NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1011939042|ref|WP_062747329|]
View 

ribosomal protein S18-alanine N-acetyltransferase [Erwinia persicina]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
1-147 1.98e-104

ribosomal-protein-alanine N-acetyltransferase; Provisional


:

Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 294.14  E-value: 1.98e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042   1 MNQISLLTAHDLEQAYAIEQRSHAFPWTEKTFTSNQGERYLNYRLTVDETLAAFAITQVVLDEATLFNLAVDPAFQRRGL 80
Cdd:PRK09491    1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011939042  81 GRELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDFNEVSIRRNYYPAADgGKEDAIMMALTI 147
Cdd:PRK09491   81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTAD-GREDAIIMALPL 146
 
Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
1-147 1.98e-104

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 294.14  E-value: 1.98e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042   1 MNQISLLTAHDLEQAYAIEQRSHAFPWTEKTFTSNQGERYLNYRLTVDETLAAFAITQVVLDEATLFNLAVDPAFQRRGL 80
Cdd:PRK09491    1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011939042  81 GRELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDFNEVSIRRNYYPAADgGKEDAIMMALTI 147
Cdd:PRK09491   81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTAD-GREDAIIMALPL 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
11-143 6.96e-56

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: 170.97  E-value: 6.96e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042  11 DLEQAYAIEQRSHAFPWTEKTFTSNQGERYLNYRLTV-DETLAAFAITQVVLDEATLFNLAVDPAFQRRGLGRELLQHLI 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARiGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1011939042  90 SELEQRGIVTLWLEVRASNHAAIALYEQLDFNEVSIRRNYYPAadgGKEDAIMM 143
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPD---PGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
62-147 1.47e-24

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 90.49  E-value: 1.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042  62 DEATLFNLAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDFNEVSIRRNYYPaadggkEDAI 141
Cdd:COG0456    12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYG------DDAL 85

                  ....*.
gi 1011939042 142 MMALTI 147
Cdd:COG0456    86 VMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
6-120 2.34e-18

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: 75.25  E-value: 2.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042   6 LLTAHDLEQAYAIEQRSHAFPWTEKTFTSNQGERYLNYRLtvDETLAAFA---ITQVVLDEATLFNLAVDPAFQRRGLGR 82
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEE--DGELVGFAslsIIDDEPPVGEIEGLAVAPEYRGKGIGT 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1011939042  83 ELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDF 120
Cdd:pfam00583  79 ALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
45-103 6.89e-10

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: 51.89  E-value: 6.89e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011939042  45 LTVDETLAAFA---ITQVVLDEATLFNLAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLE 103
Cdd:cd04301     4 AEDDGEIVGFAslsPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
 
Name Accession Description Interval E-value
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
1-147 1.98e-104

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 294.14  E-value: 1.98e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042   1 MNQISLLTAHDLEQAYAIEQRSHAFPWTEKTFTSNQGERYLNYRLTVDETLAAFAITQVVLDEATLFNLAVDPAFQRRGL 80
Cdd:PRK09491    1 MNTISSLTPADLPAAYHIEQRAHAFPWSEKTFASNQGERYLNLKLTVNGQMAAFAITQVVLDEATLFNIAVDPDYQRQGL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011939042  81 GRELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDFNEVSIRRNYYPAADgGKEDAIMMALTI 147
Cdd:PRK09491   81 GRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFNEVTIRRNYYPTAD-GREDAIIMALPL 146
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
11-143 6.96e-56

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: 170.97  E-value: 6.96e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042  11 DLEQAYAIEQRSHAFPWTEKTFTSNQGERYLNYRLTV-DETLAAFAITQVVLDEATLFNLAVDPAFQRRGLGRELLQHLI 89
Cdd:TIGR01575   1 DLKAVLEIEAAAFAFPWTEAQFAEELANYHLCYLLARiGGKVVGYAGVQIVLDEAHILNIAVKPEYQGQGIGRALLRELI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1011939042  90 SELEQRGIVTLWLEVRASNHAAIALYEQLDFNEVSIRRNYYPAadgGKEDAIMM 143
Cdd:TIGR01575  81 DEAKGRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYPD---PGEDAIVM 131
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
62-147 1.47e-24

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


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 90.49  E-value: 1.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042  62 DEATLFNLAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDFNEVSIRRNYYPaadggkEDAI 141
Cdd:COG0456    12 DEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGERPNYYG------DDAL 85

                  ....*.
gi 1011939042 142 MMALTI 147
Cdd:COG0456    86 VMEKEL 91
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
6-120 2.34e-18

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: 75.25  E-value: 2.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042   6 LLTAHDLEQAYAIEQRSHAFPWTEKTFTSNQGERYLNYRLtvDETLAAFA---ITQVVLDEATLFNLAVDPAFQRRGLGR 82
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEE--DGELVGFAslsIIDDEPPVGEIEGLAVAPEYRGKGIGT 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1011939042  83 ELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDF 120
Cdd:pfam00583  79 ALLQALLEWARERGCERIFLEVAADNLAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
69-147 2.48e-17

