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Conserved domains on  [gi|490362310|ref|WP_004242073|]
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ribosomal protein S18-alanine N-acetyltransferase [Morganella morganii]

Protein Classification

ribosomal-protein-alanine N-acetyltransferase( domain architecture ID 10013255)

ribosomal-protein-alanine N-acetyltransferase acetylates the N-terminal alanine of ribosomal protein S18; similar to Escherichia coli K-12 RimI

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 1-146 1.73e-98

ribosomal-protein-alanine N-acetyltransferase; Provisional


:

Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 279.51  E-value: 1.73e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   1 MIRLSPLLPADFAAAFRIEQAAHAYPWSEATFRSNHGERYHNLKLEADGELAGFAINQTVLDEATLFNIAVSPEHQGKGY 80
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490362310  81 GRQLLEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGFNEVTVRKNYYPAAQGKEDAVIMALYL 146
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAIIMALPL 146
 
Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 1-146 1.73e-98

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 279.51  E-value: 1.73e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   1 MIRLSPLLPADFAAAFRIEQAAHAYPWSEATFRSNHGERYHNLKLEADGELAGFAINQTVLDEATLFNIAVSPEHQGKGY 80
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490362310  81 GRQLLEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGFNEVTVRKNYYPAAQGKEDAVIMALYL 146
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAIIMALPL 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 11-142 8.98e-54

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: 165.96  E-value: 8.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   11 DFAAAFRIEQAAHAYPWSEATFRSNHGERYHNLKL-EADGELAGFAINQTVLDEATLFNIAVSPEHQGKGYGRQLLEKVI 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLaRIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490362310   90 EDLTAKGIATLWLEVRASNSPAIALYESLGFNEVTVRKNYYPAaqGKEDAVIM 142
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPD--PGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 53-147 6.98e-27

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 96.26  E-value: 6.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310  53 GFAINQTVL--DEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGFNEVTVRKNYY 130
Cdd:COG0456    1 GFALLGLVDggDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....*..
gi 490362310 131 PaaqgkEDAVIMALYLS 147
Cdd:COG0456   81 G-----DDALVMEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 12-120 1.32e-20

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: 81.02  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   12 FAAAFRIEQAAHAYPWSEATFR----SNHGERYHNLKLEADGELAGFA---INQTVLDEATLFNIAVSPEHQGKGYGRQL 84
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDlledWDEDASEGFFVAEEDGELVGFAslsIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 490362310   85 LEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGF 120
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 45-103 1.66e-12

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: 58.83  E-value: 1.66e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490362310  45 LEADGELAGFA---INQTVLDEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLE 103
Cdd:cd04301    4 AEDDGEIVGFAslsPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 1-146 1.73e-98

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 279.51  E-value: 1.73e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   1 MIRLSPLLPADFAAAFRIEQAAHAYPWSEATFRSNHGERYHNLKLEADGELAGFAINQTVLDEATLFNIAVSPEHQGKGY 80
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490362310  81 GRQLLEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGFNEVTVRKNYYPAAQGKEDAVIMALYL 146
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAIIMALPL 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 11-142 8.98e-54

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: 165.96  E-value: 8.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   11 DFAAAFRIEQAAHAYPWSEATFRSNHGERYHNLKL-EADGELAGFAINQTVLDEATLFNIAVSPEHQGKGYGRQLLEKVI 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLaRIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490362310   90 EDLTAKGIATLWLEVRASNSPAIALYESLGFNEVTVRKNYYPAaqGKEDAVIM 142
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPD--PGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 53-147 6.98e-27

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 96.26  E-value: 6.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310  53 GFAINQTVL--DEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGFNEVTVRKNYY 130
Cdd:COG0456    1 GFALLGLVDggDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYY 80

                         90
                 ....*....|....*..
gi 490362310 131 PaaqgkEDAVIMALYLS 147
Cdd:COG0456   81 G-----DDALVMEKELA 92
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
1-146 1.04e-22

