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Conserved domains on  [gi|1018192638|pdb|5ISV|B]
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Chain B, Ribosomal-protein-alanine acetyltransferase

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 5.39e-113

ribosomal-protein-alanine N-acetyltransferase; Provisional


:

Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 316.87  E-value: 5.39e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B         1 MNTISSLETTDLPAAYHIEQRAHAFPWSEKTFASNQGERYLNFQLTQNGKMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
5ISV_B        81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEATIRRNYYPTTDGREDAIIMALPI 146
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAIIMALPL 146
 
Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 1-146 5.39e-113

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 316.87  E-value: 5.39e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B         1 MNTISSLETTDLPAAYHIEQRAHAFPWSEKTFASNQGERYLNFQLTQNGKMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
5ISV_B        81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEATIRRNYYPTTDGREDAIIMALPI 146
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAIIMALPL 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 11-142 3.49e-67

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: 200.63  E-value: 3.49e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B         11 DLPAAYHIEQRAHAFPWSEKTFASNQGERYLNFQLT-QNGKMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLI 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLArIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
5ISV_B         90 DELEKRGVATLWLEVRASNAAAIALYESLGFNEATIRRNYYPttDGREDAIIM 142
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP--DPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 62-147 2.75e-29

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 103.20  E-value: 2.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B       62 DEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEATIRRNYYPttdgrEDAII 141
Cdd:COG0456  12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYG-----DDALV 86


                ....*.
5ISV_B      142 MALPIS 147
Cdd:COG0456  87 MEKELA 92
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 12-120 5.12e-21

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: 82.57  E-value: 5.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B         12 LPAAYHIEQRAHAFPWSEKT----FASNQGERYLNFQLTQNGK---MAAFAITQVVLDEATLFNIAVDPDYQRQGLGRAL 84
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPldllEDWDEDASEGFFVAEEDGElvgFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
5ISV_B         85 LEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-103 4.95e-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: 58.06  E-value: 4.95e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
5ISV_B       51 MAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLE 103
Cdd:cd04301  13 FASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
 1-146 5.39e-113

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 316.87  E-value: 5.39e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B         1 MNTISSLETTDLPAAYHIEQRAHAFPWSEKTFASNQGERYLNFQLTQNGKMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80
Cdd:PRK09491   1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
5ISV_B        81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEATIRRNYYPTTDGREDAIIMALPI 146
Cdd:PRK09491  81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTADGREDAIIMALPL 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 11-142 3.49e-67

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: 200.63  E-value: 3.49e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B         11 DLPAAYHIEQRAHAFPWSEKTFASNQGERYLNFQLT-QNGKMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLI 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLArIGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
5ISV_B         90 DELEKRGVATLWLEVRASNAAAIALYESLGFNEATIRRNYYPttDGREDAIIM 142
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP--DPGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 62-147 2.75e-29

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 103.20  E-value: 2.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B       62 DEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEATIRRNYYPttdgrEDAII 141
Cdd:COG0456  12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYG-----DDALV 86


                ....*.
5ISV_B      142 MALPIS 147
Cdd:COG0456  87 MEKELA 92
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
10-146 4.33e-23

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 89.28  E-value: 4.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B       10 TDLPA-----AYHIEQRAHAFPWSEKT-------FASNQGERYLNFQLTQNGKMAAFAI-----TQVVLDEATLFNIAVD 72
Cdd:COG1247  10 EDAPAiaaiyNEAIAEGTATFETEPPSeeereawFAAILAPGRPVLVAEEDGEVVGFASlgpfrPRPAYRGTAEESIYVD 89

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
5ISV_B       73 PDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEATIRRNYYPTTDGREDAIIMALPI 146
Cdd:COG1247  90 PDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVGFKFGRWLDLVLMQKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 12-120 5.12e-21

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: 82.57  E-value: 5.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B         12 LPAAYHIEQRAHAFPWSEKT----FASNQGERYLNFQLTQNGK---MAAFAITQVVLDEATLFNIAVDPDYQRQGLGRAL 84
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPldllEDWDEDASEGFFVAEEDGElvgFASLSIIDDEPPVGEIEGLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
5ISV_B         85 LEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 48-122 4.48e-18

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 75.48  E-value: 4.48e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
5ISV_B       48 NGKMAAFAITQVvLDEATLF--NIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNE 122
Cdd:COG0454  42 KGEPIGFAGLRR-LDDKVLElkRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKE 117
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-146 1.52e-17