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


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 73.88  E-value: 2.48e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011939042  69 LAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDFNEVSIRRNYYpAADGGKEDAIMMALTI 147
Cdd:COG1247    86 IYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEASIALYEKLGFEEVGTLPEVG-FKFGRWLDLVLMQKRL 163
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
10-147 7.67e-15

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: 66.55  E-value: 7.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042  10 HDLEQAYAIEQRSHAFpwtektftsnqgerylnYRLTVDETLAAF-AITQVVLDEATLFNLAVDPAFQRRGLGRELLQHL 88
Cdd:COG1246    15 LELIRPYALEEEIGEF-----------------WVAEEDGEIVGCaALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEAL 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1011939042  89 ISELEQRGIVTLWLEvraSNHAAIALYEQLDFNEVSirRNYYPAADGGKEDAIMMALTI 147
Cdd:COG1246    78 LAEARELGLKRLFLL---TTSAAIHFYEKLGFEEID--KEDLPYAKVWQRDSVVMEKDL 131
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
47-129 5.54e-14

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


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 64.30  E-value: 5.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042  47 VDETLAAFAITQVvLDEATLF--NLAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDFNEVS 124
Cdd:COG0454    41 DKGEPIGFAGLRR-LDDKVLElkRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAIRFYERLGFKEIE 119

                  ....*
gi 1011939042 125 IRRNY 129
Cdd:COG0454   120 RYVAY 124
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
51-123 2.29e-13

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


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 61.46  E-value: 2.29e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011939042  51 LAAFAITQVVLDE-ATLFNLAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDFNEV 123
Cdd:COG3393     2 LVAMAGVRAESPGvAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPV 75
PRK03624 PRK03624
putative acetyltransferase; Provisional
66-123 5.33e-13

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 61.87  E-value: 5.33e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1011939042  66 LFNLAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDFNEV 123
Cdd:PRK03624   71 AYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVREDNDAVLGFYEALGYEEQ 128
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
7-146 2.54e-12

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: 60.78  E-value: 2.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042   7 LTAHDLEQAYAIEQRSHAF-PWTEKTFTSNQGERYLNYRLT--VDETLAAFAITQVVLDE----ATLFNL---------- 69
Cdd:COG1670    13 LRPEDAEALAELLNDPEVArYLPGPPYSLEEARAWLERLLAdwADGGALPFAIEDKEDGEligvVGLYDIdranrsaeig 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011939042  70 -AVDPAFQRRGLGRELLQHLISEL-EQRGIVTLWLEVRASNHAAIALYEQLDFNEVSIRRNYYPaADGGKEDAIMMALT 146
Cdd:COG1670    93 yWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV-IDGRYRDHVLYSLL 170
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
4-124 8.75e-12

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


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 58.94  E-value: 8.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042   4 ISLLTAHDLEQAYAIEQRSHAFPWTEKTFTS--NQGERYLNYRLTVDETLAAFAITQVV-----LDEATLFNLAVDPAFQ 76
Cdd:COG3153     1 IRPATPEDAEAIAALLRAAFGPGREAELVDRlrEDPAAGLSLVAEDDGEIVGHVALSPVdidgeGPALLLGPLAVDPEYR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1011939042  77 RRGLGRELLQHLISELEQRGIVTLWLEvraSNHAAIALYEQLDFNEVS 124
Cdd:COG3153    81 GQGIGRALMRAALEAARERGARAVVLL---GDPSLLPFYERFGFRPAG 125
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
45-124 1.57e-11

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


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 57.89  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042  45 LTVDETLAAFA-ITQVVLDEATLFNLAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLEVRASnhaAIALYEQLDFNEV 123
Cdd:COG2153    39 AYDDGELVATArLLPPGDGEAKIGRVAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFVPV 115

                  .
gi 1011939042 124 S 124
Cdd:COG2153   116 G 116
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
48-122 2.19e-11

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


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 56.31  E-value: 2.19e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011939042  48 DETLAAFAITQVVLDEATLF--NLAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLEVRasnHAAIALYEQLDFNE 122
Cdd:pfam13508  11 DGKIVGFAALLPLDDEGALAelRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETT---NRAAAFYEKLGFEE 84
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
69-124 1.03e-10

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


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 55.74  E-value: 1.03e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1011939042  69 LAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLEVRASNHaAIALYEQLDFNEVS 124
Cdd:pfam13673  57 LFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPY-AVPFYEKLGFRATG 111
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
45-103 6.89e-10

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: 51.89  E-value: 6.89e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011939042  45 LTVDETLAAFA---ITQVVLDEATLFNLAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLE 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. ...
66-120 1.02e-08