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 87.74  E-value: 1.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   1 MIRlsPLLPADFAAAFRI------------EQAAHAYPWSEATFRSNHGERYHNLKLEADGELAGFAI-----NQTVLDE 63
Cdd:COG1247    3 TIR--PATPEDAPAIAAIyneaiaegtatfETEPPSEEEREAWFAAILAPGRPVLVAEEDGEVVGFASlgpfrPRPAYRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310  64 ATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGFNEVTVRKNYYPAAQGKEDAVIMA 143
Cdd:COG1247   81 TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQ 160


                 ...
gi 490362310 144 LYL 146
Cdd:COG1247  161 KRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 12-120 1.32e-20

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: 81.02  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   12 FAAAFRIEQAAHAYPWSEATFR----SNHGERYHNLKLEADGELAGFA---INQTVLDEATLFNIAVSPEHQGKGYGRQL 84
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDlledWDEDASEGFFVAEEDGELVGFAslsIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 490362310   85 LEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGF 120
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 45-129 2.52e-18

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 75.86  E-value: 2.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310  45 LEADGELAGFA-INQTVLDEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGFNEV 123
Cdd:COG0454   39 VDDKGEPIGFAgLRRLDDKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEI 118


                 ....*.
gi 490362310 124 TVRKNY 129
Cdd:COG0454  119 ERYVAY 124
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 46-147 5.38e-18

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: 74.64  E-value: 5.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310  46 EADGELAGF-AINQTVLDEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEvraSNSPAIALYESLGFNEVT 124
Cdd:COG1246   34 EEDGEIVGCaALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL---TTSAAIHFYEKLGFEEID 110

                         90       100
                 ....*....|....*....|...
gi 490362310 125 VRKNYYPaAQGKEDAVIMALYLS 147
Cdd:COG1246  111 KEDLPYA-KVWQRDSVVMEKDLE 132
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
2-120 2.10e-16

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 70.88  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   2 IRlsPLLPADFAAAFRIEQAAHAYPWSEATFRS--NHGERYHNLKLEADGELAGFAINQTV-----LDEATLFNIAVSPE 74
Cdd:COG3153    1 IR--PATPEDAEAIAALLRAAFGPGREAELVDRlrEDPAAGLSLVAEDDGEIVGHVALSPVdidgeGPALLLGPLAVDPE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 490362310  75 HQGKGYGRQLLEKVIEDLTAKGIATLWLEvraSNSPAIALYESLGF 120
Cdd:COG3153   79 YRGQGIGRALMRAALEAARERGARAVVLL---GDPSLLPFYERFGF 121
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 45-122 1.63e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 67.09  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   45 LEADGELAGFAINQTVLDEATLF--NIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEVRasnSPAIALYESLGFNE 122
Cdd:pfam13508   8 AEDDGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETT---NRAAAFYEKLGFEE 84
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 1-144 1.87e-15

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: 69.26  E-value: 1.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   1 MIRLSPLLPADFAAAFRIEQAAHAYPW----------SEATFRSNHGERYHN------LKLEADGELAGFA--INQTVLD 62
Cdd:COG1670    7 RLRLRPLRPEDAEALAELLNDPEVARYlpgppysleeARAWLERLLADWADGgalpfaIEDKEDGELIGVVglYDIDRAN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310  63 EATLFNIAVSPEHQGKGYGRQLLEKVIEDL-TAKGIATLWLEVRASNSPAIALYESLGFNEVTVRKNYYPAAQGKEDAVI 141
Cdd:COG1670   87 RSAEIGYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVL 166


                 ...
gi 490362310 142 MAL 144
Cdd:COG1670  167 YSL 169
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
50-123 2.28e-15

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 66.86  E-value: 2.28e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490362310  50 ELAGFA-INQTVLDEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGFNEV 123
Cdd:COG3393    1 ELVAMAgVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPV 75
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
45-123 4.18e-14

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 64.82  E-value: 4.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310  45 LEADGELAGFA-INQTVLDEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEVRASnspAIALYESLGFNEV 123
Cdd:COG2153   39 AYDDGELVATArLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFVPV 115
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 38-120 3.32e-13

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: 62.29  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   38 ERYHNLKLEADGELAGFAinqTVLDEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEVRASNsPAIALYES 117
Cdd:pfam13673  29 GEYFFFVAFEGGQIVGVI---ALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASP-YAVPFYEK 104


                  ...
gi 490362310  118 LGF 120
Cdd:pfam13673 105 LGF 107
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 45-103 1.66e-12

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: 58.83  E-value: 1.66e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490362310  45 LEADGELAGFA---INQTVLDEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLE 103
Cdd:cd04301    4 AEDDGEIVGFAslsPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 49-126 1.14e-11

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: 57.34  E-value: 1.14e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490362310   49 GELAGFAINqtvLDEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIaTLWLEVRASNSPAIALYESLGFNEVTVR 126
Cdd:pfam08445  10 GELAAWCLR---LPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGI-TPFAVVVAGNTPSRRLYEKLGFRKIDET 83
PRK03624 PRK03624
putative acetyltransferase; Provisional
 66-125 4.06e-10

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 54.55  E-value: 4.06e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310  66 LFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGFNEVTV 125
Cdd:PRK03624  71 AYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQDR 130
PRK07757 PRK07757
N-acetyltransferase;
33-131 5.14e-07

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 46.34  E-value: 5.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310  33 RSnHGERYHNLK----LEADGELAGF-AINQTVLDEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIA---TLWLEV 104
Cdd:PRK07757  31 RS-LDELYENIRdfyvAEEEGEIVGCcALHILWEDLAEIRSLAVSEDYRGQGIGRMLVEACLEEARELGVKrvfALTYQP 109

                         90       100
                 ....*....|....*....|....*..
gi 490362310 105 RasnspaiaLYESLGFNEVTvrKNYYP 131
Cdd:PRK07757 110 E--------FFEKLGFREVD--KEALP 126
PRK10562 PRK10562
putative acetyltransferase; Provisional
 1-120 5.73e-07

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 46.21  E-value: 5.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   1 MIRlsPLLPADFAA--AFRIEQAAHAYP------W--SEATFRSNHGERYHNLKLEADGELAGFAinqTVLDEATLFNIA 70
Cdd:PRK10562   1 MIR--EYQPSDLPAilQLWLESTIWAHPfikeqyWreSAPLVRDVYLPAAQTWVWEEDGKLLGFV---SVLEGRFVGALF 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490362310  71 VSPEHQGKGYGRQLLEKVIEDLTAkgiatLWLEVRASNSPAIALYESLGF 120
Cdd:PRK10562  76 VAPKAVRRGIGKALMQHVQQRYPH-----LSLEVYQKNQRAVNFYHAQGF 120
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 69-129 1.86e-05

Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.


Pssm-ID: 173920 [Multi-domain]  Cd Length: 297  Bit Score: 43.02  E-value: 1.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490362310  69 IAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEVRASNSpaiALYESLGFNEVTVRKNY 129
Cdd:cd02169   31 VAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTKPKNA---KFFRGLGFKELANASDE 88
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
39-96 2.65e-05

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 40.52  E-value: 2.65e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490362310  39 RYHnlkLEADGELAGFAinqTVLDEATLFNI---AVSPEHQGKGYGRQLLEKVIEDLTAKG 96
Cdd:COG2388   11 RFE---LEVDGELAGEL---TYRLEGGVIIIthtEVPPALRGQGIASALVEAALDDARERG 65
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 12-120 4.87e-05

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 40.63  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   12 FAAAFRIEQAAHAYPWSEATFRSNHgeryhNLKLEADGELAG--------FAINQTVLDEATLFNIAVSPEHQGKGYGRQ 83
Cdd:pfam13527  16 LEYAFQDEDSPELREYFRPLLEEGR-----VLGAFDDGELVStlalypfeLNVPGKTLPAAGITGVATYPEYRGRGVMSR 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 490362310   84 LLEKVIEDLTAKG--IATLWlevrasnsPA-IALYESLGF 120
Cdd:pfam13527  91 LLRRSLEEMRERGvpLSFLY--------PSsYPIYRRFGY 122
Eis COG4552
Predicted acetyltransferase [General function prediction only];
2-120 6.06e-05

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 41.81  E-value: 6.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   2 IRLSPLLPADFAAAFRIEQAAHAYPWS----EATFRSNHGERYhnLKLEADGELAG-FAINQTvldEATLFN-------- 68
Cdd:COG4552    1 MEIRPLTEDDLDAFARLLAYAFGPEPDdeelEAYRPLLEPGRV--LGVFDDGELVGtLALYPF---TLNVGGarvpmagi 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490362310  69 --IAVSPEHQGKGYGRQLLEKVIEDLTAKG--IATLWlevrASnspAIALYESLGF 120
Cdd:COG4552   76 tgVAVAPEHRRRGVARALLREALAELRERGqpLSALY----PF---EPGFYRRFGY 124
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
47-121 1.00e-04

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 40.68  E-value: 1.00e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490362310  47 ADGELAGF----AINQTvldEATLFNIAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWLEVRASNSPAIALYESLGFN 121
Cdd:PRK10975 109 ASGQIQGFvtlrELNDT---DARIGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGAN 184
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 2-120 5.07e-04

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 38.10  E-value: 5.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310    2 IRLSPLLPADFAAAFRI----EQAAHAYPWS----------EATFRSNHGERYHNLKL-EADGELAGFAINQTVLDEATL 66
Cdd:pfam13302   2 LLLRPLTEEDAEALFELlsdpEVMRYGVPWPltleearewlARIWAADEAERGYGWAIeLKDTGFIGSIGLYDIDGEPER 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490362310   67 FNIA--VSPEHQGKGYG----RQLLEKVIEDLtakGIATLWLEVRASNSPAIALYESLGF 120
Cdd:pfam13302  82 AELGywLGPDYWGKGYAteavRALLEYAFEEL---GLPRLVARIDPENTASRRVLEKLGF 138
PRK15130 PRK15130
spermidine N1-acetyltransferase; Provisional
 67-120 6.22e-04

spermidine N1-acetyltransferase; Provisional


Pssm-ID: 237916  Cd Length: 186  Bit Score: 38.24  E-value: 6.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490362310  67 FNIAVSPEHQGKGYGRQLLEKVIE-DLTAKGIATLWLEVRASNSPAIALYESLGF 120
Cdd:PRK15130  86 FQIIISPEYQGKGLATRAAKLAMDyGFTVLNLYKLYLIVDKENEKAIHIYRKLGF 140
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 69-97 1.24e-03

tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA(Met) C34 N-acetyltransferase TmcA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441053 [Multi-domain]  Cd Length: 703  Bit Score: 37.89  E-value: 1.24e-03
                         10        20
                 ....*....|....*....|....*....
gi 490362310  69 IAVSPEHQGKGYGRQLLEKVIEDLTAKGI 97
Cdd:COG1444  491 IAVHPALQRRGLGSRLLAEIREEAKEEGL 519
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 69-120 6.15e-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: 35.71  E-value: 6.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 490362310   69 IAVSPEHQGKGYGRQLLEKVIEDLTAKGIATLWlevRASNSPAIALYESLGF 120
Cdd:pfam12746 182 IDTHPDYRGKGLATICAAALILECLKRGLYPSW---DAHNEASVALAEKLGY 230
 
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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