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 74.35  E-value: 1.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B        4 ISSLETTDLPAAYHIEQRAHAFPWSEKTFAS--NQGERYLNFQLTQNGKMAAFAITQVV-----LDEATLFNIAVDPDYQ 76
Cdd:COG3153   1 IRPATPEDAEAIAALLRAAFGPGREAELVDRlrEDPAAGLSLVAEDDGEIVGHVALSPVdidgeGPALLLGPLAVDPEYR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B       77 RQGLGRALLEHLIDELEKRGVATLWLEvraSNAAAIALYESLGFNEATIRRNYYPttdgrEDAIIMALPI 146
Cdd:COG3153  81 GQGIGRALMRAALEAARERGARAVVLL---GDPSLLPFYERFGFRPAGELGLTLG-----PDEVFLAKEL 142
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 47-147 3.52e-17

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: 73.10  E-value: 3.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B       47 QNGKMAAF-AITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEvraSNAAAIALYESLGFNEATI 125
Cdd:COG1246  35 EDGEIVGCaALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLL---TTSAAIHFYEKLGFEEIDK 111

                        90       100
                ....*....|....*....|..
5ISV_B      126 RRNYYPTTDGReDAIIMALPIS 147
Cdd:COG1246 112 EDLPYAKVWQR-DSVVMEKDLE 132
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
64-120 4.73e-17

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 71.48  E-value: 4.73e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
5ISV_B       64 ATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
Cdd:COG3393  16 AEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGF 72
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 3-144 4.22e-16

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: 71.18  E-value: 4.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B        3 TISSLETTDLPAAYHIEQRAHAFPWSEKTFAS-NQGERYLNFQLT--QNGKMAAFAITQVVLDE----ATLFNI------ 69
Cdd:COG1670   9 RLRPLRPEDAEALAELLNDPEVARYLPGPPYSlEEARAWLERLLAdwADGGALPFAIEDKEDGEligvVGLYDIdranrs 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B       70 -----AVDPDYQRQGLGRALLEHLIDEL-EKRGVATLWLEVRASNAAAIALYESLGFNEATIRRNYYPTTDGREDAIIMA 143
Cdd:COG1670  89 aeigyWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVLYS 168


                .
5ISV_B      144 L 144
Cdd:COG1670 169 L 169
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 47-122 2.50e-15

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 67.09  E-value: 2.50e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5ISV_B         47 QNGKMAAFAITQVVLDEATLF--NIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRasnAAAIALYESLGFNE 122
Cdd:pfam13508  10 DDGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETT---NRAAAFYEKLGFEE 84
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
45-120 1.90e-14

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 65.98  E-value: 1.90e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
5ISV_B       45 LTQNGKMAAFA-ITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASnaaAIALYESLGF 120
Cdd:COG2153  39 AYDDGELVATArLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGF 112
PRK03624 PRK03624
putative acetyltransferase; Provisional
 66-122 2.76e-14

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 65.72  E-value: 2.76e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
5ISV_B        66 LFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNE 122
Cdd:PRK03624  71 AYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEE 127
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 36-120 3.17e-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: 62.67  E-value: 3.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B         36 QGERYLNFQLTQNGKMAAFAitqVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNaAAIALY 115
Cdd:pfam13673  27 DQGEYFFFVAFEGGQIVGVI---ALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASP-YAVPFY 102


                  ....*
5ISV_B        116 ESLGF 120
Cdd:pfam13673 103 EKLGF 107
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 51-103 4.95e-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: 58.06  E-value: 4.95e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
5ISV_B       51 MAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLE 103
Cdd:cd04301  13 FASLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
mycothiol_MshD TIGR03448
mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the ...
 46-120 1.17e-09

mycothiol synthase; Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 132489 [Multi-domain]  Cd Length: 292  Bit Score: 55.49  E-value: 1.17e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5ISV_B         46 TQNGKMAAFAITQVVLDEATL---FNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGF 120
Cdd:TIGR03448 206 DAPGELLGFHWTKVHPDEPALgevYVVGVDPAAQGRGLGDALTLIGLHHLAARGLPAVMLYVEADNEAAVRTYEKLGF 283
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 40-127 4.21e-09

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: 50.79  E-value: 4.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B         40 YLNFQLTQNGKMAAFAITqvvLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVaTLWLEVRASNAAAIALYESLG 119
Cdd:pfam08445   1 VLGIYRGDTGELAAWCLR---LPGGELGALQTLPEHRRRGLGSRLVAALARGIAERGI-TPFAVVVAGNTPSRRLYEKLG 76


                  ....*...
5ISV_B        120 FNEATIRR 127
Cdd:pfam08445  77 FRKIDETY 84
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
 9-120 3.94e-07