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: 49.25  E-value: 1.02e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1011939042  66 LFNLAVDPAFQRRGLGRELLQHLISELEQRGIvTLWLEVRASNHAAIALYEQLDF 120
Cdd:pfam08445  24 LGALQTLPEHRRRGLGSRLVAALARGIAERGI-TPFAVVVAGNTPSRRLYEKLGF 77
PRK10975 PRK10975
dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase;
69-124 4.31e-07

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


Pssm-ID: 182877  Cd Length: 194  Bit Score: 46.85  E-value: 4.31e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1011939042  69 LAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLEVRASNHAAIALYEQLDFNEVS 124
Cdd:PRK10975  132 LAVFPGAQGRGIGARLMQAALNWCQARGLTRLRVATQMGNLAALRLYIRSGANIES 187
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
45-129 1.89e-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: 45.72  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042  45 LTVDETLAAFAI-TQVV----LDEATLFNLAVDPAFQRRGLGRELLQHLISELEQRGIVTLWLEVRASNhaaIALYEQLD 119
Cdd:cd02169     2 LSLDYTVGIFDDaGELIatgsIAGNVLKCVAVCPKYQGEGLALKIVSELINKAYEEGIFHLFLFTKPKN---AKFFRGLG 78
                          90
                  ....*....|
gi 1011939042 120 FNEVSIRRNY 129
Cdd:cd02169    79 FKELANASDE 88
PRK07757 PRK07757
N-acetyltransferase;
69-97 1.10e-04

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 39.79  E-value: 1.10e-04
                          10        20
                  ....*....|....*....|....*....
gi 1011939042  69 LAVDPAFQRRGLGRELLQHLISELEQRGI 97
Cdd:PRK07757   71 LAVSEDYRGQGIGRMLVEACLEEARELGV 99
PseH TIGR03585
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase; Sequences in this ...
75-129 1.35e-04

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: 39.65  E-value: 1.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1011939042  75 FQRRGLGRELLQHLIS-ELEQRGIVTLWLEVRASNHAAIALYEQLDFNEVSIRRNY 129
Cdd:TIGR03585  87 FCKPGVGSVLEEAALEyAFEHLGLHKLSLEVLESNNKALKLYEKFGFEREGVFRQG 142
TmcA COG1444
tRNA(Met) C34 N-acetyltransferase TmcA [Translation, ribosomal structure and biogenesis]; tRNA ...
70-97 4.51e-04

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: 39.04  E-value: 4.51e-04
                          10        20
                  ....*....|....*....|....*...
gi 1011939042  70 AVDPAFQRRGLGRELLQHLISELEQRGI 97
Cdd:COG1444   492 AVHPALQRRGLGSRLLAEIREEAKEEGL 519
GNAT_acetyltran pfam12746
GNAT acetyltransferase; Many of the members are annotated s being Zwittermicin A resistance ...
70-120 1.16e-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: 37.64  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1011939042  70 AVDPAFQRRGLGRELLQHLISELEQRGIVTLWlevRASNHAAIALYEQLDF 120
Cdd:pfam12746 183 DTHPDYRGKGLATICAAALILECLKRGLYPSW---DAHNEASVALAEKLGY 230
PRK10562 PRK10562
putative acetyltransferase; Provisional
60-120 1.69e-03

putative acetyltransferase; Provisional


Pssm-ID: 236715 [Multi-domain]  Cd Length: 145  Bit Score: 36.58  E-value: 1.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011939042  60 VLDEATLFNLAVDPAFQRRGLGRELLQHLiseleQRGIVTLWLEVRASNHAAIALYEQLDF 120
Cdd:PRK10562   65 VLEGRFVGALFVAPKAVRRGIGKALMQHV-----QQRYPHLSLEVYQKNQRAVNFYHAQGF 120
Eis COG4552
Predicted acetyltransferase [General function prediction only];
3-101 3.79e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 36.42  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011939042   3 QISLLTAHDLEQAYAIEQRSHAFPWT----EKTFTSNQGERYlnYRLTVDETLAAfaITQVVLDEATLFN---------- 68
Cdd:COG4552     2 EIRPLTEDDLDAFARLLAYAFGPEPDdeelEAYRPLLEPGRV--LGVFDDGELVG--TLALYPFTLNVGGarvpmagitg 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1011939042  69 LAVDPAFQRRGLGRELLQHLISELEQRG--IVTLW 101
Cdd:COG4552    78 VAVAPEHRRRGVARALLREALAELRERGqpLSALY 112
YidJ COG2388
Predicted acetyltransferase, GNAT superfamily [General function prediction only];
43-96 4.66e-03

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


Pssm-ID: 441953 [Multi-domain]  Cd Length: 88  Bit Score: 34.36  E-value: 4.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1011939042  43 YRLTVDETLAAFAITQVVLDEATLFNLAVDPAFQRRGLGRELLQHLISELEQRG 96
Cdd:COG2388    12 FELEVDGELAGELTYRLEGGVIIITHTEVPPALRGQGIASALVEAALDDARERG 65
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH