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MULTISPECIES: GNAT family N-acetyltransferase [Bacillus]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

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:  15581578|10940244|9175471|27367672|26818562
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 47-132 8.87e-14

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: 63.31  E-value: 8.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378   47 GAYYLIVKEKNKVMGWILIGENTDYFSReklGFIYELYVFPEYRGRGLSRELMEAGIKELKEK-YLEIRLNVFAGNF-AK 124
Cdd:pfam00583  32 SEGFFVAEEDGELVGFASLSIIDDEPPV---GEIEGLAVAPEYRGKGIGTALLQALLEWARERgCERIFLEVAADNLaAI 108


                  ....*...
gi 446506378  125 EMYEEFGF 132
Cdd:pfam00583 109 ALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 47-132 8.87e-14

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: 63.31  E-value: 8.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378   47 GAYYLIVKEKNKVMGWILIGENTDYFSReklGFIYELYVFPEYRGRGLSRELMEAGIKELKEK-YLEIRLNVFAGNF-AK 124
Cdd:pfam00583  32 SEGFFVAEEDGELVGFASLSIIDDEPPV---GEIEGLAVAPEYRGKGIGTALLQALLEWARERgCERIFLEVAADNLaAI 108


                  ....*...
gi 446506378  125 EMYEEFGF 132
Cdd:pfam00583 109 ALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 61-140 7.19e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 60.05  E-value: 7.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378  61 GWILIGENTDyfsrEKLGFIYELYVFPEYRGRGLSRELMEAGIKELKEKYLE-IRLNVFAGNF-AKEMYEEFGFVERQVI 138
Cdd:COG0456    1 GFALLGLVDG----GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARrLRLEVREDNEaAIALYEKLGFEEVGER 76


                 ..
gi 446506378 139 MT 140
Cdd:COG0456   77 PN 78
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-116 2.78e-08

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


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 47.66  E-value: 2.78e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446506378  50 YLIVKEKNKVMGWILIgenTDYFSREKLGFIYELYVFPEYRGRGLSRELMEAGIKELKEK-YLEIRLN 116
Cdd:cd04301    1 FLVAEDDGEIVGFASL---SPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERgAKRLRLE 65
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 45-138 4.22e-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: 43.47  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378   45 EKGAYYLIVKEKNKVMGWILIgeNTDYFSREklgfIYELYVFPEYRGRGLSRELMEAGIKELKEKYL-EIRLNVFAGN-F 122
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGYAGV--QIVLDEAH----ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVnEIFLEVRVSNiA 101

                          90
                  ....*....|....*.
gi 446506378  123 AKEMYEEFGFVERQVI 138
Cdd:TIGR01575 102 AQALYKKLGFNEIAIR 117
PRK03624 PRK03624
putative acetyltransferase; Provisional
 78-139 1.13e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 42.22  E-value: 1.13e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446506378  78 GFIYELYVFPEYRGRGLSRELMEAGIKELKEK-YLEIRLNVFAGNFA-KEMYEEFGFVERQVIM 139
Cdd:PRK03624  69 GWAYYLAVHPDFRGRGIGRALVARLEKKLIARgCPKINLQVREDNDAvLGFYEALGYEEQDRIS 132
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 47-132 8.87e-14

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: 63.31  E-value: 8.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378   47 GAYYLIVKEKNKVMGWILIGENTDYFSReklGFIYELYVFPEYRGRGLSRELMEAGIKELKEK-YLEIRLNVFAGNF-AK 124
Cdd:pfam00583  32 SEGFFVAEEDGELVGFASLSIIDDEPPV---GEIEGLAVAPEYRGKGIGTALLQALLEWARERgCERIFLEVAADNLaAI 108


                  ....*...
gi 446506378  125 EMYEEFGF 132
Cdd:pfam00583 109 ALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 61-140 7.19e-13

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 60.05  E-value: 7.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378  61 GWILIGENTDyfsrEKLGFIYELYVFPEYRGRGLSRELMEAGIKELKEKYLE-IRLNVFAGNF-AKEMYEEFGFVERQVI 138
Cdd:COG0456    1 GFALLGLVDG----GDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARrLRLEVREDNEaAIALYEKLGFEEVGER 76


                 ..
gi 446506378 139 MT 140
Cdd:COG0456   77 PN 78
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-134 7.22e-13

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 61.93  E-value: 7.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378   1 MIIKANQEDTNEILKCAAQSLFEGTR--GNCQLSTEKAIEITKPIVEKGAYYLIVKEKNKVMGWILIGentDYFSREKLG 78
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNEAIAEGTAtfETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASLG---PFRPRPAYR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378  79 FIYE--LYVFPEYRGRGLSRELMEAGIKELKEK-YLEIRLNVFAGN-FAKEMYEEFGFVE 134
Cdd:COG1247   80 GTAEesIYVDPDARGRGIGRALLEALIERARARgYRRLVAVVLADNeASIALYEKLGFEE 139
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 2-134 1.32e-11

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 58.14  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378   2 IIKANQEDTNEILKCAAQSLfegtrgncqlstekaiEITKPI-VEKGAYYLIVKEKNKVMGWILIGEnTDyfsrEKLGFI 80
Cdd:COG0454    3 IRKATPEDINFILLIEALDA----------------ELKAMEgSLAGAEFIAVDDKGEPIGFAGLRR-LD----DKVLEL 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446506378  81 YELYVFPEYRGRGLSRELMEAGIKELKEKYL-EIRLNVFAGN-FAKEMYEEFGFVE 134
Cdd:COG0454   62 KRLYVLPEYRGKGIGKALLEALLEWARERGCtALELDTLDGNpAAIRFYERLGFKE 117
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 43-134 7.77e-11

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 55.77  E-value: 7.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378  43 IVEKGAYYLIVKEKNKVMGWILIgentdYFSREKLGFIYELYVFPEYRGRGLSRELMEAGIKELKEKYLEiRLNVFAGNF 122
Cdd:COG1246   23 LEEEIGEFWVAEEDGEIVGCAAL-----HPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLK-RLFLLTTSA 96

                         90
                 ....*....|..
gi 446506378 123 AKEMYEEFGFVE 134
Cdd:COG1246   97 AIHFYEKLGFEE 108
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 44-134 8.13e-11

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: 8.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378   44 VEKGAYYLIV-KEKNKVMGWILIGENtdyfsreklGFIYELYVFPEYRGRGLSRELMEAGIKELKEKYLEI-RLNVFAGN 121
Cdd:pfam13673  26 IDQGEYFFFVaFEGGQIVGVIALRDR---------GHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLsELTVNASP 96

                          90
                  ....*....|...
gi 446506378  122 FAKEMYEEFGFVE 134
Cdd:pfam13673  97 YAVPFYEKLGFRA 109
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 46-134 2.76e-10

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 53.23  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378   46 KGAYYLIVKEKNKVMGWILIGENTDYFSREKLGfiyeLYVFPEYRGRGLSRELMEAGIKELKEKYLEiRLNVFAGNFAKE 125
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGALAELR----LAVHPEYRGQGIGRALLEAAEAAAKEGGIK-LLELETTNRAAA 75


                  ....*....
gi 446506378  126 MYEEFGFVE 134
Cdd:pfam13508  76 FYEKLGFEE 84
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
51-134 5.06e-10

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 53.94  E-value: 5.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378  51 LIVKEKNKVMGWILIgENTDYFSREKLGFIYELYVFPEYRGRGLSRELMEAGIKELKEK-YLEIRLnvFAGNFAKEMYEE 129
Cdd:COG3153   42 LVAEDDGEIVGHVAL-SPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERgARAVVL--LGDPSLLPFYER 118


                 ....*
gi 446506378 130 FGFVE 134
Cdd:COG3153  119 FGFRP 123
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
78-142 1.37e-08

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 48.75  E-value: 1.37e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446506378  78 GFIYELYVFPEYRGRGLSRELMEAGIKELKEK-YLEIRLNVFAGNF-AKEMYEEFGFVERQVIMTLK 142
Cdd:COG3393   16 AEISGVYTHPEYRGRGLASALVAALAREALARgARTPFLYVDADNPaARRLYERLGFRPVGEYATVL 82
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 50-116 2.78e-08

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


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 47.66  E-value: 2.78e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446506378  50 YLIVKEKNKVMGWILIgenTDYFSREKLGFIYELYVFPEYRGRGLSRELMEAGIKELKEK-YLEIRLN 116
Cdd:cd04301    1 FLVAEDDGEIVGFASL---SPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERgAKRLRLE 65
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
45-134 2.81e-07

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 46.33  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378  45 EKGAYYLIVKEKNKVMG---WILIGENTDYFSReklgfiyeLYVFPEYRGRGLSRELMEAGIKELKEK-YLEIRLNVFAG 120
Cdd:COG2153   31 DEDARHLLAYDDGELVAtarLLPPGDGEAKIGR--------VAVLPEYRGQGLGRALMEAAIEEARERgARRIVLSAQAH 102

                         90
                 ....*....|....
gi 446506378 121 nfAKEMYEEFGFVE 134
Cdd:COG2153  103 --AVGFYEKLGFVP 114
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 54-135 4.21e-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: 42.32  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378   54 KEKNKVMGWILigentdyfsREKLGFIYELYVFPEYRGRGLSRELMEAGIKELKEKYLEIRLNVFAGNF-AKEMYEEFGF 132
Cdd:pfam08445   7 GDTGELAAWCL---------RLPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGITPFAVVVAGNTpSRRLYEKLGF 77