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: 48.04  E-value: 3.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B          9 TTDLPAAYHIE-------QRAHAFPWSeKTFASNQG--ERYLN----FQLTQNGKMAAFAITQVVLDEATLFNIAVDPDY 75
Cdd:pfam12746 110 VASLPQGYTLKkideelyEACLEEEWS-RDFVSQFSsyEDFLKnglgFVILKDGEIVSGASSYSVYEGGIEIEIDTHPDY 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
5ISV_B         76 QRQGLGRALLEHLIDELEKRGVATLWlevRASNAAAIALYESLGF 120
Cdd:pfam12746 189 RGKGLATICAAALILECLKRGLYPSW---DAHNEASVALAEKLGY 230
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
 69-158 4.09e-07

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: 48.67  E-value: 4.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B       69 IAVDPDYQRQGLGRALLEHLIDELEKRGVAtlWLEVrasnaaaialyeSLGFNEATIR---RN-YYP----TTdgREDA- 139
Cdd:COG1444 491 IAVHPALQRRGLGSRLLAEIREEAKEEGLD--WLGV------------SFGATPELLRfwqRNgFVPvhlgTT--RNASs 554

                        90       100
                ....*....|....*....|...
5ISV_B      140 ----IIMALPISMAGENLYFQSA 158
Cdd:COG1444 555 geysAMVLKPLSEAGEALVDRAA 577
Eis COG4552
Predicted acetyltransferase [General function prediction only];
69-129 6.72e-07

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 47.59  E-value: 6.72e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
5ISV_B       69 IAVDPDYQRQGLGRALLEHLIDELEKRG--VATLWlevrasnAAAIALYESLGFNEATIRRNY 129
Cdd:COG4552  78 VAVAPEHRRRGVARALLREALAELRERGqpLSALY-------PFEPGFYRRFGYELAGDRRRY 133
PRK07757 PRK07757
N-acetyltransferase;
70-131 1.31e-06

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 45.57  E-value: 1.31e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
5ISV_B        70 AVDPDYQRQGLGRALLEHLIDELEKRGVA---TLWLEVRasnaaaiaLYESLGFNEatIRRNYYP 131
Cdd:PRK07757  72 AVSEDYRGQGIGRMLVEACLEEARELGVKrvfALTYQPE--------FFEKLGFRE--VDKEALP 126
PRK10514 PRK10514
putative acetyltransferase; Provisional
 18-121 3.52e-06

putative acetyltransferase; Provisional


Pssm-ID: 182510 [Multi-domain]  Cd Length: 145  Bit Score: 44.22  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B        18 IEQRAHAF-PWSEKTFASNQGERYLNFQLTQNGKMAAfaitqvvldeatLFniaVDPDYQRQGLGRALLEH---LIDELE 93
Cdd:PRK10514  38 IEELVRSFlPEAPLWVAVDERDQPVGFMLLSGGHMEA------------LF---VDPDVRGCGVGRMLVEHalsLHPELT 102

                         90       100
                 ....*....|....*....|....*...
5ISV_B        94 krgvatlwLEVRASNAAAIALYESLGFN 121
Cdd:PRK10514 103 --------TDVNEQNEQAVGFYKKMGFK 122
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 69-122 9.17e-06

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: 44.18  E-value: 9.17e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
5ISV_B       69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAaaiALYESLGFNE 122
Cdd:cd02169  31 VAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTKPKNA---KFFRGLGFKE 81
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 69-120 1.45e-05

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


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 42.17  E-value: 1.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
5ISV_B         69 IAVDPDYQRQGLGRALLEHLIDELEKRGV--ATLWlevrasnAAAIALYESLGF 120
Cdd:pfam13527  76 VATYPEYRGRGVMSRLLRRSLEEMRERGVplSFLY-------PSSYPIYRRFGY 122
PTZ00330 PTZ00330
acetyltransferase; Provisional
 4-120 3.06e-05

acetyltransferase; Provisional


Pssm-ID: 140351 [Multi-domain]  Cd Length: 147  Bit Score: 41.75  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B         4 ISSLETTDLPAayHIEQRAH---AFPWSEKTFASNQGERYLNFQLTqngKMAAFAITQVVLDEATLF------------- 67
Cdd:PTZ00330   9 LRDLEEGDLGS--VLELLSHltsAPALSQEELEQIAARRRLAGVVT---RVFVHSPTQRIVGTASLFvepkftrggkcvg 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
5ISV_B        68 ---NIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEvraSNAAAIALYESLGF 120
Cdd:PTZ00330  84 hieDVVVDPSYRGQGLGRALISDLCEIARSSGCYKVILD---CTEDMVAFYKKLGF 136
PRK10562 PRK10562
putative acetyltransferase; Provisional
 47-120 9.51e-05

