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Conserved domains on  [gi|616567803|gb|KAD69035|]
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hypothetical protein W576_00393 [Staphylococcus aureus VET0312R]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 18514852)

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

CATH:  3.40.630.30
EC:  2.3.1.-
Gene Ontology:  GO:0008080
PubMed:  15581578|9175471|10940244
SCOP:  3000403

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 108-183 1.89e-12

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: 1.89e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616567803 108 DDEYYIETIATFAAYRGRGIATKLLTSLLE---SNTHVKWSLNCDINNEAALKLYKKVGFISDGQIELYKHMYHHLIVK 183
Cdd:COG0456   11 GDEAEIEDLAVDPEYRGRGIGRALLEAALErarERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVMEK 89
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-171 5.34e-06

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


:

Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 44.22  E-value: 5.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616567803   1 MIRQARPEDRFDIAKLVY-------MVWDDMELELvkhlpkDMVLDAIEKSCIDAtyrtfyQHVLVYEIENKVAGCIISY 73
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNeaiaegtATFETEPPSE------EEREAWFAAILAPG------RPVLVAEEDGEVVGFASLG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616567803  74 SGENELKYEKAWEqldlpeeikqygtplpvkeakdDEYYIEtiatfAAYRGRGIATKLLTSLLEsntHVK----WSLNCD 149
Cdd:COG1247   71 PFRPRPAYRGTAE----------------------ESIYVD-----PDARGRGIGRALLEALIE---RARargyRRLVAV 120

                        170       180
                 ....*....|....*....|....
gi 616567803 150 I--NNEAALKLYKKVGFISDGQIE 171
Cdd:COG1247  121 VlaDNEASIALYEKLGFEEVGTLP 144
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 108-183 1.89e-12

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: 1.89e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616567803 108 DDEYYIETIATFAAYRGRGIATKLLTSLLE---SNTHVKWSLNCDINNEAALKLYKKVGFISDGQIELYKHMYHHLIVK 183
Cdd:COG0456   11 GDEAEIEDLAVDPEYRGRGIGRALLEAALErarERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVMEK 89
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 107-164 7.92e-09

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: 51.36  E-value: 7.92e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616567803  107 KDDEYYIETIATFAAYRGRGIATKLLTSLLE---SNTHVKWSLNCDINNEAALKLYKKVGF 164
Cdd:pfam00583  56 EPPVGEIEGLAVAPEYRGKGIGTALLQALLEwarERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 109-178 3.47e-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: 44.24  E-value: 3.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616567803  109 DEYYIETIATFAAYRGRGIATKLLTSL---LESNTHVKWSLNCDINNEAALKLYKKVGFisdGQIELYKHMYH 178
Cdd:TIGR01575  53 DEAHILNIAVKPEYQGQGIGRALLRELideAKGRGVNEIFLEVRVSNIAAQALYKKLGF---NEIAIRRNYYP 122
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-171 5.34e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 44.22  E-value: 5.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616567803   1 MIRQARPEDRFDIAKLVY-------MVWDDMELELvkhlpkDMVLDAIEKSCIDAtyrtfyQHVLVYEIENKVAGCIISY 73
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNeaiaegtATFETEPPSE------EEREAWFAAILAPG------RPVLVAEEDGEVVGFASLG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616567803  74 SGENELKYEKAWEqldlpeeikqygtplpvkeakdDEYYIEtiatfAAYRGRGIATKLLTSLLEsntHVK----WSLNCD 149
Cdd:COG1247   71 PFRPRPAYRGTAE----------------------ESIYVD-----PDARGRGIGRALLEALIE---RARargyRRLVAV 120

                        170       180
                 ....*....|....*....|....
gi 616567803 150 I--NNEAALKLYKKVGFISDGQIE 171
Cdd:COG1247  121 VlaDNEASIALYEKLGFEEVGTLP 144
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-137 1.20e-03

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: 35.71  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616567803  57 VLVYEIENKVAGCIISYsgenelkyekaweqldlpeeikqygtplpVKEAKDDEYYIETIATFAAYRGRGIATKLLTSLL 136
Cdd:cd04301    1 FLVAEDDGEIVGFASLS-----------------------------PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAE 51


                 .
gi 616567803 137 E 137
Cdd:cd04301   52 E 52
PTZ00330 PTZ00330
acetyltransferase; Provisional
 112-164 6.29e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 35.59  E-value: 6.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 616567803 112 YIETIATFAAYRGRGIATKLLTSLLE---SNTHVKWSLNCdinNEAALKLYKKVGF 164
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEiarSSGCYKVILDC---TEDMVAFYKKLGF 136
 
Name Accession Description Interval E-value
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 108-183 1.89e-12

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: 1.89e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616567803 108 DDEYYIETIATFAAYRGRGIATKLLTSLLE---SNTHVKWSLNCDINNEAALKLYKKVGFISDGQIELYKHMYHHLIVK 183
Cdd:COG0456   11 GDEAEIEDLAVDPEYRGRGIGRALLEAALErarERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYGDDALVMEK 89
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
112-174 3.03e-09

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 51.45  E-value: 3.03e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616567803 112 YIETIATFAAYRGRGIATKLLTSLLE---SNTHVKWSLNCDINNEAALKLYKKVGFISDGQIELYK 174
Cdd:COG3393   17 EISGVYTHPEYRGRGLASALVAALARealARGARTPFLYVDADNPAARRLYERLGFRPVGEYATVL 82
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 107-164 7.92e-09

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: 51.36  E-value: 7.92e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616567803  107 KDDEYYIETIATFAAYRGRGIATKLLTSLLE---SNTHVKWSLNCDINNEAALKLYKKVGF 164
Cdd:pfam00583  56 EPPVGEIEGLAVAPEYRGKGIGTALLQALLEwarERGCERIFLEVAADNLAAIALYEKLGF 116
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 109-178 3.47e-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: 44.24  E-value: 3.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616567803  109 DEYYIETIATFAAYRGRGIATKLLTSL---LESNTHVKWSLNCDINNEAALKLYKKVGFisdGQIELYKHMYH 178
Cdd:TIGR01575  53 DEAHILNIAVKPEYQGQGIGRALLRELideAKGRGVNEIFLEVRVSNIAAQALYKKLGF---NEIAIRRNYYP 122
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 56-164 4.00e-06

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 43.21  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616567803   56 HVLVYEIENKVAGCIISYsgenelkyekaweqldlpeeikqygtplpvKEAKDDEYYIETIATFAAYRGRGIATKLLTSL 135
Cdd:pfam13508   4 RFFVAEDDGKIVGFAALL------------------------------PLDDEGALAELRLAVHPEYRGQGIGRALLEAA 53

                          90       100
                  ....*....|....*....|....*....
gi 616567803  136 LESNTHVKWSLNCDINNEAALKLYKKVGF 164
Cdd:pfam13508  54 EAAAKEGGIKLLELETTNRAAAFYEKLGF 82
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-171 5.34e-06

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 44.22  E-value: 5.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616567803   1 MIRQARPEDRFDIAKLVY-------MVWDDMELELvkhlpkDMVLDAIEKSCIDAtyrtfyQHVLVYEIENKVAGCIISY 73
Cdd:COG1247    3 TIRPATPEDAPAIAAIYNeaiaegtATFETEPPSE------EEREAWFAAILAPG------RPVLVAEEDGEVVGFASLG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616567803  74 SGENELKYEKAWEqldlpeeikqygtplpvkeakdDEYYIEtiatfAAYRGRGIATKLLTSLLEsntHVK----WSLNCD 149
Cdd:COG1247   71 PFRPRPAYRGTAE----------------------ESIYVD-----PDARGRGIGRALLEALIE---RARargyRRLVAV 120

                        170       180
                 ....*....|....*....|....
gi 616567803 150 I--NNEAALKLYKKVGFISDGQIE 171
Cdd:COG1247  121 VlaDNEASIALYEKLGFEEVGTLP 144
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 2-176 8.64e-05

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: 41.14  E-value: 8.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616567803   2 IRQARPEDRFDIAKLVYMvWDDMELELVKHLPKDMVLDAIEKSCIDATYRTFYQHVLVYEIENKVAGCIiSYSGenelkY 81
Cdd:COG1670   10 LRPLRPEDAEALAELLND-PEVARYLPGPPYSLEEARAWLERLLADWADGGALPFAIEDKEDGELIGVV-GLYD-----I 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616567803  82 EKAWEQLDLpeeikqyGtplpvkeakddeYYIetiatFAAYRGRGIATKLLTSLLE-SNTHVKWS---LNCDINNEAALK 157
Cdd:COG1670   83 DRANRSAEI-------G------------YWL-----APAYWGKGYATEALRALLDyAFEELGLHrveAEVDPDNTASIR 138

                        170
                 ....*....|....*....
gi 616567803 158 LYKKVGFISDGQIELYKHM 176
Cdd:COG1670  139 VLEKLGFRLEGTLRDALVI 157
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 108-164 2.08e-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: 2.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616567803 108 DDEYYIETIATFAAYRGRGIATKLLTSLLEsnthvkWS---------LNCDINNEAALKLYKKVGF 164
Cdd:COG0454   56 DKVLELKRLYVLPEYRGKGIGKALLEALLE------WArergctaleLDTLDGNPAAIRFYERLGF 115
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 57-137 1.20e-03

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: 35.71  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616567803  57 VLVYEIENKVAGCIISYsgenelkyekaweqldlpeeikqygtplpVKEAKDDEYYIETIATFAAYRGRGIATKLLTSLL 136
Cdd:cd04301    1 FLVAEDDGEIVGFASLS-----------------------------PDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAE 51


                 .
gi 616567803 137 E 137
Cdd:cd04301   52 E 52
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 113-165 1.60e-03

GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance proteins, whereas others are listed as being GNAT acetyltransferases. The family has similarities to the GNAT acetyltransferase family.


Pssm-ID: 403833  Cd Length: 239  Bit Score: 38.02  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 616567803  113 IEtIATFAAYRGRGIATKLLTSL----LESNTHVKWslncDINNEAALKLYKKVGFI 165
Cdd:pfam12746 180 IE-IDTHPDYRGKGLATICAAALilecLKRGLYPSW----DAHNEASVALAEKLGYE 231
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
108-172 4.52e-03

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 35.55  E-value: 4.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616567803 108 DDEYYIETIATFAAYRGRGIATKLLTSLLE---SNTHVKWSLNCDinnEAALKLYKKVGFISDGQIEL 172
Cdd:COG2153   56 DGEAKIGRVAVLPEYRGQGLGRALMEAAIEearERGARRIVLSAQ---AHAVGFYEKLGFVPVGEEFL 120
PTZ00330 PTZ00330
acetyltransferase; Provisional
 112-164 6.29e-03

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 35.59  E-value: 6.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 616567803 112 YIETIATFAAYRGRGIATKLLTSLLE---SNTHVKWSLNCdinNEAALKLYKKVGF 164
Cdd:PTZ00330  84 HIEDVVVDPSYRGQGLGRALISDLCEiarSSGCYKVILDC---TEDMVAFYKKLGF 136
 
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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