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


Pssm-ID: 433280  Cd Length: 145  Bit Score: 42.51  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313    41 WQERLADRPGIKQLVACIDGDVVGHLTIDvqqRPRRSHVA--------DFGICV---DSRWKNRGVASALMREMIEMCDN 109
Cdd:pfam13523  34 YLARLAADPHSHPYIGLLDGEPFGYFEIY---WAKEDRLGeyydarpgDRGIHLligEPAFRGRGFTTALLRALVHYLFA 110

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 16131313   110 WLRVDRIeltVF---VDNAPAIKVYKKYGFEIEGT 141
Cdd:pfam13523 111 DPRTRRV---VVepdVRNERAIRLLERAGFRKVKE 142
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 80-158 1.76e-05

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 42.86  E-value: 1.76e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131313   80 ADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTVFVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYM 158
Cdd:PRK15130  84 AEFQIIISPEYQGKGLATRAAKLAMDYGFTVLNLYKLYLIVDKENEKAIHIYRKLGFEVEGELIHEFFINGEYRNTIRM 162
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 54-119 3.67e-05

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: 3.67e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131313  54 LVACIDGDVVGHLTIDVQQ-RPRRSHVADfgICVDSRWKNRGVASALMREMIEMCDNWlRVDRIELT 119
Cdd:cd04301   2 LVAEDDGEIVGFASLSPDGsGGDTAYIGD--LAVLPEYRGKGIGSALLEAAEEEARER-GAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
54-140 4.32e-05

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 40.94  E-value: 4.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313  54 LVACIDGDVVGHLTIdvqqRPRRSHVADFG-ICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELtvfvdNA--PAIKV 130
Cdd:COG2153  37 LLAYDDGELVATARL----LPPGDGEAKIGrVAVLPEYRGQGLGRALMEAAIEEARE-RGARRIVL-----SAqaHAVGF 106

                        90
                ....*....|
gi 16131313 131 YKKYGFEIEG 140
Cdd:COG2153 107 YEKLGFVPVG 116
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 6-138 1.05e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 37.17  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131313     6 IRHAETRDYEAIRQIHAqpevYCntLQVPhPSDHMWQERladRPGIKQ---LVACIDGDVVGHL-----TIDVQQRPRR- 76
Cdd:pfam13527   1 IRPLTEDEFDEVLRLLE----YA--FQDE-DSPELREYF---RPLLEEgrvLGAFDDGELVSTLalypfELNVPGKTLPa 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131313    77 SHVAdfGICVDSRWKNRGVASALMREMIEMCdnwlRVDRIELTVFVDNAPAIkvYKKYGFEI 138
Cdd:pfam13527  71 AGIT--GVATYPEYRGRGVMSRLLRRSLEEM----RERGVPLSFLYPSSYPI--YRRFGYEI 124
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 82-137 2.77e-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: 35.00  E-value: 2.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 16131313    82 FGICVDSRWKNRGVASALMREMIEMcdnwLRVDRIELTVFV--DNAPAIKVYKKYGFE 137
Cdd:pfam08445  25 GALQTLPEHRRRGLGSRLVAALARG----IAERGITPFAVVvaGNTPSRRLYEKLGFR 78
 
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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