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 40.44  E-value: 9.51e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
5ISV_B        47 QNGKMAAFAitqVVLDEATLFNIAVDPDYQRQGLGRALLEHLideleKRGVATLWLEVRASNAAAIALYESLGF 120
Cdd:PRK10562  55 EDGKLLGFV---SVLEGRFVGALFVAPKAVRRGIGKALMQHV-----QQRYPHLSLEVYQKNQRAVNFYHAQGF 120
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
44-124 9.65e-05

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 40.68  E-value: 9.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B        44 QLTQNGKMAAFaITQVVLD--EATLFNIAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFN 121
Cdd:PRK10975 106 LRDASGQIQGF-VTLRELNdtDARIGLLAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGAN 184


                 ....
5ISV_B       122 -EAT 124
Cdd:PRK10975 185 iEST 188
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
43-96 1.32e-04

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 38.98  E-value: 1.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
5ISV_B       43 FQLTQNGKMAAFAITQVVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRG 96
Cdd:COG2388  12 FELEVDGELAGELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERG 65
Acetyltransf_4 pfam13420
Acetyltransferase (GNAT) domain;
67-130 4.23e-04

Acetyltransferase (GNAT) domain;


Pssm-ID: 433192 [Multi-domain]  Cd Length: 153  Bit Score: 38.50  E-value: 4.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
5ISV_B         67 FNIAVDPDyqrQGLGRALLEHLIDELEKR-GVATLWLEVRASNAAAIALYESLGFNEATIRRNYY 130
Cdd:pfam13420  81 FYVVKNND---EGINRELINAIIQYARKNqNIENLEACIASNNINAIVFLKAIGFEWLGIERNAI 142
PRK10140 PRK10140
N-acetyltransferase;
67-143 9.62e-04

N-acetyltransferase;


Pssm-ID: 182263 [Multi-domain]  Cd Length: 162  Bit Score: 37.65  E-value: 9.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5ISV_B        67 FNIAVDPDYQRQGLGRALLEHLIDELEK-RGVATLWLEVRASNAAAIALYESLGFN-EATIRRnyYPTTDGRE-DAIIMA 143
Cdd:PRK10140  82 FGICVDSRWKNRGVASALMREMIEMCDNwLRVDRIELTVFVDNAPAIKVYKKYGFEiEGTGKK--YALRNGEYvDAYYMA 159
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 69-120 1.45e-03

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


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 36.94  E-value: 1.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
5ISV_B         69 IAVDPDYQRQGLG----RALLEHLIDELekrGVATLWLEVRASNAAAIALYESLGF 120
Cdd:pfam13302  86 YWLGPDYWGKGYAteavRALLEYAFEEL---GLPRLVARIDPENTASRRVLEKLGF 138
PRK05279 PRK05279
N-acetylglutamate synthase; Validated
 70-100 1.91e-03

N-acetylglutamate synthase; Validated


Pssm-ID: 235386 [Multi-domain]  Cd Length: 441  Bit Score: 37.44  E-value: 1.91e-03
                         10        20        30
                 ....*....|....*....|....*....|.
5ISV_B        70 AVDPDYQRQGLGRALLEHLIDELEKRGVATL 100
Cdd:PRK05279 366 AVHPDYRGSGRGERLLKRIEQRARQLGLKRL 396
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
 75-129 3.50e-03

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this family are members of the pfam00583 (GNAT) superfamily of acetyltransferases and are proposed to perform a N-acetylation step in the process of pseudaminic acid biosynthesis in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci. Significantly, many genomes containing other components of this pathway lack this gene, indicating that some other N-acetyl transferases may be incolved and/or the step is optional, resulting in a non-acetylated pseudaminic acid variant sugar.


Pssm-ID: 274661 [Multi-domain]  Cd Length: 152  Bit Score: 36.18  E-value: 3.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
5ISV_B         75 YQRQGLGRALLEHLID-ELEKRGVATLWLEVRASNAAAIALYESLGFNEATIRRNY 129
Cdd:TIGR03585  87 FCKPGVGSVLEEAALEyAFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQG 142
PRK01346 PRK01346
enhanced intracellular survival protein Eis;
59-129 4.83e-03

enhanced intracellular survival protein Eis;


Pssm-ID: 234945 [Multi-domain]  Cd Length: 411  Bit Score: 36.45  E-value: 4.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
5ISV_B        59 VVLDEATLFNIAVDPDYQRQGLGRALLEHLIDELEKRG--VATLWlevrASNAaaiALYESLGFNEATIRRNY 129
Cdd:PRK01346  75 AVLPAAGVTAVTVAPTHRRRGLLTALMREQLRRIRERGepVAALT----ASEG---GIYGRFGYGPATYSQSL 140
 
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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