                  ...
gi 446506378  133 VER 135
Cdd:pfam08445  78 RKI 80
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 45-138 4.22e-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: 43.47  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378   45 EKGAYYLIVKEKNKVMGWILIgeNTDYFSREklgfIYELYVFPEYRGRGLSRELMEAGIKELKEKYL-EIRLNVFAGN-F 122
Cdd:TIGR01575  28 NYHLCYLLARIGGKVVGYAGV--QIVLDEAH----ILNIAVKPEYQGQGIGRALLRELIDEAKGRGVnEIFLEVRVSNiA 101

                          90
                  ....*....|....*.
gi 446506378  123 AKEMYEEFGFVERQVI 138
Cdd:TIGR01575 102 AQALYKKLGFNEIAIR 117
PRK03624 PRK03624
putative acetyltransferase; Provisional
 78-139 1.13e-05

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 42.22  E-value: 1.13e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446506378  78 GFIYELYVFPEYRGRGLSRELMEAGIKELKEK-YLEIRLNVFAGNFA-KEMYEEFGFVERQVIM 139
Cdd:PRK03624  69 GWAYYLAVHPDFRGRGIGRALVARLEKKLIARgCPKINLQVREDNDAvLGFYEALGYEEQDRIS 132
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 85-134 9.64e-05

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 39.91  E-value: 9.64e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446506378  85 VFPEYRGRGLSRELMEAGIKELKEK-----YLEIRlnvfAGNF-AKEMYEEFGFVE 134
Cdd:PRK09491  71 VDPDYQRQGLGRALLEHLIDELEKRgvatlWLEVR----ASNAaAIALYESLGFNE 122
PRK07757 PRK07757
N-acetyltransferase;
50-134 3.72e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 38.25  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378  50 YLIVKEKNKVMGWILIgentdYFSREKLGFIYELYVFPEYRGRGLSRELMEAGIKELKEkyLEIRlNVFAGNFAKEMYEE 129
Cdd:PRK07757  43 FYVAEEEGEIVGCCAL-----HILWEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARE--LGVK-RVFALTYQPEFFEK 114


                 ....*
gi 446506378 130 FGFVE 134
Cdd:PRK07757 115 LGFRE 119
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 38-134 9.57e-04

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: 37.29  E-value: 9.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446506378  38 EITKPIVEKGAYYLIV--KEKNKVMGWILIGENTDYFSREKLGFiyelYVFPEYRGRGLSRELMEAGIKELKE--KYLEI 113
Cdd:COG1670   50 RLLADWADGGALPFAIedKEDGELIGVVGLYDIDRANRSAEIGY----WLAPAYWGKGYATEALRALLDYAFEelGLHRV 125

                         90       100
                 ....*....|....*....|..
gi 446506378 114 RLNVFAGNFA-KEMYEEFGFVE 134
Cdd:COG1670  126 EAEVDPDNTAsIRVLEKLGFRL 147
Eis COG4552
Predicted acetyltransferase [General function prediction only];
85-109 1.45e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 37.19  E-value: 1.45e-03
                         10        20
                 ....*....|....*....|....*
gi 446506378  85 VFPEYRGRGLSRELMEAGIKELKEK 109
Cdd:COG4552   80 VAPEHRRRGVARALLREALAELRER 104
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
45-109 6.46e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 33.98  E-value: 6.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446506378  45 EKGAYYLIVKekNKVMGWIligentDYFSREKLGFIYELYVFPEYRGRGLSRELMEAGIKELKEK 109
Cdd:COG2388    8 EKGRFELEVD--GELAGEL------TYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARER 64
Acetyltransf_CG pfam14542
GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both ...
 50-114 7.92e-03

GCN5-related N-acetyl-transferase; This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.


Pssm-ID: 434030 [Multi-domain]  Cd Length: 79  Bit Score: 33.26  E-value: 7.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446506378   50 YLIVKEKNKVMGWIligentDYFSREKLGFIYELYVFPEYRGRGLSRELMEAGIKELKEKYLEIR 114
Cdd:pfam14542   2 FEIRVDGGAEVAFL------TYRRGDGVLIITHTEVPPALRGQGIASKLVKAALDDAREEGLKIV 60
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 85-132 8.93e-03

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 34.08  E-value: 8.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446506378   85 VFPEYRGRGLSRELMEAGIKELKEKylEIRLNVFAGnFAKEMYEEFGF 132
Cdd:pfam13527  78 TYPEYRGRGVMSRLLRRSLEEMRER--GVPLSFLYP-SSYPIYRRFGY 122
 
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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